|
Name |
Accession |
Description |
Interval |
E-value |
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-495 |
0e+00 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 707.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTENVALGLSTG----ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPK 156
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGLEPTkggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMIGND 236
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGRE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 237 -PPTVREGTAKAGEVVFEMRHVSAPGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSP 315
Cdd:COG3845 242 vLLRVEKAPAEPGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 316 VGELDTHARRISGLRYVPEQRLGHAAVPELSLTANTYLT---GDSLVRSGFILRDRARSFANLVIERFHVKTPNAEKAAG 392
Cdd:COG3845 322 ITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGryrRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPAR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 393 SLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALS 472
Cdd:COG3845 402 SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
490 500
....*....|....*....|...
gi 2549828669 473 PAVPKPTISIEEVGRWMSGLWPD 495
Cdd:COG3845 482 GEVPAAEATREEIGLLMAGVKEE 504
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-491 |
3.36e-173 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 497.23 E-value: 3.36e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTENVALG--LSTG--ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPK 156
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGrePRRGglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMIGND 236
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGRE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 237 PPTVR-EGTAKAGEVVFEMRHVSAPGstrvcGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSP 315
Cdd:COG1129 241 LEDLFpKRAAAPGEVVLEVEGLSVGG-----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 316 VGELDTHARRISGLRYVPEQRLGHAAVPELSLTANTYLTG-DSLVRSGFILRDRARSFANLVIERFHVKTPNAEKAAGSL 394
Cdd:COG1129 316 VRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASlDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 395 SGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALSPA 474
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGE 475
|
490
....*....|....*..
gi 2549828669 475 VPKPTISIEEVGRWMSG 491
Cdd:COG1129 476 LDREEATEEAIMAAATG 492
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-471 |
1.94e-114 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 347.30 E-value: 1.94e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKII-----YGAArpdEGEISFDGHPLGVETPAQ 75
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvypHGTY---EGEIIFEGEELQASNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 76 ARELGIAMVHQHFALFDTLSVTENVALG--LSTG--ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRAL 151
Cdd:PRK13549 79 TERAGIAIIHQELALVKELSVLENIFLGneITPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARL 231
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 232 MIGndpptvREGTA-------KAGEVVFEMRHVSA--PGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEY 302
Cdd:PRK13549 239 MVG------RELTAlyprephTIGEVILEVRNLTAwdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 303 --LCEADrVLLFNSPVgELDTHARRIS-GLRYVPEQRLGHAAVPELSLTANTYLTG-DSLVRSGFILRDRARSFANLVIE 378
Cdd:PRK13549 313 pgRWEGE-IFIDGKPV-KIRNPQQAIAqGIAMVPEDRKRDGIVPVMGVGKNITLAAlDRFTGGSRIDDAAELKTILESIQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 379 RFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFE 458
Cdd:PRK13549 391 RLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLG 470
|
490
....*....|...
gi 2549828669 459 ISDRIAVMYRGAL 471
Cdd:PRK13549 471 LSDRVLVMHEGKL 483
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-506 |
6.38e-103 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 317.76 E-value: 6.38e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTENVALGLSTgiSAAEIEREIRLLGEkYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGLPK--RQASMQKMKQLLAA-LGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMigndPPTV 240
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI----TPAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 241 REGTAKAGEVVF----EMRHVSAPGST--RVC-----GIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRV 309
Cdd:PRK15439 241 REKSLSASQKLWlelpGNRRQQAAGAPvlTVEdltgeGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 310 LLFNSPVGELDTHARRISGLRYVPEQRLGHAAVPELSLTANTYltgdSLV--RSGFILRdRARSFAnlVIERFH----VK 383
Cdd:PRK15439 321 MLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVC----ALThnRRGFWIK-PARENA--VLERYRralnIK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 384 TPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRI 463
Cdd:PRK15439 394 FNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRV 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2549828669 464 AVMYRGALSPAVPKPTISIEEVGRWMSGlwpdspfTQKTSEAH 506
Cdd:PRK15439 474 LVMHQGEISGALTGAAINVDTIMRLAFG-------EHQAQEAS 509
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-478 |
3.35e-101 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 313.00 E-value: 3.35e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTENVALG-LSTG---ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPK 156
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGqLPHKggiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAE-SEENLARLMIGN 235
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQvDRDQLVQAMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 236 DPPTV-----REgtakAGEVVFEMRHVSAPGSTrvcgiDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVL 310
Cdd:PRK11288 241 EIGDIygyrpRP----LGEVRLRLDGLKGPGLR-----EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 311 LFNSPVGELDTHARRISGLRYVPEQRLGHAAVPELSLTANTYLTG-DSLVRSGFILRDRA-RSFANLVIERFHVKTPNAE 388
Cdd:PRK11288 312 LDGKPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISArRHHLRAGCLINNRWeAENADRFIRSLNIKTPSRE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 389 KAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYR 468
Cdd:PRK11288 392 QLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMRE 471
|
490
....*....|
gi 2549828669 469 GALSPAVPKP 478
Cdd:PRK11288 472 GRIAGELARE 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-472 |
1.24e-100 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 311.55 E-value: 1.24e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTENVALGLST-----GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKP 155
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGREFvnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 156 KLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMIG- 234
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGr 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 235 ---------NDPPtvregtakaGEVVFEMRHVSAPgstrvcGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCE 305
Cdd:PRK10762 241 kledqyprlDKAP---------GEVRLKVDNLSGP------GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 306 ADRVLLFNSPVGELDTHARRISGLRYVPEQRLGHAAVPELSLTANTYLTG-DSLVRSGFILRDRARSFA-NLVIERFHVK 383
Cdd:PRK10762 306 SGYVTLDGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTAlRYFSRAGGSLKHADEQQAvSDFIRLFNIK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 384 TPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRI 463
Cdd:PRK10762 386 TPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRI 465
|
....*....
gi 2549828669 464 AVMYRGALS 472
Cdd:PRK10762 466 LVMHEGRIS 474
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-488 |
1.23e-99 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 309.41 E-value: 1.23e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTENVALG-LSTG-------ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALM 152
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGrHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLM 232
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 233 IGNDP----PTVREGTAK-AGEVVFEMRHVSAPGSTRVcgiDNVSLAVRAGEIVGIAGISGNGQARFMAA-------ASG 300
Cdd:PRK09700 242 VGRELqnrfNAMKENVSNlAHETVFEVRNVTSRDRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNClfgvdkrAGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 301 EYLCEADRVllfnSPVGELDTHARrisGLRYVPEQRLGHAAVPELSLTANTYLTgDSLVRSGF-----ILRDR-ARSFAN 374
Cdd:PRK09700 319 EIRLNGKDI----SPRSPLDAVKK---GMAYITESRRDNGFFPNFSIAQNMAIS-RSLKDGGYkgamgLFHEVdEQRTAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 375 LVIERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEID 454
Cdd:PRK09700 391 NQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELP 470
|
490 500 510
....*....|....*....|....*....|....*
gi 2549828669 455 ELFEISDRIAVMYRGALSPAVP-KPTISIEEVGRW 488
Cdd:PRK09700 471 EIITVCDRIAVFCEGRLTQILTnRDDMSEEEIMAW 505
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-489 |
6.38e-97 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 302.09 E-value: 6.38e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYG--AARPDEGEISFDGHPLGVETPAQARELGIA 82
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyPHGSYEGEILFDGEVCRFKDIRDSEALGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTLSVTENVALGLSTG----ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLL 158
Cdd:NF040905 82 IIHQELALIPYLSIAENIFLGNERAkrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAE--SEENLARLMIGND 236
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRADevTEDRIIRGMVGRD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 237 -----PPTvregTAKAGEVVFEMRHVSA--PG-STRVCgIDNVSLAVRAGEIVGIAGISGNGQARFMAA---------AS 299
Cdd:NF040905 242 ledryPER----TPKIGEVVFEVKNWTVyhPLhPERKV-VDDVSLNVRRGEIVGIAGLMGAGRTELAMSvfgrsygrnIS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 300 GEylceadrVLLFNSPVgELDTHARRI-SGLRYVPEQRLGHAAVPELSLTANTYLTG-DSLVRSGFILRDRARSFANLVI 377
Cdd:NF040905 317 GT-------VFKDGKEV-DVSTVSDAIdAGLAYVTEDRKGYGLNLIDDIKRNITLANlGKVSRRGVIDENEEIKVAEEYR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 378 ERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELF 457
Cdd:NF040905 389 KKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELL 468
|
490 500 510
....*....|....*....|....*....|..
gi 2549828669 458 EISDRIAVMYRGALSPAVPKPTISIEEVGRWM 489
Cdd:NF040905 469 GMCDRIYVMNEGRITGELPREEASQERIMRLI 500
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-471 |
4.06e-92 |
|
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: 289.80 E-value: 4.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAaRPD---EGEISFDGHPLGVETPAQARELGI 81
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFALFDTLSVTENVALG----LSTGISA-AEIEREIRLLGEKYGLEVDPAS-VVMELSMGERQRVEILRALMTKP 155
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneitLPGGRMAyNAMYLRAKNLLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 156 KLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMIGn 235
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 236 dpptvREGTA-------KAGEVVFEMRHVSA--PGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEY--LC 304
Cdd:TIGR02633 240 -----REITSlyphephEIGDVILEARNLTCwdVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpgKF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 305 EADrVLLFNSPVgELDTHARRI-SGLRYVPEQRLGHAAVPELSLTANTYLTgdSLVRSGFILRDRARSFANLV---IERF 380
Cdd:TIGR02633 315 EGN-VFINGKPV-DIRNPAQAIrAGIAMVPEDRKRHGIVPILGVGKNITLS--VLKSFCFKMRIDAAAELQIIgsaIQRL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 381 HVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEIS 460
Cdd:TIGR02633 391 KVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLS 470
|
490
....*....|.
gi 2549828669 461 DRIAVMYRGAL 471
Cdd:TIGR02633 471 DRVLVIGEGKL 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-485 |
7.64e-90 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 283.54 E-value: 7.64e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 7 LRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAMVHQ 86
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 87 HFALFDTLSVTENVALGL----STGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDE 162
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRyptkGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 163 PTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMIGNDpPTVR- 241
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRS-LTQRf 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 242 -EGTAKAGEVVFEMRHVSApgsTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELD 320
Cdd:PRK10982 240 pDKENKPGEVILEVRNLTS---LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 321 THARRISGLRYVPEQRLGHAAVPELSLTANTYLTGDSLVRSGFILRD--RARSFANLVIERFHVKTPNAEKAAGSLSGGN 398
Cdd:PRK10982 317 ANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDnsRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 399 LQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALSPAVPKP 478
Cdd:PRK10982 397 QQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTK 476
|
....*..
gi 2549828669 479 TISIEEV 485
Cdd:PRK10982 477 TTTQNEI 483
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-217 |
1.68e-81 |
|
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: 250.42 E-value: 1.68e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAMV 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQhfalfdtlsvtenvalglstgisaaeiereirllgekyglevdpasvvmeLSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:cd03216 81 YQ--------------------------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 165 SVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-469 |
2.26e-70 |
|
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: 233.26 E-value: 2.26e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPG--ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPD---EGEISFDGHPLgVETPAQ 75
Cdd:COG1123 1 MTPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL-LELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 76 ARELGIAMVHQHF-ALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMT 153
Cdd:COG1123 80 LRGRRIGMVFQDPmTQLNPVTVGDQIAEALEnLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA--ESEENLAR 230
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEilAAPQALAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 231 LMIGNDPPTVREGTAKAGEVVFEMRHVS----APGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAAS 299
Cdd:COG1123 240 VPRLGAARGRAAPAAAAAEPLLEVRNLSkrypVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKstlarllLGLLRPTS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 300 GEylceadrVLLFNSPVGELDTHARRisGLR----YVPeQRlghaavPELSLtaNTYLT-----GDSLVRSGFILRDRAR 370
Cdd:COG1123 320 GS-------ILFDGKDLTKLSRRSLR--ELRrrvqMVF-QD------PYSSL--NPRMTvgdiiAEPLRLHGLLSRAERR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 371 SFANLVIERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVV 449
Cdd:COG1123 382 ERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFI 461
|
490 500
....*....|....*....|
gi 2549828669 450 SEEIDELFEISDRIAVMYRG 469
Cdd:COG1123 462 SHDLAVVRYIADRVAVMYDG 481
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-228 |
5.31e-66 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 213.00 E-value: 5.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARELgIAMV 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV-ARDPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVAL-GLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:COG1131 79 PQEPALYPDLTVRENLRFfARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENL 228
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
248-471 |
1.37e-59 |
|
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: 194.19 E-value: 1.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 248 GEVVFEMRHVSAPGSTRvcgidNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRIS 327
Cdd:cd03215 1 GEPVLEVRGLSVKGAVR-----DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 328 GLRYVPEQRLGHAAVPELSLtantyltgdslvrsgfilrdrarsFANLVIERFhvktpnaekaagsLSGGNLQKFIMGRE 407
Cdd:cd03215 76 GIAYVPEDRKREGLVLDLSV------------------------AENIALSSL-------------LSGGNQQKVVLARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 408 ILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-217 |
1.20e-58 |
|
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: 194.49 E-value: 1.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTENVALG-------------LSTGISAAEiEREIR-----LLgEKYGLEVDPASVVMELSMGER 142
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAaharlgrgllaalLRLPRARRE-EREAReraeeLL-ERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 143 QRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-214 |
1.24e-58 |
|
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: 191.46 E-value: 1.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQARELgIAMV 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK-KEPEEVKRR-IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENValglstgisaaeiereirllgekyglevdpasvvmELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:cd03230 79 PEEPSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2549828669 165 SVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-220 |
2.32e-57 |
|
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: 190.34 E-value: 2.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAMV 84
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVALGL----STGISAAEIEREIRLLGEK----------YGLEVDPASvvmELSMGERQRVEILRA 150
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAqartGSGLLLARARREEREARERaeellervglADLADRPAG---ELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-222 |
2.57e-56 |
|
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: 187.54 E-value: 2.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIAM 83
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 VHQH-----FALfdtlSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:COG1122 80 VFQNpddqlFAP----TVEEDVAFGPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-223 |
7.60e-56 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 189.97 E-value: 7.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARelGIAMV 84
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRER--RVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGLE----VDPAsvvmELSMGERQRVEILRALMTKPKLLI 159
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVrPPSKAEIRARVEELLELVQLEgladRYPS----QLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 160 LDEPTSVLTPQaVRK-----LFKTLHQLsseGVSILFISHKLDEIRELADRCVVLRAGKVVAsVDPKAE 223
Cdd:COG1118 157 LDEPFGALDAK-VRKelrrwLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQ-VGTPDE 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-226 |
2.29e-55 |
|
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: 185.45 E-value: 2.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARELgIAMV 84
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-RKEPREARRQ-IGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVA-LGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:COG4555 80 PDERGLYDRLTVRENIRyFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEE 226
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-216 |
3.06e-54 |
|
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: 181.56 E-value: 3.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARelGIAMV 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERR--NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVALGL-STGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 164 TSVLTPQ---AVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:cd03259 158 LSALDAKlreELREELKELQR--ELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-213 |
4.32e-53 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 178.43 E-value: 4.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 6 SLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIAM 83
Cdd:cd03225 1 ELKNLSFSYPDGARPalDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 VHQHFAL-FDTLSVTENVALGL-STGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILD 161
Cdd:cd03225 80 VFQNPDDqFFGPTVEEEVAFGLeNLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 162 EPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGK 213
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-222 |
4.73e-53 |
|
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: 187.03 E-value: 4.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPRLSLRNITKRYP-----GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQA 76
Cdd:COG1123 258 EPLLEVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 77 RELG--IAMVHQH-FA-LFDTLSVTENVALGLS--TGISAAEIEREIRLLGEKYGLEVD-----PAsvvmELSMGERQRV 145
Cdd:COG1123 338 RELRrrVQMVFQDpYSsLNPRMTVGDIIAEPLRlhGLLSRAERRERVAELLERVGLPPDladryPH----ELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 146 EILRALMTKPKLLILDEPTSVLTP--QA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVsvQAqILNLLRDLQR--ELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-219 |
5.26e-53 |
|
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: 178.43 E-value: 5.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAqarelg 80
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLE--VD--PAsvvmELSMGERQRVEILRALMTKP 155
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLElQGVPKAEARERAEELLELVGLSgfENayPH----QLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 156 KLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVL--RAGKVVASVD 219
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVE 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-222 |
5.74e-53 |
|
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: 178.40 E-value: 5.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAMV 84
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVALGLSTGISA---AEIEREIRL---LGEKYGlevDPASvvmELSMGERQRVEILRALMTKPKLL 158
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAkrkARLERVYELfprLKERRK---QLAG---TLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-281 |
6.71e-53 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 182.61 E-value: 6.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARelG 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLPPEKR--N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTENVALGLST-GISAAEIEREIR--L-------LGEKYglevdPAsvvmELSMGERQRVEILRA 150
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGLRMrGVPKAEIRARVAelLelvglegLADRY-----PH----QLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQ---AVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA--ESE 225
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKlreEMREELRRLQR--ELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEiyERP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 226 ENL--ARLmIGND---PPTVREGTakAGEVVFEMRHVSAPGSTRVCGIDNVSLAVRAGEIV 281
Cdd:COG3842 228 ATRfvADF-IGEAnllPGTVLGDE--GGGVRTGGRTLEVPADAGLAAGGPVTVAIRPEDIR 285
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
7.15e-53 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 178.31 E-value: 7.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYP----GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ- 75
Cdd:COG1136 1 MSPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 76 ----ARELGIamVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLE--VD--PAsvvmELSMGERQRVE 146
Cdd:COG1136 81 arlrRRHIGF--VFQFFNLLPELTALENVALPLLlAGVSRKERRERARELLERVGLGdrLDhrPS----QLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 147 ILRALMTKPKLLILDEPTSVL---TPQAVRKLFKTLHQlsSEGVSILFISHklD-EIRELADRCVVLRAGKVVA 216
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLdskTGEEVLELLRELNR--ELGTTIVMVTH--DpELAARADRVIRLRDGRIVS 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-231 |
2.62e-52 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 177.56 E-value: 2.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL--GI 81
Cdd:COG3638 3 LELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFALFDTLSVTENVALG----------LSTGISAAEIEREIRLLgEKYGLE---VDPASvvmELSMGERQRVEIL 148
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGrlgrtstwrsLLGLFPPEDRERALEAL-ERVGLAdkaYQRAD---QLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 149 RALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEEN 227
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDAV 238
|
....
gi 2549828669 228 LARL 231
Cdd:COG3638 239 LREI 242
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-280 |
1.62e-51 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 178.73 E-value: 1.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQARelGIAM 83
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-DLPPKDR--NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 VHQHFALFDTLSVTENVALGLST-GISAAEIEREIR----LLG-EKYgLEVDPAsvvmELSMGERQRVEILRALMTKPKL 157
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLrKVPKAEIDRRVReaaeLLGlEDL-LDRKPK----QLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 158 LILDEPTSVLTPQ---AVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKV--VASVD-----PKaeseeN 227
Cdd:COG3839 155 FLLDEPLSNLDAKlrvEMRAEIKRLHR--RLGTTTIYVTHDQVEAMTLADRIAVMNDGRIqqVGTPEelydrPA-----N 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 228 L--ARLmIGNDPPTVREGTAKAGEVVFEMRHVSAPGSTRVCGIDNVSLAVRAGEI 280
Cdd:COG3839 228 LfvAGF-IGSPPMNLLPGTVEGGGVRLGGVRLPLPAALAAAAGGEVTLGIRPEHL 281
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-217 |
1.97e-51 |
|
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: 175.17 E-value: 1.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL- 79
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 80 -GIAMVHQHFALFDTLSVTENVALGL--STGISAAEIEREIRLLGEKYGLEVD----PAsvvmELSMGERQRVEILRALM 152
Cdd:COG1127 82 rRIGMLFQGGALFDSLTVFENVAFPLreHTDLSEAEIRELVLEKLELVGLPGAadkmPS----ELSGGMRKRVALARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-219 |
3.64e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 174.89 E-value: 3.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYP----GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgVETPAQA 76
Cdd:COG1116 4 AAPALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP--VTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 77 RelgiAMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLE--VD--PAsvvmELSMGERQRVEILRAL 151
Cdd:COG1116 82 R----GVVFQEPALLPWLTVLDNVALGLElRGVPKAERRERARELLELVGLAgfEDayPH----QLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 152 MTKPKLLILDEPTS---VLTPQAVRKLFKTLHQlsSEGVSILFISHKLDE-IReLADRCVVLRA--GKVVASVD 219
Cdd:COG1116 154 ANDPEVLLMDEPFGaldALTRERLQDELLRLWQ--ETGKTVLFVTHDVDEaVF-LADRVVVLSArpGRIVEEID 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-214 |
3.70e-51 |
|
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: 173.44 E-value: 3.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ----- 75
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 76 ARELGIamVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTK 154
Cdd:cd03255 81 RRHIGF--VFQSFNLLPDLTALENVELPLLlAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKlDEIRELADRCVVLRAGKV 214
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-215 |
3.90e-51 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 173.70 E-value: 3.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGV----ETPAQAREL 79
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 80 GIamVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLL 158
Cdd:COG2884 82 GV--VFQDFRLLPDRTVYENVALPLRvTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-222 |
7.14e-51 |
|
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: 173.24 E-value: 7.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGI 81
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFALFDTLSVTENVALGLSTGISAAEIEREIRL-------LGEKYGlevDPASvvmELSMGERQRVEILRALMTK 154
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERvyelfprLKERRR---QRAG---TLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAE 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-215 |
9.18e-50 |
|
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: 170.45 E-value: 9.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL- 79
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 80 -GIAMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:cd03258 82 rRIGMIFQHFNLLSSRTVFENVALPLEiAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-216 |
1.02e-49 |
|
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: 170.38 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG--IA 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTLSVTENVALGLS--TGISAAEIEREIRLLGEKYGLEVD----PAsvvmELSMGERQRVEILRALMTKPK 156
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLRehTRLSEEEIREIVLEKLEAVGLRGAedlyPA----ELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 157 LLILDEPTSVLTPQAVRK---LFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:cd03261 157 LLLYDEPTAGLDPIASGViddLIRSLKK--ELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-231 |
1.03e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 167.96 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgvetPAQARELg 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFAlFDT---LSVTENVALGLSTGI------SAAEIEREIRLLgEKYGLEvDPASV-VMELSMGERQRVEILRA 150
Cdd:COG1121 77 IGYVPQRAE-VDWdfpITVRDVVLMGRYGRRglfrrpSRADREAVDEAL-ERVGLE-DLADRpIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLrAGKVVASVDPK-AESEENLA 229
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEeVLTPENLS 232
|
..
gi 2549828669 230 RL 231
Cdd:COG1121 233 RA 234
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-215 |
2.24e-48 |
|
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: 166.53 E-value: 2.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:cd03257 2 LEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 --IAMVHQH--FALFDTLSVTENVA--LGLSTGISAAEIEREIRLLGEKyglEVDPASVVM-----ELSMGERQRVEILR 149
Cdd:cd03257 82 keIQMVFQDpmSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLV---GVGLPEEVLnryphELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 150 ALMTKPKLLILDEPTS---VLTPQAVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03257 159 ALALNPKLLIADEPTSaldVSVQAQILDLLKKLQE--ELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-213 |
3.29e-48 |
|
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: 164.28 E-value: 3.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL---GVETPAQARELGi 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdlEDELPPLRRRIG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 aMVHQHFALFDTLSVTENVALGLSTgisaaeiereirllgekyglevdpasvvmelsmGERQRVEILRALMTKPKLLILD 161
Cdd:cd03229 80 -MVFQDFALFPHLTVLENIALGLSG---------------------------------GQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 162 EPTSVLTPQA---VRKLFKTLHQLSseGVSILFISHKLDEIRELADRCVVLRAGK 213
Cdd:cd03229 126 EPTSALDPITrreVRALLKSLQAQL--GITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-231 |
6.20e-48 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 165.82 E-value: 6.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL--GI 81
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFALFDTLSVTENVALG----------LSTGISAAEIEREIRLLgEKYGLEVDPASVVMELSMGERQRVEILRAL 151
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrstwrsLFGLFPKEEKQRALAAL-ERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLAR 230
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDE 239
|
.
gi 2549828669 231 L 231
Cdd:cd03256 240 I 240
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-217 |
4.65e-47 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 166.41 E-value: 4.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL- 79
Cdd:COG1135 2 IELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 80 -GIAMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEvD-----PAsvvmELSMGERQRVEILRALM 152
Cdd:COG1135 82 rKIGMIFQHFNLLSSRTVAENVALPLEiAGVPKAEIRKRVAELLELVGLS-DkadayPS----QLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 153 TKPKLLILDEPTSVLTPQ---AVRKLFKTLHQ-LsseGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:COG1135 157 NNPKVLLCDEATSALDPEttrSILDLLKDINReL---GLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-217 |
6.86e-47 |
|
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: 162.00 E-value: 6.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAReLGiAMV 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-IG-ALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHfALFDTLSVTENV-ALGLSTGISAAEIEREIRLLGekygLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03268 79 EAP-GFYPNLTARENLrLLARLLGIRKKRIDEVLDVVG----LKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-214 |
7.01e-47 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 161.93 E-value: 7.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQAREL--GIA 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELrqKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTLSVTENVALGLST--GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKvkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-213 |
7.80e-47 |
|
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: 160.10 E-value: 7.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 6 SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIAMVH 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-RIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 86 QhfalfdtlsvtenvalglstgisaaeiereirllgekyglevdpasvvmeLSMGERQRVEILRALMTKPKLLILDEPTS 165
Cdd:cd00267 80 Q--------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2549828669 166 VLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGK 213
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-214 |
1.10e-46 |
|
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: 162.51 E-value: 1.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 8 RNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQARELGiaMVHQH 87
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT-DVPVQERNVG--FVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 88 FALFDTLSVTENVALGL-----STGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDE 162
Cdd:cd03296 83 YALFRHMTVFDNVAFGLrvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 163 PTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-217 |
3.69e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 162.97 E-value: 3.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ------ARe 78
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeER- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 lgiamvhqhfALFDTLSVTEN-VALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:COG4152 81 ----------GLYPKMKVGEQlVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-216 |
3.95e-46 |
|
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: 160.14 E-value: 3.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETpaqarELGIAMV 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTEN-VALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03269 76 PEERGLYPKMKVIDQlVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-221 |
1.46e-45 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 159.39 E-value: 1.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQAREL--GIA 82
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLrrKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTLSVTENVALGLST--GISAAEIEREIRLLGEKYGL----EVDPAsvvmELSMGERQRVEILRALMTKPK 156
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKvkKMSKAEAEERAMELLERVGLadkaDAYPA----QLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:COG1126 157 VMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPE 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-165 |
3.07e-45 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 155.50 E-value: 3.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIAMVHQHFALFDTLSVTENV 100
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 ALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVM----ELSMGERQRVEILRALMTKPKLLILDEPTS 165
Cdd:pfam00005 81 RLGLLlKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-231 |
3.93e-45 |
|
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: 158.67 E-value: 3.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ-ARElgIA 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElARR--IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTLSVTENVALGLSTGISA---------AEIEREIRLLG-----EKYglevdpasvVMELSMGERQRVEIL 148
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGRYPHLGLfgrpsaedrEAVEEALERTGlehlaDRP---------VDELSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 149 RALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPkAE--SE 225
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP-EEvlTP 228
|
....*.
gi 2549828669 226 ENLARL 231
Cdd:COG1120 229 ELLEEV 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-215 |
5.44e-45 |
|
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: 157.78 E-value: 5.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARelGIAMV 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKR--PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLkKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 164 TSVLTPQAVRKL---FKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03300 158 LGALDLKLRKDMqleLKRLQK--ELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-217 |
7.34e-45 |
|
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: 167.70 E-value: 7.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARE 78
Cdd:COG2274 470 LKGDIELENVSFRYPGDSPPvlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 LgIAMVHQHFALFDTlSVTENVALGlSTGISAAEIEREIRLLG-----EK--YGLEvdpaSVVME----LSMGERQRVEI 147
Cdd:COG2274 550 Q-IGVVLQDVFLFSG-TIRENITLG-DPDATDEEIIEAARLAGlhdfiEAlpMGYD----TVVGEggsnLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIReLADRCVVLRAGKVVAS 217
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIR-LADRIIVLDKGRIVED 690
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-217 |
1.72e-44 |
|
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: 156.13 E-value: 1.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGI--TANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIA 82
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MvhQHFALFDTLSVTENVAL-GLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILD 161
Cdd:cd03263 81 P--QFDALFDELTVREHLRFyARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 162 EPTSVLTPQAVRKLFKTLHQLSSeGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCI 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-213 |
1.25e-43 |
|
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: 151.77 E-value: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIA 82
Cdd:cd03228 1 IEFKNVSFSYPGRPKPvlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTlSVTENValglstgisaaeiereirllgekyglevdpasvvmeLSMGERQRVEILRALMTKPKLLILDE 162
Cdd:cd03228 80 YVPQDPFLFSG-TIRENI------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 163 PTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIReLADRCVVLRAGK 213
Cdd:cd03228 123 ATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-214 |
1.82e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 152.66 E-value: 1.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIAMV 84
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ-VAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTlSVTENVALGLSTGISAAEIEREIRLLgEKYGLevdPASV----VMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:COG4619 80 PQEPALWGG-TVRDNLPFPFQLRERKFDRERALELL-ERLGL---PPDIldkpVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLS-SEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLaEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-220 |
8.23e-43 |
|
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: 151.93 E-value: 8.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAMV 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVALGL-STGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLeIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-215 |
8.71e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 154.96 E-value: 8.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 7 LRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL--G 80
Cdd:PRK11153 4 LKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLE----VDPAsvvmELSMGERQRVEILRALMTKP 155
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLElAGTPKAEIKARVTELLELVGLSdkadRYPA----QLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 156 KLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
7-213 |
1.33e-42 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 150.86 E-value: 1.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 7 LRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL----GVETPAQARELGI 81
Cdd:TIGR02673 4 FHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVnrlrGRQLPLLRRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 amVHQHFALFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:TIGR02673 84 --VFQDFRLLPDRTVYENVALPLEVrGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGK 213
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-222 |
1.51e-42 |
|
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: 151.49 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYP----GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElG 80
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQH-FALFD-TLSVTENVALGL-STGIsaAEIEREIRLLGEKYGLEVD-----PAsvvmELSMGERQRVEILRALM 152
Cdd:COG1124 81 VQMVFQDpYASLHpRHTVDRILAEPLrIHGL--PDREERIAELLEQVGLPPSfldryPH----QLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 153 TKPKLLILDEPTSVLTP--QA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:COG1124 155 LEPELLLLDEPTSALDVsvQAeILNLLKDLRE--ERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-219 |
2.71e-42 |
|
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: 153.29 E-value: 2.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARP---DEGEISFDGHPLGVETPAQAR 77
Cdd:COG0444 2 LEVRNLKVYFPTrrgvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 78 EL---GIAMVHQhfalfDTLS-----------VTEnvALGLSTGISAAEIEREIRLLGEKYGLEvDPASVVM----ELSM 139
Cdd:COG0444 82 KIrgrEIQMIFQ-----DPMTslnpvmtvgdqIAE--PLRIHGGLSKAEARERAIELLERVGLP-DPERRLDryphELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 140 GERQRVEILRALMTKPKLLILDEPTSVL--TPQA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVV- 215
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALdvTIQAqILNLLKDLQR--ELGLAILFITHDLGVVAEIADRVAVMYAGRIVe 231
|
....*
gi 2549828669 216 -ASVD 219
Cdd:COG0444 232 eGPVE 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-215 |
4.71e-42 |
|
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: 149.33 E-value: 4.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHplgVETPAQARELGIAMV 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR---DVTDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVALGL-STGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLkLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 164 TSVLTPQ---AVRKLFKTLHQLssEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03301 158 LSNLDAKlrvQMRAELKRLQQR--LGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-215 |
1.13e-41 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 149.37 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL--GI 81
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFALFDTLSVTENV---ALGLSTGI-------SAAEIEREIRLLgEKYGLEVDPASVVMELSMGERQRVEILRAL 151
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVlhgRLGYKPTWrsllgrfSEEDKERALSAL-ERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-215 |
1.47e-41 |
|
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: 149.72 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 19 ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL---GIAMVHQHFALFDTLS 95
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 96 VTENVALGLS-TGISAAE-IEREIRLLgEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVR 173
Cdd:cd03294 119 VLENVAFGLEvQGVPRAErEERAAEAL-ELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2549828669 174 KLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03294 198 EMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-217 |
3.08e-41 |
|
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: 147.13 E-value: 3.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRY----PGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQAReLG 80
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEAR-RR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTENVA-LGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLI 159
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEyFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-217 |
9.78e-41 |
|
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: 145.75 E-value: 9.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 6 SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgvetPAQARELgIAMVH 85
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP-----LEKERKR-IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 86 QHFaLFDT---LSVTENVALGL------STGISAAEIEREIRLLgEKYGLEVDPASVVMELSMGERQRVEILRALMTKPK 156
Cdd:cd03235 75 QRR-SIDRdfpISVRDVVLMGLyghkglFRRLSKADKAKVDEAL-ERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLrAGKVVAS 217
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVAS 212
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-227 |
2.35e-40 |
|
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: 152.99 E-value: 2.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgI 81
Cdd:COG4988 335 PSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ-I 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFALFDTlSVTENVALGlSTGISAAEIEREIR---LLGEKYGLEVDPASVVME----LSMGERQRVEILRALMTK 154
Cdd:COG4988 414 AWVPQNPYLFAG-TIRENLRLG-RPDASDEELEAALEaagLDEFVAALPDGLDTPLGEggrgLSGGQAQRLALARALLRD 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVVASVDPKAESEEN 227
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-241 |
3.57e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 144.90 E-value: 3.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITAndHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQaRelGIAMV 84
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-R--PVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVALGLSTG--ISAAEIEREIRLLgEKYGLE--VD--PAsvvmELSMGERQRVEILRALMTKPKLL 158
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRPGlkLTAEQRAQVEQAL-ERVGLAglLDrlPG----QLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 159 ILDEPTSVLTPqAVRK----LFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPkaeseenlARLMIG 234
Cdd:COG3840 152 LLDEPFSALDP-ALRQemldLVDELCR--ERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPT--------AALLDG 220
|
....*..
gi 2549828669 235 NDPPTVR 241
Cdd:COG3840 221 EPPPALA 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-221 |
5.55e-40 |
|
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: 144.40 E-value: 5.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgveTPAQARELGIAMVHQHFALFDTLSVTENVAL 102
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI---TNLPPEKRDISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 103 GLST-GISAAEIEREIRLLGEKYG----LEVDPASvvmeLSMGERQRVEILRALMTKPKLLILDEPTSVLTPQ---AVRK 174
Cdd:cd03299 95 GLKKrKVDKKEIERKVLEIAEMLGidhlLNRKPET----LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRtkeKLRE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2549828669 175 LFKTLHQLSseGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:cd03299 171 ELKKIRKEF--GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-213 |
7.43e-40 |
|
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: 143.00 E-value: 7.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIA 82
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MvhQHFALFDTLSVTENVAL---GLSTGISAAEIEREIRLLGeKYGLEVDPASvvmELSMGERQRVEILRALMTKPKLLI 159
Cdd:COG4133 81 G--HADGLKPELTVRENLRFwaaLYGLRADREAIDEALEAVG-LAGLADLPVR---QLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHklDEIRELADRCVVLRAGK 213
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH--QPLELAAARVLDLGDFK 206
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-217 |
7.66e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 151.86 E-value: 7.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYPG-ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIA 82
Cdd:COG1132 339 EIEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ-IG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTlSVTENVALGlSTGISAAEIER---------EIRLLGEKYGLEVDPASVvmELSMGERQRVEILRALMT 153
Cdd:COG1132 418 VVPQDTFLFSG-TIRENIRYG-RPDATDEEVEEaakaaqaheFIEALPDGYDTVVGERGV--NLSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVVAS 217
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
9-263 |
2.15e-39 |
|
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: 146.40 E-value: 2.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 9 NITKRYPGITANdhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL-----GVETPAQARELGiaM 83
Cdd:COG4148 6 DFRLRRGGFTLD--VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsarGIFLPPHRRRIG--Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 VHQHFALFDTLSVTENVALGLS---TGISAAEIEREIRLLGEKYGLEVDPASvvmeLSMGERQRVEILRALMTKPKLLIL 160
Cdd:COG4148 82 VFQEARLFPHLSVRGNLLYGRKrapRAERRISFDEVVELLGIGHLLDRRPAT----LSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASvDPKAE--SEENLARLMIGNDP 237
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVAS-GPLAEvlSRPDLLPLAGGEEA 236
|
250 260
....*....|....*....|....*.
gi 2549828669 238 PTVREGTAKAGEVVFEMRHVSAPGST 263
Cdd:COG4148 237 GSVLEATVAAHDPDYGLTRLALGGGR 262
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
4-217 |
3.10e-39 |
|
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: 141.66 E-value: 3.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRnITKRYPGITANdhVSLDIaPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL-----GVETPAQARe 78
Cdd:cd03297 1 MLCVD-IEKRLPDFTLK--IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkKINLPPQQR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 lGIAMVHQHFALFDTLSVTENVALGLStGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLL 158
Cdd:cd03297 76 -KIGLVFQQYALFPHLNVRENLAFGLK-RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:cd03297 154 LLDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-221 |
1.31e-38 |
|
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: 140.39 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYG-----AARPDEGEISFDGHPL-GVETPAQARE 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 LGIAMVHQHFALFDtLSVTENVALGLS-TGI-SAAEIEREIRLLGEKYGL--EVDPASVVMELSMGERQRVEILRALMTK 154
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRlHGIkLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSEgVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-217 |
1.54e-38 |
|
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: 138.72 E-value: 1.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 6 SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ-ARELGIamV 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElARKIAY--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQhfalfdtlsvtenvALGLsTGISAaeiereirlLGEKYglevdpasvVMELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:cd03214 79 PQ--------------ALEL-LGLAH---------LADRP---------FNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 165 SVLTPQAVRKLFKTLHQLS-SEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:cd03214 126 SHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-215 |
5.93e-38 |
|
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: 138.97 E-value: 5.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGIT-ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIAM 83
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR-KIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 VHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLevDPASVV----MELSMGERQRVEILRALMTKPKLL 158
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKlLKWPKEKIRERADELLALVGL--DPAEFAdrypHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 159 ILDEPTSVLTP---QAVRKLFKTLHQLSseGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03295 158 LMDEPFGALDPitrDQLQEEFKRLQQEL--GKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-221 |
6.44e-38 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 138.95 E-value: 6.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQAR-ELGIA 82
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI-THLPMHERaRLGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTLSVTENV--ALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:TIGR04406 80 YLPQEASIFRKLTVEENImaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPA 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-221 |
9.19e-38 |
|
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: 145.68 E-value: 9.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYPG--ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELg 80
Cdd:COG4987 332 PSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTlSVTENVALG--------LSTGISAAEIEREIRLLGEKYGLEVDPASvvMELSMGERQRVEILRALM 152
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENLRLArpdatdeeLWAALERVGLGDWLAALPDGLDTWLGEGG--RRLSGGERRRLALARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIrELADRCVVLRAGKVVASVDPK 221
Cdd:COG4987 488 RDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHE 554
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-214 |
1.10e-37 |
|
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: 136.41 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITkrypGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIA 82
Cdd:cd03215 3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MV---HQHFALFDTLSVTENVALGLStgisaaeiereirllgekyglevdpasvvmeLSMGERQRVEILRALMTKPKLLI 159
Cdd:cd03215 79 YVpedRKREGLVLDLSVAENIALSSL-------------------------------LSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-231 |
1.16e-37 |
|
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: 138.68 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEG-EISFDGHPLGVETPAQARELg 80
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQhfALFDTLSVTENV----------ALGLSTGISAAEIEREIRLLGEkYGLEVDPASVVMELSMGERQRVEILRA 150
Cdd:COG1119 80 IGLVSP--ALQLRFPRDETVldvvlsgffdSIGLYREPTDEQRERARELLEL-LGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEG-VSILFISHKLDEIRELADRCVVLRAGKVVASVdPKAE--SEEN 227
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG-PKEEvlTSEN 235
|
....
gi 2549828669 228 LARL 231
Cdd:COG1119 236 LSEA 239
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-220 |
1.34e-37 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 138.84 E-value: 1.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYPGITAN----DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgVETPAQARe 78
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPqpalQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP--VTGPGADR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 lgiAMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:COG4525 79 ---GVVFQKDALLPWLNVLDNVAFGLRlRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 158 LILDEPTSVL---TPQAVRKLFKTLHQLSseGVSILFISHKLDEIRELADRCVVL--RAGKVVASVDP 220
Cdd:COG4525 156 LLMDEPFGALdalTREQMQELLLDVWQRT--GKGVFLITHSVEEALFLATRLVVMspGPGRIVERLEL 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
9-216 |
1.53e-37 |
|
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: 141.40 E-value: 1.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 9 NITKRYPGITANdhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL-----GVETPAQARELGIam 83
Cdd:TIGR02142 4 RFSKRLGDFSLD--ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkGIFLPPEKRRIGY-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 VHQHFALFDTLSVTENVALGLS------TGISAAEIereIRLLGEKYGLEVDPASvvmeLSMGERQRVEILRALMTKPKL 157
Cdd:TIGR02142 80 VFQEARLFPHLSVRGNLRYGMKrarpseRRISFERV---IELLGIGHLLGRLPGR----LSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-290 |
5.25e-37 |
|
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: 143.29 E-value: 5.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKS-TLMKII----YGAARPDeGEISFDGHPLGVE 71
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHPS-GSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 72 TPAQAREL---GIAMVHQH--FALFDTLSVTENVA--LGLSTGISAAEIEREIRLLGEKYGLEvDPASVV----MELSMG 140
Cdd:COG4172 82 SERELRRIrgnRIAMIFQEpmTSLNPLHTIGKQIAevLRLHRGLSGAAARARALELLERVGIP-DPERRLdaypHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 141 ERQRVEILRALMTKPKLLILDEPTSVL--TPQA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALdvTVQAqILDLLKDLQR--ELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 218 vdpkAESEENLA-------RLMIGNDPPTVREGTAKAGEVVFEMRHVS----------APGSTRVCGIDNVSLAVRAGEI 280
Cdd:COG4172 239 ----GPTAELFAapqhpytRKLLAAEPRGDPRPVPPDAPPLLEARDLKvwfpikrglfRRTVGHVKAVDGVSLTLRRGET 314
|
330
....*....|
gi 2549828669 281 VGIAGISGNG 290
Cdd:COG4172 315 LGLVGESGSG 324
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-241 |
5.70e-37 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 136.38 E-value: 5.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 7 LRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhpLGVETPAQA-----RELGi 81
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDerlirQEAG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 aMVHQHFALFDTLSVTENVALG--LSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLI 159
Cdd:PRK09493 81 -MVFQQFYLFPHLTALENVMFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAeseenlarlMIGNdPPT 239
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV---------LIKN-PPS 229
|
..
gi 2549828669 240 VR 241
Cdd:PRK09493 230 QR 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-214 |
1.37e-36 |
|
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: 134.46 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 7 LRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL----GVETPAQARELGi 81
Cdd:cd03292 3 FINVTKTYPnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKIG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 aMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:cd03292 82 -VVFQDFRLLPDRNVYENVAFALEvTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-230 |
2.41e-36 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 135.24 E-value: 2.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ-ARELgiAM 83
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElARRR--AV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 VHQHFAL-FDtLSVTENVALGLSTGISAAEIEREI-----------RLLGEKYglevdpasvvMELSMGERQRVEILRAL 151
Cdd:COG4559 80 LPQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIvrealalvglaHLAGRSY----------QTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 152 -------MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPkAE- 223
Cdd:COG4559 149 aqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTP-EEv 227
|
....*...
gi 2549828669 224 -SEENLAR 230
Cdd:COG4559 228 lTDELLER 235
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-221 |
2.70e-36 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 134.39 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgveTP----AQARe 78
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI---THlpmhKRAR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 LGIAMVHQHFALFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGLE--VD-PAsvvMELSMGERQRVEILRALMTK 154
Cdd:COG1137 78 LGIGYLPQEASIFRKLTVEDNILAVLELrKLSKKEREERLEELLEEFGIThlRKsKA---YSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPE 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-237 |
4.14e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 136.88 E-value: 4.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdghpLGVETPAQAR--ELGIA 82
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV----LGVPVPARARlaRARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQhfalFDTL----SVTEN-VALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:PRK13536 118 VVPQ----FDNLdlefTVRENlLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLARLMI---G 234
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVIeiyG 273
|
...
gi 2549828669 235 NDP 237
Cdd:PRK13536 274 GDP 276
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-238 |
6.80e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 134.76 E-value: 6.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGIT--ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARE 78
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 LgIAMVHQH-FALFDTLSVTENVALGL-STGISAAE-IER---EIRLLGEKYGLEVDPASvvmeLSMGERQRVEILRALM 152
Cdd:PRK13635 82 Q-VGMVFQNpDNQFVGATVQDDVAFGLeNIGVPREEmVERvdqALRQVGMEDFLNREPHR----LSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRElADRCVVLRAGKVVASVDPKAESEENLARL 231
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQ 235
|
....*..
gi 2549828669 232 MIGNDPP 238
Cdd:PRK13635 236 EIGLDVP 242
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-215 |
7.03e-36 |
|
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: 139.82 E-value: 7.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPRLSLRNITKRYPG-----------ITANDHVSLDIAPGEVLAILGENGAGKSTL----MKIIygaarPDEGEISFDGH 66
Cdd:COG4172 273 PPLLEARDLKVWFPIkrglfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 67 PLGVETPAQAREL--GIAMVHQH-FALFDT-LSVTENVALGLST---GISAAEIEREIRLLGEKYGLevDPASvvM---- 135
Cdd:COG4172 348 DLDGLSRRALRPLrrRMQVVFQDpFGSLSPrMTVGQIIAEGLRVhgpGLSAAERRARVAEALEEVGL--DPAA--Rhryp 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 136 -ELSMGERQRVEILRALMTKPKLLILDEPTSVL--TPQA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRA 211
Cdd:COG4172 424 hEFSGGQRQRIAIARALILEPKLLVLDEPTSALdvSVQAqILDLLRDLQR--EHGLAYLFISHDLAVVRALAHRVMVMKD 501
|
....
gi 2549828669 212 GKVV 215
Cdd:COG4172 502 GKVV 505
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-471 |
9.32e-36 |
|
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: 139.55 E-value: 9.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYG--AARPDEGEI----------------SFDGH 66
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 67 PLGV------------------ETPAQARELGIaMVHQHFALFDTLSVTENVALGL-STGISAAE-IEREIRLLgEKYGL 126
Cdd:TIGR03269 81 PCPVcggtlepeevdfwnlsdkLRRRIRKRIAI-MLQRTFALYGDDTVLDNVLEALeEIGYEGKEaVGRAVDLI-EMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 127 EVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQL-SSEGVSILFISHKLDEIRELADR 205
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 206 CVVLRAGKVVASVDPkaesEENLARLMIGNDPPTvREGTAKAGEVVFEMRHVsapgSTRVCGI--------DNVSLAVRA 277
Cdd:TIGR03269 239 AIWLENGEIKEEGTP----DEVVAVFMEGVSEVE-KECEVEVGEPIIKVRNV----SKRYISVdrgvvkavDNVSLEVKE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 278 GEIVGIAGISGNGQ---ARFMAA----ASGEYLCE-ADRVLLFNSPVGELDTHARRISGLRYVPEQRLGHAAVPElSLTA 349
Cdd:TIGR03269 310 GEIFGIVGTSGAGKttlSKIIAGvlepTSGEVNVRvGDEWVDMTKPGPDGRGRAKRYIGILHQEYDLYPHRTVLD-NLTE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 350 NTYLT-GDSLVRSGFILRDRARSFANLVIERFHVKTPNaekaagSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGA 428
Cdd:TIGR03269 389 AIGLElPDELARMKAVITLKMVGFDEEKAEEILDKYPD------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPIT 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2549828669 429 AAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:TIGR03269 463 KVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-214 |
1.35e-35 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 136.23 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARElgI 81
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENRH--V 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFALFDTLSVTENVALGLS-TGISAAEIE-------REIRLlgEKYGlEVDPAsvvmELSMGERQRVEILRALMT 153
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRmQKTPAAEITprvmealRMVQL--EEFA-QRKPH----QLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-216 |
2.87e-35 |
|
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: 131.17 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYPG--ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGI 81
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-NI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFALFDTlSVTENVALGlSTGISAAEIEREIRLLG-------EKYGLEVDPASVVMELSMGERQRVEILRALMTK 154
Cdd:cd03245 81 GYVPQDVTLFYG-TLRDNITLG-APLADDERILRAAELAGvtdfvnkHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSeGVSILFISHKLdEIRELADRCVVLRAGKVVA 216
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRP-SLLDLVDRIIVMDSGRIVA 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-270 |
2.99e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 133.78 E-value: 2.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgvetPAQARE-- 78
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARHar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 LGIAMVHQHFALFDTLSVTENV-ALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVRENLlVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA--ESEENLARLMI-G 234
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAliESEIGCDVIEIyG 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 2549828669 235 NDPPTVREGTAKAGEvvfemrHVSAPGSTRVCGIDN 270
Cdd:PRK13537 240 PDPVALRDELAPLAE------RTEISGETLFCYVRD 269
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-230 |
3.47e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 132.20 E-value: 3.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ-ARELgi 81
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElARRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFAL-FDtLSVTENVALGLST-GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALM------T 153
Cdd:PRK13548 79 AVLPQHSSLsFP-FTVEEVVAMGRAPhGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASvDPKAE--SEENLAR 230
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD-GTPAEvlTPETLRR 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-215 |
7.35e-35 |
|
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: 129.68 E-value: 7.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 6 SLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgvetPAQARELGIAMV 84
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI----KAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQH--FALFdTLSVTENVALGL-STGISAAEIEREIRLLGEKYGLEVDPASvvmeLSMGERQRVEILRALMTKPKLLILD 161
Cdd:cd03226 77 MQDvdYQLF-TDSVREELLLGLkELDAGNEQAETVLKDLDLYALKERHPLS----LSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 162 EPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-209 |
7.46e-35 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 129.66 E-value: 7.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 7 LRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL---GIAM 83
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFrreKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 VHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDE 162
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKyKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2549828669 163 PTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLdEIRELADRCVVL 209
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-216 |
2.68e-34 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 128.64 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 9 NITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARElGIAMVHQHF 88
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRR-RIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 89 ALFDTLSVTENVAL-GLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVL 167
Cdd:cd03265 83 SVDDELTGWENLYIhARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2549828669 168 TPQAVRKLFKTLHQL-SSEGVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:cd03265 163 DPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIA 212
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-215 |
3.29e-34 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 135.61 E-value: 3.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYPG--ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGI 81
Cdd:TIGR02203 330 DVEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRR-QV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFALFDTlSVTENVALGLSTGISAAEIEREIRLLGEK-------YGLEVDPASVVMELSMGERQRVEILRALMTK 154
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYGRTEQADRAEIERALAAAYAQdfvdklpLGLDTPIGENGVLLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIrELADRCVVLRAGKVV 215
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTI-EKADRIVVMDDGRIV 546
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-215 |
3.83e-34 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 131.01 E-value: 3.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPG-----------ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLG 69
Cdd:COG4608 4 AEPLLEVRDLKKHFPVrgglfgrtvgvVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 70 VETPAQAREL--GIAMVHQH-FALFDT-LSVTENVALGL--STGISAAEIEREIRLLGEKYGLEVD-----PAsvvmELS 138
Cdd:COG4608 84 GLSGRELRPLrrRMQMVFQDpYASLNPrMTVGDIIAEPLriHGLASKAERRERVAELLELVGLRPEhadryPH----EFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 139 MGERQRVEILRALMTKPKLLILDEPTSVL--TPQA-VRKLFKTLHQlssE-GVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALdvSIQAqVLNLLEDLQD---ElGLTYLFISHDLSVVRHISDRVAVMYLGKI 236
|
.
gi 2549828669 215 V 215
Cdd:COG4608 237 V 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-217 |
5.37e-34 |
|
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: 127.31 E-value: 5.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGeVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlGVETPAQARELgIAMV 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRR-IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVA-LGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03264 78 PQEFGVYPNFTVREFLDyIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 164 TSVLTPqAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:cd03264 158 TAGLDP-EERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-215 |
6.49e-34 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 128.07 E-value: 6.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTENVALGlstGISAAE------IEREIRLLGEKYGLEVDPASVvmeLSMGERQRVEILRALMTK 154
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMG---GFFAERdqfqerIKWVYELFPRLHERRIQRAGT---MSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
1.35e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.18 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPRLSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARE- 78
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENNalKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 LGIamVHQH-FALFDTLSVTENVALGLSTG-ISAAEIEREIRLLGEKYG----LEVDPASvvmeLSMGERQRVEILRALM 152
Cdd:PRK13632 85 IGI--IFQNpDNQFIGATVEDDIAFGLENKkVPPKKMKDIIDDLAKKVGmedyLDKEPQN----LSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGV-SILFISHKLDEIReLADRCVVLRAGKVVASVDPK 221
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPK 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-221 |
2.95e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 129.96 E-value: 2.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARelg 80
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTENVALGLSTG-ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLI 159
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDkLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 160 LDEPTSVLTPQAVRKL-FKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:PRK11607 173 LDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-214 |
5.24e-33 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 128.66 E-value: 5.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 9 NITKRYpGITA--NDhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgveTPAQARELGIAMVHQ 86
Cdd:PRK10851 7 NIKKSF-GRTQvlND-ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 87 HFALFDTLSVTENVALGLST-----GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILD 161
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVlprreRPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 162 EPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-209 |
6.72e-33 |
|
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: 131.25 E-value: 6.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYPGIT-ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGI 81
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-QI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFALFDTlSVTENVALGLStGISAAEIEREIRL---------LGEKYGLEVDPASVvmELSMGERQRVEILRALM 152
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLARP-DASDAEIREALERagldefvaaLPQGLDTPIGEGGA--GLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLdEIRELADRCVVL 209
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-216 |
8.18e-33 |
|
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: 124.14 E-value: 8.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPgiTANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAqarELGIAMV 84
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA---DRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVALGLSTGISAAEIERE-IRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03298 76 FQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 164 TSVLTP---QAVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:cd03298 156 FAALDPalrAEMLDLVLDLHA--ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-215 |
8.73e-33 |
|
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: 124.91 E-value: 8.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAR-ELGI 81
Cdd:cd03252 1 ITFEHVRFRYKPDGPVilDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMvhQHFALFDTlSVTENVALGlSTGISAAEIEREIRLLG---------EKYGLEVDPASVvmELSMGERQRVEILRALM 152
Cdd:cd03252 81 VL--QENVLFNR-SIRDNIALA-DPGMSMERVIEAAKLAGahdfiselpEGYDTIVGEQGA--GLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSeGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIV 215
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-241 |
9.99e-33 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 125.49 E-value: 9.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG 80
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTEN--VA--LGLSTGISA----------AE---IEREIRLLgEKYGLEVDPASVVMELSMGERQ 143
Cdd:PRK11300 82 VVRTFQHVRLFREMTVIENllVAqhQQLKTGLFSgllktpafrrAEseaLDRAATWL-ERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 144 RVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
250
....*....|....*....
gi 2549828669 223 eseenlarlmIGNDPPTVR 241
Cdd:PRK11300 241 ----------IRNNPDVIK 249
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-223 |
2.62e-32 |
|
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: 123.31 E-value: 2.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPRLSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGV---ETPA 74
Cdd:COG4181 6 APIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldeDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 75 QARELGIAMVHQHFALFDTLSVTENVALGLS-TGISAAEiEREIRLLgEKYGLE--VD--PAsvvmELSMGERQRVEILR 149
Cdd:COG4181 86 RLRARHVGFVFQSFQLLPTLTALENVMLPLElAGRRDAR-ARARALL-ERVGLGhrLDhyPA----QLSGGEQQRVALAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 150 ALMTKPKLLILDEPTSVL---TPQAVRKLFKTLHQLSseGVSILFISHklDEirELADRC---VVLRAGKVVASVDPKAE 223
Cdd:COG4181 160 AFATEPAILFADEPTGNLdaaTGEQIIDLLFELNRER--GTTLVLVTH--DP--ALAARCdrvLRLRAGRLVEDTAATAA 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-215 |
3.56e-32 |
|
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: 123.42 E-value: 3.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 7 LRNITKRYP---GITANDHVSLDIAPGEVLAILGENGAGKSTLMKII---YGaarPDEGEISFDGHPLGVETPAQARELg 80
Cdd:cd03249 3 FKNVSFRYPsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfYD---PTSGEILLDGVDIRDLNLRWLRSQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTlSVTENVALGLSTGIS--------AAEIEREIRLLGEKYGLEVDPASVvmELSMGERQRVEILRALM 152
Cdd:cd03249 79 IGLVSQEPVLFDG-TIAENIRYGKPDATDeeveeaakKANIHDFIMSLPDGYDTLVGERGS--QLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-217 |
4.46e-32 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 126.14 E-value: 4.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL-----GVETPAQARELGiaMVHQHFALFDTLSVT 97
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaekGICLPPEKRRIG--YVFQDARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 98 ENVALGLStGISAAEIEREIRLLGEKYGLEVDPASvvmeLSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFK 177
Cdd:PRK11144 95 GNLRYGMA-KSMVAQFDKIVALLGIEPLLDRYPGS----LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2549828669 178 TLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:PRK11144 170 YLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAF 210
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-217 |
6.94e-32 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 123.11 E-value: 6.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISF---DGHPLGVETPAQAR 77
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 78 -------ELGIamVHQHfalfdtlsvtenVALGLSTGISA-AEIEREIRLLGEK-YG------------LEVDPASV--- 133
Cdd:PRK11701 83 rrrllrtEWGF--VHQH------------PRDGLRMQVSAgGNIGERLMAVGARhYGdiratagdwlerVEIDAARIddl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 134 VMELSMGERQRVEILRALMTKPKLLILDEPTSVL--TPQAvrKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLR 210
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLdvSVQA--RLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMK 226
|
....*..
gi 2549828669 211 AGKVVAS 217
Cdd:PRK11701 227 QGRVVES 233
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-215 |
1.46e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 124.04 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 6 SLRNITKR-YPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHplgveTPAQ-----AREL 79
Cdd:COG4586 23 ALKGLFRReYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY-----VPFKrrkefARRI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 80 GIAM-----VHQHFALFDTLSVtenvaLGLSTGISAAEIEREIRLLGEKygLEVDP--ASVVMELSMGERQRVEILRALM 152
Cdd:COG4586 98 GVVFgqrsqLWWDLPAIDSFRL-----LKAIYRIPDAEYKKRLDELVEL--LDLGEllDTPVRQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 153 TKPKLLILDEPT---SVLTPQAVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:COG4586 171 HRPKILFLDEPTiglDVVSKEAIREFLKEYNR--ERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-215 |
2.24e-31 |
|
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: 120.80 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIA 82
Cdd:cd03251 1 VEFKNVTFRYPGDGPPvlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-IG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTlSVTENVALGLStGISAAEIEREIRL---------LGEKYGLEVDPASVvmELSMGERQRVEILRALMT 153
Cdd:cd03251 80 LVSQDVFLFND-TVAENIAYGRP-GATREEVEEAARAanahefimeLPEGYDTVIGERGV--KLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIV 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-221 |
3.63e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 121.72 E-value: 3.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPA--QARE-LG 80
Cdd:PRK13639 2 LETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKtVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTlSVTENVALG-LSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLI 159
Cdd:PRK13639 82 IVFQNPDDQLFAP-TVEEDVAFGpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-216 |
6.30e-31 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 119.38 E-value: 6.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYP----GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDG---HPLGVETPAQAR 77
Cdd:TIGR02211 2 LKCENLGKRYQegklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGqslSKLSSNERAKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 78 ELGIAMVHQHFALFDTLSVTENVALGLSTG-ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPK 156
Cdd:TIGR02211 82 NKKLGFIYQFHHLLPDFTALENVAMPLLIGkKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELaDRCVVLRAGKVVA 216
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRElNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-214 |
6.40e-31 |
|
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: 117.70 E-value: 6.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIA 82
Cdd:cd03246 1 LEVENVSFRYPGAEPPvlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-VG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTlSVTENValglstgisaaeiereirllgekyglevdpasvvmeLSMGERQRVEILRALMTKPKLLILDE 162
Cdd:cd03246 80 YLPQDDELFSG-SIAENI------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 163 PTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLdEIRELADRCVVLRAGKV 214
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-222 |
1.52e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 121.75 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARElgIAMV 84
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRD--ICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVALGLST-GISAAEIEREIrllgeKYGLE-VDPASV----VMELSMGERQRVEILRALMTKPKLL 158
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKMlGVPKEERKQRV-----KEALElVDLAGFedryVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-226 |
2.30e-30 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 120.68 E-value: 2.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 35 ILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARelGIAMVHQHFALFDTLSVTENVALGLST-GISAAEI 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-TNVPPHLR--HINMVFQSYALFPHMTVEENVAFGLKMrKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 114 EREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLT----PQAVRKLFKTLHQLsseGVSI 189
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQL---GITF 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 2549828669 190 LFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEE 226
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-215 |
2.58e-30 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 118.19 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVET---PAQAREL-- 79
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQkpsEKAIRLLrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 80 GIAMVHQHFALFDTLSVTENV------ALGLStgiSAAEIEREIRLLGEkygLEVDPASVV--MELSMGERQRVEILRAL 151
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLieapckVLGLS---KEQAREKAMKLLAR---LRLTDKADRfpLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-214 |
3.29e-30 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 120.72 E-value: 3.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPG-ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAqarELGIAM 83
Cdd:PRK11650 4 LKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA---DRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 VHQHFALFDTLSVTENVALGLST-GISAAEIEREI----RLLG-EKYgLEVDPAsvvmELSMGERQRVEILRALMTKPKL 157
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIrGMPKAEIEERVaeaaRILElEPL-LDRKPR----ELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 158 LILDEPTSVLTPQ---AVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK11650 156 FLFDEPLSNLDAKlrvQMRLEIQRLHR--RLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-228 |
4.32e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 118.26 E-value: 4.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKR-YPGiTAN-----DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARE 78
Cdd:COG1101 2 LELKNLSKTfNPG-TVNekralDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 LGIAMVHQhfalfD-------TLSVTENVAL--------GLSTGISAAEIER---EIRLLGekYGLEVDPASVVMELSMG 140
Cdd:COG1101 80 KYIGRVFQ-----DpmmgtapSMTIEENLALayrrgkrrGLRRGLTKKRRELfreLLATLG--LGLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 141 ERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVasVD 219
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEEnNLTTLMVTHNMEQALDYGNRLIMMHEGRII--LD 230
|
....*....
gi 2549828669 220 PKAESEENL 228
Cdd:COG1101 231 VSGEEKKKL 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-222 |
4.54e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 117.93 E-value: 4.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 7 LRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEG-----EISFDG-HPLGvETPAQAREL- 79
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTaRSLS-QQKGLIRQLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 80 -GIAMVHQHFALFDTLSVTENVALG--LSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPK 156
Cdd:PRK11264 85 qHVGFVFQNFNLFPHRTVLENIIEGpvIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-216 |
9.70e-30 |
|
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: 116.66 E-value: 9.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 6 SLRNITKR-YPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAMv 84
Cdd:cd03267 22 SLKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVF- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:cd03267 101 GQKTQLWWDLPVIDSFYLLAAIyDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-211 |
1.33e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 115.27 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPD---EGEISFDGHPLGvETPAQARELGI 81
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLT-ALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMvhQHFALFDTLSVTENVALGLSTGISAAEIEREIRLLGEKYGL----EVDPAsvvmELSMGERQRVEILRALMTKPKL 157
Cdd:COG4136 81 LF--QDDLLFPHLSVGENLAFALPPTIGRAQRRARVEQALEEAGLagfaDRDPA----TLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 158 LILDEPTSVLTP---QAVRKL-FKTLHQLsseGVSILFISHKLDEIrELADRCVVLRA 211
Cdd:COG4136 155 LLLDEPFSKLDAalrAQFREFvFEQIRQR---GIPALLVTHDEEDA-PAAGRVLDLGN 208
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-221 |
1.40e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 116.33 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYP----------------------GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDE 58
Cdd:COG1134 1 MSSMIEVENVSKSYRlyhepsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 59 GEISFDGH---PLgvetpaqarELGIAMVHQhfalfdtLSVTENVAL-GLSTGISAAEIER---EIRL---LGEKygleV 128
Cdd:COG1134 81 GRVEVNGRvsaLL---------ELGAGFHPE-------LTGRENIYLnGRLLGLSRKEIDEkfdEIVEfaeLGDF----I 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 129 D-PasvVMELSMGERQRveiLR---ALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELAD 204
Cdd:COG1134 141 DqP---VKTYSSGMRAR---LAfavATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCD 214
|
250
....*....|....*..
gi 2549828669 205 RCVVLRAGKVVASVDPK 221
Cdd:COG1134 215 RAIWLEKGRLVMDGDPE 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-212 |
1.63e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 116.34 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgVETPAQARelgiAMV 84
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP--VEGPGAER----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQlAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 164 TSVL---TPQAVRKLFKTLHQLSseGVSILFISHKLDEIRELADRCVVLRAG 212
Cdd:PRK11248 156 FGALdafTREQMQTLLLKLWQET--GKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-215 |
2.39e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 115.50 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVET---PAQAREL-- 79
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKtpsDKAIRELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 80 GIAMVHQHFALFDTLSVTENV------ALGLStgiSAAEIEREIRLLgEKYGLEVDPASVVMELSMGERQRVEILRALMT 153
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLieapcrVLGLS---KDQALARAEKLL-ERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-222 |
4.32e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.45 E-value: 4.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGH----------PLGVETP 73
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 74 AQARELG--IAMVHQHFALFDTLSVTENV------ALGLStgiSAAEIEREIRLLgEKYGL-EVDPASVVMELSMGERQR 144
Cdd:PRK10619 85 NQLRLLRtrLTMVFQHFNLWSHMTVLENVmeapiqVLGLS---KQEARERAVKYL-AKVGIdERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 145 VEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-215 |
5.69e-29 |
|
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: 113.03 E-value: 5.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYPGITANDH------VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARP--DEGEISFDGHPLGVETPAQ 75
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKSGkqllknVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 76 ArelgIAMVHQHFALFDTLSVTENVALglstgisAAEIEReirllgekyglevdpasvvmeLSMGERQRVEILRALMTKP 155
Cdd:cd03213 83 I----IGYVPQDDILHPTLTVRETLMF-------AAKLRG---------------------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 156 KLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKL-DEIRELADRCVVLRAGKVV 215
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-221 |
5.76e-29 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 119.91 E-value: 5.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYPG-----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISF-------DGHPLGV 70
Cdd:TIGR03269 278 PIIKVRNVSKRYISvdrgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 71 ETPAQARELgIAMVHQHFALFDTLSVTENV--ALGLSTGISAAEIEREIRL----LGEKYGLEVDPaSVVMELSMGERQR 144
Cdd:TIGR03269 358 DGRGRAKRY-IGILHQEYDLYPHRTVLDNLteAIGLELPDELARMKAVITLkmvgFDEEKAEEILD-KYPDELSEGERHR 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 145 VEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-219 |
7.90e-29 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 114.90 E-value: 7.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPG---------ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ 75
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 76 AREL--GIAMVHQ--HFALFDTLSVTENVALGLS--TGISAAEIEREIRLLGEKYGLEVDPAS-VVMELSMGERQRVEIL 148
Cdd:TIGR02769 83 RRAFrrDVQLVFQdsPSAVNPRMTVRQIIGEPLRhlTSLDESEQKARIAELLDMVGLRSEDADkLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 149 RALMTKPKLLILDEPTS----VLTPQAVRkLFKTLHQLSseGVSILFISHKLDEIRELADRCVVLRAGKVVASVD 219
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSnldmVLQAVILE-LLRKLQQAF--GTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECD 234
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-217 |
9.78e-29 |
|
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: 112.02 E-value: 9.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPG--ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgVETPAQARELGIA 82
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP--VSDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTlSVTENvalglstgisaaeiereirlLGEKyglevdpasvvmeLSMGERQRVEILRALMTKPKLLILDE 162
Cdd:cd03247 79 VLNQRPYLFDT-TLRNN--------------------LGRR-------------FSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 163 PTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIrELADRCVVLRAGKVVAS 217
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEV-LKDKTLIWITHHLTGI-EHMDKILFLENGKIIMQ 177
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-290 |
1.19e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.01 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 7 LRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdghplgvetPAQARelgIAMVHQ 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLR---IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 87 HFALFDTLSVTENVALGLStgiSAAEIEREIRLLGEKY----------------------------------GL---EVD 129
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDA---ELRALEAELEELEAKLaepdedlerlaelqeefealggweaearaeeilsGLgfpEED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 130 PASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSegvSILFISHKLDEIRELADRCVVL 209
Cdd:COG0488 146 LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG---TVLVVSHDRYFLDRVATRILEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 210 RAGKVV-------ASVDPKAESEEN-----------LARL--------------------------MIGNDPPtVREGTA 245
Cdd:COG0488 223 DRGKLTlypgnysAYLEQRAERLEQeaaayakqqkkIAKEeefirrfrakarkakqaqsrikalekLEREEPP-RRDKTV 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 246 K--------AGEVVFEMRHVS-APGSTRVcgIDNVSLAVRAGEIVGIAGISGNG 290
Cdd:COG0488 302 EirfppperLGKKVLELEGLSkSYGDKTL--LDDLSLRIDRGDRIGLIGPNGAG 353
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-212 |
1.37e-28 |
|
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: 113.33 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgVETPAQARelgiAMVHQHFALFDTLSVTENV 100
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQ--ITEPGPDR----MVVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 ALG-------LSTGISAAEIEREIRLLGEKYGLEVDPAsvvmELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVR 173
Cdd:TIGR01184 76 ALAvdrvlpdLSKSERRAIVEEHIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2549828669 174 KLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAG 212
Cdd:TIGR01184 152 NLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-215 |
1.75e-28 |
|
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: 113.09 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRY-PGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIAM 83
Cdd:cd03253 1 IEFENVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRR-AIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 VHQHFALFDTlSVTENVALG--------LSTGISAAEIEREIRLLGEKYglevdpASVVME----LSMGERQRVEILRAL 151
Cdd:cd03253 80 VPQDTVLFND-TIGYNIRYGrpdatdeeVIEAAKAAQIHDKIMRFPDGY------DTIVGErglkLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-212 |
1.99e-28 |
|
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: 112.53 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITK----------RYPGItanDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDgHPLGV 70
Cdd:COG4778 1 MTTLLEVENLSKtftlhlqggkRLPVL---DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 71 ETPAQA--------RELGIAMVHQHfalfdtLSV-----TENV---ALgLSTGISAAEIEREIRLLGEKYGL-----EVD 129
Cdd:COG4778 77 VDLAQAspreilalRRRTIGYVSQF------LRViprvsALDVvaePL-LERGVDREEARARARELLARLNLperlwDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 130 PASvvmeLSMGERQRVEILRALMTKPKLLILDEPTSVLTP---QAVRKLfktLHQLSSEGVSILFISHKLDEIRELADRC 206
Cdd:COG4778 150 PAT----FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVEL---IEEAKARGTAIIGIFHDEEVREAVADRV 222
|
....*.
gi 2549828669 207 VVLRAG 212
Cdd:COG4778 223 VDVTPF 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-215 |
2.04e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 112.75 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITAndHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQaRElgIAMV 84
Cdd:PRK10771 2 LKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR-RP--VSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVALGLSTGIS-AAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEP 163
Cdd:PRK10771 77 FQENNLFSHLTVAQNIGLGLNPGLKlNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-215 |
4.58e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 117.50 E-value: 4.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKST----LMKIIygaarPDEGEISFDGHPLGVETPAQAREL--GIAMVHQ--HFALFDTL 94
Cdd:PRK15134 305 ISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVrhRIQVVFQdpNSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 95 SVTENVALGLST---GISAAEIEREIRLLGEKYGLevDPAS---VVMELSMGERQRVEILRALMTKPKLLILDEPTSVL- 167
Cdd:PRK15134 380 NVLQIIEEGLRVhqpTLSAAQREQQVIAVMEEVGL--DPETrhrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLd 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2549828669 168 -TPQA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK15134 458 kTVQAqILALLKSLQQ--KHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-235 |
4.93e-28 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 117.03 E-value: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKryPGItanDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAM 83
Cdd:PRK10762 257 RLKVDNLSG--PGV---NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 V---HQHFALFDTLSVTENVALGLSTGIS--------AAE---IEREIRLLGEKyglevDPA--SVVMELSMGERQRVEI 147
Cdd:PRK10762 332 IsedRKRDGLVLGMSVKENMSLTALRYFSraggslkhADEqqaVSDFIRLFNIK-----TPSmeQAIGLLSGGNQQKVAI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEEN 227
Cdd:PRK10762 407 ARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQEK 486
|
....*...
gi 2549828669 228 LARLMIGN 235
Cdd:PRK10762 487 LMAAAVGK 494
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-215 |
1.17e-27 |
|
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: 110.39 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRY-PGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIA 82
Cdd:cd03254 2 EIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM-IG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTlSVTENVALGLSTgISAAEIEREIRLLGEKYGLEVDP---ASVVME----LSMGERQRVEILRALMTKP 155
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGRPN-ATDEEVIEAAKEAGAHDFIMKLPngyDTVLGEnggnLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 156 KLLILDEPTSVLTP-------QAVRKLFKtlhqlsseGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:cd03254 159 KILILDEATSNIDTetekliqEALEKLMK--------GRTSIIIAHRLSTIKN-ADKILVLDDGKII 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-222 |
1.31e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.75 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITAN---DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAR 77
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKytlNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 78 ELgIAMVHQH-FALFDTLSVTENVALGL-STGISAAE----IEREIRLLGEKYGLEVDPAsvvmELSMGERQRVEILRAL 151
Cdd:PRK13650 81 HK-IGMVFQNpDNQFVGATVEDDVAFGLeNKGIPHEEmkerVNEALELVGMQDFKEREPA----RLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIrELADRCVVLRAGKVVASVDPKA 222
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRE 226
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-220 |
1.48e-27 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 110.54 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYG--AARPDEGEISFDGHPLGVETPAQ-AReLGIAMVHQHFALFDTLSVTE- 98
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSPDErAR-AGIFLAFQYPVEIPGVSVSNf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 99 -NVALGLSTG--ISAAEIEREIRLLGEKYGLEVDPA--SVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVR 173
Cdd:COG0396 98 lRTALNARRGeeLSAREFLKLLKEKMKELGLDEDFLdrYVNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2549828669 174 KLFKTLHQLSSEGVSILFISHK---LDEIRelADRCVVLRAGKVVASVDP 220
Cdd:COG0396 178 IVAEGVNKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGRIVKSGGK 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-221 |
1.50e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.86 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPA--QARElGI 81
Cdd:PRK13636 6 LKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRE-SV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQH--FALFdTLSVTENVALG-LSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLL 158
Cdd:PRK13636 85 GMVFQDpdNQLF-SASVYQDVSFGaVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-209 |
1.69e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 108.86 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 13 RYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEIsfdghplgvetpAQARELGIAMVHQHFALFD 92
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 93 TLSVT--ENVALGL---------STGISAAEIEREIRLLGEKyGLEVDPASvvmELSMGERQRVEILRALMTKPKLLILD 161
Cdd:NF040873 69 SLPLTvrDLVAMGRwarrglwrrLTRDDRAAVDDALERVGLA-DLAGRQLG---ELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2549828669 162 EPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIReLADRCVVL 209
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVR-RADPCVLL 191
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-215 |
2.51e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 110.55 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRY---------PGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ 75
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 76 AREL--GIAMVHQhfalfDTLS-------VTENVALGLS--TGISAAEIEREIRLLGEKYGLEVDPAS-VVMELSMGERQ 143
Cdd:PRK10419 84 RKAFrrDIQMVFQ-----DSISavnprktVREIIREPLRhlLSLDKAERLARASEMLRAVDLDDSVLDkRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 144 RVEILRALMTKPKLLILDEPTS----VLTPQAVRKLFKTLHQLsseGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSnldlVLQAGVIRLLKKLQQQF---GTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-214 |
3.56e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 112.43 E-value: 3.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 6 SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAqarELGIAMVH 85
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA---ERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 86 QHFALFDTLSVTENVALGLS-TGISAAEIEREI----RLLGEKYGLEVDPAsvvmELSMGERQRVEILRALMTKPKLLIL 160
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKlAGAKKEEINQRVnqvaEVLQLAHLLDRKPK----ALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 161 DEPTSVLTpQAVR--------KLFKTLhqlsseGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK11000 158 DEPLSNLD-AALRvqmrieisRLHKRL------GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-214 |
3.74e-27 |
|
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: 108.80 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 24 SLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARelgIAMVHQHFALFDTLSVTENVALG 103
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP---VSMLFQENNLFAHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 104 LSTGISAAEIERE-IRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQL 182
Cdd:TIGR01277 95 LHPGLKLNAEQQEkVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQL 174
|
170 180 190
....*....|....*....|....*....|...
gi 2549828669 183 SSE-GVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:TIGR01277 175 CSErQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-232 |
9.08e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 113.69 E-value: 9.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYPG----ITANdhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPaqaREL 79
Cdd:COG4618 330 RLSVENLTVVPPGskrpILRG--VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR---EEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 80 G--IAMVHQHFALFDTlSVTENVA-LGlstGISAAEIEREIRLLG---------EKYGLEVDPASVVmeLSMGERQRVEI 147
Cdd:COG4618 405 GrhIGYLPQDVELFDG-TIAENIArFG---DADPEKVVAAAKLAGvhemilrlpDGYDTRIGEGGAR--LSGGQRQRIGL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRElADRCVVLRAGKVVAsVDPKaesEEN 227
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAA-VDKLLVLRDGRVQA-FGPR---DEV 553
|
....*
gi 2549828669 228 LARLM 232
Cdd:COG4618 554 LARLA 558
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-205 |
1.01e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 107.98 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPRLSLRNITKRY-PGITAND---HVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLG-VETPAQA 76
Cdd:PRK11629 3 KILLQCDNLCKRYqEGSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSkLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 77 ----RELGiaMVHQHFALFDTLSVTENVALGLSTG-ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRAL 151
Cdd:PRK11629 83 elrnQKLG--FIYQFHHLLPDFTALENVAMPLLIGkKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLS-SEGVSILFISHKLdeirELADR 205
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDL----QLAKR 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-236 |
1.45e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 107.67 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVeTPAQAREL-GIA 82
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISL-LPLHARARrGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTLSVTENVALGLSTGISAAEIEREIRL--LGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRAneLMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA-ESEENLARLMIGND 236
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEiLQDEHVKRVYLGED 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-215 |
2.37e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.08 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdGHplGVEtpaqarelgIAMV 84
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE--TVK---------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFD-TLSVTENVALGLSTGisaaeIEREIRLLGEKYGLEVD----PASVvmeLSMGERQRVEILRALMTKPKLLI 159
Cdd:COG0488 384 DQHQEELDpDKTVLDELRDGAPGG-----TEQEVRGYLGRFLFSGDdafkPVGV---LSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 160 LDEPTSVLTPQavrklfkTLHQLSS-----EGvSILFISHklDE--IRELADRCVVLRAGKVV 215
Cdd:COG0488 456 LDEPTNHLDIE-------TLEALEEalddfPG-TVLLVSH--DRyfLDRVATRILEFEDGGVR 508
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-215 |
2.52e-26 |
|
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: 112.61 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIAMVHQHFALF-DTLSvtEN 99
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA-AIGIVPQDTVLFnDTIA--YN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 100 VALGlSTGISAAEIEREIRL---------LGEKYglevdpASVVME----LSMGERQRVEILRALMTKPKLLILDEPTSV 166
Cdd:COG5265 452 IAYG-RPDASEEEVEAAARAaqihdfiesLPDGY------DTRVGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 167 L---TPQAVRklfKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:COG5265 525 LdsrTERAIQ---AALREV-ARGRTTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-214 |
4.37e-26 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 106.02 E-value: 4.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYPgiTANDH-----VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARE 78
Cdd:cd03248 11 IVKFQNVTFAYP--TRPDTlvlqdVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 LgIAMVHQHFALFdTLSVTENVALGLST--------GISAAEIEREIRLLGEKYGLEVDPASVvmELSMGERQRVEILRA 150
Cdd:cd03248 89 K-VSLVGQEPVLF-ARSLQDNIAYGLQScsfecvkeAAQKAHAHSFISELASGYDTEVGEKGS--QLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAvRKLFKTLHQLSSEGVSILFISHKLDEIrELADRCVVLRAGKV 214
Cdd:cd03248 165 LIRNPQVLILDEATSALDAES-EQQVQQALYDWPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-221 |
7.25e-26 |
|
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: 104.53 E-value: 7.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYG--AARPDEGEISFDGHPLGVETPAQARELGIAMVHQHFALFdtlsvtenv 100
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEI--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 alglsTGISAAEIereIRLLGEKyglevdpasvvmeLSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLH 180
Cdd:cd03217 90 -----PGVKNADF---LRYVNEG-------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVIN 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2549828669 181 QLSSEGVSILFISHK---LDEIRelADRCVVLRAGKVVASVDPK 221
Cdd:cd03217 149 KLREEGKSVLIITHYqrlLDYIK--PDRVHVLYDGRIVKSGDKE 190
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-215 |
8.49e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 107.74 E-value: 8.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYP---GI-------TANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGV 70
Cdd:PRK11308 2 QQPLLQAIDLKKHYPvkrGLfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 71 ETPAQAREL--GIAMVHQHfaLFDTLSVTENVA------LGLSTGISAAEIEREIRLLGEKYGLEVDPASVV--MeLSMG 140
Cdd:PRK11308 82 ADPEAQKLLrqKIQIVFQN--PYGSLNPRKKVGqileepLLINTSLSAAERREKALAMMAKVGLRPEHYDRYphM-FSGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 141 ERQRVEILRALMTKPKLLILDEPTSVL--TPQA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALdvSVQAqVLNLMMDLQQ--ELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-219 |
1.45e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 104.57 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLG----VETPAQARELGiaMVHQHFALFDTLSVTE 98
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknREVPFLRRQIG--MIFQDHHLLMDRTVYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 99 NVALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFK 177
Cdd:PRK10908 99 NVAIPLIiAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2549828669 178 TLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVD 219
Cdd:PRK10908 179 LFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVG 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-217 |
2.82e-25 |
|
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: 108.76 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRY---PGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPD-EGEISFDGHPLGVETPAQARELG 80
Cdd:TIGR02633 258 LEARNLTCWDvinPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMV---HQHFALFDTLSVTENVAL-------GLSTGISAAE---IEREIRLLGEKyglEVDPASVVMELSMGERQRVEI 147
Cdd:TIGR02633 338 IAMVpedRKRHGIVPILGVGKNITLsvlksfcFKMRIDAAAElqiIGSAIQRLKVK---TASPFLPIGRLSGGNQQKAVL 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-469 |
4.64e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 108.79 E-value: 4.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRY----PGITANDHVSLDIAPGEVLAILGENGAGKS----TLMKIIYGAArpdeGEISFDGH---------- 66
Cdd:PRK10261 13 LAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAG----GLVQCDKMllrrrsrqvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 67 PLGVETPAQAREL---GIAMVHQH--FALFDTLSVTENVA--LGLSTGISAAEIEREIRLLGEKYGLevdPASVVM---- 135
Cdd:PRK10261 89 ELSEQSAAQMRHVrgaDMAMIFQEpmTSLNPVFTVGEQIAesIRLHQGASREEAMVEAKRMLDQVRI---PEAQTIlsry 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 136 --ELSMGERQRVEILRALMTKPKLLILDEPTSVL--TPQA-VRKLFKTLHQLSSEGVsiLFISHKLDEIRELADRCVVLR 210
Cdd:PRK10261 166 phQLSGGMRQRVMIAMALSCRPAVLIADEPTTALdvTIQAqILQLIKVLQKEMSMGV--IFITHDMGVVAEIADRVLVMY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 211 AGKVV--ASVD------------------PK--AESEENLAR---LMIGNDP----PTVREGTAKAGEVVFEMRHVSAPG 261
Cdd:PRK10261 244 QGEAVetGSVEqifhapqhpytrallaavPQlgAMKGLDYPRrfpLISLEHPakqePPIEQDTVVDGEPILQVRNLVTRF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 262 STR----------VCGIDNVSLAVRAGEIVGIAGISGNGQA-------RFMAAASGEYLCEADRV--------------- 309
Cdd:PRK10261 324 PLRsgllnrvtreVHAVEKVSFDLWPGETLSLVGESGSGKSttgrallRLVESQGGEIIFNGQRIdtlspgklqalrrdi 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 310 -LLFNSPVGELDtharrisglryvPEQRLGHAAVPELSLtantyltgdslvrSGFILRDRARSFANLVIERFHVKTPNAE 388
Cdd:PRK10261 404 qFIFQDPYASLD------------PRQTVGDSIMEPLRV-------------HGLLPGKAAAARVAWLLERVGLLPEHAW 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 389 KAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMY 467
Cdd:PRK10261 459 RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMY 538
|
..
gi 2549828669 468 RG 469
Cdd:PRK10261 539 LG 540
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-221 |
6.67e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 104.36 E-value: 6.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 19 ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL---GVETPAQARELGIAMVHQHFALFDTlS 95
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRKKVGLVFQYPEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 96 VTENVALGLST-GISAAEIEREIRLLGEKYGLEVD------PasvvMELSMGERQRVEILRALMTKPKLLILDEPTSVLT 168
Cdd:PRK13637 101 IEKDIAFGPINlGLSEEEIENRVKRAMNIVGLDYEdykdksP----FELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 169 PQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:PRK13637 177 PKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPR 230
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-216 |
9.54e-25 |
|
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: 107.58 E-value: 9.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYPGITANDH-----VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARE 78
Cdd:COG4615 327 TLELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 LgIAMVHQHFALFDTLsvtenvaLGLSTGISAAEIEREIRLLG--EKYGLEVDPASVVmELSMGERQRVEILRALMTKPK 156
Cdd:COG4615 407 L-FSAVFSDFHLFDRL-------LGLDGEADPARARELLERLEldHKVSVEDGRFSTT-DLSQGQRKRLALLVALLEDRP 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 157 LLILDE------PTsvltpqaVRKLFKT--LHQLSSEGVSILFISHklDEiR--ELADRCVVLRAGKVVA 216
Cdd:COG4615 478 ILVFDEwaadqdPE-------FRRVFYTelLPELKARGKTVIAISH--DD-RyfDLADRVLKMDYGKLVE 537
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-213 |
1.04e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.10 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGI 81
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ-QV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFALF-DTlsVTENVALGLSTGISAAEIEREIRLLgEKYGLevdPASV----VMELSMGERQRVEILRALMTKPK 156
Cdd:PRK10247 84 SYCAQTPTLFgDT--VYDNLIFPWQIRNQQPDPAIFLDDL-ERFAL---PDTIltknIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 157 LLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRElADRCVVL--RAGK 213
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEINH-ADKVITLqpHAGE 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-216 |
2.11e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 101.07 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 12 KRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhplgveTPAQARELGIAMVhqhfalf 91
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLGLGGGFN------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 92 DTLSVTENVAL-GLSTGISAAEIEREIRL------LGEKYGLevdPasvVMELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:cd03220 97 PELTGRENIYLnGRLLGLSRKEIDEKIDEiiefseLGDFIDL---P---VKTYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 165 SVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-231 |
4.45e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 104.99 E-value: 4.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKryPGITANdhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAM 83
Cdd:PRK11288 257 RLRLDGLKG--PGLREP--ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIML 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 V---HQHFALFDTLSVTENVALG-----------LSTGISAAEIEREIRLLGEKyglEVDPASVVMELSMGERQRVEILR 149
Cdd:PRK11288 333 CpedRKAEGIIPVHSVADNINISarrhhlragclINNRWEAENADRFIRSLNIK---TPSREQLIMNLSGGNQQKAILGR 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 150 ALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLA 229
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQATERQAL 489
|
..
gi 2549828669 230 RL 231
Cdd:PRK11288 490 SL 491
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
7-229 |
5.03e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.35 E-value: 5.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 7 LRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIAMVH 85
Cdd:PRK13647 7 VEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK-VGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 86 QH-----FALfdtlSVTENVALG-LSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLI 159
Cdd:PRK13647 86 QDpddqvFSS----TVWDDVAFGpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLA 229
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-242 |
5.83e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 101.32 E-value: 5.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 18 TANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhplgVETPAQARELGI----AMVHQH--FALF 91
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG----LDTSDEENLWDIrnkaGMVFQNpdNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 92 DTLsVTENVALGLST-GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQ 170
Cdd:PRK13633 100 ATI-VEEDVAFGPENlGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 171 AVRKLFKTLHQLSSE-GVSILFISHKLDEIRElADRCVVLRAGKVVASVDPKAESEENLARLMIGNDPPTVRE 242
Cdd:PRK13633 179 GRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMKKIGLDVPQVTE 250
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-220 |
5.93e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.57 E-value: 5.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 24 SLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL---GIAMVHQHFALFDTLSVTENV 100
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 ALGLS-TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTL 179
Cdd:PRK10070 128 AFGMElAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2549828669 180 HQLSSEGV-SILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:PRK10070 208 VKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-231 |
6.45e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 100.30 E-value: 6.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAArPDEGEISFDGHPLG-VETPAQARELgiAMVHQHFALFDTLSVTENVA 101
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSdWSAAELARHR--AYLSQQQSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 102 LGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMT-------KPKLLILDEPTSVL--TPQAV 172
Cdd:COG4138 92 LHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLdvAQQAA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 173 rkLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAE-SEENLARL 231
Cdd:COG4138 172 --LDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVmTPENLSEV 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-238 |
8.39e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.60 E-value: 8.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPRLSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREl 79
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 80 GIAMVHQHFA-LFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGL----EVDPASvvmeLSMGERQRVEILRALMT 153
Cdd:PRK13648 84 HIGIVFQNPDnQFVGSIVKYDVAFGLENhAVPYDEMHRRVSEALKQVDMleraDYEPNA----LSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRElADRCVVLRAGKVVASVDPKAESEENLARLM 232
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTR 238
|
....*.
gi 2549828669 233 IGNDPP 238
Cdd:PRK13648 239 IGLDLP 244
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-221 |
1.06e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.59 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhplgVETPAQARELGIAMVHQHFAL---------FDT 93
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDD----TLITSTSKNKDIKQIRKKVGLvfqfpesqlFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 94 lSVTENVALGLST-GISAAEIER----EIRLLGEKYGL-EVDPasvvMELSMGERQRVEILRALMTKPKLLILDEPTSVL 167
Cdd:PRK13649 102 -TVLKDVAFGPQNfGVSQEEAEAlareKLALVGISESLfEKNP----FELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 168 TPQAVRKL---FKTLHQlssEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:PRK13649 177 DPKGRKELmtlFKKLHQ---SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPK 230
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-214 |
1.40e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 99.08 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGV---ETPAQARELGIAMVHQHFALFDTLSVTEN 99
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeEARAKLRAKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 100 VAL-GLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKT 178
Cdd:PRK10584 109 VELpALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 2549828669 179 LHQLSSE-GVSILFISHKlDEIRELADRCVVLRAGKV 214
Cdd:PRK10584 189 LFSLNREhGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-215 |
2.55e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 103.65 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 24 SLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgVETPAQARELGIAMVHQHFALFDTlSVTENVALG 103
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL-VQYDHHYLHRQVALVGQEPVLFSG-SVRENIAYG 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 104 LS--------TGISAAEIEREIRLLGEKYGLEVDPASVvmELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRkl 175
Cdd:TIGR00958 579 LTdtpdeeimAAAKAANAHDFIMEFPNGYDTEVGEKGS--QLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ-- 654
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2549828669 176 fkTLHQL-SSEGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:TIGR00958 655 --LLQESrSRASRTVLLIAHRLSTVER-ADQILVLKKGSVV 692
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-215 |
3.26e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 103.17 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPG--ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIA 82
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN-QVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALF-DTlsVTENVALGLSTGISAAEIEREIRLL-------GEKYGLEvdpaSVVME----LSMGERQRVEILRA 150
Cdd:PRK11176 421 LVSQNVHLFnDT--IANNIAYARTEQYSREQIEEAARMAyamdfinKMDNGLD----TVIGEngvlLSGGQRQRIAIARA 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSiLFISHKLDEIrELADRCVVLRAGKVV 215
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTS-LVIAHRLSTI-EKADEILVVEDGEIV 557
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-215 |
3.61e-23 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 100.17 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 19 ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL--GIAMVHQH--FALFDTL 94
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 95 SVTENVALGLST---GISAAEIEREIRLLGEKYGLEvdPASV---VMELSMGERQRVEILRALMTKPKLLILDEPTSVLT 168
Cdd:PRK15079 116 TIGEIIAEPLRTyhpKLSRQEVKDRVKAMMLKVGLL--PNLInryPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2549828669 169 PQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-292 |
5.45e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.09 E-value: 5.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 21 DHVSLDIAPGEVLAILGENGAGKS-TLMKIIYGAARPD----EGEISFDGHPLGVETPAQAREL---GIAMVHQH--FAL 90
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGVrgnKIAMIFQEpmVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 91 FDTLSVTENVA--LGLSTGISAAEIEREIRLLGEKYGLEvDPASVVM----ELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:PRK15134 106 NPLHTLEKQLYevLSLHRGMRREAARGEILNCLDRVGIR-QAAKRLTdyphQLSGGERQRVMIAMALLTRPELLIADEPT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 165 SVL--TPQAvrKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVasvdpkaesEENLARLMIG------- 234
Cdd:PRK15134 185 TALdvSVQA--QILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCV---------EQNRAATLFSapthpyt 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 235 ---------NDPPTVREGTAKAGEVvfEMRHVSAPGS----TRVCG----IDNVSLAVRAGEIVGIAGISGNGQA 292
Cdd:PRK15134 254 qkllnsepsGDPVPLPEPASPLLDV--EQLQVAFPIRkgilKRTVDhnvvVKNISFTLRPGETLGLVGESGSGKS 326
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-196 |
5.77e-23 |
|
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: 102.05 E-value: 5.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYPG-ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgI 81
Cdd:TIGR02868 333 PTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-V 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFALFDTlSVTENVALG--------LSTGISAAEIEREIRLLGEkyGLEVDPASVVMELSMGERQRVEILRALMT 153
Cdd:TIGR02868 412 SVCAQDAHLFDT-TVRENLRLArpdatdeeLWAALERVGLADWLRALPD--GLDTVLGEGGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQlSSEGVSILFISHKL 196
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-213 |
6.28e-23 |
|
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: 94.44 E-value: 6.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHplgvetpaqareLGIAMV 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------VKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQhfalfdtlsvtenvalglstgisaaeiereirllgekyglevdpasvvmeLSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:cd03221 69 EQ--------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2549828669 165 SVLTPQAVRKLFKTLHQLSSegvSILFISHKLDEIRELADRCVVLRAGK 213
Cdd:cd03221 99 NHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-242 |
6.48e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 102.49 E-value: 6.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGH---PLGVETP 73
Cdd:PRK10535 1 MTALLELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvaTLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 74 AQARELGIAMVHQHFALFDTLSVTENVAL-GLSTGISAAE-IEREIRLLGeKYGLEVDPASVVMELSMGERQRVEILRAL 151
Cdd:PRK10535 81 AQLRREHFGFIFQRYHLLSHLTAAQNVEVpAVYAGLERKQrLLRAQELLQ-RLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKlDEIRELADRCVVLRAGKVVASVDPKAESEENLARL 231
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTE 238
|
250
....*....|.
gi 2549828669 232 MIGNDPPTVRE 242
Cdd:PRK10535 239 PVVNTASGWRQ 249
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-222 |
6.65e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 102.90 E-value: 6.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 8 RNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvetpaqARELGIAM---- 83
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD------AGDIATRRrvgy 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 VHQHFALFDTLSVTENVALG--LsTGISAAEIEREIRLLGEKYGLE--VD--PASvvmeLSMGERQRVEILRALMTKPKL 157
Cdd:NF033858 344 MSQAFSLYGELTVRQNLELHarL-FHLPAAEIAARVAEMLERFDLAdvADalPDS----LPLGIRQRLSLAVAVIHKPEL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 158 LILDEPTSVLTPQAvRKLF-KTLHQLSSE-GVSIlFIS-HKLDEIrELADRCVVLRAGKVVASVDPKA 222
Cdd:NF033858 419 LILDEPTSGVDPVA-RDMFwRLLIELSREdGVTI-FIStHFMNEA-ERCDRISLMHAGRVLASDTPAA 483
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
268-471 |
7.82e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 97.06 E-value: 7.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAASGEylceadrVLLFNSPVGELDTHARRISGlrYVPEQrlgHA 340
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKtttirmlLGLLRPTSGE-------VRVLGEDVARDPAEVRRRIG--YVPQE---PA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 341 AVPELSLTANTYLTGDSLVRSGFILRDRARSfanlVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQP 420
Cdd:COG1131 84 LYPDLTVRENLRFFARLYGLPRKEARERIDE----LLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 421 TWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-215 |
9.76e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 97.41 E-value: 9.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKII------YGAARPdEGEISFDGHPL---GVE 71
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlIPGARV-EGEILLDGEDIydpDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 72 TPAQARELGiaMVHQH---FALfdtlSVTENVALGLST-GI-SAAEIErEI--RLLgEKYGL--EV-----DPAsvvMEL 137
Cdd:COG1117 87 VVELRRRVG--MVFQKpnpFPK----SIYDNVAYGLRLhGIkSKSELD-EIveESL-RKAALwdEVkdrlkKSA---LGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 138 SMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEgVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-220 |
1.02e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.95 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPG--ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGE---ISFDGHPLGVETPAQARE- 78
Cdd:PRK13640 6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 LGIamVHQH-FALFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGL----EVDPASvvmeLSMGERQRVEILRALM 152
Cdd:PRK13640 86 VGI--VFQNpDNQFVGATVGDDVAFGLENrAVPRPEMIKIVRDVLADVGMldyiDSEPAN----LSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 153 TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIrELADRCVVLRAGKVVASVDP 220
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSP 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-231 |
1.02e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.08 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 6 SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQ--ARELGIAM 83
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA-TTPSRelAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 VHQHFALfdTLSVTENVALG--------LsTGISAAEIEREIRLLG-----EKYgleVDpasvvmELSMGERQRVEILRA 150
Cdd:COG4604 82 QENHINS--RLTVRELVAFGrfpyskgrL-TAEDREIIDEAIAYLDledlaDRY---LD------ELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASvDPKAE--SEEN 227
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ-GTPEEiiTPEV 228
|
....
gi 2549828669 228 LARL 231
Cdd:COG4604 229 LSDI 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-217 |
1.17e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.57 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPG-ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARE-LGIA 82
Cdd:PRK13652 4 IETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKfVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTlSVTENVA-----LGLSTGISAAEIEREIRLLGekygLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:PRK13652 84 FQNPDDQIFSP-TVEQDIAfgpinLGLDEETVAHRVSSALHMLG----LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-220 |
1.20e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 98.23 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 7 LRNITKRYPG-----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISF---DGHPLGVETPAQA-- 76
Cdd:PRK13651 5 VKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEKvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 77 --------------------RELGIAMVHQHFALFDTlSVTENVALG-LSTGISAAEIERE----IRLLG--EKYgLEVD 129
Cdd:PRK13651 85 eklviqktrfkkikkikeirRRVGVVFQFAEYQLFEQ-TIEKDIIFGpVSMGVSKEEAKKRaakyIELVGldESY-LQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 130 PasvvMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVL 209
Cdd:PRK13651 163 P----FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|.
gi 2549828669 210 RAGKVVASVDP 220
Cdd:PRK13651 239 KDGKIIKDGDT 249
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-222 |
1.31e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.59 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQA-----RELGIAMVHQHFALFDTlS 95
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkklrKKVSLVFQFPEAQLFEN-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 96 VTENVALG-LSTGISAAEIEREIRLLGEKYGLEVDPAS-VVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVR 173
Cdd:PRK13641 103 VLKDVEFGpKNFGFSEDEAKEKALKWLKKVGLSEDLISkSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2549828669 174 KLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:PRK13641 183 EMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKE 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-214 |
2.11e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 96.29 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPrLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgvetpAQARElGI 81
Cdd:PRK11247 11 TP-LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEARE-DT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFALFDTLSVTENVALGLSTGISAAEIEREirllgEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILD 161
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNVGLGLKGQWRDAALQAL-----AAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 162 EP---TSVLTPQAVRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK11247 159 EPlgaLDALTRIEMQDLIESLWQ--QHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-242 |
2.60e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 96.37 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgvetPAQAREL------GIAMVHQHFALFDTL 94
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI----PAMSRSRlytvrkRMSMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 95 SVTENVALGLS--TGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAV 172
Cdd:PRK11831 100 NVFDNVAYPLRehTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 173 RKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEenlarlmigNDPPTVRE 242
Cdd:PRK11831 180 GVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA---------NPDPRVRQ 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-220 |
2.64e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.61 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVEtpaqarELGIAMVHQHFA---------LFDT 93
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYS------KRGLLALRQQVAtvfqdpeqqIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 94 lSVTENVALGL-STGISAAEIEREIR---LLGEKYGLEVDPasvVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTP 169
Cdd:PRK13638 94 -DIDSDIAFSLrNLGVPEAEITRRVDealTLVDAQHFRHQP---IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 170 QAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-262 |
4.16e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.82 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGIAM 83
Cdd:PRK13644 2 IRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 VHQH-FALFDTLSVTENVALGLST-GISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILD 161
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENlCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 162 EPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRElADRCVVLRAGKVVASVDPKAE-SEENLARLmiGNDPPTV 240
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVlSDVSLQTL--GLTPPSL 238
|
250 260
....*....|....*....|....
gi 2549828669 241 RE--GTAKAGEVVFEMRHVSAPGS 262
Cdd:PRK13644 239 IElaENLKMHGVVIPWENTSSPSS 262
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-237 |
5.61e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.08 E-value: 5.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ-ARELgiAM 83
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlARRL--AL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 VHQHFALFDTLSVTENVALGLSTGIS-----AAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLL 158
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPWLSlwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAESEENLAR------LM 232
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRtvfdveAE 240
|
....*
gi 2549828669 233 IGNDP 237
Cdd:PRK11231 241 IHPEP 245
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-217 |
6.16e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.13 E-value: 6.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITAN--DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIA 82
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPvlKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ-AIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALF-DTLSvtENVALGLSTgisaAEIEREIRLLgEKYGLEV---DPASVVM-------ELSMGERQRVEILRAL 151
Cdd:PRK11160 418 VVSQRVHLFsATLR--DNLLLAAPN----ASDEALIEVL-QQVGLEKlleDDKGLNAwlgeggrQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIrELADRCVVLRAGKVVAS 217
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGL-EQFDRICVMDNGQIIEQ 554
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-214 |
9.31e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 94.69 E-value: 9.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPD---EGEISFDGHPLGVETPAqAR 77
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVQREGRL-AR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 78 ELGIAMVH-----QHFALFDTLSVTENVALGL--STGI--------SAAEIEREIRLLgEKYGLEVDPASVVMELSMGER 142
Cdd:PRK09984 80 DIRKSRANtgyifQQFNLVNRLSVLENVLIGAlgSTPFwrtcfswfTREQKQRALQAL-TRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 143 QRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLS-SEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-215 |
1.00e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.46 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKII--YGAARPD---EGEISFDGHPL---GVET 72
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIyspRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 73 PAQARELGiaMVHQHFALFdTLSVTENVALGLS-TGISAAEIEREI---RLLGEKYGLEV-----DPAsvvMELSMGERQ 143
Cdd:PRK14239 82 VDLRKEIG--MVFQQPNPF-PMSIYENVVYGLRlKGIKDKQVLDEAvekSLKGASIWDEVkdrlhDSA---LGLSGGQQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 144 RVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEgVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
25-220 |
2.19e-21 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 92.61 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 25 LDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvetpAQARELGIAMVHQHFALFDTLSVTENVALGL 104
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPG----KGWRHIGYVPQRHEFAWDFPISVAHTVMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 105 STGI-----SAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTL 179
Cdd:TIGR03771 77 TGHIgwlrrPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2549828669 180 HQLSSEGVSILFISHKLDEIRELADRcVVLRAGKVVASVDP 220
Cdd:TIGR03771 157 IELAGAGTAILMTTHDLAQAMATCDR-VVLLNGRVIADGTP 196
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-220 |
3.44e-21 |
|
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: 91.79 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYP--GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELg 80
Cdd:cd03244 1 GDIEFKNVSLRYRpnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTlSVTENVA-LGLStgiSAAEIEREIRLLGEK-------YGLEvdpaSVVME----LSMGERQRVEIL 148
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLDpFGEY---SDEELWQALERVGLKefveslpGGLD----TVVEEggenLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 149 RALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSeGVSILFISHKLDEIRElADRCVVLRAGKVVASVDP 220
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-217 |
4.26e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.57 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 8 RNITKRYPGIT-ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIAMVHQ 86
Cdd:PRK13657 338 DDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRR-NIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 87 HFALFDTlSVTENVALGlSTGISAAEIEREIR-------LLGEKYGLEvdpaSVVME----LSMGERQRVEILRALMTKP 155
Cdd:PRK13657 417 DAGLFNR-SIEDNIRVG-RPDATDEEMRAAAEraqahdfIERKPDGYD----TVVGErgrqLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 156 KLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVVAS 217
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVES 550
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-220 |
5.15e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.54 E-value: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 6 SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGV-ETPAQARElgIAMV 84
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARK--VAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENVALGL-----STGISAAE----IEREIRLLGEKyglevdPAS--VVMELSMGERQRVEILRALMT 153
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAIGRypwhgALGRFGAAdrekVEEAISLVGLK------PLAhrLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-202 |
8.65e-21 |
|
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: 90.11 E-value: 8.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElgIAMV 84
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEN--ILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDTLSVTENvaLGLSTGISAAEiEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:TIGR01189 79 GHLPGLKPELSALEN--LHFWAAIHGGA-QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2549828669 165 SVLTPQAVRKLFKTLHQLSSEGVSILFISHK---LDEIREL 202
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLARGGIVLLTTHQdlgLVEAREL 196
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-215 |
1.03e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 91.77 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITK---------RYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQ 75
Cdd:PRK15112 5 LEVRNLSKtfryrtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 76 aRELGIAMVHQHFALF----DTLSVTENVALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVME-LSMGERQRVEILRA 150
Cdd:PRK15112 85 -RSQRIRMIFQDPSTSlnprQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHmLAPGQKQRLGLARA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-230 |
1.38e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 90.76 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAArPDEGEISFDGHPLG-VETPAQARELGIaMVHQHFALFdTLSVTENVA 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEaWSAAELARHRAY-LSQQQTPPF-AMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 102 LGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRV-------EILRALMTKPKLLILDEPTSVL--TPQAV 172
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEPMNSLdvAQQAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 173 rkLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK-AESEENLAR 230
Cdd:PRK03695 172 --LDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDeVLTPENLAQ 228
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
3-217 |
2.96e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 91.51 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPD----EGEISFDGHPLGVETPA 74
Cdd:COG4170 2 PLLDIRNLTIEIDTpqgrVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 75 QAREL---GIAMVHQHFAlfDTLSVTENVALGLSTGISAAE------------IEREIRLLgEKYGLEvDPaSVVM---- 135
Cdd:COG4170 82 ERRKIigrEIAMIFQEPS--SCLDPSAKIGDQLIEAIPSWTfkgkwwqrfkwrKKRAIELL-HRVGIK-DH-KDIMnsyp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 136 -ELSMGERQRVEILRALMTKPKLLILDEPTSVL--TPQA-VRKLFKTLHQLSseGVSILFISHKLDEIRELADRCVVLRA 211
Cdd:COG4170 157 hELTEGECQKVMIAMAIANQPRLLIADEPTNAMesTTQAqIFRLLARLNQLQ--GTSILLISHDLESISQWADTITVLYC 234
|
....*.
gi 2549828669 212 GKVVAS 217
Cdd:COG4170 235 GQTVES 240
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-215 |
3.90e-20 |
|
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: 89.25 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDE---GEISFDGHPLgveTPAQARELgIAMVHQHFALFDTLSVTE- 98
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR---KPDQFQKC-VAYVRQDDILLPGLTVREt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 99 -----NVALGLSTGISAAEIEREIRLLGEkYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVR 173
Cdd:cd03234 102 ltytaILRLPRKSSDAIRKKRVEDVLLRD-LALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2549828669 174 KLFKTLHQLSSEGVSILFISHK-LDEIRELADRCVVLRAGKVV 215
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-238 |
4.47e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 90.15 E-value: 4.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRY---PGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAR 77
Cdd:PRK13642 1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 78 ElGIAMVHQH-FALFDTLSVTENVALGL-STGISAAE-IEREIRLLGEKYGLEV---DPAsvvmELSMGERQRVEILRAL 151
Cdd:PRK13642 81 R-KIGMVFQNpDNQFVGATVEDDVAFGMeNQGIPREEmIKRVDEALLAVNMLDFktrEPA----RLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRElADRCVVLRAGKVVASVDPKAESEENLAR 230
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDM 234
|
....*...
gi 2549828669 231 LMIGNDPP 238
Cdd:PRK13642 235 VEIGLDVP 242
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-196 |
5.61e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.40 E-value: 5.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEIsfdghplgvETPAQARelg 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLR--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTENVALGLSTGISAAEIEREIRLLGEKYGLEvdpaSVVMELSMGERQRVEILRALMTKPKLLIL 160
Cdd:PRK09544 69 IGYVPQKLYLDTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLID----APMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKL 196
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-220 |
9.46e-20 |
|
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: 93.54 E-value: 9.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYP--GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHplGVETPAQARE 78
Cdd:TIGR01257 925 LVPGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK--DIETNLDAVR 1002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 LGIAMVHQHFALFDTLSVTENVAL-GLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKL 157
Cdd:TIGR01257 1003 QSLGMCPQHNILFHHLTVAEHILFyAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSeGVSILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-212 |
1.19e-19 |
|
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: 93.15 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPRLSLRNITKRYPGIT--ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVEtpaqarel 79
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN-------- 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 80 gIAMVHQHF-------ALFDTLSVTENVAL-GLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRAL 151
Cdd:TIGR01257 2007 -ISDVHQNMgycpqfdAIDDLLTGREHLYLyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2085
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAG 212
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-220 |
2.13e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.14 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 17 ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEIS----FDGHPLGVETPA---------QARELG--I 81
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELItnpyskkikNFKELRrrV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQ--HFALF-DTLS---VTENVALGLSTGISAAEIEREIRLLGEKYG-LEVDPasvvMELSMGERQRVEILRALMTK 154
Cdd:PRK13631 119 SMVFQfpEYQLFkDTIEkdiMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSP----FGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-194 |
2.57e-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: 86.01 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIAMVHQHfALFDTLSVTENV-- 100
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL-LYLGHAP-GIKTTLSVLENLrf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 --ALGLSTGISAAEIEREIRllgekyGLEVDPASvvmELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKT 178
Cdd:cd03231 97 whADHSDEQVEEALARVGLN------GFEDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*.
gi 2549828669 179 LHQLSSEGVSILFISH 194
Cdd:cd03231 168 MAGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-220 |
2.64e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 88.25 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdGHPLGVETPAQA------RELGIAMVHQHFALFDTlSV 96
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKeikpvrKKVGVVFQFPESQLFEE-TV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 97 TENVALGLST-GISAAEIER----EIRLLG-EKYGLEVDPasvvMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQ 170
Cdd:PRK13643 103 LKDVAFGPQNfGIPKEKAEKiaaeKLEMVGlADEFWEKSP----FELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 171 A---VRKLFKTLHQlssEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDP 220
Cdd:PRK13643 179 ArieMMQLFESIHQ---SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-195 |
2.92e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 85.77 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgiAMVHQHFALFDTLSVTENV 100
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQL--CFVGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 ALGLSTGISAAEIEREIRLLGEKYGLEVdPASVvmeLSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLH 180
Cdd:PRK13540 96 LYDIHFSPGAVGITELCRLFSLEHLIDY-PCGL---LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
170
....*....|....*
gi 2549828669 181 QLSSEGVSILFISHK 195
Cdd:PRK13540 172 EHRAKGGAVLLTSHQ 186
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-204 |
3.28e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.40 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIyGAARPDEGEISFDGHplgVETPAQA---R 77
Cdd:PRK14258 4 LIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGR---VEFFNQNiyeR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 78 ELGI-------AMVHQHFALFdTLSVTENVALGL---------------STGISAAEIEREIRLLGEKYGLEvdpasvvm 135
Cdd:PRK14258 80 RVNLnrlrrqvSMVHPKPNLF-PMSVYDNVAYGVkivgwrpkleiddivESALKDADLWDEIKHKIHKSALD-------- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 136 eLSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLH--QLSSEgVSILFISHKLDEIRELAD 204
Cdd:PRK14258 151 -LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSE-LTMVIVSHNLHQVSRLSD 219
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
3-226 |
4.13e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 88.32 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYPG----ITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARpDEGEIS-----FDGHPLGVETP 73
Cdd:PRK15093 2 PLLDIRNLTIEFKTsdgwVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTadrmrFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 74 AQAREL---GIAMVHQHFAlfDTLSVTENVALGLSTGISAAEIE------------REIRLLgEKYGLEvDPASVV---- 134
Cdd:PRK15093 81 RERRKLvghNVSMIFQEPQ--SCLDPSERVGRQLMQNIPGWTYKgrwwqrfgwrkrRAIELL-HRVGIK-DHKDAMrsfp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 135 MELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLS-SEGVSILFISHKLDEIRELADRCVVLRAGK 213
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
250
....*....|...
gi 2549828669 214 VVASvdpkAESEE 226
Cdd:PRK15093 237 TVET----APSKE 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-215 |
4.25e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.89 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKI------IYGAARPdEGEISFDGHPLgVETPAQAR 77
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlieLYPEARV-SGEVYLDGQDI-FKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 78 ELGIAMVHQHFALFDTLSVTENVALGLSTG---ISAAEIEREIRLLGEKYGL--EVD-----PASvvmELSMGERQRVEI 147
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNrlvKSKKELQERVRWALEKAQLwdEVKdrldaPAG---KLSGGQQQRLCI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEgVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-194 |
1.22e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.09 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL---GiamvHQHfALFDTLSVT 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylG----HQP-GIKTELTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 98 ENV--ALGLSTGISAAEIEREIRLLGEKyGLEVDPASVvmeLSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKL 175
Cdd:PRK13538 93 ENLrfYQRLHGPGDDEALWEALAQVGLA-GFEDVPVRQ---LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
|
170
....*....|....*....
gi 2549828669 176 FKTLHQLSSEGVSILFISH 194
Cdd:PRK13538 169 EALLAQHAEQGGMVILTTH 187
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
261-469 |
1.30e-18 |
|
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: 83.22 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 261 GSTRVcgIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGlrYVPEqrlgHA 340
Cdd:cd03230 11 GKKTA--LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIG--YLPE----EP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 341 AVPElSLTANTYLTgdslvrsgfilrdrarsfanlvierfhvktpnaekaagsLSGGNLQKFIMGREILNRPRVLLVHQP 420
Cdd:cd03230 83 SLYE-NLTVRENLK---------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2549828669 421 TWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-213 |
1.50e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 88.49 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYPGIT-ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIA 82
Cdd:PRK10522 322 TLELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-FS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTLSVTENVAlglstgISAAEIEREIRLLGEKYGLEVDPASVV-MELSMGERQRVEILRALMTKPKLLILD 161
Cdd:PRK10522 401 AVFTDFHLFDQLLGPEGKP------ANPALVEKWLERLKMAHKLELEDGRISnLKLSKGQKKRLALLLALAEERDILLLD 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 162 EPTSVLTPQaVRKLF--KTLHQLSSEGVSILFISHKlDEIRELADRCVVLRAGK 213
Cdd:PRK10522 475 EWAADQDPH-FRREFyqVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-215 |
2.28e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 87.98 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAArPDEGEISFDGHPLGVETPAQARELgIAMVHQHFALFDTlSVTENVAL 102
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKH-LSWVGQNPQLPHG-TLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 103 GLSTgISAAEIEReirLLGEKYGLEVDPA------SVVME----LSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAV 172
Cdd:PRK11174 446 GNPD-ASDEQLQQ---ALENAWVSEFLPLlpqgldTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2549828669 173 RKLFKTLHQLsSEGVSILFISHKLDEIRELaDRCVVLRAGKVV 215
Cdd:PRK11174 522 QLVMQALNAA-SRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIV 562
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-215 |
2.53e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 87.85 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 22 HVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARElGIAMVHQH-FALFDTLSVteNV 100
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ-GVAMVQQDpVVLADTFLA--NV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 ALG-----------LSTgISAAEIEREI-----RLLGEKYGlevdpasvvmELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:PRK10790 436 TLGrdiseeqvwqaLET-VQLAELARSLpdglyTPLGEQGN----------NLSVGQKQLLALARVLVQTPQILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 165 SVL---TPQAVRKLFKTLHQLSsegvSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:PRK10790 505 ANIdsgTEQAIQQALAAVREHT----TLVVIAHRLSTIVE-ADTILVLHRGQAV 553
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
4-214 |
2.87e-18 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 87.79 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYPG---ITANDhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPaqaRELG 80
Cdd:TIGR01842 316 HLSVENVTIVPPGgkkPTLRG-ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR---ETFG 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 --IAMVHQHFALFDTlSVTENVA-----LGLSTGISAAEI---EREIRLLGEKYGLEVDPASVvmELSMGERQRVEILRA 150
Cdd:TIGR01842 392 khIGYLPQDVELFPG-TVAENIArfgenADPEKIIEAAKLagvHELILRLPDGYDTVIGPGGA--TLSGGQRQRIALARA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIrELADRCVVLRAGKV 214
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLL-GCVDKILVLQDGRI 531
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3-239 |
3.48e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.43 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgveTPAQARELG-- 80
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV---EALSARAASrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 IAMVHQHFALFDTLSVTENVALG-------LSTGISA--AEIEREIrllgEKYGLEVDPASVVMELSMGERQRVEILRAL 151
Cdd:PRK09536 79 VASVPQDTSLSFEFDVRQVVEMGrtphrsrFDTWTETdrAAVERAM----ERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 152 MTKPKLLILDEPTSVL-TPQAVRKLfKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKAE-SEENL- 228
Cdd:PRK09536 155 AQATPVLLLDEPTASLdINHQVRTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVlTADTLr 233
|
250
....*....|....*
gi 2549828669 229 ----ARLMIGNDPPT 239
Cdd:PRK09536 234 aafdARTAVGTDPAT 248
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-469 |
4.52e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.49 E-value: 4.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 6 SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgvetpAQARELgiAMVH 85
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM-----ADARHR--RAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 86 QHFA---------LFDTLSVTENVAL-GLSTGISAAEIEREIRLLGEKYGLE--VD-PASvvmELSMGERQRVEILRALM 152
Cdd:NF033858 76 PRIAympqglgknLYPTLSVFENLDFfGRLFGQDAAERRRRIDELLRATGLApfADrPAG---KLSGGMKQKLGLCCALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 153 TKPKLLILDEPTSVLTPQAvRKLFKTL---HQLSSEGVSILFISHKLDEIrELADRCVVLRAGKVVASVDPK-------A 222
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLS-RRQFWELidrIRAERPGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATGTPAellartgA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 223 ES-EENLARLMigndPPTVREGTA----------KAGEVVFEMRHVsapgsTRVCG----IDNVSLAVRAGEIVGIAGIS 287
Cdd:NF033858 231 DTlEAAFIALL----PEEKRRGHQpvvipprpadDDDEPAIEARGL-----TMRFGdftaVDHVSFRIRRGEIFGFLGSN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 288 GNGQARFM-------AAASGEylceadrVLLFNSPV---------------------GE------LDTHARrisgLRYVP 333
Cdd:NF033858 302 GCGKSTTMkmltgllPASEGE-------AWLFGQPVdagdiatrrrvgymsqafslyGEltvrqnLELHAR----LFHLP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 334 EQRLGhAAVPELsltantyltgdslvrsgfilrdrarsfanlvIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPR 413
Cdd:NF033858 371 AAEIA-ARVAEM-------------------------------LERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 414 VLLVHQPTWGVDVGAaaviRNS----LIRL-RDDGAAIIVVSEEIDELfEISDRIAVMYRG 469
Cdd:NF033858 418 LLILDEPTSGVDPVA----RDMfwrlLIELsREDGVTIFISTHFMNEA-ERCDRISLMHAG 473
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-215 |
6.26e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 86.69 E-value: 6.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 13 RYPGIT--ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLgveTPAQAREL--GIAMVHQHF 88
Cdd:PRK10789 322 TYPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL---TKLQLDSWrsRLAVVSQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 89 ALFDTlSVTENVALGlSTGISAAEIEREIRL---------LGEKYGLEVDPASVVmeLSMGERQRVEILRALMTKPKLLI 159
Cdd:PRK10789 399 FLFSD-TVANNIALG-RPDATQQEIEHVARLasvhddilrLPQGYDTEVGERGVM--LSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLSALTE-ASEILVMQHGHIA 528
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-215 |
1.08e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.93 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAA--RPDEGEISFDGHPLGVETPaqarelgiaMVHQHFALFDTLSVTE 98
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREAS---------LIDAIGRKGDFKDAVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 99 NVAL-GLSTGIsaaeiereirLLGEKYGlevdpasvvmELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFK 177
Cdd:COG2401 118 LLNAvGLSDAV----------LWLRRFK----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2549828669 178 TLHQLSSE-GVSILFISHKLDEIRELA-DRCVVLRAGKVV 215
Cdd:COG2401 178 NLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYGGVP 217
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-217 |
1.34e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 83.64 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 19 ANDHVSLDIAPGEVLAILGENGAGKS----TLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL---GIAMVHQH---- 87
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLvgaEVAMIFQDpmts 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 88 --------FALFDTLSVTENvalglstGISAAEIEREIRLLgEKYGLEvDPASVV----MELSMGERQRVEILRALMTKP 155
Cdd:PRK11022 102 lnpcytvgFQIMEAIKVHQG-------GNKKTRRQRAIDLL-NQVGIP-DPASRLdvypHQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 156 KLLILDEPTSVL--TPQA-VRKLFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:PRK11022 173 KLLIADEPTTALdvTIQAqIIELLLELQQ--KENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-221 |
1.82e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 82.76 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 22 HVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVET-PAQAREL--GIAMVHQhFA---LFDTlS 95
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKkNKKLKPLrkKVGIVFQ-FPehqLFEE-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 96 VTENVALG-LSTGISAAEIEREIRLLGEKYGLevdPASVV----MELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQ 170
Cdd:PRK13634 103 VEKDICFGpMNFGVSEEDAKQKAREMIELVGL---PEELLarspFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 171 AvRK----LFKTLHQlsSEGVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:PRK13634 180 G-RKemmeMFYKLHK--EKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPR 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-222 |
2.37e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.52 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 19 ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVET------PAQARelgIAMVHQ--HFAL 90
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyirPVRKR---IGMVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 91 FDTlSVTENVALGLST-GISAAEI-EREIRLLGEkYGLEVDpasvVMELS---M--GERQRVEILRALMTKPKLLILDEP 163
Cdd:PRK13646 99 FED-TVEREIIFGPKNfKMNLDEVkNYAHRLLMD-LGFSRD----VMSQSpfqMsgGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 164 TSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA 222
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-215 |
3.38e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.25 E-value: 3.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPL-------GVETPAQARELGiaMVHQHFALFDTLS 95
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifQIDAIKLRKEVG--MVFQQPNPFPHLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 96 VTENVALGL-STGIS--------AAEIEREIRLLGEKYGLEVDPASvvmELSMGERQRVEILRALMTKPKLLILDEPTSV 166
Cdd:PRK14246 107 IYDNIAYPLkSHGIKekreikkiVEECLRKVGLWKEVYDRLNSPAS---QLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2549828669 167 LTPQAVRKLFKTLHQLSSEgVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-215 |
6.95e-17 |
|
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: 79.38 E-value: 6.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRY----PGITANdhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQAREL 79
Cdd:cd03369 6 EIEVENLSVRYapdlPPVLKN--VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-TIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 80 GIAMVHQHFALFDTlSVTENvaLGLSTGISAAEIEREIRLLGEkyGLEvdpasvvmeLSMGERQRVEILRALMTKPKLLI 159
Cdd:cd03369 83 SLTIIPQDPTLFSG-TIRSN--LDPFDEYSDEEIYGALRVSEG--GLN---------LSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSeGVSILFISHKLDEIRELaDRCVVLRAGKVV 215
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-213 |
7.86e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 81.69 E-value: 7.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 17 ITANDHVSLDIAPGEVLAILGENGAGKS----TLMKIIYGAARPdEGEISFDGHPLgVETPAQA----RELGIAMVHQH- 87
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRI-GGSATFNGREI-LNLPEKElnklRAEQISMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 88 -FALFDTLSVTENVA--LGLSTGISAAE-IEREIRLLGekyGLEVDPASVVM-----ELSMGERQRVEILRALMTKPKLL 158
Cdd:PRK09473 107 mTSLNPYMRVGEQLMevLMLHKGMSKAEaFEESVRMLD---AVKMPEARKRMkmyphEFSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 159 ILDEPTSVL--TPQAvrKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGK 213
Cdd:PRK09473 184 IADEPTTALdvTVQA--QIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-238 |
1.00e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.44 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 7 LRNITKRYPGIT-----ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGH--PLGV----ETPAQ 75
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaiPANLkkikEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 76 ARELGIAMVHQHFALFDTlSVTENVALG-LSTGISAAEIEREIRLLGEKYGLEVDPAS-VVMELSMGERQRVEILRALMT 153
Cdd:PRK13645 89 RKEIGLVFQFPEYQLFQE-TIEKDIAFGpVNLGENKQEAYKKVPELLKLVQLPEDYVKrSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPKA--ESEENLAR 230
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEifSNQELLTK 247
|
....*...
gi 2549828669 231 LMIgnDPP 238
Cdd:PRK13645 248 IEI--DPP 253
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-227 |
1.03e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.98 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYP-----------GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVE 71
Cdd:PRK10261 312 PILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 72 TPAQAREL--GIAMVHQH-FALFDT-----LSVTENVAL-GLSTGISAAeieREIRLLGEKYGLEVDPA-SVVMELSMGE 141
Cdd:PRK10261 392 SPGKLQALrrDIQFIFQDpYASLDPrqtvgDSIMEPLRVhGLLPGKAAA---ARVAWLLERVGLLPEHAwRYPHEFSGGQ 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 142 RQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVaSVDP 220
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV-EIGP 547
|
....*..
gi 2549828669 221 KAESEEN 227
Cdd:PRK10261 548 RRAVFEN 554
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-215 |
1.76e-16 |
|
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: 77.67 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 27 IAPGEVLAILGENGAGKSTLMKIIygAARPD----EGEISFDGHPLGVETPAQarelgIAMVHQHFALFDTLSVTEnval 102
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVL--AGRKTagviTGEILINGRPLDKNFQRS-----TGYVEQQDVHSPNLTVRE---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 103 glSTGISAAeiereIRllgekyglevdpasvvmELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQL 182
Cdd:cd03232 99 --ALRFSAL-----LR-----------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 2549828669 183 SSEGVSIL-FISHKLDEIRELADRCVVL-RAGKVV 215
Cdd:cd03232 155 ADSGQAILcTIHQPSASIFEKFDRLLLLkRGGKTV 189
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
23-215 |
2.58e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 78.53 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIygAARPD----EGEISFDGHPLGVETPAQARELGIAMVHQHfalfdTLSVte 98
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHPAykilEGDILFKGESILDLEPEERAHLGIFLAFQY-----PIEI-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 99 nvalglsTGISAAEIEREIRLLGEK-YGL-EVDPAS-----------VVME-----------LSMGERQRVEILRALMTK 154
Cdd:CHL00131 97 -------PGVSNADFLRLAYNSKRKfQGLpELDPLEfleiineklklVGMDpsflsrnvnegFSGGEKKRNEILQMALLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHK---LDEIRelADRCVVLRAGKVV 215
Cdd:CHL00131 170 SELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrlLDYIK--PDYVHVMQNGKII 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-179 |
3.09e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.22 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPA-QARELGi 81
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeACHYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 amvHQHfALFDTLSVTENVAL------GLSTGISAAeIER-EIRLLGE-KYGlevdpasvvmELSMGERQRVEILRALMT 153
Cdd:PRK13539 80 ---HRN-AMKPALTVAENLEFwaaflgGEELDIAAA-LEAvGLAPLAHlPFG----------YLSAGQKRRVALARLLVS 144
|
170 180
....*....|....*....|....*.
gi 2549828669 154 KPKLLILDEPTSVLTPQAVRkLFKTL 179
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAVA-LFAEL 169
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-227 |
3.43e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 78.35 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKI------IYGAARPdEGEISFDGHPLGVE--TPAQARElGIAMVHQHFALFDTL 94
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTfnrlleLNEEARV-EGEVRLFGRNIYSPdvDPIEVRR-EVGMVFQYPNPFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 95 SVTENVALGLSTG---ISAAEIEREIRLLGEKYGL--EV-----DPASvvmELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:PRK14267 101 TIYDNVAIGVKLNglvKSKKELDERVEWALKKAALwdEVkdrlnDYPS---NLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 165 SVLTPQAVRKLFKTLHQLSSEgVSILFISHKLDEIRELADRCVVLRAGKVVaSVDPKAESEEN 227
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLI-EVGPTRKVFEN 238
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-215 |
5.40e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 80.76 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdghplgvetpaqARELGIAMVHQHFALFDTLSVTENV 100
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY------------EQDLIVARLQQDPPRNVEGTVYDFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 ALGLSTGISAAEIEREI-RLLGEKYG--------------------------------LEVDPASVVMELSMGERQRVEI 147
Cdd:PRK11147 88 AEGIEEQAEYLKRYHDIsHLVETDPSeknlnelaklqeqldhhnlwqlenrinevlaqLGLDPDAALSSLSGGWLRKAAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLhqLSSEGvSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIETIEWLEGFL--KTFQG-SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
268-469 |
7.22e-16 |
|
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: 76.70 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGLRYVPEqrlGHAAVPELSL 347
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPE---GRRIFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 TANtyltgdslVRSGFILRDRARSFANL--VIERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVD 425
Cdd:cd03224 93 EEN--------LLLGAYARRRAKRKARLerVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2549828669 426 VGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03224 165 PKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-212 |
1.70e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.08 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYP-GITANDHVSLDIAPGEVLAILGENGAGKSTLMKII-----YGaarpdEGEISFdghplgvetPAQA 76
Cdd:COG4178 361 GALALEDLTLRTPdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpYG-----SGRIAR---------PAGA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 77 RelgiamvhqhfALF---------DTLsvTENVAL-GLSTGISAAEIE---REIRL--LGEKYGLEVDPASVvmeLSMGE 141
Cdd:COG4178 427 R-----------VLFlpqrpylplGTL--REALLYpATAEAFSDAELRealEAVGLghLAERLDEEADWDQV---LSLGE 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 142 RQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQlSSEGVSILFISHKlDEIRELADRCVVLRAG 212
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
268-471 |
5.83e-15 |
|
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: 74.40 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRisglryvpeqRLG------HAA 341
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA----------RLGigrtfqIPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 342 V-PELSLTANTYLTGDSLVRSGFILRDRARSFANL------VIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPRV 414
Cdd:cd03219 86 LfPELTVLENVMVAAQARTGSGLLLARARREEREAreraeeLLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 415 LLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-215 |
8.11e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.01 E-value: 8.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPD---EGEISFDGHPLGVEtpaQARELGiAMVHQHFALFDTLSVTE- 98
Cdd:TIGR00955 44 VSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAK---EMRAIS-AYVQQDDLFIPTLTVREh 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 99 -NVALGLSTGISAAEIEREIRL--LGEKYGLE------VDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTP 169
Cdd:TIGR00955 120 lMFQAHLRMPRRVTKKEKRERVdeVLQALGLRkcantrIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2549828669 170 QAVRKLFKTLHQLSSEGVSILFISHK-LDEIRELADRCVVLRAGKVV 215
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVA 246
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-237 |
1.17e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.87 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDG-HPLGVETPAQARELG 80
Cdd:PRK10253 5 VARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGeHIQHYASKEVARRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 81 iaMVHQHFALFDTLSVTENVALG------LSTGISaAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTK 154
Cdd:PRK10253 85 --LLAQNATTPGDITVQELVARGryphqpLFTRWR-KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK----AESEENL- 228
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKeivtAELIERIy 241
|
250
....*....|
gi 2549828669 229 -ARLMIGNDP 237
Cdd:PRK10253 242 gLRCMIIDDP 251
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-221 |
1.32e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.09 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYG----AARPD----EGEISFDGHPLGVETPAQARELGIAMVHQHFALFd 92
Cdd:PRK13547 18 RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 93 TLSVTENVALG-LSTGISAAEIEREIRLLG----EKYGLEVDPASVVMELSMGERQRVEILRAL---------MTKPKLL 158
Cdd:PRK13547 97 AFSAREIVLLGrYPHARRAGALTHRDGEIAwqalALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVVASVDPK 221
Cdd:PRK13547 177 LLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-291 |
1.92e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 75.44 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 24 SLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEI--SFDgHP--LGVETPAQarelgiaMVHQHFALFDT--LSVT 97
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsQFS-HItrLSFEQLQK-------LVSDEWQRNNTdmLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 98 ENvalglSTGISAAE-IEREIR------LLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQ 170
Cdd:PRK10938 95 ED-----DTGRTTAEiIQDEVKdparceQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 171 AVRKLFKTLHQLSSEGVSILFISHKLDEIRELADR------CVVLRAGK--------VVASVdpkAESEENLARLMIGND 236
Cdd:PRK10938 170 SRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFagvladCTLAETGEreeilqqaLVAQL---AHSEQLEGVQLPEPD 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 237 PPTVREgTAKAGEVVFEMRHVSAPGSTRVCgIDNVSLAVRAGEIVGIAGISGNGQ 291
Cdd:PRK10938 247 EPSARH-ALPANEPRIVLNNGVVSYNDRPI-LHNLSWQVNPGEHWQIVGPNGAGK 299
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-290 |
2.28e-14 |
|
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: 75.36 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 6 SLRNITKRYPG---ITANdhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEIsfdghplgveTPAQARELGia 82
Cdd:TIGR03719 6 TMNRVSKVVPPkkeILKD--ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA----------RPQPGIKVG-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTLSVTENVALGLS---------TGISA--AEIEREIRLLGEKYG-----------------LEV------ 128
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEEGVAeikdaldrfNEISAkyAEPDADFDKLAAEQAelqeiidaadawdldsqLEIamdalr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 129 --DPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSegvSILFISH------------ 194
Cdd:TIGR03719 152 cpPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTHdryfldnvagwi 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 195 -KLD------------------------EIRELADRCVVLRAGKVVASVDPKAESEENLARL-----MIGNDPPTvREGT 244
Cdd:TIGR03719 229 lELDrgrgipwegnysswleqkqkrleqEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLaryeeLLSQEFQK-RNET 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 245 A--------KAGEVVFEMRHVSAPGSTRVCgIDNVSLAVRAGEIVGIAGISGNG 290
Cdd:TIGR03719 308 AeiyippgpRLGDKVIEAENLTKAFGDKLL-IDDLSFKLPPGGIVGVIGPNGAG 360
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
268-471 |
3.58e-14 |
|
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: 71.77 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAASGEylceadrVLLFNSPVGELDTHARRISGLR--YVPEQrlg 338
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKstlaraiLGLLKPTSGS-------IIFDGKDLLKLSRRLRKIRRKEiqMVFQD--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 339 haavPELSLtaNTYLT-GDSLVRSGFILR-DRARSFANLVIERFHVKTPNAEKAAGS----LSGGNLQKFIMGREILNRP 412
Cdd:cd03257 91 ----PMSSL--NPRMTiGEQIAEPLRIHGkLSKKEARKEAVLLLLVGVGLPEEVLNRypheLSGGQRQRVAIARALALNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 413 RVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
251-499 |
3.64e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 74.86 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 251 VFEMRHVSAPGSTrVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLC-EADRVLLFN-SPV---GELDTHARR 325
Cdd:TIGR02633 1 LLEMKGIVKTFGG-VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgTWDGEIYWSgSPLkasNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 326 ISglryVPEQRLghAAVPELSLTANTYLtGDSLVRSGFILRDRARSF-ANLVIERFHVKTPNAEKAAGSLSGGNLQKFIM 404
Cdd:TIGR02633 80 IV----IIHQEL--TLVPELSVAENIFL-GNEITLPGGRMAYNAMYLrAKNLLRELQLDADNVTRPVGDYGGGQQQLVEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 405 GREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALSPAVPKPTISIEE 484
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDD 232
|
250 260
....*....|....*....|
gi 2549828669 485 -----VGRWMSGLWPDSPFT 499
Cdd:TIGR02633 233 iitmmVGREITSLYPHEPHE 252
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
5-215 |
4.30e-14 |
|
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: 71.14 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNIT----KRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPD---EGEISFDGHPLGVETPAQAR 77
Cdd:cd03233 4 LSWRNISfttgKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 78 ElgIAMVHQHFALFDTLSVTENvalglstgisaaeIEREIRLLGEKYglevdpasvVMELSMGERQRVEILRALMTKPKL 157
Cdd:cd03233 84 E--IIYVSEEDVHFPTLTVRET-------------LDFALRCKGNEF---------VRGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLS--SEGVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMAdvLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
264-469 |
8.16e-14 |
|
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: 70.39 E-value: 8.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 264 RVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHArrisgLRYVPEQRlghAAVP 343
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-----IGYLPEER---GLYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 344 ELSLTAN-TYLTgdSLvrSGFILRDrARSFANLVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTW 422
Cdd:cd03269 84 KMKVIDQlVYLA--QL--KGLKKEE-ARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2549828669 423 GVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-230 |
2.79e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.70 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 13 RY-PGITANDH-VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELgIAMVHQHFAL 90
Cdd:PLN03232 1243 RYrPGLPPVLHgLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV-LSIIPQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 91 F--------DTLSvtENVALGLSTGISAAEIEREIRllGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDE 162
Cdd:PLN03232 1322 FsgtvrfniDPFS--EHNDADLWEALERAHIKDVID--RNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 163 PTS-------VLTPQAVRKLFKTlhqlssegVSILFISHKLDEIRElADRCVVLRAGKVVASVDPkaesEENLAR 230
Cdd:PLN03232 1398 ATAsvdvrtdSLIQRTIREEFKS--------CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSP----QELLSR 1459
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-194 |
2.81e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 67.56 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIygaarpdeGEI--SFDGHplgVETPAQArelGIAMVHQHfALFDTLSVTE 98
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRAL--------AGLwpWGSGR---IGMPEGE---DLLFLPQR-PYLPLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 99 NVALGLStgisaaeiereirllgekyglevdpasvvMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKT 178
Cdd:cd03223 83 QLIYPWD-----------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170
....*....|....*.
gi 2549828669 179 LHQlssEGVSILFISH 194
Cdd:cd03223 134 LKE---LGITVISVGH 146
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-231 |
2.93e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.68 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNIT-KRYPGItanDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELGiam 83
Cdd:PRK10982 251 LEVRNLTsLRQPSI---RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHG--- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 vhqhFALfdtlsVTENVAlglSTGISAA-EIE-----REIRLLGEKYGL------------EVDPASV--------VMEL 137
Cdd:PRK10982 325 ----FAL-----VTEERR---STGIYAYlDIGfnsliSNIRNYKNKVGLldnsrmksdtqwVIDSMRVktpghrtqIGSL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 138 SMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVAS 217
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
250
....*....|....
gi 2549828669 218 VDPKAESEENLARL 231
Cdd:PRK10982 473 VDTKTTTQNEILRL 486
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-199 |
3.15e-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: 71.89 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRL-----SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDghplgvETpaqar 77
Cdd:TIGR03719 316 PRLgdkviEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG------ET----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 78 eLGIAMVHQ-HFALFDTLSVTENVALGLstgisaaeierEIRLLGekyGLEV--------------DPASVVMELSMGER 142
Cdd:TIGR03719 385 -VKLAYVDQsRDALDPNKTVWEEISGGL-----------DIIKLG---KREIpsrayvgrfnfkgsDQQKKVGQLSGGER 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 143 QRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLhqLSSEGVSILfISHK---LDEI 199
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL--LNFAGCAVV-ISHDrwfLDRI 506
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
262-471 |
3.71e-13 |
|
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: 68.55 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 262 STRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGeyLCEADRvllFNSPVGELDTH-----ARRisGLRYVPEQR 336
Cdd:cd03266 15 KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAG--LLEPDA---GFATVDGFDVVkepaeARR--RLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 337 lghAAVPELSLTANTYLTGDSLVRSGFILRDRArsfaNLVIERFHVKtPNAEKAAGSLSGGNLQKFIMGREILNRPRVLL 416
Cdd:cd03266 88 ---GLYDRLTARENLEYFAGLYGLKGDELTARL----EELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 417 VHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
249-497 |
3.91e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.50 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 249 EVVFEMRHV--SAPGstrVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLC---EADrvLLFNspvGEL---- 319
Cdd:PRK13549 3 EYLLEMKNItkTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtyEGE--IIFE---GEElqas 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 320 ---DTHARRISglryVPEQRLghAAVPELSLTANTYLtGDSLVRSGFILRDRARSFANLVIERFHVKTPNAEKAaGSLSG 396
Cdd:PRK13549 75 nirDTERAGIA----IIHQEL--ALVKELSVLENIFL-GNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPV-GNLGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 397 GNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALSPAVP 476
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRP 226
|
250 260
....*....|....*....|....*.
gi 2549828669 477 KPTISIEE-----VGRWMSGLWPDSP 497
Cdd:PRK13549 227 AAGMTEDDiitmmVGRELTALYPREP 252
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-215 |
4.06e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.06 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIygAARPDEGEISFD-----GHPLgvETPAQARelgIAMVHQHFALFDTLS 95
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVL--AERVTTGVITGGdrlvnGRPL--DSSFQRS---IGYVQQQDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 96 VTENV----ALGLSTGISAAE----IEREIRLLG-EKYGLEVdpASVVME-LSMGERQRVEILRALMTKPKLLI-LDEPT 164
Cdd:TIGR00956 853 VRESLrfsaYLRQPKSVSKSEkmeyVEEVIKLLEmESYADAV--VGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPT 930
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 165 SVLTPQAVRKLFKTLHQLSSEGVSILFISHKLD-EIRELADRCVVL-RAGKVV 215
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLADHGQAILCTIHQPSaILFEEFDRLLLLqKGGQTV 983
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
268-469 |
4.33e-13 |
|
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: 66.88 E-value: 4.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRiSGLRYVPEqrlghaavpelsl 347
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR-RRIGYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 tantyltgdslvrsgfilrdrarsfanlvierfhvktpnaekaagsLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVG 427
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2549828669 428 AAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd00267 115 SRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-213 |
4.47e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.83 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 27 IAPGEVLAILGENGAGKSTLMKIIYGAARPDegeiSFDGHPLGVE-TPAQARELGIAMVHQHFALFDTLSVTENVA---- 101
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGRIQGN----NFTGTILANNrKPTKQILKRTGFVTQDDILYPHLTVRETLVfcsl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 102 LGLSTGISAAE----IEREIRLLG-EKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLF 176
Cdd:PLN03211 167 LRLPKSLTKQEkilvAESVISELGlTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180 190
....*....|....*....|....*....|....*...
gi 2549828669 177 KTLHQLSSEGVSILFISHK-LDEIRELADRCVVLRAGK 213
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
261-469 |
4.97e-13 |
|
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: 68.31 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 261 GSTRVcgIDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAASGEylceadrVLLFNSPVGELDTHARRISglrYVP 333
Cdd:cd03259 11 GSVRA--LDDLSLTVEPGEFLALLGPSGCGKttllrliAGLERPDSGE-------ILIDGRDVTGVPPERRNIG---MVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 334 EQrlgHAAVPELSLTANTyltgdslvrsGFILRDRARSFAN------LVIERFHVkTPNAEKAAGSLSGGNLQKFIMGRE 407
Cdd:cd03259 79 QD---YALFPHLTVAENI----------AFGLKLRGVPKAEirarvrELLELVGL-EGLLNRYPHELSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 408 ILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-204 |
6.00e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 69.04 E-value: 6.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMK-------IIYGAARpdEGEISFDGHPL---GVEtPA 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLyapDVD-PV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 75 QARELgIAMVHQHFALFDTlSVTENVALGLST----GISAAEIEREIR---LLGE-KYGLEVDPASvvmeLSMGERQRVE 146
Cdd:PRK14243 88 EVRRR-IGMVFQKPNPFPK-SIYDNIAYGARIngykGDMDELVERSLRqaaLWDEvKDKLKQSGLS----LSGGQQQRLC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 147 ILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLsSEGVSILFISHKLDEIRELAD 204
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSD 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
268-487 |
1.02e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.00 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGLRYVPEQRlghAAVPELSL 347
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEA---SIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 TANtyLTGDSLVRSGFILRDRARSfANLVIERFHVKTPNaEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVG 427
Cdd:PRK10895 96 YDN--LMAVLQIRDDLSAEQREDR-ANELMEEFHIEHLR-DSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 428 AAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL-SPAVPKPTISIEEVGR 487
Cdd:PRK10895 172 SVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLiAHGTPTEILQDEHVKR 232
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-216 |
1.08e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 69.38 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAG--KSTLMKIIYGaarPDEGEISFDGHPLGVETPAQARELGIa 82
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 mvHQ--HFALFDTLSVTENV-ALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLI 159
Cdd:NF000106 90 --HRpvR*GRRESFSGRENLyMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKVVA 216
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
253-469 |
1.22e-12 |
|
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: 67.53 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 253 EMRHVS-APGSTRVcgIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRisGLRy 331
Cdd:cd03261 2 ELRGLTkSFGGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELY--RLR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 332 vpeQRLG----HAAvpeL--SLTantylTGDSLvrsGFILRDRARSFANLVIERFHVK------TPNAEKAAGSLSGGNL 399
Cdd:cd03261 77 ---RRMGmlfqSGA---LfdSLT-----VFENV---AFPLREHTRLSEEEIREIVLEKleavglRGAEDLYPAELSGGMK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 400 QKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDG 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
9-208 |
1.64e-12 |
|
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: 69.81 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 9 NITKRYPGItandhvSLDIAPG-----EVLAILGENGAGKSTLMKIIYGAARPDEGE------ISFDGHPLGVETPAQAR 77
Cdd:COG1245 346 DLTKSYGGF------SLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEvdedlkISYKPQYISPDYDGTVE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 78 ELgiamvhqhfaLFDTLSVTenvalgLSTGISAAEIEREIRL--LGEKYglevdpasvVMELSMGERQRVEILRALMTKP 155
Cdd:COG1245 420 EF----------LRSANTDD------FGSSYYKTEIIKPLGLekLLDKN---------VKDLSGGELQRVAIAACLSRDA 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 156 KLLILDEPTS-------VLTPQAVRKLFKtlhqlsSEGVSILFISHKLDEIRELADRCVV 208
Cdd:COG1245 475 DLYLLDEPSAhldveqrLAVAKAIRRFAE------NRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-214 |
4.30e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 68.38 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 19 ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhplgvetpaqarelGIAMVHQHFALFDTLSVTE 98
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--------------SAALIAISSGLNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 99 NVAL-GLSTGISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFK 177
Cdd:PRK13545 105 NIELkGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 2549828669 178 TLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-215 |
6.41e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.61 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdghplgvetpAQARELGIaMV 84
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW----------SENANIGY-YA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 85 HQHFALFDT-LSVTENVALGLSTGisaaEIEREIR-LLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDE 162
Cdd:PRK15064 389 QDHAYDFENdLTLFDWMSQWRQEG----DDEQAVRgTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDE 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 163 PTSVLTPQAVRKLFKTLHQLssEGvSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK15064 465 PTNHMDMESIESLNMALEKY--EG-TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-212 |
7.99e-12 |
|
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: 68.01 E-value: 7.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHplgvetpaqarelgIAMVHQhFALFDTLSVTENVAL 102
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQ-TSWIMPGTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 103 GLS-------TGISAAEIEREIRLLGEKyglevdPASVVME----LSMGERQRVEILRALMTKPKLLILDEPTSVLTPQA 171
Cdd:TIGR01271 510 GLSydeyrytSVIKACQLEEDIALFPEK------DKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2549828669 172 VRKLFKT-LHQLSSEGVSILFIShKLDEIRElADRCVVLRAG 212
Cdd:TIGR01271 584 EKEIFEScLCKLMSNKTRILVTS-KLEHLKK-ADKILLLHEG 623
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
268-469 |
9.63e-12 |
|
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: 63.75 E-value: 9.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMaaasgeylceadrvllfnspvgeldthaRRISGLryvpeqrlghaavpeLSL 347
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLL----------------------------RCIAGL---------------EEP 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 TANTYLTGDSLVRSGFILRDRARSFANLVIERFHVkTPN---AEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGV 424
Cdd:cd03229 53 DSGSILIDGEDLTDLEDELPPLRRRIGMVFQDFAL-FPHltvLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2549828669 425 DVGAAAVIRNSLIRLRD-DGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03229 132 DPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-172 |
1.02e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.48 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 27 IAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPlgVETPAQARElgIAMVHQHFALFDTLSVTENVALglst 106
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT--ATRGDRSRF--MAYLGHLPGLKADLSTLENLHF---- 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 107 gISAAEIEREIRLLGEKY---GLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAV 172
Cdd:PRK13543 106 -LCGLHGRRAKQMPGSALaivGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI 173
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-215 |
1.12e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.84 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 22 HVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARE-LGIamVHQHFALF--------D 92
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKvLGI--IPQAPVLFsgtvrfnlD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 93 TLSvtENVALGLSTGISAAEIEREIRllGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTS------- 165
Cdd:PLN03130 1335 PFN--EHNDADLWESLERAHLKDVIR--RNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAavdvrtd 1410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2549828669 166 VLTPQAVRKLFKTlhqlssegVSILFISHKLDEIRElADRCVVLRAGKVV 215
Cdd:PLN03130 1411 ALIQKTIREEFKS--------CTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-219 |
1.18e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.81 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 5 LSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAA--RPDEGEISFDGHPLGVETPAQARELGIA 82
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MVHQHFALFDTLSVTenvaLGLSTGISAAE----------------IEREIRLLgeKYGLEVDPASVVMELSMGERQRVE 146
Cdd:PRK09580 82 MAFQYPVEIPGVSNQ----FFLQTALNAVRsyrgqepldrfdfqdlMEEKIALL--KMPEDLLTRSVNVGFSGGEKKRND 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 147 ILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHK---LDEIRelADRCVVLRAGKVVASVD 219
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYqriLDYIK--PDYVHVLYQGRIVKSGD 229
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-215 |
1.37e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.72 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 1 MTPRLSLRNITKRYPGITAnDHVSLDIAPGEVLAILGENGAGKS----TLMKIIYGAARPDEGEISFDGHPLgveTPAQA 76
Cdd:PRK10418 1 MPQQIELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV---APCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 77 RELGIAMVHQH----FALFDTLSvtenvALGLSTGISAAEIEREIRLLG--EKYGLEvDPASVV----MELSMGERQRVE 146
Cdd:PRK10418 77 RGRKIATIMQNprsaFNPLHTMH-----THARETCLALGKPADDATLTAalEAVGLE-NAARVLklypFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 147 ILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE-GVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-214 |
1.74e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 66.73 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdghplgvetpAQARELGI 81
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----------AKGIKLGY 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQhfalFDTLSVTENvALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVME-LSMGERQRVEILRALMTKPKLLIL 160
Cdd:PRK10636 380 FAQHQ----LEFLRADES-PLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 161 DEPTSVLTPQAVRKLFKTLhqLSSEGvSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK10636 455 DEPTNHLDLDMRQALTEAL--IDFEG-ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
256-471 |
2.41e-11 |
|
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: 65.69 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 256 HVSAPGSTRVcGIDNVSLAVRAGEIVGIAGISGNGQ---ARFMAAASGEYLCEADRVLLFNSPVGELDTHAR--RISglr 330
Cdd:COG1123 11 SVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKstlALALMGLLPHGGRISGEVLLDGRDLLELSEALRgrRIG--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 331 YVPEQrlghaavPELSLTANTylTGDSLV---RSGFILRDRARSFANLVIERFHVKTPnAEKAAGSLSGGNLQKFIMGRE 407
Cdd:COG1123 87 MVFQD-------PMTQLNPVT--VGDQIAealENLGLSRAEARARVLELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 408 ILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-181 |
2.74e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.91 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 6 SLRNITKRYPG---ITANdhVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEIsfdghplgveTPAQARELGIA 82
Cdd:PRK11819 8 TMNRVSKVVPPkkqILKD--ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA----------RPAPGIKVGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 83 MvhQHFALFDTLSVTENVALGLS---------TGISA--AEIEREIRLLGEKYG-----------------LEV------ 128
Cdd:PRK11819 76 P--QEPQLDPEKTVRENVEEGVAevkaaldrfNEIYAayAEPDADFDALAAEQGelqeiidaadawdldsqLEIamdalr 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 129 --DPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQ 181
Cdd:PRK11819 154 cpPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHD 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
268-469 |
2.86e-11 |
|
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: 62.94 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAA-------ASGEylceadrVLLFNSPVGELDthaRRISglrYVPEQRLGHA 340
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAilgllkpTSGS-------IRVFGKPLEKER---KRIG---YVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 341 AVPelsltantyLTGDSLVRSG--------FILRDRARSFANLVIER---FHVktpnAEKAAGSLSGGNLQKFIMGREIL 409
Cdd:cd03235 82 DFP---------ISVRDVVLMGlyghkglfRRLSKADKAKVDEALERvglSEL----ADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 410 NRPRVLLVHQPTWGVDV-GAAAVIRNsLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPkTQEDIYEL-LRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-208 |
3.13e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 9 NITKRYPGItandhvSLDIAPG-----EVLAILGENGAGKSTLMKIIYGAARPDEGEISFDghplgvetpaqareLGIAM 83
Cdd:PRK13409 345 DLTKKLGDF------SLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--------------LKISY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 84 VHQHFALFDTLSVTE---NVALGLSTGISAAEIEREIRL--LGEKYglevdpasvVMELSMGERQRVEILRALMTKPKLL 158
Cdd:PRK13409 405 KPQYIKPDYDGTVEDllrSITDDLGSSYYKSEIIKPLQLerLLDKN---------VKDLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 159 ILDEPTS-------VLTPQAVRKLFKtlhqlsSEGVSILFISHKLDEIRELADRCVV 208
Cdd:PRK13409 476 LLDEPSAhldveqrLAVAKAIRRIAE------EREATALVVDHDIYMIDYISDRLMV 526
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
268-471 |
3.62e-11 |
|
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: 62.77 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAASGE-------YLCEADRVllfnspvgeldthARRISglrYVP 333
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKtttikmlTTLLKPTSGRatvaghdVVREPREV-------------RRRIG---IVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 334 EQRlghAAVPELSLTANTYLTGDSLVRSGFILRDRARSfanlVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPR 413
Cdd:cd03265 80 QDL---SVDDELTGWENLYIHARLYGVPGAERRERIDE----LLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 414 VLLVHQPTWGVDVGAaaviRNSLIR-----LRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03265 152 VLFLDEPTIGLDPQT----RAHVWEyieklKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
23-213 |
3.72e-11 |
|
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: 62.49 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhplgvetpaqarelGIAMVHQHFALFDTlSVTENVAL 102
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWIQNG-TIRENILF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 103 GLS-------TGISAAEIEREIRLL--------GEKyGlevdpasvvMELSMGERQRVEILRALMTKPKLLILDEPTSVL 167
Cdd:cd03250 89 GKPfdeeryeKVIKACALEPDLEILpdgdlteiGEK-G---------INLSGGQKQRISLARAVYSDADIYLLDDPLSAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2549828669 168 TPQAVRKLF-KTLHQLSSEGVSILFISHKLDEIRElADRCVVLRAGK 213
Cdd:cd03250 159 DAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-214 |
5.58e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.35 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRY-PGIT-ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGvETPAQARELGI 81
Cdd:TIGR00957 1284 RVEFRNYCLRYrEDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA-KIGLHDLRFKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFALFdtlSVTENVALGLSTGISAAEIEREIRLLGEKYGLEVDPASVVME-------LSMGERQRVEILRALMTK 154
Cdd:TIGR00957 1363 TIIPQDPVLF---SGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRK 1439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 155 PKLLILDEPTSVLTPQAvRKLFKTLHQLSSEGVSILFISHKLDEIRELAdRCVVLRAGKV 214
Cdd:TIGR00957 1440 TKILVLDEATAAVDLET-DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEV 1497
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-214 |
5.66e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 62.91 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 19 ANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHplgvetpaqarelgIAMVHQHFALFDTLSVTE 98
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--------------VSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 99 NVALG-LSTGISAAEIER------EIRLLGEkygLEVDPasvVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQA 171
Cdd:PRK13546 105 NIEFKmLCMGFKRKEIKAmtpkiiEFSELGE---FIYQP---VKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2549828669 172 VRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRAGKV 214
Cdd:PRK13546 179 AQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-215 |
8.49e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.81 E-value: 8.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQAREL--- 79
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVlef 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 80 --GIAMVHQHFALFdTLSVTENVAlglsTGISAAEI--EREIRLLGEKYGLEVDPASVVME--------LSMGERQRVEI 147
Cdd:PRK14271 100 rrRVGMLFQRPNPF-PMSIMDNVL----AGVRAHKLvpRKEFRGVAQARLTEVGLWDAVKDrlsdspfrLSGGQQQLLCL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEgVSILFISHKLDEIRELADRCVVLRAGKVV 215
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-194 |
1.08e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPRLSLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGaarpdegeisfdGHPLG----VETPAQAR 77
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG------------DHPQGysndLTLFGRRR 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 78 ELG---------IAMVHQHFALFDTLSVT-ENVAL-GL--STGISAAEIEREiRLLGEKY----GLEVDPA-SVVMELSM 139
Cdd:PRK10938 326 GSGetiwdikkhIGYVSSSLHLDYRVSTSvRNVILsGFfdSIGIYQAVSDRQ-QKLAQQWldilGIDKRTAdAPFHSLSW 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 140 GERQRVEILRALMTKPKLLILDEPTSVLTP---QAVRKLfktLHQLSSEG-VSILFISH 194
Cdd:PRK10938 405 GQQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRF---VDVLISEGeTQLLFVSH 460
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
239-469 |
1.14e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.22 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 239 TVREGTAKAGEVVFEMRHVSapgstRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGE 318
Cdd:NF000106 5 TISNGARNAVEVRGLVKHFG-----EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 319 LDTHARRISGLRYVpeqRLGHAAvpELSLTANTYLTGDSLVRSgfilRDRARSFANLVIERFHVkTPNAEKAAGSLSGGN 398
Cdd:NF000106 80 RRALRRTIG*HRPV---R*GRRE--SFSGRENLYMIGR*LDLS----RKDARARADELLERFSL-TEAAGRAAAKYSGGM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 399 LQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:NF000106 150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRG 220
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-214 |
1.25e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 62.18 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYP--GITANDHVSLDIAPGEVLAILGENGAGKSTL----MKIIYgaarpDEGEISFDGHPLGVETPAQAR 77
Cdd:cd03289 2 QMTVKDLTAKYTegGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVPLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 78 ElGIAMVHQHFALFdtlSVTENVALGLSTGISAAEIEREIRLLGEKYGLEVDPASV--VME-----LSMGERQRVEILRA 150
Cdd:cd03289 77 K-AFGVIPQKVFIF---SGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfVLVdggcvLSHGHKQLMCLARS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 151 LMTKPKLLILDEPTSVLTPQAVRKLFKTLHQlSSEGVSILFISHKLDEIRElADRCVVLRAGKV 214
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
253-466 |
1.28e-10 |
|
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: 61.33 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 253 EMRHVS---APGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAASGEylceadrVLLFNSPVGELDTH 322
Cdd:cd03293 2 EVRNVSktyGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKstllriiAGLERPTSGE-------VLVDGEPVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 323 arrisgLRYVPEQrlgHAAVPELSLTANTYLtGDSLVR-SGFILRDRARSFANLV-IERFHVKTPNAekaagsLSGGNLQ 400
Cdd:cd03293 75 ------RGYVFQQ---DALLPWLTVLDNVAL-GLELQGvPKAEARERAEELLELVgLSGFENAYPHQ------LSGGMRQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 401 KFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVM 466
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
261-469 |
1.35e-10 |
|
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: 61.40 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 261 GSTRVcgIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGLRYVPEQrlgHA 340
Cdd:cd03218 11 GKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQE---AS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 341 AVPELSLTANTYLtgdsLVRSGFILRDRARSFANLVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQP 420
Cdd:cd03218 86 IFRKLTVEENILA----VLEIRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2549828669 421 TWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEG 209
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-217 |
2.17e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 16 GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFdghpLGVETPAQARELGIAMVHQHFALFDTLS 95
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI----LGQPTRQALQKNLVAYVPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 96 V-TENVALGLSTG------ISAAEIEREIRLLGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLT 168
Cdd:PRK15056 95 VlVEDVVMMGRYGhmgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2549828669 169 PQAVRKLFKTLHQLSSEGVSILFISHKLDEIRELADRCVVLRaGKVVAS 217
Cdd:PRK15056 175 VKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLAS 222
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-201 |
2.96e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.01 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYP--GITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARpDEGEISFDGHPLGVETPAQARElGI 81
Cdd:TIGR01271 1217 QMDVQGLTAKYTeaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRK-AF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 82 AMVHQHFALFdtlSVTENVALGLSTGISAAEIEREIRLLGEKYGLEVDPASV--VME-----LSMGERQRVEILRALMTK 154
Cdd:TIGR01271 1295 GVIPQKVFIF---SGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfVLVdggyvLSNGHKQLMCLARSILSK 1371
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2549828669 155 PKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILfISHKLDEIRE 201
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVIL-SEHRVEALLE 1417
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
253-471 |
3.38e-10 |
|
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: 59.81 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 253 EMRHVS---APGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGeyLCEAD--RVLLFNSPVGELDTHARriS 327
Cdd:cd03255 2 ELKNLSktyGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG--LDRPTsgEVRVDGTDISKLSEKEL--A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 328 GLR-----YVPEQrlgHAAVPELSLTANT----YLTGdslvRSGFILRDRARSfanlVIERFHVKTpNAEKAAGSLSGGN 398
Cdd:cd03255 78 AFRrrhigFVFQS---FNLLPDLTALENVelplLLAG----VPKKERRERAEE----LLERVGLGD-RLNHYPSELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 399 LQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEiDELFEISDRIAVMYRGAL 471
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-212 |
3.41e-10 |
|
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: 61.03 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHplgvetpaqarelgIAMVHQhFALFDTLSVTENVAL 102
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQ-FSWIMPGTIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 103 GLS-------TGISAAEIEREIRLLGEKYGLEVDPASVVmeLSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKL 175
Cdd:cd03291 121 GVSydeyrykSVVKACQLEEDITKFPEKDNTVLGEGGIT--LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190
....*....|....*....|....*....|....*...
gi 2549828669 176 F-KTLHQLSSEGVSILfISHKLDEIRElADRCVVLRAG 212
Cdd:cd03291 199 FeSCVCKLMANKTRIL-VTSKMEHLKK-ADKILILHEG 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-217 |
4.37e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 57 DEGEISFDGHPLGVETPAQARELgIAMVHQHFALFDtLSVTENVALG--------LSTGISAAEIEREIRLLGEKYGLEV 128
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNL-FSIVSQEPMLFN-MSIYENIKFGkedatredVKRACKFAAIDEFIESLPNKYDTNV 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 129 DPASvvMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEG-VSILFISHKLDEIRElADRCV 207
Cdd:PTZ00265 1353 GPYG--KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKR-SDKIV 1429
|
170
....*....|....
gi 2549828669 208 VL----RAGKVVAS 217
Cdd:PTZ00265 1430 VFnnpdRTGSFVQA 1443
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
261-471 |
4.37e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.31 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 261 GSTRVcgIDNVSLAVRAGEIVGIAGISGNGQARFM------------AAASGEYLCEADRVllFNSPVGELdthARRISG 328
Cdd:PRK14247 14 GQVEV--LDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrlielypeARVSGEVYLDGQDI--FKMDVIEL---RRRVQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 329 LRYVPEqrlghaAVPELSLTANTYL--TGDSLVRSGFILRDRAR---SFANLVIErfhVKTpNAEKAAGSLSGGNLQKFI 403
Cdd:PRK14247 87 VFQIPN------PIPNLSIFENVALglKLNRLVKSKKELQERVRwalEKAQLWDE---VKD-RLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 404 MGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDgAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
268-471 |
5.60e-10 |
|
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: 59.14 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRiSGLRYVPEQrlghaavPEL-- 345
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR-RNIGYVPQD-------VTLfy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 346 -SLTANTYLtGDSLVRSGFILrdRARSFAnlVIERFHVKTPN------AEKAAGsLSGGNLQKFIMGREILNRPRVLLVH 418
Cdd:cd03245 92 gTLRDNITL-GAPLADDERIL--RAAELA--GVTDFVNKHPNgldlqiGERGRG-LSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 419 QPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEidELFEISDRIAVMYRGAL 471
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP--SLLDLVDRIIVMDSGRI 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
253-487 |
7.01e-10 |
|
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: 59.17 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 253 EMRHVS-APGSTRVcgIDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAASGEylceadrVLLFNSPVGELDTHAR 324
Cdd:cd03300 2 ELENVSkFYGGFVA--LDGVSLDIKEGEFFTLLGPSGCGKttllrliAGFETPTSGE-------ILLDGKDITNLPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 325 RISGL--RYvpeqrlghAAVPELSLTANTyltgdslvrsGFILRDRARSFANL---VIERFH-VKTPN-AEKAAGSLSGG 397
Cdd:cd03300 73 PVNTVfqNY--------ALFPHLTVFENI----------AFGLRLKKLPKAEIkerVAEALDlVQLEGyANRKPSQLSGG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 398 NLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRGalspavp 476
Cdd:cd03300 135 QQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKG------- 207
|
250
....*....|.
gi 2549828669 477 kptiSIEEVGR 487
Cdd:cd03300 208 ----KIQQIGT 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
258-471 |
8.69e-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: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 258 SAPGSTRVCgidnvsLAVRAGEIVGIAGISGNGQARFMAAASGEY-LCEADRVLLFNSPVGEL-DTHarriSGLRYVPEq 335
Cdd:TIGR01257 1951 SSPAVDRLC------VGVRPGECFGLLGVNGAGKTTTFKMLTGDTtVTSGDATVAGKSILTNIsDVH----QNMGYCPQ- 2019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 336 rlgHAAVPELsltantyLTGdslvRSGFILRDRARSFANLVIER---FHVK----TPNAEKAAGSLSGGNLQKFIMGREI 408
Cdd:TIGR01257 2020 ---FDAIDDL-------LTG----REHLYLYARLRGVPAEEIEKvanWSIQslglSLYADRLAGTYSGGNKRKLSTAIAL 2085
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 409 LNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAF 2148
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
266-471 |
1.11e-09 |
|
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: 58.36 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 266 CGIDNVSLAVRAGeIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGlrYVPEQRLGHAavpel 345
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG--YLPQEFGVYP----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 346 SLTANTYLtgDSLVRSGFILRDRARSFANLVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVD 425
Cdd:cd03264 86 NFTVREFL--DYIAWLKGIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2549828669 426 VGAAAVIRNSLIRLRDDgaAIIVVSEEIDELFE-ISDRIAVMYRGAL 471
Cdd:cd03264 163 PEERIRFRNLLSELGED--RIVILSTHIVEDVEsLCNQVAVLNKGKL 207
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
264-469 |
1.28e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.74 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 264 RVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDThaRRIsglryvpeQRLGHAAVP 343
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT--AKI--------MREAVAIVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 344 ELSLTANTYLTGDSLVRSGFIL-RDRARSFANLVIERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTW 422
Cdd:PRK11614 87 EGRRVFSRMTVEENLAMGGFFAeRDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2549828669 423 GVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK11614 167 GLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-215 |
1.40e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 22 HVSLDIAPGEVLAILGENGAGKSTLMKII----YGAARPDEGEISFDGHPLGVETPAQAREL---GIAMVH-QHFALFDT 93
Cdd:TIGR00956 79 PMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVvynAETDVHfPHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 94 LsvteNVALGLST------GISAAE-IEREIRLLGEKYGLEVDPASVVME-----LSMGERQRVEILRALMTKPKLLILD 161
Cdd:TIGR00956 159 L----DFAARCKTpqnrpdGVSREEyAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWD 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 162 EPT----SVLTPQAVRKLFKTLHQL-SSEGVSILFIShklDEIRELADRCVVLRAGKVV 215
Cdd:TIGR00956 235 NATrgldSATALEFIRALKTSANILdTTPLVAIYQCS---QDAYELFDKVIVLYEGYQI 290
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-164 |
1.92e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRL-----SLRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISfdghpLGvETpaqar 77
Cdd:PRK11819 318 PRLgdkviEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-----IG-ET----- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 78 eLGIAMVHQ-HFALFDTLSVTENVALGLstgisaaeierEIRLLGEKyglEV--------------DPASVVMELSMGER 142
Cdd:PRK11819 387 -VKLAYVDQsRDALDPNKTVWEEISGGL-----------DIIKVGNR---EIpsrayvgrfnfkggDQQKKVGVLSGGER 451
|
170 180
....*....|....*....|..
gi 2549828669 143 QRVEILRALMTKPKLLILDEPT 164
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPT 473
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-212 |
2.03e-09 |
|
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: 57.73 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 15 PGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHPLGVETPAQARELG---IAMVHQHFALF 91
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 92 DTlSVTENVALG-------LSTGISAAEIEREIRLLgeKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPT 164
Cdd:cd03290 92 NA-TVEENITFGspfnkqrYKAVTDACSLQPDIDLL--PFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2549828669 165 SVLTPQAVRKLFKT--LHQLSSEGVSILFISHKLDEIRElADRCVVLRAG 212
Cdd:cd03290 169 SALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
268-469 |
2.55e-09 |
|
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: 57.67 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEAD---RVLLFNSPVgELDTHARRISglrYVPEQrlgHAAVPe 344
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTtsgQILFNGQPR-KPDQFQKCVA---YVRQD---DILLP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 345 lSLTANTYLTGDSLVRSGFILRDRARSFANLVIERFHVK-TPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWG 423
Cdd:cd03234 95 -GLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLAlTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2549828669 424 VDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03234 174 LDSFTALNLVSTLSQLaRRNRIVILTIHQPRSDLFRLFDRILLLSSG 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-227 |
3.49e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISF-DGHPLGVETPAQARElGIAMVHQHFALFDTlSVTENVA 101
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRS-KIGVVSQDPLLFSN-SIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 102 LGL----------------------------------------------STGISAAEIERE------------------- 116
Cdd:PTZ00265 482 YSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdSNELIEMRKNYQtikdsevvdvskkvlihdf 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 117 IRLLGEKYGLEVdpASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLS-SEGVSILFISHK 195
Cdd:PTZ00265 562 VSALPDKYETLV--GSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHR 639
|
250 260 270
....*....|....*....|....*....|....*...
gi 2549828669 196 LDEIRE------LADRCVVLRAGKVVASVDPKAESEEN 227
Cdd:PTZ00265 640 LSTIRYantifvLSNRERGSTVDVDIIGEDPTKDNKEN 677
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-167 |
3.65e-09 |
|
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: 57.42 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 26 DIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGE-------ISFDGHPLGVETPAQARELgiamvhqhfaLFdtlSVTE 98
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDieieldtVSYKPQYIKADYEGTVRDL----------LS---SITK 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 99 NVAlglstgiSAAEIEREIrllGEKYGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVL 167
Cdd:cd03237 88 DFY-------THPYFKTEI---AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
268-471 |
3.70e-09 |
|
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: 56.74 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGlrYVPEqrlgHAAVPELsL 347
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLG--YCPQ----FDALFDE-L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 TANTYLTGDSLVRSGFilRDRARSFANLVIErfHVK-TPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDV 426
Cdd:cd03263 91 TVREHLRFYARLKGLP--KSEIKEEVELLLR--VLGlTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2549828669 427 GAAAVIRNSLIRLRDdGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03263 167 ASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
265-469 |
8.53e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.04 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 265 VCGIDNVSLAVRAGEIVGIAGISGNG--QARF----MAAASGEYLCEAdrvlLFNspvgeldthARRISGLryvPEQRLG 338
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGksQTAFalmgLLAANGRIGGSA----TFN---------GREILNL---PEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 339 HAAVPELSL-------TANTYL-TGDSLVRsgfILR-----DRARSFANLVIERFHVKTPNAEKAAG----SLSGGNLQK 401
Cdd:PRK09473 93 KLRAEQISMifqdpmtSLNPYMrVGEQLME---VLMlhkgmSKAEAFEESVRMLDAVKMPEARKRMKmyphEFSGGMRQR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 402 FIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-220 |
9.76e-09 |
|
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: 58.10 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 137 LSMGERQRVEILRALM---TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRElADRCVVL---- 209
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKT-ADYIIDLgpeg 908
|
90
....*....|...
gi 2549828669 210 --RAGKVVASVDP 220
Cdd:TIGR00630 909 gdGGGTVVASGTP 921
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
136-220 |
1.26e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 56.08 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 136 ELSMGERQRVEILRALM---TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIReLADRCVVL--- 209
Cdd:cd03271 169 TLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CADWIIDLgpe 247
|
90
....*....|....
gi 2549828669 210 ---RAGKVVASVDP 220
Cdd:cd03271 248 ggdGGGQVVASGTP 261
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-214 |
1.26e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.87 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTL----MKIIYGAArpdeGEISFDGHPLGVETPAQARELgIAMVHQHFALFDTlSVTE 98
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLlltfMRMVEVCG----GEIRVNGREIGAYGLRELRRQ-FSMIPQDPVLFDG-TVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 99 NVALGLSTgiSAAEIEREIRLLG-------EKYGLEvdpaSVVME----LSMGERQRVEILRALMTKPKLLIL-DEPTSV 166
Cdd:PTZ00243 1403 NVDPFLEA--SSAEVWAALELVGlrervasESEGID----SRVLEggsnYSVGQRQLMCMARALLKKGSGFILmDEATAN 1476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2549828669 167 LTPQAVRKLFKTLHQLSSeGVSILFISHKLDEIRELaDRCVVLRAGKV 214
Cdd:PTZ00243 1477 IDPALDRQIQATVMSAFS-AYTVITIAHRLHTVAQY-DKIIVMDHGAV 1522
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
268-471 |
1.53e-08 |
|
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: 55.18 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELD-THARRISGlrYVPEQRLghaaVPELS 346
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADpAWLRRQVG--VVLQENV----LFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 347 LTANTYLTGDSLVRSGFILRDR---ARSFANLVIERFhvKTPNAEKAAGsLSGGNLQKFIMGREILNRPRVLLVHQPTWG 423
Cdd:cd03252 92 IRDNIALADPGMSMERVIEAAKlagAHDFISELPEGY--DTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2549828669 424 VDVGAAAVIRNSLIRLRdDGAAIIVVSEEIDELfEISDRIAVMYRGAL 471
Cdd:cd03252 169 LDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTV-KNADRIIVMEKGRI 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
268-486 |
2.06e-08 |
|
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: 55.04 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISglrYVPEQrlgHAAVPELSL 347
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVG---FVFQH---YALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 TANTyltgdslvrsGFILRDRARSF---ANLVIERFH-----VKTPN-AEKAAGSLSGGNLQKFIMGREILNRPRVLLVH 418
Cdd:cd03296 92 FDNV----------AFGLRVKPRSErppEAEIRAKVHellklVQLDWlADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 419 QPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRGAlspavpkptisIEEVG 486
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGR-----------IEQVG 219
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-204 |
3.08e-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: 54.68 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 28 APGEVLAILGENGAGKSTLMKIIYGAARPDEGEisFDGHP---------LGVETP---AQARELGIAMVH--QHFALFDT 93
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeildefRGSELQnyfTKLLEGDVKVIVkpQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 94 lSVTENVALGLSTGISAAEIEREIRLLGEKYGLEVDpasvVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVR 173
Cdd:cd03236 102 -AVKGKVGELLKKKDERGKLDELVDQLELRHVLDRN----IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|.
gi 2549828669 174 KLFKTLHQLSSEGVSILFISHKLDEIRELAD 204
Cdd:cd03236 177 NAARLIRELAEDDNYVLVVEHDLAVLDYLSD 207
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-205 |
3.15e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 21 DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGHP----LGVETPA--------------QAREL--- 79
Cdd:PRK10636 18 DNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWqlawVNQETPAlpqpaleyvidgdrEYRQLeaq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 80 -----------GIAMVHQHFALFDTLSVTENVALGLS-TGISAAEIEREIRllgekyglevdpasvvmELSMGERQRVEI 147
Cdd:PRK10636 98 lhdanerndghAIATIHGKLDAIDAWTIRSRAASLLHgLGFSNEQLERPVS-----------------DFSGGWRMRLNL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 148 LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHqlSSEGVSILfISHKLDEIRELADR 205
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLK--SYQGTLIL-ISHDRDFLDPIVDK 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
268-421 |
3.25e-08 |
|
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: 52.65 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRiSGLRYVPEQrlgHAAVPELSL 347
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLR-KEIGYVFQD---PQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 348 TANTYLTGDSLVRSGFILRDRARSFANLVIERFHVKTPnAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPT 421
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRP-VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-167 |
4.43e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 7 LRNITKRYPGITANDHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISfdghplgVETpaqarELGIAMVHQ 86
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-------CGT-----KLEVAYFDQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 87 HFALFD-TLSVTENVALGLSTgISAAEIEREIrlLGEKYGLEVDPASV---VMELSMGERQRVeILRALMTKP-KLLILD 161
Cdd:PRK11147 390 HRAELDpEKTVMDNLAEGKQE-VMVNGRPRHV--LGYLQDFLFHPKRAmtpVKALSGGERNRL-LLARLFLKPsNLLILD 465
|
....*.
gi 2549828669 162 EPTSVL 167
Cdd:PRK11147 466 EPTNDL 471
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-214 |
4.70e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 33 LAILGENGAGKSTLMKIIYGAARPDEGeisfdghplgveTPAQARELGIAMVHQHFAlfDTLSVTENVALGLSTGISAAe 112
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSG------------TVFRSAKVRMAVFSQHHV--DGLDLSSNPLLYMMRCFPGV- 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 113 IEREIRLLGEKYGLEVDPASVVM-ELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSegvSILF 191
Cdd:PLN03073 603 PEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG---GVLM 679
|
170 180
....*....|....*....|...
gi 2549828669 192 ISHKLDEIRELADRCVVLRAGKV 214
Cdd:PLN03073 680 VSHDEHLISGSVDELWVVSEGKV 702
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
268-469 |
6.29e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.84 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDT--HARRISGLRYV-PE-QRLGHAAVP 343
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlqGIRKLVGIVFQnPEtQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 344 ELSLTAntyltgDSLVRSGFILRDRA-RSFANLVIERFHVKTPNaekaagSLSGGNLQKFIMGREILNRPRVLLVHQPTW 422
Cdd:PRK13644 98 DLAFGP------ENLCLPPIEIRKRVdRALAEIGLEKYRHRSPK------TLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2549828669 423 GVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELfEISDRIAVMYRG 469
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRG 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
253-471 |
9.16e-08 |
|
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: 52.80 E-value: 9.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 253 EMRHVSAPGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELdtHARRISGLRyv 332
Cdd:cd03292 2 EFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDL--RGRAIPYLR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 333 peQRLGHA-----AVPELSLTANTYLtgdSLVRSGFILRDRARSFANlVIERFHVKTPNAEKAAGsLSGGNLQKFIMGRE 407
Cdd:cd03292 78 --RKIGVVfqdfrLLPDRNVYENVAF---ALEVTGVPPREIRKRVPA-ALELVGLSHKHRALPAE-LSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 408 ILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAiIVVSEEIDELFE-ISDRIAVMYRGAL 471
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTT-VVVATHAKELVDtTRHRVIALERGKL 214
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
3-217 |
1.33e-07 |
|
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: 51.55 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 3 PRLSLRNITKrypgitandhVSLDIAPGEVLAILGENGAGKSTLMK-IIY--GAARPDEGEISFDGHPLgvetpaqarel 79
Cdd:cd03238 4 SGANVHNLQN----------LDVSIPLNVLVVVTGVSGSGKSTLVNeGLYasGKARLISFLPKFSRNKL----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 80 giamvhqhfALFDTLSVTENVALGLSTgisaaeiereirlLGEKYGlevdpasvvmELSMGERQRVEILRALM--TKPKL 157
Cdd:cd03238 63 ---------IFIDQLQFLIDVGLGYLT-------------LGQKLS----------TLSGGELQRVKLASELFsePPGTL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 158 LILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRElADRCVVL------RAGKVVAS 217
Cdd:cd03238 111 FILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFS 175
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
390-471 |
1.90e-07 |
|
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: 51.80 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 390 AAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDgAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03260 138 HALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNG 216
|
..
gi 2549828669 470 AL 471
Cdd:cd03260 217 RL 218
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-209 |
1.99e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.03 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 26 DIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhplgvETPAqarelgiamvhqhfalfdtlsvtenvalgls 105
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-----ITPV------------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 106 tgisaaeiereirllgekygleVDPASVvmELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSE 185
Cdd:cd03222 65 ----------------------YKPQYI--DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....*
gi 2549828669 186 GV-SILFISHKLDEIRELADRCVVL 209
Cdd:cd03222 121 GKkTALVVEHDLAVLDYLSDRIHVF 145
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
378-471 |
2.08e-07 |
|
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: 50.50 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 378 ERFHVKTPNAEKAAG-----SLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEE 452
Cdd:cd03216 62 KEVSFASPRDARRAGiamvyQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHR 141
|
90
....*....|....*....
gi 2549828669 453 IDELFEISDRIAVMYRGAL 471
Cdd:cd03216 142 LDEVFEIADRVTVLRDGRV 160
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
268-476 |
3.08e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.13 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADR---VLLFNSPVGEldTHARRISGlrYVPEQRLghaAVPe 344
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGsgsVLLNGMPIDA--KEMRAISA--YVQQDDL---FIP- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 345 lSLTANTYLTGDSLVRSG--------------FILRDRARSFANLVIerfhvKTPNAEKaagSLSGGNLQKFIMGREILN 410
Cdd:TIGR00955 113 -TLTVREHLMFQAHLRMPrrvtkkekrervdeVLQALGLRKCANTRI-----GVPGRVK---GLSGGERKRLAFASELLT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 411 RPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVV----SEEIDELFeisDRIAVM------YRGALSPAVP 476
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF---DKIILMaegrvaYLGSPDQAVP 256
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-178 |
4.66e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 22 HVSLDIAPGEVLAILGENGAGKSTLMKIIYG--AARPDeGEISFDGHplgvetpaqarelgIAMVHQHFALFDTlSVTEN 99
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGelPPRSD-ASVVIRGT--------------VAYVPQVSWIFNA-TVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 100 VALGLStgISAAEIEREIRLLGEKYGLEVDPASVVME-------LSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAV 172
Cdd:PLN03130 699 ILFGSP--FDPERYERAIDVTALQHDLDLLPGGDLTEigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVG 776
|
....*.
gi 2549828669 173 RKLFKT 178
Cdd:PLN03130 777 RQVFDK 782
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
137-204 |
5.05e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 52.34 E-value: 5.05e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 137 LSMGERQRVEILRALM---TKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIReLAD 204
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIK-TAD 896
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
256-501 |
5.11e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 51.37 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 256 HVSAPGST-RVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVgELDTHARRISGLRyvpe 334
Cdd:PRK13641 10 YIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI-TPETGNKNLKKLR---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 335 QRLGHA-AVPELSLTANTYLTGDSLVRSGF-ILRDRARSFANLVIERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRP 412
Cdd:PRK13641 85 KKVSLVfQFPEAQLFENTVLKDVEFGPKNFgFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 413 RVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAL-SPAVPKPTISIEEvgrWMSG 491
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLiKHASPKEIFSDKE---WLKK 241
|
250
....*....|
gi 2549828669 492 LWPDSPFTQK 501
Cdd:PRK13641 242 HYLDEPATSR 251
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
261-476 |
5.76e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 51.77 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 261 GSTRVcgIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDthARRISglRYVpeqrlghA 340
Cdd:PRK09536 14 GDTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS--ARAAS--RRV-------A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 341 AVP-ELSLTANtyLTGDSLVRSG-------FILRDRA-RSFANLVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNR 411
Cdd:PRK09536 81 SVPqDTSLSFE--FDVRQVVEMGrtphrsrFDTWTETdRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 412 PRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALSPAVP 476
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGP 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
268-469 |
5.78e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 51.34 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGLryVPE-QRLGhaavPELS 346
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV--VPQfDNLD----PDFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 347 LTANTYLTGDSLVRSGFILRDRARSFanLVIERFHVKtpnAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDV 426
Cdd:PRK13537 97 VRENLLVFGRYFGLSAAAARALVPPL--LEFAKLENK---ADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2549828669 427 GAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK13537 172 QARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
268-469 |
6.10e-07 |
|
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: 51.21 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQ---AR-FM------AAASGEylceadrVLLFNSPVGELDTHARRisglryvpEQRL 337
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKstlARaILgllpppGITSGE-------ILFDGEDLLKLSEKELR--------KIRG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 338 GHAAV----PELSLtaNTYLT-GDSLVRSGFILRDRARSFA-NLVIERF-HVKTPNAEKAAGS----LSGGNLQKFIMGR 406
Cdd:COG0444 86 REIQMifqdPMTSL--NPVMTvGDQIAEPLRIHGGLSKAEArERAIELLeRVGLPDPERRLDRypheLSGGMRQRVMIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 407 EILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:COG0444 164 ALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAG 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
261-453 |
8.07e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.50 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 261 GSTRVcgIDNVSLAVRAGEIVGIAGISGNGQARFMaaasgeylceadRVLLfnSPVGELDTHARRISGLR--YVPeQRLg 338
Cdd:PRK09544 15 GQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLV------------RVVL--GLVAPDEGVIKRNGKLRigYVP-QKL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 339 HAAvPELSLTANTYLTGDSLVRSGFILRDRARSFANLVIERFHVKtpnaekaagsLSGGNLQKFIMGREILNRPRVLLVH 418
Cdd:PRK09544 77 YLD-TTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQK----------LSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 2549828669 419 QPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEI 453
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
268-469 |
8.52e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 50.99 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGLRYvpeqrlGHAAVPELSL 347
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ------SYALFPHMTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 TANTY--LTGDSLVRSGfiLRDRARSFANLV-IERFHVKTPNaekaagSLSGGNLQKFIMGREILNRPRVLLVHQPTWGV 424
Cdd:PRK11607 109 EQNIAfgLKQDKLPKAE--IASRVNEMLGLVhMQEFAKRKPH------QLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 425 DVgaaavirnsliRLRDD------------GAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK11607 181 DK-----------KLRDRmqlevvdilervGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
268-471 |
9.31e-07 |
|
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: 49.99 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQA-------RFMAAASGEylceadrVLLFNSPVGELD-THARRISGlrYVPeQRLGh 339
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTttmkminRLIEPTSGE-------IFIDGEDIREQDpVELRRKIG--YVI-QQIG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 340 aAVPELSLTANTYLTGDSLVRSGFILRDRARSFANLV---IERFhvktpnAEKAAGSLSGGNLQKFIMGREILNRPRVLL 416
Cdd:cd03295 86 -LFPHMTVEENIALVPKLLKWPKEKIRERADELLALVgldPAEF------ADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 417 VHQPTWGVDvgaaAVIRNSL----IRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03295 159 MDEPFGALD----PITRDQLqeefKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
268-464 |
9.53e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.42 E-value: 9.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARF------MAAASGEYLCEAdRVLLFNSPVGELDTHARRISglRYV----PEQRL 337
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFlkclnrMNELESEVRVEG-RVEFFNQNIYERRVNLNRLR--RQVsmvhPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 338 GHAAVPElSLTANTYLTG-------DSLVRSGFilrdRARSFANLVIERFHvktpnaeKAAGSLSGGNLQKFIMGREILN 410
Cdd:PRK14258 100 FPMSVYD-NVAYGVKIVGwrpkleiDDIVESAL----KDADLWDEIKHKIH-------KSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 411 RPRVLLVHQPTWGVDVGAAAVIRNSL--IRLRDDgAAIIVVSEEIDELFEISDRIA 464
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSE-LTMVIVSHNLHQVSRLSDFTA 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-196 |
1.10e-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: 51.32 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 29 PGEVLAILGENGAGKSTLMKIIYGAARPDEGEISfdghplgvetpaqaRELGIAMVHQHFA---LFDTLsvtENVALGls 105
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYD--------------EEPSWDEVLKRFRgteLQDYF---KKLANG-- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 106 tGISAA------------------EI-----ER-EIRLLGEKYGLE--VDPAsvVMELSMGERQRVEILRALMTKPKLLI 159
Cdd:COG1245 159 -EIKVAhkpqyvdlipkvfkgtvrELlekvdERgKLDELAEKLGLEniLDRD--ISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2549828669 160 LDEPTSVLTpqaVR---KLFKTLHQLSSEGVSILFISHKL 196
Cdd:COG1245 236 FDEPSSYLD---IYqrlNVARLIRELAEEGKYVLVVEHDL 272
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
394-471 |
1.20e-06 |
|
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: 49.18 E-value: 1.20e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03301 131 LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
268-471 |
1.28e-06 |
|
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: 48.75 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRisglryvpeQRLGhaavpelsl 347
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG---------DHVG--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 tantYLTGDSLVRSGFIlrdrarsfanlvierfhvktpnaekAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVG 427
Cdd:cd03246 80 ----YLPQDDELFSGSI-------------------------AENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2549828669 428 AAAVIRNSLIRLRDDGAAIIVVSEEIdELFEISDRIAVMYRGAL 471
Cdd:cd03246 131 GERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
265-500 |
1.43e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.19 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 265 VCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASG----EYLCEADRvLLFNSpvgeldtharrISGLRYVPEQR---L 337
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdNWRVTADR-MRFDD-----------IDLLRLSPRERrklV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 338 GHAAV-----PELSLTANTYLtGDSLVRS--GFILRDRARSFANL----VIERFH-VKTPNAEKAAGS----LSGGNLQK 401
Cdd:PRK15093 88 GHNVSmifqePQSCLDPSERV-GRQLMQNipGWTYKGRWWQRFGWrkrrAIELLHrVGIKDHKDAMRSfpyeLTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 402 FIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG-ALSPAVPKPT 479
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGqTVETAPSKEL 246
|
250 260
....*....|....*....|.
gi 2549828669 480 ISIeevgrwmsglwPDSPFTQ 500
Cdd:PRK15093 247 VTT-----------PHHPYTQ 256
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
391-471 |
1.67e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 49.66 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 391 AGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDgAAIIVVSEEIDELFEISDRIAVMYRGA 470
Cdd:PRK14246 151 ASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGE 229
|
.
gi 2549828669 471 L 471
Cdd:PRK14246 230 L 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-214 |
1.72e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 2 TPRLSLRNITKRYPGITAN---DHVSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPdegeisfdghplgVETPAQARE 78
Cdd:PLN03232 612 APAISIKNGYFSWDSKTSKptlSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-------------AETSSVVIR 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 LGIAMVHQHFALFDTlSVTENVALG-------LSTGISAAEIEREIRLLGEKYGLEVDPASVvmELSMGERQRVEILRAL 151
Cdd:PLN03232 679 GSVAYVPQVSWIFNA-TVRENILFGsdfeserYWRAIDVTALQHDLDLLPGRDLTEIGERGV--NISGGQKQRVSMARAV 755
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2549828669 152 MTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLdEIRELADRCVVLRAGKV 214
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGMI 817
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
37-194 |
1.91e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 37 GENGAGKSTLMKIIYGAARPDEGEISFD-GHPLGVETPAQarelgiamvhqhFAlFDTLSVTENVALGLST--------- 106
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQDQ------------FA-FEEFTVLDTVIMGHTElwevkqerd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 107 ------------GISAAEIE----------REIR----LLGekYGLEVDPASVVM-ELSMGERQRVEILRALMTKPKLLI 159
Cdd:PRK15064 101 riyalpemseedGMKVADLEvkfaemdgytAEARagelLLG--VGIPEEQHYGLMsEVAPGWKLRVLLAQALFSNPDILL 178
|
170 180 190
....*....|....*....|....*....|....*
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSegvSILFISH 194
Cdd:PRK15064 179 LDEPTNNLDINTIRWLEDVLNERNS---TMIIISH 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
391-471 |
3.12e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.68 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 391 AGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDgAAIIVVSEEIDELFEISDRIAVMYRGA 470
Cdd:PRK14267 147 PSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGK 225
|
.
gi 2549828669 471 L 471
Cdd:PRK14267 226 L 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
267-469 |
3.12e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.77 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 267 GIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGE---------Y------------LCEADRVLLFNSPVGELDTHARr 325
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARlapdagevhYrmrdgqlrdlyaLSEAERRRLLRTEWGFVHQHPR- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 326 iSGLRyvpeqrlghaavPELSLTANTyltGDSLVRSGFILRDRARSFANLVIERFHVKTPNAEKAAGSLSGGNLQKFIMG 405
Cdd:PRK11701 100 -DGLR------------MQVSAGGNI---GERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2549828669 406 REILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
264-500 |
3.43e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 264 RVCGIDNVSLAVRAGEIVGIAGISGNGQA-------RFMAAASGEYLCEADRVLLFNSPVGEL----DTHARRISG--LR 330
Cdd:PRK10261 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSvtalalmRLLEQAGGLVQCDKMLLRRRSRQVIELseqsAAQMRHVRGadMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 331 YVPEQrlghaavPELSLTAnTYLTGDSLVRS-----GFIlRDRARSFANLVIERfhVKTPNAEKAAG----SLSGGNLQK 401
Cdd:PRK10261 108 MIFQE-------PMTSLNP-VFTVGEQIAESirlhqGAS-REEAMVEAKRMLDQ--VRIPEAQTILSryphQLSGGMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 402 FIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNsLIRL--RDDGAAIIVVSEEIDELFEISDRIAVMYRGAlspAVpkPT 479
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQ-LIKVlqKEMSMGVIFITHDMGVVAEIADRVLVMYQGE---AV--ET 250
|
250 260
....*....|....*....|.
gi 2549828669 480 ISIEEVGRwmsglWPDSPFTQ 500
Cdd:PRK10261 251 GSVEQIFH-----APQHPYTR 266
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
137-217 |
3.77e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 49.69 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 137 LSMGERQRVEILRALMTKPK---LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRElADRCVVL---- 209
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKT-ADWIIDLgpeg 909
|
90
....*....|
gi 2549828669 210 --RAGKVVAS 217
Cdd:PRK00349 910 gdGGGEIVAT 919
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
268-471 |
5.57e-06 |
|
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: 47.71 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGeylceadrvLLFNSPvGELdtharRISGlrYVP-EQRLGHAAVPELS 346
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSG---------LLQPTS-GEV-----RVAG--LVPwKRRKKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 347 LTANTYLTGDSLVRSGFIL------------RDRARSFANLV-IERFhVKTPnaekaAGSLSGGNLQKFIMGREILNRPR 413
Cdd:cd03267 100 FGQKTQLWWDLPVIDSFYLlaaiydlpparfKKRLDELSELLdLEEL-LDTP-----VRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 414 VLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRGAL 471
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
270-492 |
7.06e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.57 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 270 NVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGEldthARRISGLRYVPEQRLGHAAVPelSLTA 349
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNLVAYVPQSEEVDWSFP--VLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 350 NTYLTGdSLVRSGFILRDRA--RSFANLVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVG 427
Cdd:PRK15056 99 DVVMMG-RYGHMGWLRRAKKrdRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 428 AAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDrIAVMYRGALSPAVP-KPTISIEEVGRWMSGL 492
Cdd:PRK15056 177 TEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPtETTFTAENLELAFSGV 241
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
390-471 |
8.14e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 47.46 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 390 AAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDgAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK14239 145 SALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDG 223
|
..
gi 2549828669 470 AL 471
Cdd:PRK14239 224 DL 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-214 |
8.26e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.79 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEISFDGhplgvetpaqarelGIAMVHQHfALFDTLSVTENVAL 102
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------------SVAYVPQQ-AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 103 G-------LSTGISAAEIEREIRLLGEKYGLEVDPASVvmELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKL 175
Cdd:TIGR00957 722 GkalnekyYQQVLEACALLPDLEILPSGDRTEIGEKGV--NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2549828669 176 FKtlHQLSSEGV----SILFISHKLDEIRELaDRCVVLRAGKV 214
Cdd:TIGR00957 800 FE--HVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKI 839
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-465 |
1.00e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 29 PGEVLAILGENGAGKSTLMKIIYGAARPDEGEisfdghplgVETPAQARElgiamVHQHFA---LFDTLSvtenvalGLS 105
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGD---------YEEEPSWDE-----VLKRFRgteLQNYFK-------KLY 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 106 TG-ISAA------------------EI-----EREIRL-LGEKYGLE--VDPAsvVMELSMGERQRVEILRALMTKPKLL 158
Cdd:PRK13409 157 NGeIKVVhkpqyvdlipkvfkgkvrELlkkvdERGKLDeVVERLGLEniLDRD--ISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 159 ILDEPTSVL-------TPQAVRKLfktlhqlsSEGVSILFISHKLDEIRELADRCVVLRaGK-----VVAsvDPKAE--- 223
Cdd:PRK13409 235 FFDEPTSYLdirqrlnVARLIREL--------AEGKYVLVVEHDLAVLDYLADNVHIAY-GEpgaygVVS--KPKGVrvg 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 224 ---------SEENLaRlmIGNDPPTVREGTAKagEVVFEMRHVSAPGSTRvcGIDNVSLAV-----RAGEIVGIAGISGN 289
Cdd:PRK13409 304 ineylkgylPEENM-R--IRPEPIEFEERPPR--DESERETLVEYPDLTK--KLGDFSLEVeggeiYEGEVIGIVGPNGI 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 290 GQARFMAAASGEYlcEADRvllfnspvGELDThARRISglrYVPEqrlghaavpelsltantYLTGDSLVRSGFILRDRA 369
Cdd:PRK13409 377 GKTTFAKLLAGVL--KPDE--------GEVDP-ELKIS---YKPQ-----------------YIKPDYDGTVEDLLRSIT 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 370 RSFA-----NLVIERFHVKtPNAEKAAGSLSGGNLQKFI----MGRE----ILNRPRVLL-VHQptwgvDVGAAAVIRNs 435
Cdd:PRK13409 426 DDLGssyykSEIIKPLQLE-RLLDKNVKDLSGGELQRVAiaacLSRDadlyLLDEPSAHLdVEQ-----RLAVAKAIRR- 498
|
490 500 510
....*....|....*....|....*....|
gi 2549828669 436 LIRLRDdgAAIIVVSEEIDELFEISDRIAV 465
Cdd:PRK13409 499 IAEERE--ATALVVDHDIYMIDYISDRLMV 526
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
252-469 |
1.16e-05 |
|
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: 47.91 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 252 FEMRHVS---APGSTRVcgIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRiSG 328
Cdd:COG2274 474 IELENVSfryPGDSPPV--LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLR-RQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 329 LRYVPeQrlghaavpelsltaNTYLTGDSlVRSGFILRDRARSFANLV-------IERFHVKTPN------AEKAAGsLS 395
Cdd:COG2274 551 IGVVL-Q--------------DVFLFSGT-IRENITLGDPDATDEEIIeaarlagLHDFIEALPMgydtvvGEGGSN-LS 613
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 396 GGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRdDGAAIIVVSEEiDELFEISDRIAVMYRG 469
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHR-LSTIRLADRIIVLDKG 685
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-205 |
1.26e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 29 PGEVLAILGENGAGKSTLMKIIYGAARPDEGEIsfdghplgvetpaqarelgiamvhqhfalfdtlsvtenVALGLSTGI 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------------IYIDGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 109 SAAEIEREIRLLGEKYGLEVDpasvvmelsmGERQRVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLH------QL 182
Cdd:smart00382 43 EEVLDQLLLIIVGGKKASGSG----------ELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllLK 112
|
170 180
....*....|....*....|...
gi 2549828669 183 SSEGVSILFISHKLDEIRELADR 205
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPALLR 135
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-205 |
1.65e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.04 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 24 SLDIAPGEVLAILGENGAGKSTLMK-IIYGaarpdegeisfdghplgvetpaqareLGIAMVHQHFALFdtlsvtenval 102
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDaIGLA--------------------------LGGAQSATRRRSG----------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 103 GLSTGISAAEiereirllgekyglEVDPASVVMELSMGERQRVE---ILRALMTKPK-LLILDEPTSVLTPQAVRKLFKT 178
Cdd:cd03227 58 VKAGCIVAAV--------------SAELIFTRLQLSGGEKELSAlalILALASLKPRpLYILDEIDRGLDPRDGQALAEA 123
|
170 180
....*....|....*....|....*..
gi 2549828669 179 LHQLSSEGVSILFISHKLdEIRELADR 205
Cdd:cd03227 124 ILEHLVKGAQVIVITHLP-ELAELADK 149
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-217 |
1.72e-05 |
|
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: 46.10 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTL-MKIIYGaarpdEGEISFdghplgVET-PAQARELGIAMVHQHFALFDTLSVTENV 100
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSLaFDTIYA-----EGQRRY------VESlSAYARQFLGQMDKPDVDSIEGLSPAIAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 101 ALGL------STGISAAEIEREIRLLGEKYGLE-------------VDPASVVMELSMGERQRVEILRALMTKPK--LLI 159
Cdd:cd03270 83 DQKTtsrnprSTVGTVTEIYDYLRLLFARVGIRerlgflvdvglgyLTLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 160 LDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIReLADRCVVL------RAGKVVAS 217
Cdd:cd03270 163 LDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIR-AADHVIDIgpgagvHGGEIVAQ 225
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-221 |
2.06e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 137 LSMGERQRVEI---LRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLdEIRELADRCVVL---- 209
Cdd:PRK00635 810 LSGGEIQRLKLayeLLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVADYVLELgpeg 888
|
90
....*....|....
gi 2549828669 210 --RAGKVVASVDPK 221
Cdd:PRK00635 889 gnLGGYLLASCSPE 902
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-249 |
2.14e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.47 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEI----SFdghplgVETPAQARELGiAMVHQHFALFDtlsvtE 98
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaerSI------AYVPQQAWIMN-ATVRGNILFFD-----E 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 99 NVALGLSTGISAAEIEREIRLLGEkyGLEVDPASVVMELSMGERQRVEILRALMTKPKLLILDEPTSVLTPQA----VRK 174
Cdd:PTZ00243 747 EDAARLADAVRVSQLEADLAQLGG--GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgervVEE 824
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 175 LFktLHQLSseGVSILFISHKLdEIRELADRCVVLRAGKVVASVDPKAESEENLARLMIGN--DPPTVREGTAKAGE 249
Cdd:PTZ00243 825 CF--LGALA--GKTRVLATHQV-HVVPRADYVVALGDGRVEFSGSSADFMRTSLYATLAAElkENKDSKEGDADAEV 896
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
88-290 |
2.28e-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: 47.32 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 88 FALFDTLSVTENVALglstgiSAAEIEREIRllgEKYGLEVD-------PASVVMELSMGERQRVEILRALMTKPK--LL 158
Cdd:TIGR00630 442 HEFFNQLTLTPEEKK------IAEEVLKEIR---ERLGFLIDvgldylsLSRAAGTLSGGEAQRIRLATQIGSGLTgvLY 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 159 ILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKLDEIRElADRCVVL--RAGK----VVASVDPKAeseenlarLM 232
Cdd:TIGR00630 513 VLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRA-ADYVIDIgpGAGEhggeVVASGTPEE--------IL 583
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 233 IGNDPPTvreGTAKAGEV---VFEMRHVSAPGSTRVCG-----IDNVSLAVRAGEIVGIAGISGNG 290
Cdd:TIGR00630 584 ANPDSLT---GQYLSGRKkieVPAERRPGNGKFLTLKGarennLKNITVSIPLGLFTCITGVSGSG 646
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
394-495 |
3.60e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.47 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRnSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALSP 473
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE-EFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
90 100
....*....|....*....|....*.
gi 2549828669 474 AVPKPTI----SIEEVGRWMSGLWPD 495
Cdd:PRK14271 243 EGPTEQLfsspKHAETARYVAGLSGD 268
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
264-469 |
4.40e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 45.67 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 264 RVCGIDNVSLAVRAGEIVGIAGISGNGQARF----MAAASGEYLCEADRvLLFNSpvgeldtharrISGLRYVPEQR--- 336
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIakaiCGITKDNWHVTADR-FRWNG-----------IDLLKLSPRERrki 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 337 LGHaavpELSLT---ANTYL-----TGDSLVRS-------GFILRdRARSFANLVIERFH-VKTPNAEKAAGS----LSG 396
Cdd:COG4170 87 IGR----EIAMIfqePSSCLdpsakIGDQLIEAipswtfkGKWWQ-RFKWRKKRAIELLHrVGIKDHKDIMNSypheLTE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 397 GNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCG 235
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
394-469 |
5.14e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 45.32 E-value: 5.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
271-476 |
8.50e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 44.19 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 271 VSLAVRAGEIVGIAGISGNGQARFM-------AAASGEYLCEADRVLLFNSPVGEL---DTHARRISGLR----YVPEQR 336
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLrcinfleKPSEGSIVVNGQTINLVRDKDGQLkvaDKNQLRLLRTRltmvFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 337 LGHAAVPELSLTANTYLTGDSLVRSgfilRDRARSFANLV--IERFHVKTPNaekaagSLSGGNLQKFIMGREILNRPRV 414
Cdd:PRK10619 104 WSHMTVLENVMEAPIQVLGLSKQEA----RERAVKYLAKVgiDERAQGKYPV------HLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 415 LLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGALSPAVP 476
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
267-469 |
9.28e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 44.23 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 267 GIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLL--FNSPVG-----ELDTHARRISGLRYVPEQRLGH 339
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdYAIPANlkkikEVKRLRKEIGLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 340 AAVPELSLTANTYLTGDslvrsgfilRDRARSFANLVIERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQ 419
Cdd:PRK13645 106 ETIEKDIAFGPVNLGEN---------KQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 420 PTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEG 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
268-325 |
1.13e-04 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 43.99 E-value: 1.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTH--ARR 325
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelARR 77
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
271-469 |
1.15e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 43.85 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 271 VSLAVRAGEIVGIAGISGNGQARFMAAASGeyLCEAD-----RVLLFNSPVGELDTHARRISGLR----YVPEQrlgHAA 341
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSG--LITGDksagsHIELLGRTVQREGRLARDIRKSRantgYIFQQ---FNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 342 VPELSLTANTY---LTGDSLVRSGF-----ILRDRA-RSFANLVIERFhvktpnAEKAAGSLSGGNLQKFIMGREILNRP 412
Cdd:PRK09984 98 VNRLSVLENVLigaLGSTPFWRTCFswftrEQKQRAlQALTRVGMVHF------AHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2549828669 413 RVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
394-469 |
1.27e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 43.84 E-value: 1.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQG 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
268-484 |
1.42e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 44.05 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 268 IDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRisglryvpeqRLGhaAVPELSL 347
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARA----------RIG--VVPQFDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 348 TANTYLTGDSLVRSGFILRDRARSFANLV--IERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVD 425
Cdd:PRK13536 125 LDLEFTVRENLLVFGRYFGMSTREIEAVIpsLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 426 VGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRGAlSPAVPKPTISIEE 484
Cdd:PRK13536 205 PHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR-KIAEGRPHALIDE 262
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
267-469 |
1.55e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 44.25 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 267 GIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELDTHARRISGLRYVPEQRLGHAAVPELS 346
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 347 LTANTYLTGDSLVRSGFILRDRA-RSFANLVIERFHVKTPNaekaagSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVD 425
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKAlDALRQVGLENYAHSYPD------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2549828669 426 VGAAAVIRNSLIRLR-DDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK10070 197 PLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-195 |
1.60e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 44.35 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 15 PGITANDHV-----SLDIAPGEVLAILGENGAGKSTLMKI------IYGAAR--PDEGEISF-------------DG--H 66
Cdd:TIGR00954 458 PLVTPNGDVlieslSFEVPSGNNLLICGPNGCGKSSLFRIlgelwpVYGGRLtkPAKGKLFYvpqrpymtlgtlrDQiiY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 67 PLGVETpaqarelgiaMVHQHFALFDTLSVTENVALGlstgisaaeiereiRLLGEKYGLEVdPASVVMELSMGERQRVE 146
Cdd:TIGR00954 538 PDSSED----------MKRRGLSDKDLEQILDNVQLT--------------HILEREGGWSA-VQDWMDVLSGGEKQRIA 592
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2549828669 147 ILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLsseGVSILFISHK 195
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF---GITLFSVSHR 638
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
370-467 |
2.05e-04 |
|
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: 43.12 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 370 RSFANLVIERFHVKtPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVG----AAAVIRnsliRLRDDGAA 445
Cdd:cd03236 117 RGKLDELVDQLELR-HVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlnAARLIR----ELAEDDNY 191
|
90 100
....*....|....*....|..
gi 2549828669 446 IIVVSEEIDELFEISDRIAVMY 467
Cdd:cd03236 192 VLVVEHDLAVLDYLSDYIHCLY 213
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
394-469 |
2.24e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 2.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAG 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
253-471 |
2.27e-04 |
|
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: 42.57 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 253 EMRHVS---APGSTRVCGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGEYLCEADRVLLFNSPVGELD----THARR 325
Cdd:cd03258 3 ELKNVSkvfGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 326 ISGL----------RYVpeqrLGHAAVP-ELSLTANTYLtgdslvrsgfilRDRARSFANLV-IERFHVKTPnaekaaGS 393
Cdd:cd03258 83 RIGMifqhfnllssRTV----FENVALPlEIAGVPKAEI------------EERVLELLELVgLEDKADAYP------AQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDvgaAAVIRNSLIRLRDD----GAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALD---PETTQSILALLRDInrelGLTIVLITHEMEVVKRICDRVAVMEKG 217
|
..
gi 2549828669 470 AL 471
Cdd:cd03258 218 EV 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
368-465 |
2.76e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 368 RARSFAnlVIERFHVKTPNAEKA-----AGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD 442
Cdd:PTZ00265 1330 RACKFA--AIDEFIESLPNKYDTnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK 1407
|
90 100
....*....|....*....|....
gi 2549828669 443 G-AAIIVVSEEIDELfEISDRIAV 465
Cdd:PTZ00265 1408 AdKTIITIAHRIASI-KRSDKIVV 1430
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
387-469 |
2.85e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 42.73 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 387 AEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAV 465
Cdd:PRK13637 138 KDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIV 217
|
....
gi 2549828669 466 MYRG 469
Cdd:PRK13637 218 MNKG 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
258-469 |
3.01e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 42.80 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 258 SAPGSTRvcGIDNVSLAVRAGEIVGIAGISGNGQARFMAAASGeYLCEADRVLLFNSPVGELDTHARRISGLRyvpeQRL 337
Cdd:PRK13643 14 NSPFASR--ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNG-LLQPTEGKVTVGDIVVSSTSKQKEIKPVR----KKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 338 GHA-AVPELSLTANTYLTGDSLVRSGF-ILRDRARSFANLVIERFHVKTPNAEKAAGSLSGGNLQKFIMGREILNRPRVL 415
Cdd:PRK13643 87 GVVfQFPESQLFEETVLKDVAFGPQNFgIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2549828669 416 LVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-207 |
5.33e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 130 PASVVMELSMGERQRVEILRALMTKPK--LLILDEPTSVLTPQAVRKLFKTLHQLSSEGVSILFISHKlDEIRELADRCV 207
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRII 548
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
111-194 |
6.74e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 111 AEIEREIRLLGEKYGLEVDPAsvvmELSMGERQ---RVEILRALMTKPKLLILDEPTSVLTPQAVRKLFKTLHQLSSEGV 187
Cdd:pfam13304 215 RLRERGLILLENGGGGELPAF----ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGA 290
|
....*..
gi 2549828669 188 SILFISH 194
Cdd:pfam13304 291 QLILTTH 297
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
395-483 |
7.79e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 41.62 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 395 SGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEIDELFEISDRIAVMYRG---- 469
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGhave 242
|
90 100 110
....*....|....*....|....*....|.
gi 2549828669 470 -----------------ALSPAVPKPTISIE 483
Cdd:PRK15079 243 lgtydevyhnplhpytkALMSAVPIPDPDLE 273
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
23-194 |
7.84e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.63 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 23 VSLDIAPGEVLAILGENGAGKSTLMKIIYGAARPDEGEI---------------SFDGHPLGVETpaqarelgiamvhqH 87
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykncninniakpycTYIGHNLGLKL--------------E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 88 FALFDTLSVTENVALGLSTGISAAEIEREIRLLGEKyglevdpasvVMELSMGERQRVEILRALMTKPKLLILDEPTSVL 167
Cdd:PRK13541 85 MTVFENLKFWSEIYNSAETLYAAIHYFKLHDLLDEK----------CYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
|
170 180
....*....|....*....|....*...
gi 2549828669 168 TPQAvRKLFKTLHQL-SSEGVSILFISH 194
Cdd:PRK13541 155 SKEN-RDLLNNLIVMkANSGGIVLLSSH 181
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
387-487 |
8.05e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 41.22 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 387 AEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVM 466
Cdd:PRK13639 131 ENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVM 210
|
90 100
....*....|....*....|..
gi 2549828669 467 YRGA-LSPAVPKPTISIEEVGR 487
Cdd:PRK13639 211 SDGKiIKEGTPKEVFSDIETIR 232
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
4-62 |
1.24e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.75 E-value: 1.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2549828669 4 RLSLRNItKRYpgitANDHVSLDIAPGeVLAILGENGAGKSTLMKIIYGAARPDEGEIS 62
Cdd:COG3950 5 SLTIENF-RGF----EDLEIDFDNPPR-LTVLVGENGSGKTTLLEAIALALSGLLSRLD 57
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
391-471 |
1.25e-03 |
|
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: 41.92 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 391 AGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRdDGAAIIVVSEEIDELFEISDRIAVMYRGA 470
Cdd:TIGR01257 1059 AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
.
gi 2549828669 471 L 471
Cdd:TIGR01257 1138 L 1138
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
236-333 |
2.88e-03 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 40.15 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 236 DPPTVREGTAKAGEVVFEmrHVSA--PGSTRVcgIDNVSLAVRAGEIVGIAGISGNGQ-------ARFMAAASGeylcea 306
Cdd:COG1132 326 DPPGAVPLPPVRGEIEFE--NVSFsyPGDRPV--LKDISLTIPPGETVALVGPSGSGKstlvnllLRFYDPTSG------ 395
|
90 100
....*....|....*....|....*....
gi 2549828669 307 dRVLLFNSPVGELDTHA--RRISglrYVP 333
Cdd:COG1132 396 -RILIDGVDIRDLTLESlrRQIG---VVP 420
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
366-469 |
4.14e-03 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 38.84 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 366 RDRARSFANLVIERFHVkTPNAEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAA 445
Cdd:PRK11124 115 KDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGIT 193
|
90 100
....*....|....*....|....
gi 2549828669 446 IIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK11124 194 QVIVTHEVEVARKTASRVVYMENG 217
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
394-469 |
5.63e-03 |
|
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: 38.24 E-value: 5.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNsLIRLRDDGAAIIVVSEEIDELFEiSDRIAVMYRG 469
Cdd:cd03244 140 LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQK-TIREAFKDCTVLTIAHRLDTIID-SDRILVLDKG 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
235-290 |
7.70e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 38.79 E-value: 7.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2549828669 235 NDPPTVREGTAKAGEVVFEMRHVSAPGSTRvcGIDNVSLAVRAGEIVGIAGISGNG 290
Cdd:PRK13657 320 RDPPGAIDLGRVKGAVEFDDVSFSYDNSRQ--GVEDVSFEAKPGQTVAIVGPTGAG 373
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
18-47 |
8.20e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 8.20e-03
10 20 30
....*....|....*....|....*....|
gi 2549828669 18 TANDHVsLDIAPGEVLAILGENGAGKSTLM 47
Cdd:pfam13555 11 TFDGHT-IPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
387-469 |
8.75e-03 |
|
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: 37.89 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 387 AEKAAGSLSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDDGAAIIVVSEEIDELFEISDRIAVM 466
Cdd:cd03262 129 ADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFM 208
|
...
gi 2549828669 467 YRG 469
Cdd:cd03262 209 DDG 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
249-454 |
9.05e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 38.23 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 249 EVVFEMRHVS--APGSTRvcgIDNVSLAVRAGEIVGIAGISGNGQA-------RFMAAASGEylceadrVLLFNSPVGEL 319
Cdd:PRK10575 9 DTTFALRNVSfrVPGRTL---LHPLSLTFPAGKVTGLIGHNGSGKStllkmlgRHQPPSEGE-------ILLDAQPLESW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 320 DTH--ARRISglrYVPEQrLGHA---AVPELsLTANTYLTGDSLVRSGFILRDRARSFANLVierfhVKTPNAEKAAGSL 394
Cdd:PRK10575 79 SSKafARKVA---YLPQQ-LPAAegmTVREL-VAIGRYPWHGALGRFGAADREKVEEAISLV-----GLKPLAHRLVDSL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2549828669 395 SGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRL-RDDGAAIIVVSEEID 454
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDIN 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
394-469 |
9.28e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 38.53 E-value: 9.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2549828669 394 LSGGNLQKFIMGREILNRPRVLLVHQPTWGVDVGAAAVIRNSLIRLRDD-GAAIIVVSEEIDELFEISDRIAVMYRG 469
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-204 |
9.59e-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: 37.59 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 4 RLSLRNITKRYpgitanDHVSLDIAPGeVLAILGENGAGKSTLMKII----YGAARPDEGEISFDGHPLGV-ETPAQare 78
Cdd:cd03240 3 KLSIRNIRSFH------ERSEIEFFSP-LTLIVGQNGAGKTTIIEALkyalTGELPPNSKGGAHDPKLIREgEVRAQ--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2549828669 79 lgiamVHQHFALFD--------TLSVTENVALgLSTGISAAEIEREIRLlgekyglevdpasvvmeLSMGERQ------R 144
Cdd:cd03240 73 -----VKLAFENANgkkytitrSLAILENVIF-CHQGESNWPLLDMRGR-----------------CSGGEKVlasliiR 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2549828669 145 VEILRALMTKPKLLILDEPTSVLTPQAVR-KLFKTLHQLSSEGVS-ILFISHKlDEIRELAD 204
Cdd:cd03240 130 LALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQKNFqLIVITHD-EELVDAAD 190
|
|
|