|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-643 |
0e+00 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 1266.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDIE 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 GTIFDFVAQGVAEDAQYITEYHRVSKVIETDPSEKNLNRLAQLQEVLDNRNLWLLDSRIAEVLEKLGLNGEAELSSLSGG 160
Cdd:PRK11147 81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 161 WLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLSSWPGNYDK 240
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 241 YLESKEEALRVEEQQNAEFDRKLAQEEAWIRQGIKARRTRNEGRVRALKALRVERSERREVLGSARMQVEEATRSGKIVF 320
Cdd:PRK11147 241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRSGKIVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQHRATLDPDKTV 400
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 401 MDNLAEGKQEVMVNGRPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:PRK11147 401 MDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 481 ELVDAYQGTVLLVSHDREFVDNSVTECWIFEGDGVINSYVGGYYDAQQQRAQSVSLKNEANKsrnapektEKETKPKQNA 560
Cdd:PRK11147 481 ELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQQQAQYLALKQPAVK--------KKEEAAAPKA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 561 KKATRSNNKLSYHLIRELEQLPAKLERLEEELGCLQEEVAAADFFTRPHEETEKVLKALADKENELETAFDRWQELEMMQ 640
Cdd:PRK11147 553 ETVKRSSKKLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLADLADAEQELEVAFERWEELEALK 632
|
...
gi 1437745527 641 NGE 643
Cdd:PRK11147 633 NGG 635
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-529 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 667.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 6 LTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDIEGTIFD 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 86 FVAQGVAEDAQYITEYHRVSKviETDPSEKNLNRLAQLQEVLDNRNLWLLDSRIAEVLEKLGLNGE---AELSSLSGGWL 162
Cdd:COG0488 81 TVLDGDAELRALEAELEELEA--KLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEdldRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 163 RKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLSSWPGNYDKYL 242
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 243 ESKEEALRVEEQQNAEFDRKLAQEEAWIRQ-GIKARR-TRNEGRVRALKALRVERSERREvlGSARMQVEEATRSGKIVF 320
Cdd:COG0488 239 EQRAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARKaKQAQSRIKALEKLEREEPPRRD--KTVEIRFPPPERLGKKVL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQHRATLDPDKTV 400
Cdd:COG0488 317 ELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 401 MDNLAEGKQevmvNGRPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:COG0488 397 LDELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1437745527 481 ELVDAYQGTVLLVSHDREFVDNSVTECWIFEgDGVINSYVGGYYDAQQQ 529
Cdd:COG0488 473 EALDDFPGTVLLVSHDRYFLDRVATRILEFE-DGGVREYPGGYDDYLEK 520
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-530 |
6.96e-125 |
|
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: 380.43 E-value: 6.96e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 34 LVGRNGAGKSTLLRVLAKeqpLD---DGQVVYEQDLVTARLQQDPPRDIEGTIFDFVAQGVAEDAQYITEYHRVSKVI-- 108
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAG---VDkdfNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEISAKYae 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 109 ETDPSEKNLNRLAQLQEVLDNRNLWLLDSRIAEVLEKLGL-NGEAELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHL 187
Cdd:TIGR03719 113 PDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCpPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 188 DIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLSSWPGNYDKYLESKEEALRVEEQQNAEFDRKLAQEE 267
Cdd:TIGR03719 193 DAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLEQEEKEESARQKTLKREL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 268 AWIRQGIKARRTRNEGRVRALKALRVERSERREvlGSARMQVEEATRSGKIVFELEDVNYSIGTRRLVRDFSAKVQRGDK 347
Cdd:TIGR03719 273 EWVRQSPKGRQAKSKARLARYEELLSQEFQKRN--ETAEIYIPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGI 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 348 IALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQHRATLDPDKTVMDNLAEGKQEVMVNGRPRHVLGYLQDF 427
Cdd:TIGR03719 351 VGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRF 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 428 LFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQGTVLLVSHDREFVDNSVTEC 507
Cdd:TIGR03719 431 NFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHI 510
|
490 500
....*....|....*....|....*
gi 1437745527 508 WIFEGDGVINSYVGGY--YDAQQQR 530
Cdd:TIGR03719 511 LAFEGDSHVEWFEGNFseYEEDKKR 535
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-525 |
1.53e-120 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 369.45 E-value: 1.53e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 34 LVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDIEGTIFDFVAQGVAEDAQYITEYHRVSKVI--ETD 111
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRFNEIYAAYaePDA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 112 PSEKNLNRLAQLQEVLDNRNLWLLDSRIAEVLEKLGL-NGEAELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIE 190
Cdd:PRK11819 118 DFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCpPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 191 TILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLSSWPGNYDKYLESKEEALRVEEQQNAEFDRKLAQEEAWI 270
Cdd:PRK11819 198 SVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 271 RQGIKARRTRNEGRVRALKALRVERSERRevLGSARMQVEEATRSGKIVFELEDVNYSIGTRRLVRDFSAKVQRGDKIAL 350
Cdd:PRK11819 278 RQSPKARQAKSKARLARYEELLSEEYQKR--NETNEIFIPPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 351 VGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQHRATLDPDKTVMDNLAEGKQEVMVNGRPRHVLGYLQDFLFP 430
Cdd:PRK11819 356 IGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKVGNREIPSRAYVGRFNFK 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 431 PKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQGTVLLVSHDREFVDNSVTECWIF 510
Cdd:PRK11819 436 GGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAF 515
|
490
....*....|....*
gi 1437745527 511 EGDGVINSYVGGYYD 525
Cdd:PRK11819 516 EGDSQVEWFEGNFQE 530
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-525 |
1.38e-80 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 264.45 E-value: 1.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDIEGTIFDFVAQGVA 92
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVIMGHT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 93 EDAQYITEYHRVSKVIETdpSEKNLNRLAQLQEVLDNRNLWLLDSRIAEVLekLGLNGEAEL-----SSLSGGWLRKAAL 167
Cdd:PRK15064 91 ELWEVKQERDRIYALPEM--SEEDGMKVADLEVKFAEMDGYTAEARAGELL--LGVGIPEEQhyglmSEVAPGWKLRVLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 168 GRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLSSWPGNYDKYLESKEE 247
Cdd:PRK15064 167 AQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 248 AlrvEEQQNAEFDRKLAQ-EEAwirQGIKARRTRNEGRVR--ALKALRVERSERREVLGSARM----QVEEATRSGKIVF 320
Cdd:PRK15064 247 A---RERLLADNAKKKAQiAEL---QSFVSRFSANASKAKqaTSRAKQIDKIKLEEVKPSSRQnpfiRFEQDKKLHRNAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQ-HRATLDPDKT 399
Cdd:PRK15064 321 EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdHAYDFENDLT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 400 VMDNLAEGKQ----EVMVngrpRHVLGYLqdfLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
Cdd:PRK15064 401 LFDWMSQWRQegddEQAV----RGTLGRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1437745527 476 LELLEELVDAYQGTVLLVSHDREFVDNSVTECWIFEGDGVINsYVGGYYD 525
Cdd:PRK15064 474 IESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVD-FSGTYEE 522
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-643 |
1.17e-66 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 230.06 E-value: 1.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 18 LLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRdIEGTIFDFVAQGVAEDAQY 97
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPA-LPQPALEYVIDGDREYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 98 ITEYHrvskvietDPSEKNL-NRLAQLQEVLDNRNLWLLDSRIAEVLEKLGLNGEA---ELSSLSGGWLRKAALGRALVS 173
Cdd:PRK10636 95 EAQLH--------DANERNDgHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQlerPVSDFSGGWRMRLNLAQALIC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 174 APKVLFLDEPTNHLDIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLSSWPGNYDKYleSKEEALRVEE 253
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSF--EVQRATRLAQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 254 QQnAEFD---RKLAQEEAWI-RQGIKARRTRN-EGRVRALKalRVERSERREVLGSARMQVEEATRSGKIVFELEDVNYS 328
Cdd:PRK10636 245 QQ-AMYEsqqERVAHLQSYIdRFRAKATKAKQaQSRIKMLE--RMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 329 IGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQHRAT-LDPDKTVMDNLAEG 407
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEfLRADESPLQHLARL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 408 KQEVMvngrPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQ 487
Cdd:PRK10636 402 APQEL----EQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 488 GTVLLVSHDREFVDNSVTECWIFEgDGVINSYVGGYYDAQQQRAqsvslknEANKSRNAPEKTEKETKPK--QNAKKATR 565
Cdd:PRK10636 478 GALVVVSHDRHLLRSTTDDLYLVH-DGKVEPFDGDLEDYQQWLS-------DVQKQENQTDEAPKENNANsaQARKDQKR 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 566 SNNKL---SYHLIRELEQLPAKLERLEEELGCLQEEVAAADFF--TRPHEETEkVLKALADKENELETAFDRWQEL---- 636
Cdd:PRK10636 550 REAELrtqTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYdqSRKAELTA-CLQQQASAKSGLEECEMAWLEAqeql 628
|
....*...
gi 1437745527 637 -EMMQNGE 643
Cdd:PRK10636 629 eQMLLEGQ 636
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-525 |
4.87e-59 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 210.87 E-value: 4.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 34 LVGRNGAGKSTLLRVLAKEQPldDG-----QVVY-EQDLV---TARLQQDPPRDIEGT-IFDFVAQGVAEDAQYITEYHR 103
Cdd:PLN03073 208 LVGRNGTGKTTFLRYMAMHAI--DGipkncQILHvEQEVVgddTTALQCVLNTDIERTqLLEEEAQLVAQQRELEFETET 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 104 V-SKVIETDPSEKNL--NRLAQLQEVLDNRNLWLLDSRIAEVLEKLGLNGEAEL---SSLSGGWLRKAALGRALVSAPKV 177
Cdd:PLN03073 286 GkGKGANKDGVDKDAvsQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVkatKTFSGGWRMRIALARALFIEPDL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 178 LFLDEPTNHLDIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLSSWPGNYDKYLESKEEALRVEEQQNA 257
Cdd:PLN03073 366 LLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 258 EFDRKLAQEEAWI---RQGIKaRRTRNEGRVRALKalRVERSErrEVLGSARMQVEEAT---RSGKIVFELEDVNYSI-G 330
Cdd:PLN03073 446 SNERSRSHMQAFIdkfRYNAK-RASLVQSRIKALD--RLGHVD--AVVNDPDYKFEFPTpddRPGPPIISFSDASFGYpG 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 331 TRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQHRAT-LDPDKTVMDNLAEgkq 409
Cdd:PLN03073 521 GPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDgLDLSSNPLLYMMR--- 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 410 evMVNGRPRHVL-GYLQDFLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQG 488
Cdd:PLN03073 598 --CFPGVPEQKLrAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG 675
|
490 500 510
....*....|....*....|....*....|....*..
gi 1437745527 489 TVLLVSHDREFVDNSVTECWIFEgDGVINSYVGGYYD 525
Cdd:PLN03073 676 GVLMVSHDEHLISGSVDELWVVS-EGKVTPFHGTFHD 711
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-591 |
3.49e-52 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 187.96 E-value: 3.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 322 LEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQHrATLDPDKTVM 401
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQE-PPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 402 DNLAEGKQEVMVNGRPRHVL-------------------------GY---------LQDFLFPPKRAMTPVRALSGGERN 447
Cdd:COG0488 80 DTVLDGDAELRALEAELEELeaklaepdedlerlaelqeefealgGWeaearaeeiLSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 448 RLLLARLFLKPSNLLILDEPTNDLDVetlelleelvDA----------YQGTVLLVSHDREFVDNSVTecWIFE-GDGVI 516
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDL----------ESiewleeflknYPGTVLVVSHDRYFLDRVAT--RILElDRGKL 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 517 NSYVGGYYDAQQQRAQsvSLKNEANKSRNAPEKTEKET----KPKQNAKKATRSNNKlsyhlIRELEqlpaKLERLEEE 591
Cdd:COG0488 228 TLYPGNYSAYLEQRAE--RLEQEAAAYAKQQKKIAKEEefirRFRAKARKAKQAQSR-----IKALE----KLEREEPP 295
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
321-514 |
3.93e-50 |
|
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: 170.71 E-value: 3.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQhratldpdktv 400
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 401 mdnlaegkqevmvngrprhvlgylqdflfppkramtpvraLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd03221 71 ----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190
....*....|....*....|....*....|....
gi 1437745527 481 ELVDAYQGTVLLVSHDREFVDNSVTECWIFEGDG 514
Cdd:cd03221 111 EALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-500 |
2.73e-46 |
|
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: 171.24 E-value: 2.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAF--SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPlddgqvvyeqdlvtarlqqdPPRDI 79
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLP--------------------HGGRI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 80 EGTIF----DFVAQGVAEDAQYITeyhrvskVIETDPsEKNLNRL---AQLQEVLDNRNL--WLLDSRIAEVLEKLGLN- 149
Cdd:COG1123 63 SGEVLldgrDLLELSEALRGRRIG-------MVFQDP-MTQLNPVtvgDQIAEALENLGLsrAEARARVLELLEAVGLEr 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 150 -GEAELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIET---ILWLEKFLKDFQG-SIVFISHDRSFIRNMATRII 224
Cdd:COG1123 135 rLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 225 DLDRGKLsswpgnydkyleskeealrVEEQQNAEFDRklaqeeawirqgikarrtrnegRVRALKAlrverserREVLGS 304
Cdd:COG1123 215 VMDDGRI-------------------VEDGPPEEILA----------------------APQALAA--------VPRLGA 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 305 ARMQVEEATRSGKIVFELEDVNYS-----IGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG 379
Cdd:COG1123 246 ARGRAAPAAAAAEPLLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 380 ----TKLEVAYFDQHR-----------ATLDPDKTVMDNLAEGkqeVMVNG------RPRHVLGYLQDFLFPPKRAMTPV 438
Cdd:COG1123 326 gkdlTKLSRRSLRELRrrvqmvfqdpySSLNPRMTVGDIIAEP---LRLHGllsraeRRERVAELLERVGLPPDLADRYP 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 439 RALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELVDAYQ----GTVLLVSHDREFV 500
Cdd:COG1123 403 HELSGGQRQRVAIARaLALEPK-LLILDEPTSALDVSVQAQILNLLRDLQrelgLTYLFISHDLAVV 468
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-243 |
1.33e-44 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 166.78 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPR-DIE 80
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEElDPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 GTIFDFVAQGvAEDAQyiteyhrvskvietdpseknlnrlaqlqevldnrnlwllDSRIAEVLEKLGLNGE---AELSSL 157
Cdd:COG0488 394 KTVLDELRDG-APGGT---------------------------------------EQEVRGYLGRFLFSGDdafKPVGVL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 158 SGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLSSWPGN 237
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGG 513
|
....*.
gi 1437745527 238 YDKYLE 243
Cdd:COG0488 514 YDDYLE 519
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-230 |
1.94e-43 |
|
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: 152.60 E-value: 1.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQdpprdiegti 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 84 fdfvaqgvaedaqyiteyhrvskvietdpseknlnrlaqlqevldnrnlwlldsriaevleklglngeaelssLSGGWLR 163
Cdd:cd03221 71 -------------------------------------------------------------------------LSGGEKM 77
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 164 KAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:cd03221 78 RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
320-498 |
3.73e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.47 E-value: 3.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 320 FELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKL-----------EVAYFD 388
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 389 QhRATLdPDKTVMDNLAEGKQEVMVNGRPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLAR-LFLKPSNLLiLDEP 467
Cdd:COG4619 81 Q-EPAL-WGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRaLLLQPDVLL-LDEP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1437745527 468 TNDLDVETLELLEELVDAY----QGTVLLVSHDRE 498
Cdd:COG4619 158 TSALDPENTRRVEELLREYlaeeGRAVLWVSHDPE 192
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-268 |
1.14e-32 |
|
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: 126.13 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 3 LISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEqDLVTARLQQDPPRDIegt 82
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID-GEDVRKEPREARRQI--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 83 ifdfvaqGVAEDAQYITEYHRVskvietdpsEKNLNRLAQLQEVLDNRNlwllDSRIAEVLEKLGLNGEAE--LSSLSGG 160
Cdd:COG4555 77 -------GVLPDERGLYDRLTV---------RENIRYFAELYGLFDEEL----KKRIEELIELLGLEEFLDrrVGELSTG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 161 WLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGS---IVFISHDRSFIRNMATRIIDLDRGKLsswpgn 237
Cdd:COG4555 137 MKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEgktVLFSSHIMQEVEALCDRVVILHKGKV------ 210
|
250 260 270
....*....|....*....|....*....|...
gi 1437745527 238 ydKYLESKEE--ALRVEEQQNAEFDRKLAQEEA 268
Cdd:COG4555 211 --VAQGSLDElrEEIGEENLEDAFVALIGSEEG 241
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-501 |
6.34e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.05 E-value: 6.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 319 VFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKLE-----VAYFDQhRA 392
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlFGKPPRrarrrIGYVPQ-RA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 393 TLDPDK--TVMDnlaegkqeVMVNGRPRHvLGylqdFLFPPKRA-------------MT-----PVRALSGGERNRLLLA 452
Cdd:COG1121 85 EVDWDFpiTVRD--------VVLMGRYGR-RG----LFRRPSRAdreavdealervgLEdladrPIGELSGGQQQRVLLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 453 RLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQG---TVLLVSHD----REFVD 501
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDlgavREYFD 207
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-230 |
6.56e-32 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 122.59 E-value: 6.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVvyeqdlvtaRLQQDPPRDIEG 81
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEV---------LWNGEPIRDARE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 82 TIFDFVAqgvaedaqYITEYHRVS---KVIEtdpsekNLNRLAQLQEVLDNRnlwlldSRIAEVLEKLGLNGEAEL--SS 156
Cdd:COG4133 72 DYRRRLA--------YLGHADGLKpelTVRE------NLRFWAALYGLRADR------EAIDEALEAVGLAGLADLpvRQ 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 157 LSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF---QGSIVFISHDRSFIRnmATRIIDLDRGK 230
Cdd:COG4133 132 LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-231 |
1.37e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.19 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVvyeqdlvtaRLQQDPPRDIE 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTV---------RLFGKPPRRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 GTIfDFVAQGVAEDAQY-ITeyhrVSKVIEtdpseknLNRLAQlqevldnRNLWLLDSR-----IAEVLEKLGLNGEAE- 153
Cdd:COG1121 75 RRI-GYVPQRAEVDWDFpIT----VRDVVL-------MGRYGR-------RGLFRRPSRadreaVDEALERVGLEDLADr 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 154 -LSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG---SIVFISHDRSFIRNMATRIIDLDRG 229
Cdd:COG1121 136 pIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRG 215
|
..
gi 1437745527 230 KL 231
Cdd:COG1121 216 LV 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
321-507 |
3.13e-30 |
|
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: 118.40 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKLE-----VAYFDQHRaTL 394
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvFGKPLEkerkrIGYVPQRR-SI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 DPDK--TVMDnlaegkqeVMVNGRPRHVlgylqDFLFPPKRA-------------MT-----PVRALSGGERNRLLLARL 454
Cdd:cd03235 80 DRDFpiSVRD--------VVLMGLYGHK-----GLFRRLSKAdkakvdealervgLSeladrQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 455 FLKPSNLLILDEPTNDLDVETLELLEELVDAYQG---TVLLVSHDREFVDNSVTEC 507
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRV 202
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
319-502 |
3.19e-30 |
|
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: 117.97 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 319 VFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLEVAYFDQ----- 389
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgepiRDAREDYRRRlaylg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 390 HRATLDPDKTVMDNL---AEGKQEVMVNGRPRHVLgylqDFLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:COG4133 82 HADGLKPELTVRENLrfwAALYGLRADREAIDEAL----EAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1437745527 467 PTNDLDVETLELLEELVDAY---QGTVLLVSHDREFVDN 502
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAA 196
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-230 |
3.92e-30 |
|
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: 117.95 E-value: 3.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 14 SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK-EQPLD-----DGQVVYEQDLVTARLQ-----QDPpRD--IE 80
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGlLGPTSgevlvDGKDLTKLSLKELRRKvglvfQNP-DDqfFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 GTIFDFVAQGVaedaqyiteyhrvskvietdpseKNLnrlaQLQEVLDNRnlwlldsRIAEVLEKLGLNG--EAELSSLS 158
Cdd:cd03225 91 PTVEEEVAFGL-----------------------ENL----GLPEEEIEE-------RVEEALELVGLEGlrDRSPFTLS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 159 GGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG---SIVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:cd03225 137 GGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-231 |
4.78e-30 |
|
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: 118.99 E-value: 4.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 3 LISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLVT------AR----L 71
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgRDLASlsrrelARriayV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 72 QQDPPRDIEGTIFDFVAQGvaedaqyiteyhrvskvietdpseknlnRLAQlqevldnRNLWLLDSR-----IAEVLEKL 146
Cdd:COG1120 81 PQEPPAPFGLTVRELVALG----------------------------RYPH-------LGLFGRPSAedreaVEEALERT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 147 GLNGEAE--LSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDI---ETILWLEKFLKDFQG-SIVFISHDRSFIRNMA 220
Cdd:COG1120 126 GLEHLADrpVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqLEVLELLRRLARERGrTVVMVLHDLNLAARYA 205
|
250
....*....|.
gi 1437745527 221 TRIIDLDRGKL 231
Cdd:COG1120 206 DRLVLLKDGRI 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
335-469 |
5.04e-30 |
|
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: 115.44 E-value: 5.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 335 VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG-----------TKLEVAYFDQHrATLDPDKTVMDN 403
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745527 404 LAEGKQEVMV-----NGRPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTN 469
Cdd:pfam00005 80 LRLGLLLKGLskrekDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-231 |
2.10e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 116.70 E-value: 2.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQV-VYEQDLVTArlqqdpPRDIEGTIFdFVAQGV 91
Cdd:COG1131 10 YGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrVLGEDVARD------PAEVRRRIG-YVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 92 AedaqyiteYHRVSKVIEtdpsekNLNRLAQLQEVldnrNLWLLDSRIAEVLEKLGLNGEAE--LSSLSGGWLRKAALGR 169
Cdd:COG1131 83 A--------LYPDLTVRE------NLRFFARLYGL----PRKEARERIDELLELFGLTDAADrkVGTLSGGMKQRLGLAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 170 ALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QGSIVFIS-HDRSFIRNMATRIIDLDRGKL 231
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVAIIDKGRI 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-231 |
6.41e-29 |
|
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: 115.67 E-value: 6.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 3 LISLTGAYLAFS----DAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRD 78
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 79 IegtifdfvaQGVAEDAqyiteY------HRVSKVIEtdpseknlnrlaqlqEVLDNRNLWLLDSRIAEVLEKLGLnGEA 152
Cdd:COG1124 81 V---------QMVFQDP-----YaslhprHTVDRILA---------------EPLRIHGLPDREERIAELLEQVGL-PPS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 153 ELS----SLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIET---ILWLEKFLKDFQG-SIVFISHDRSFIRNMATRII 224
Cdd:COG1124 131 FLDryphQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqaeILNLLKDLREERGlTYLFVSHDLAVVAHLCDRVA 210
|
....*..
gi 1437745527 225 DLDRGKL 231
Cdd:COG1124 211 VMQNGRI 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-233 |
8.52e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 114.38 E-value: 8.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFS-DAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQV-VYEQDLVTARLQQDPP--RDI 79
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlVNGQDLSRLKRREIPYlrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 80 eGTIF-DF-------VAQGVAedaqyiteyhRVSKVIETDPSEknlnrlaqlqevldnrnlwlLDSRIAEVLEKLGLNGE 151
Cdd:COG2884 82 -GVVFqDFrllpdrtVYENVA----------LPLRVTGKSRKE--------------------IRRRVREVLDLVGLSDK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 152 AEL--SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QGSIVFI-SHDRSFIRNMATRIIDL 226
Cdd:COG2884 131 AKAlpHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRMPKRVLEL 210
|
....*..
gi 1437745527 227 DRGKLSS 233
Cdd:COG2884 211 EDGRLVR 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-245 |
9.62e-29 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 120.77 E-value: 9.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 12 AFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDIEG--TIFDFVAQ 89
Cdd:PRK15064 328 GFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENdlTLFDWMSQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 90 --GVAEDAQYITEYhrvskvietdpseknLNRLaqlqevldnrnLWLLDsriaEVLEKLglngeaelSSLSGGWLRKAAL 167
Cdd:PRK15064 408 wrQEGDDEQAVRGT---------------LGRL-----------LFSQD----DIKKSV--------KVLSGGEKGRMLF 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 168 GRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLSSWPGNYDKYLESK 245
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
321-495 |
3.73e-28 |
|
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: 110.94 E-value: 3.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTR--RLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklevaYFDQHratldpdk 398
Cdd:cd03228 2 EFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI---------LIDGV-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 399 tvmdNLAEGKQEVMvngrpRHVLGYL-QD-FLFppkrAMTpVRA--LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03228 65 ----DLRDLDLESL-----RKNIAYVpQDpFLF----SGT-IREniLSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180
....*....|....*....|...
gi 1437745527 475 TLELLEELVDAYQG--TVLLVSH 495
Cdd:cd03228 131 TEALILEALRALAKgkTVIVIAH 153
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-231 |
5.07e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 111.83 E-value: 5.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTA------R-----LQ 72
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmpppewRrqvayVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 73 QDPPRdIEGTIFDFvaqgvaedaqyiteyhrvskvietdpseknlnrlaqLQEVLDNRNLWLLDSRIAEVLEKLGLNGEA 152
Cdd:COG4619 81 QEPAL-WGGTVRDN------------------------------------LPFPFQLRERKFDRERALELLERLGLPPDI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 153 ---ELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIET----ILWLEKFLKDFQGSIVFISHDRSFIRNMATRIID 225
Cdd:COG4619 124 ldkPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLT 203
|
....*.
gi 1437745527 226 LDRGKL 231
Cdd:COG4619 204 LEAGRL 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-231 |
1.01e-27 |
|
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: 111.66 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDA-PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK-EQPLD-----DGQVVYEQDLVTARLQ---- 72
Cdd:COG1122 1 IELENLSFSYPGGtPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGlLKPTSgevlvDGKDITKKNLRELRRKvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 73 -QDPprD---IEGTIFDFVAQGVaedaqyitEYHRVSKvietdpseknlnrlaqlQEVldnrnlwllDSRIAEVLEKLGL 148
Cdd:COG1122 81 fQNP--DdqlFAPTVEEDVAFGP--------ENLGLPR-----------------EEI---------RERVEEALELVGL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 149 NGEAELS--SLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG---SIVFISHDRSFIRNMATRI 223
Cdd:COG1122 125 EHLADRPphELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRV 204
|
....*...
gi 1437745527 224 IDLDRGKL 231
Cdd:COG1122 205 IVLDDGRI 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-496 |
1.36e-27 |
|
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: 109.45 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKL------EVAyfdQHRAT 393
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILlDGKDLaslspkELA---RKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 394 LdpdKTVMDnlaegkqevmvngrprhVLGyLQDFlfppkrAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03214 78 V---PQALE-----------------LLG-LAHL------ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180
....*....|....*....|....*..
gi 1437745527 474 ETLELLEELVDAY----QGTVLLVSHD 496
Cdd:cd03214 131 AHQIELLELLRRLarerGKTVVMVLHD 157
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-511 |
3.16e-27 |
|
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: 107.72 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklevaYFDQHRATLDPDKTV 400
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI---------LIDGKDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 401 MDNLAegkqevmvngrprhvlgylqdFLFppkramtpvrALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd00267 72 RRRIG---------------------YVP----------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....
gi 1437745527 481 ELVDAYQG---TVLLVSHDREFVDNSVTECWIFE 511
Cdd:cd00267 121 ELLRELAEegrTVIIVTHDPELAELAADRVIVLK 154
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
292-501 |
8.67e-27 |
|
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: 115.25 E-value: 8.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 292 RVERSERR--EVLG---SARMQVEEATRSGKIVFELEDVN--YSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKL 364
Cdd:COG4987 301 RVRAAARRlnELLDappAVTEPAEPAPAPGGPSLELEDVSfrYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 365 MLGDLKADSGRIHC-GTKLE----------VAYFDQhratlDP---DKTVMDNLAEGKQEV----MvngrpRHVLG--YL 424
Cdd:COG4987 381 LLRFLDPQSGSITLgGVDLRdldeddlrrrIAVVPQ-----RPhlfDTTLRENLRLARPDAtdeeL-----WAALErvGL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 425 QDFLF-PPKRAMTPV----RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQG--TVLLVSHDR 497
Cdd:COG4987 451 GDWLAaLPDGLDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRL 530
|
....
gi 1437745527 498 EFVD 501
Cdd:COG4987 531 AGLE 534
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
310-502 |
8.72e-27 |
|
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: 114.86 E-value: 8.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 310 EEATRSGKIVFELEDVNYSIGTRR-LVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKLE---- 383
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILiNGVDLSdldp 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 384 ------VAYFDQHrATLdPDKTVMDNLAEGK-----QEVmvngrpRHVLG--YLQDFLfppkRAM-----TPV----RAL 441
Cdd:COG4988 407 aswrrqIAWVPQN-PYL-FAGTIRENLRLGRpdasdEEL------EAALEaaGLDEFV----AALpdgldTPLgeggRGL 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAY-QG-TVLLVSHDREFVDN 502
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaKGrTVILITHRLALLAQ 537
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
321-501 |
1.25e-26 |
|
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: 106.71 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklevaYFDQHRATLDPDKTv 400
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEI---------KVLGKDIKKEPEEV- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 401 mdnlaegkqevmvngrpRHVLGYL-QDFLFPPKraMTpVR---ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL 476
Cdd:cd03230 72 -----------------KRRIGYLpEEPSLYEN--LT-VRenlKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESR 131
|
170 180
....*....|....*....|....*...
gi 1437745527 477 ELLEELVDAY---QGTVLLVSHDREFVD 501
Cdd:cd03230 132 REFWELLRELkkeGKTILLSSHILEEAE 159
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-496 |
1.95e-26 |
|
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: 108.59 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 319 VFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKLE----------VAYF 387
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLlDGRDLAslsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 388 DQHRaTLDPDKTVMDnlaegkqeVMVNGRPRHvlgylQDFLFPPK--------RAMT----------PVRALSGGERNRL 449
Cdd:COG1120 81 PQEP-PAPFGLTVRE--------LVALGRYPH-----LGLFGRPSaedreaveEALErtglehladrPVDELSGGERQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745527 450 LLARLFLKPSNLLILDEPTNDLDVetlelleelvdAYQ---------------GTVLLVSHD 496
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDL-----------AHQlevlellrrlarergRTVVMVLHD 197
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-230 |
2.85e-26 |
|
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: 105.02 E-value: 2.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 5 SLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYeqdlvtarlqqdpprdiegtif 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 85 dfvaqgvaedaqyiteyhrvskvietdpseknlnrlaqlqevlDNRNLWLLDSRiaEVLEKLGLngeaeLSSLSGGWLRK 164
Cdd:cd00267 59 -------------------------------------------DGKDIAKLPLE--ELRRRIGY-----VPQLSGGQRQR 88
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 165 AALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG---SIVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:cd00267 89 VALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
317-590 |
4.12e-26 |
|
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: 112.72 E-value: 4.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 317 KIVFELEDVNYSIGTRRLV-RDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQhRATLD 395
Cdd:TIGR03719 2 QYIYTMNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQ-EPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 396 PDKTVMDNLAEGKQEVmvngrpRHVL------------------------GYLQDFL--------------------FPP 431
Cdd:TIGR03719 81 PTKTVRENVEEGVAEI------KDALdrfneisakyaepdadfdklaaeqAELQEIIdaadawdldsqleiamdalrCPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 432 KRAmtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQGTVLLVSHDREFVDNsVTEcWIFE 511
Cdd:TIGR03719 155 WDA--DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDN-VAG-WILE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 512 ---GDGVinSYVGGY---YDAQQQRaqsvsLKNEAnKSRNAPEKT-EKETKPKQNAKKATRSNNKlsyhlireleqlpAK 584
Cdd:TIGR03719 231 ldrGRGI--PWEGNYsswLEQKQKR-----LEQEE-KEESARQKTlKRELEWVRQSPKGRQAKSK-------------AR 289
|
....*.
gi 1437745527 585 LERLEE 590
Cdd:TIGR03719 290 LARYEE 295
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-231 |
7.29e-26 |
|
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: 104.40 E-value: 7.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVvyeqdlvtarlqqdpprdiegTIFDFVAQGVA 92
Cdd:cd03230 10 YGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEI---------------------KVLGKDIKKEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 93 EDAQyiteyHRVSKVIETDPSEKNLNrlaqlqeVLDNrnlwlLDsriaevleklglngeaelssLSGGWLRKAALGRALV 172
Cdd:cd03230 69 EEVK-----RRIGYLPEEPSLYENLT-------VREN-----LK--------------------LSGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745527 173 SAPKVLFLDEPTNHLDIETILWLEKFLKDF---QGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
321-496 |
1.69e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 105.53 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKLE---------VAYFDQH 390
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVArdpaevrrrIGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 391 rATLDPDKTVMDNL---AE--GKQEVMVNGRPRHVLGYLQdfLfpPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:COG1131 82 -PALYPDLTVRENLrffARlyGLPRKEARERIDELLELFG--L--TDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190
....*....|....*....|....*....|....
gi 1437745527 466 EPTNDLDVETLELLEELVDAY--QG-TVLLVSHD 496
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELaaEGkTVLLSTHY 190
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-231 |
3.24e-25 |
|
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: 104.51 E-value: 3.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLVTARLQQDPPRdieGTIFDFVAQgvaeda 95
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgKDLLKLSRRLRKIR---RKEIQMVFQ------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 96 qyiteyhrvskvietDPSEkNLNRL----AQLQEVL----DNRNLWLLDSRIAEVLEKLGLNgEAELSS----LSGGWLR 163
Cdd:cd03257 90 ---------------DPMS-SLNPRmtigEQIAEPLrihgKLSKKEARKEAVLLLLVGVGLP-EEVLNRypheLSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745527 164 KAALGRALVSAPKVLFLDEPTNHLDIET---ILWLEKFLKD-FQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVqaqILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-231 |
7.87e-25 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 103.29 E-value: 7.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARlqqdPPRDIegtifdfVAQGVAEDAQYI 98
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL----PPHEI-------ARLGIGRTFQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 99 TEYHRVSkVIEtdpsekNLnRLAQLqevLDNRNLWLLDS----------RIAEVLEKLGLNGEAEL--SSLSGGWLRKAA 166
Cdd:cd03219 85 RLFPELT-VLE------NV-MVAAQ---ARTGSGLLLARarreereareRAEELLERVGLADLADRpaGELSYGQQRRLE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 167 LGRALVSAPKVLFLDEPT---NHLDIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03219 154 IARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
330-535 |
1.12e-24 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 109.10 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 330 GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQHRATLdpDKTVMDNLAEGKQ 409
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPAL--PQPALEYVIDGDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 410 E--------------------VMVNG----------RPR-----HVLGYLQDFLfppkraMTPVRALSGGERNRLLLARL 454
Cdd:PRK10636 90 EyrqleaqlhdanerndghaiATIHGkldaidawtiRSRaasllHGLGFSNEQL------ERPVSDFSGGWRMRLNLAQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 455 FLKPSNLLILDEPTNDLDVETLELLEELVDAYQGTVLLVSHDREFVDNSVTECWIFEGDgVINSYVGGYYDAQQQRAQSV 534
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQ-SLFEYTGNYSSFEVQRATRL 242
|
.
gi 1437745527 535 S 535
Cdd:PRK10636 243 A 243
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-231 |
1.51e-24 |
|
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: 101.83 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARlqqdPP--RDIeG 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV----PPerRNI-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 82 TIFDFVA----QGVAEDAQYITEYHRVSKvietdpseknlnrlAQLQEvldnrnlwlldsRIAEVLEKLGLNGEAEL--S 155
Cdd:cd03259 76 MVFQDYAlfphLTVAENIAFGLKLRGVPK--------------AEIRA------------RVRELLELVGLEGLLNRypH 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 156 SLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGS----IVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03259 130 ELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRElgitTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-231 |
1.66e-24 |
|
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: 100.97 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 5 SLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQV-VYEQDLvtarlQQDPPRDIegti 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlLDGKDL-----ASLSPKEL---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 84 fdfvAQGVAedaqyiteYhrvskvietdpseknlnrLAQlqevldnrnlwlldsriaeVLEKLGLNGEAE--LSSLSGGW 161
Cdd:cd03214 72 ----ARKIA--------Y------------------VPQ-------------------ALELLGLAHLADrpFNELSGGE 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 162 LRKAALGRALVSAPKVLFLDEPTNHLDI----ETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03214 103 RQRVLLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
315-502 |
2.28e-24 |
|
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: 108.38 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 315 SGKIvfELEDVN--YSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklevaYFDQH-R 391
Cdd:COG2274 471 KGDI--ELENVSfrYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI---------LIDGIdL 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 392 ATLDPDK-----------------TVMDNLAEGKQEV----------MVNgrprhvlgyLQDFLfppkRAM-----TPV- 438
Cdd:COG2274 540 RQIDPASlrrqigvvlqdvflfsgTIRENITLGDPDAtdeeiieaarLAG---------LHDFI----EALpmgydTVVg 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 439 ---RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQG--TVLLVSHDREFVDN 502
Cdd:COG2274 607 eggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL 675
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
19-231 |
3.16e-24 |
|
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: 102.42 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARlqqdPPRDIegtifdfVAQGVAEDAQYI 98
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGL----PPHRI-------ARLGIARTFQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 99 TEYHRVSkVIEtdpsekN--LNRLAQLQEVLDNRNLWL---------LDSRIAEVLEKLGLNGEAEL--SSLSGGWLRKA 165
Cdd:COG0411 89 RLFPELT-VLE------NvlVAAHARLGRGLLAALLRLprarreereARERAEELLERVGLADRADEpaGNLSYGQQRRL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 166 ALGRALVSAPKVLFLDEPT---NHLDIETILWLEKFLKDFQG-SIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:COG0411 162 EIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-250 |
7.63e-24 |
|
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: 100.65 E-value: 7.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE----QDLVTARLQQDPPRdi 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgediSGLSEAELYRLRRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 80 egtiFDFVAQG--------VAEDAQYITEYHRvskvietdpseknlnrlaQLQEvldnrnlWLLDSRIAEVLEKLGLNGE 151
Cdd:cd03261 79 ----MGMLFQSgalfdsltVFENVAFPLREHT------------------RLSE-------EEIREIVLEKLEAVGLRGA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 152 AEL--SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLD-------IETILWLEKFLkdfQGSIVFISHDRSFIRNMATR 222
Cdd:cd03261 130 EDLypAELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKEL---GLTSIMVTHDLDTAFAIADR 206
|
250 260
....*....|....*....|....*...
gi 1437745527 223 IIDLDRGKLsSWPGNYDKYLESKEEALR 250
Cdd:cd03261 207 IAVLYDGKI-VAEGTPEELRASDDPLVR 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
321-511 |
7.95e-24 |
|
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: 99.85 E-value: 7.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGT--RRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLEVAYFDQHRATL 394
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdlTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 --DPD-----KTVMDNLAEGkqevMVN-GRPRH-----VLGYLQDFLFPPKRAmTPVRALSGGERNRLLLAR-LFLKPsN 460
Cdd:cd03225 81 fqNPDdqffgPTVEEEVAFG----LENlGLPEEeieerVEEALELVGLEGLRD-RSPFTLSGGQKQRVAIAGvLAMDP-D 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 461 LLILDEPTNDLDVETLELLEELVDAYQG---TVLLVSHDREFVDNSVTECWIFE 511
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLE 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-231 |
9.88e-24 |
|
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: 105.37 E-value: 9.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLVTA----------RLQ---QDP-----PRDi 79
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgKDLTKLsrrslrelrrRVQmvfQDPysslnPRM- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 80 egTIFDFVAQGvaedaqyITEYHRVSKvietdpseknlnrlAQLQEvldnrnlwlldsRIAEVLEKLGLNGEAEL---SS 156
Cdd:COG1123 360 --TVGDIIAEP-------LRLHGLLSR--------------AERRE------------RVAELLERVGLPPDLADrypHE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 157 LSGGWLRKAALGRALVSAPKVLFLDEPTNHLDI---ETILwleKFLKDFQ----GSIVFISHDRSFIRNMATRIIDLDRG 229
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVsvqAQIL---NLLRDLQrelgLTYLFISHDLAVVRYIADRVAVMYDG 481
|
..
gi 1437745527 230 KL 231
Cdd:COG1123 482 RI 483
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
320-512 |
9.93e-24 |
|
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: 100.10 E-value: 9.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 320 FELEDVNYSI-GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKLEVAYFDQHRATL--- 394
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvDGKDITKKNLRELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 --DPD-----KTVMD-------NLAEGKQEVmvNGRPRHVLGY--LQDFLfppKRamtPVRALSGGERNRLLLAR-LFLK 457
Cdd:COG1122 81 fqNPDdqlfaPTVEEdvafgpeNLGLPREEI--RERVEEALELvgLEHLA---DR---PPHELSGGQKQRVAIAGvLAME 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 458 PSnLLILDEPTNDLDVETLELLEELVDAYQG---TVLLVSHDREFVDNSVTECWIFEG 512
Cdd:COG1122 153 PE-VLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-256 |
1.15e-23 |
|
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: 106.07 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 14 SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVY-EQDLvtarlQQDPPRDI------------- 79
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdGIDL-----RQIDPASLrrqigvvlqdvfl 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 80 -EGTIFDFVAQGvaedAQYITEyHRVSKVIetdpseknlnRLAQLQEVLDNrnlwL---LDSRIAEvleklglNGeaelS 155
Cdd:COG2274 561 fSGTIRENITLG----DPDATD-EEIIEAA----------RLAGLHDFIEA----LpmgYDTVVGE-------GG----S 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 156 SLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETilwlEKFLKD-----FQG-SIVFISHDRSFIRNmATRIIDLDRG 229
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAET----EAIILEnlrrlLKGrTVIIIAHRLSTIRL-ADRIIVLDKG 685
|
250 260
....*....|....*....|....*..
gi 1437745527 230 KLSSwPGNYDKYLESKEEALRVEEQQN 256
Cdd:COG2274 686 RIVE-DGTHEELLARKGLYAELVQQQL 711
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
280-498 |
2.53e-23 |
|
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: 104.29 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 280 RNEGRVRALKALRVERSERREVLGSARMqveEATRSGKIVFELEDVNYSiGTRRLVRDFSAKVQRGDKIALVGPNGCGKT 359
Cdd:TIGR02857 287 RADGVAAAEALFAVLDAAPRPLAGKAPV---TAAPASSLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKS 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 360 TLLKLMLGDLKADSGRIHC-GTKL----------EVAYFDQHrATLdPDKTVMDNLAEGKQEV---MVNGRPRHVlgYLQ 425
Cdd:TIGR02857 363 TLLNLLLGFVDPTEGSIAVnGVPLadadadswrdQIAWVPQH-PFL-FAGTIAENIRLARPDAsdaEIREALERA--GLD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 426 DFLFP-PKRAMTPV----RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAY-QG-TVLLVSHDRE 498
Cdd:TIGR02857 439 EFVAAlPQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaQGrTVLLVTHRLA 518
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-473 |
2.99e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.56 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEqdlvTARLQQDPPRDIE 80
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD----GEPVRFRSPRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 gtifdfvAQGVAedaqyiteyhrvskVIetdPSEKNLnrLAQLqEVLDN-------RNLWLLD-----SRIAEVLEKLGL 148
Cdd:COG1129 78 -------AAGIA--------------II---HQELNL--VPNL-SVAENiflgrepRRGGLIDwramrRRARELLARLGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 149 --NGEAELSSLSGGwlRKA--ALGRALVSAPKVLFLDEPT---NHLDIETILWLEKFLKDfQG-SIVFISHDRSFIRNMA 220
Cdd:COG1129 131 diDPDTPVGDLSVA--QQQlvEIARALSRDARVLILDEPTaslTEREVERLFRIIRRLKA-QGvAIIYISHRLDEVFEIA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 221 TRIIDLDRGKLsswpgnydkyleskeealrVEEQQNAEFDrklaqEEAWIRQ--GikarrtrnegrvRALKALRVERser 298
Cdd:COG1129 208 DRVTVLRDGRL-------------------VGTGPVAELT-----EDELVRLmvG------------RELEDLFPKR--- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 299 revlgsarmqveeATRSGKIVFELEDVNysigTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH- 377
Cdd:COG1129 249 -------------AAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRl 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 378 CGTKLE-----------VAYF--DQHRATLDPDKTVMDNLAEGKQEVMVNGRP-------RHVLGYLQDFLFPPKRAMTP 437
Cdd:COG1129 312 DGKPVRirsprdairagIAYVpeDRKGEGLVLDLSIRENITLASLDRLSRGGLldrrrerALAEEYIKRLRIKTPSPEQP 391
|
490 500 510
....*....|....*....|....*....|....*..
gi 1437745527 438 VRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG1129 392 VGNLSGGNQQKVVLAKwLATDPK-VLILDEPTRGIDV 427
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-250 |
3.80e-23 |
|
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: 98.51 E-value: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLVTARLQQ--DPPRD 78
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDgQDITGLSEKElyELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 79 I-----EGTIFDF--VAQGVAedaQYITEYHRVSKvietdpseknlnrlAQLQEvldnrnlwlldsRIAEVLEKLGLNGE 151
Cdd:COG1127 84 IgmlfqGGALFDSltVFENVA---FPLREHTDLSE--------------AEIRE------------LVLEKLELVGLPGA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 152 AEL--SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIET---ILWLEKFLKD-FQGSIVFISHDRSFIRNMATRIID 225
Cdd:COG1127 135 ADKmpSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITsavIDELIRELRDeLGLTSVVVTHDLDSAFAIADRVAV 214
|
250 260
....*....|....*....|....*
gi 1437745527 226 LDRGKLsSWPGNYDKYLESKEEALR 250
Cdd:COG1127 215 LADGKI-IAEGTPEELLASDDPWVR 238
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-230 |
4.64e-23 |
|
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: 96.49 E-value: 4.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLVTARLQQDPPRDIEGTIFdfvaqgv 91
Cdd:cd03229 10 YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgEDLTDLEDELPPLRRRIGMVF------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 92 aedaqyiteyhrvskvietdpseknlnrlaqlQEVLDNRNLwlldsriaEVLEKLGLngeaelsSLSGGWLRKAALGRAL 171
Cdd:cd03229 83 --------------------------------QDFALFPHL--------TVLENIAL-------GLSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 172 VSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGS----IVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgitVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
321-496 |
5.30e-23 |
|
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: 97.96 E-value: 5.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTR----RLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKL------------- 382
Cdd:cd03257 3 EVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfDGKDLlklsrrlrkirrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 383 EVAYFDQH-RATLDPDKTVMDNLAEG--KQEVMVNGRPRHVLGYLQDFLFP-PKRAMT--PvRALSGGERNRLLLAR-LF 455
Cdd:cd03257 83 EIQMVFQDpMSSLNPRMTIGEQIAEPlrIHGKLSKKEARKEAVLLLLVGVGlPEEVLNryP-HELSGGQRQRVAIARaLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1437745527 456 LKPSnLLILDEPTNDLDVETLELL----EELVDAYQGTVLLVSHD 496
Cdd:cd03257 162 LNPK-LLIADEPTSALDVSVQAQIldllKKLQEELGLTLLFITHD 205
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
317-513 |
7.45e-23 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 102.89 E-value: 7.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 317 KIVFELEDVNYSIGTRRLV-RDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQhRATLD 395
Cdd:PRK11819 4 QYIYTMNRVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ-EPQLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 396 PDKTVMDNLAEGKQEVM--------VN---GRPRHVL-------GYLQDFL--------------------FPPKRAmtP 437
Cdd:PRK11819 83 PEKTVRENVEEGVAEVKaaldrfneIYaayAEPDADFdalaaeqGELQEIIdaadawdldsqleiamdalrCPPWDA--K 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 438 VRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQGTVLLVSHDREFVDNsVTEcWIFEGD 513
Cdd:PRK11819 161 VTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDN-VAG-WILELD 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-185 |
1.04e-22 |
|
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: 94.64 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDIegtifdfvaqgvaedaQYI 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEI----------------GYV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 99 TEYHRVskvietDPSEKNLNRLAQLQEVLDNRNLWlLDSRIAEVLEKLGLNGEAE------LSSLSGGWLRKAALGRALV 172
Cdd:pfam00005 65 FQDPQL------FPRLTVRENLRLGLLLKGLSKRE-KDARAEEALEKLGLGDLADrpvgerPGTLSGGQRQRVAIARALL 137
|
170
....*....|...
gi 1437745527 173 SAPKVLFLDEPTN 185
Cdd:pfam00005 138 TKPKLLLLDEPTA 150
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-500 |
1.92e-22 |
|
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: 94.95 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 320 FELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGtklevayfdqhratldpDKT 399
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-----------------GED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 400 VMDNLAEGKQEvmvngrpRHVLGYL-QDF-LFPPKRAMTPVR-ALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDVET 475
Cdd:cd03229 64 LTDLEDELPPL-------RRRIGMVfQDFaLFPHLTVLENIAlGLSGGQQQRVALARaLAMDP-DVLLLDEPTSALDPIT 135
|
170 180
....*....|....*....|....*....
gi 1437745527 476 LELLEELV----DAYQGTVLLVSHDREFV 500
Cdd:cd03229 136 RREVRALLkslqAQLGITVVLVTHDLDEA 164
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-231 |
3.21e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 98.63 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARlqqdPP--RD 78
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL----PPekRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 79 IeGTIF-DF-------VAQGVAedaqYITEYHRVSKvietdpseknlnrlAQLQEvldnrnlwlldsRIAEVLEKLGLNG 150
Cdd:COG3842 79 V-GMVFqDYalfphltVAENVA----FGLRMRGVPK--------------AEIRA------------RVAELLELVGLEG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 151 EAEL--SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLD----IETILWLEKFLKDFQGSIVFISHDRS--FIrnMATR 222
Cdd:COG3842 128 LADRypHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQEeaLA--LADR 205
|
....*....
gi 1437745527 223 IIDLDRGKL 231
Cdd:COG3842 206 IAVMNDGRI 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
321-502 |
3.63e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 95.50 E-value: 3.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLV-RDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKL------EVAY------ 386
Cdd:COG2884 3 RFENVSKRYPGGREAlSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvNGQDLsrlkrrEIPYlrrrig 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 387 --FDQHRatLDPDKTVMDNLA-----EGKQEVMVNGRPRHVLGY--LQDflfppkRAMTPVRALSGGERNRLLLARLFL- 456
Cdd:COG2884 83 vvFQDFR--LLPDRTVYENVAlplrvTGKSRKEIRRRVREVLDLvgLSD------KAKALPHELSGGEQQRVAIARALVn 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 457 KPSnLLILDEPTNDLDvetlelleelvDAY-------------QG-TVLLVSHDREFVDN 502
Cdd:COG2884 155 RPE-LLLADEPTGNLD-----------PETsweimelleeinrRGtTVLIATHDLELVDR 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-502 |
6.20e-22 |
|
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: 99.88 E-value: 6.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 12 AFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVL--AKEQPLDDGQVVYEQDLVTARLQQDPPRDI-------EGT 82
Cdd:TIGR03269 9 KFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHVALCEKCGYVERPSKVgepcpvcGGT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 83 IFDFVAQGVAEDAqyiTEYHRVSKVIETdpsekNLNRLAQL---QEVLDNrnlwlldsrIAEVLEKLGLNGEAELS---- 155
Cdd:TIGR03269 89 LEPEEVDFWNLSD---KLRRRIRKRIAI-----MLQRTFALygdDTVLDN---------VLEALEEIGYEGKEAVGravd 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 156 ----------------SLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILW----LEKFLKDFQGSIVFISHDRSF 215
Cdd:TIGR03269 152 liemvqlshrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 216 IRNMATRIIDLDRGKLSSwPGNYD----KYLESKEEalrveeqqnaefdrklaqeeawirqgikarrtrnegrvralkal 291
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKE-EGTPDevvaVFMEGVSE-------------------------------------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 292 rVERSERREVlgsarmqveeatrsGKIVFELEDVN---YSI--GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLML 366
Cdd:TIGR03269 267 -VEKECEVEV--------------GEPIIKVRNVSkryISVdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIA 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 367 GDLKADSGRIHCG--------TKLEVayFDQHRAT-----------LDPDKTVMDNLAE--GKQEVMVNGRPRHVLgYLQ 425
Cdd:TIGR03269 332 GVLEPTSGEVNVRvgdewvdmTKPGP--DGRGRAKryigilhqeydLYPHRTVLDNLTEaiGLELPDELARMKAVI-TLK 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 426 DFLFPPKRAMTPVR----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLD----VETLELLEELVDAYQGTVLLVSHDR 497
Cdd:TIGR03269 409 MVGFDEEKAEEILDkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDM 488
|
....*
gi 1437745527 498 EFVDN 502
Cdd:TIGR03269 489 DFVLD 493
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
327-496 |
8.30e-22 |
|
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: 94.11 E-value: 8.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 327 YSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----------TKLEVAYFDQHRaTLDP 396
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgysirtdrkaARQSLGYCPQFD-ALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 397 DKTVMDNL---AegkqevMVNGRPRH-----VLGYLQDFLFPPKRAmTPVRALSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:cd03263 89 ELTVREHLrfyA------RLKGLPKSeikeeVELLLRVLGLTDKAN-KRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190
....*....|....*....|....*....|
gi 1437745527 469 NDLDVETLELLEELVDAYQG--TVLLVSHD 496
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-230 |
1.15e-21 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 94.77 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVY---EQ-------DL---- 66
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgERrggedvwELrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 67 --VTARLQQDPPRDIegTIFDFVAQGvAEDAqyITEYHRVSKvietdpseknlnrlAQLQevldnrnlwlldsRIAEVLE 144
Cdd:COG1119 81 glVSPALQLRFPRDE--TVLDVVLSG-FFDS--IGLYREPTD--------------EQRE-------------RARELLE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 145 KLGLNGEAE--LSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDI---ETIL-WLEKFLKDFQGSIVFISHDRSFIRN 218
Cdd:COG1119 129 LLGLAHLADrpFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLgarELLLaLLDKLAAEGAPTLVLVTHHVEEIPP 208
|
250
....*....|..
gi 1437745527 219 MATRIIDLDRGK 230
Cdd:COG1119 209 GITHVLLLKDGR 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-224 |
1.17e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 94.77 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDA----PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTArlqqdPP 76
Cdd:COG1116 5 APALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 77 RDIeGtifdFVAQG--------VAEDAQYITEYHRVSKvietdpseknlnrlAQLQEvldnrnlwlldsRIAEVLEKLGL 148
Cdd:COG1116 80 PDR-G----VVFQEpallpwltVLDNVALGLELRGVPK--------------AERRE------------RARELLELVGL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 149 NGEAEL--SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETIL----WLEKFLKDFQGSIVFISHDrsfIRN---M 219
Cdd:COG1116 129 AGFEDAypHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRErlqdELLRLWQETGKTVLFVTHD---VDEavfL 205
|
....*
gi 1437745527 220 ATRII 224
Cdd:COG1116 206 ADRVV 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-473 |
1.41e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 99.11 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 34 LVGRNGAGKSTLLRVLAKE-QP-LDDGQVVYEQDLVTAR-----LQqdpprdiegTIFDFVAQG---VAEDAQYIteyHR 103
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGElIPnLGDYEEEPSWDEVLKRfrgteLQ---------NYFKKLYNGeikVVHKPQYV---DL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 104 VSKVIEtdpseknlNRLAQLQEVLDNRNLWLldsriaEVLEKLGLNG--EAELSSLSGGWLRKAALGRALVSAPKVLFLD 181
Cdd:PRK13409 172 IPKVFK--------GKVRELLKKVDERGKLD------EVVERLGLENilDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 182 EPTNHLDIETILWLEKFLKDF-QGSIVF-ISHDRSfIRNMATRIIDLDRGKlsswPGNYDKYleSKEEALRVeeQQNAEF 259
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELaEGKYVLvVEHDLA-VLDYLADNVHIAYGE----PGAYGVV--SKPKGVRV--GINEYL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 260 DRKLAQEEAWIRQgikarrtrnegrvralKALRVE-RSERREVlgsarmqveeatrSGKIVFELEDVNYSIGTRRLVRDf 338
Cdd:PRK13409 309 KGYLPEENMRIRP----------------EPIEFEeRPPRDES-------------ERETLVEYPDLTKKLGDFSLEVE- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 339 SAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcGTKLEVAYFDQHRATlDPDKTVMDNLAEGKQEVMVNgrpr 418
Cdd:PRK13409 359 GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYIKP-DYDGTVEDLLRSITDDLGSS---- 431
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 419 hvlgYLQDFLFPP---KRAMT-PVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13409 432 ----YYKSEIIKPlqlERLLDkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
321-502 |
1.42e-21 |
|
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: 94.15 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI-HCG---------TKLEVAYFDQH 390
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlIDGedvrkepreARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 391 RAtLDPDKTVMDNL---AEGKQEVMVNGRPRhVLGYLQDFLFPPKRAmTPVRALSGGERNRLLLARLFLKPSNLLILDEP 467
Cdd:COG4555 83 RG-LYDRLTVRENIryfAELYGLFDEELKKR-IEELIELLGLEEFLD-RRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1437745527 468 TNDLDVETLELLEELVDAY--QG-TVLLVSHDREFVDN 502
Cdd:COG4555 160 TNGLDVMARRLLREILRALkkEGkTVLFSSHIMQEVEA 197
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-231 |
1.46e-21 |
|
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: 93.05 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYeqdlvtarLQQDPPRDIE-----GTIFDfv 87
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF--------DGKSYQKNIEalrriGALIE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 88 AQGVAEdaqYITeyhrvskvietdpSEKNLNRLAQLqevldnrnLWLLDSRIAEVLEKLGLNGEAEL--SSLSGGWLRKA 165
Cdd:cd03268 80 APGFYP---NLT-------------ARENLRLLARL--------LGIRKKRIDEVLDVVGLKDSAKKkvKGFSLGMKQRL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 166 ALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QGSIVFI-SHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03268 136 GIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLrdQGITVLIsSHLLSEIQKVADRIGIINKGKL 204
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
330-500 |
1.73e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.30 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 330 GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQHRAtlDPDK---TVMDNLAE 406
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSE--VPDSlplTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 407 GK-QEVMVNGRPRHV-----------LGyLQDFLfppKRamtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
Cdd:NF040873 81 GRwARRGLWRRLTRDdraavddalerVG-LADLA---GR---QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180
....*....|....*....|....*....
gi 1437745527 475 TLELLEELVDAYQG---TVLLVSHDREFV 500
Cdd:NF040873 154 SRERIIALLAEEHArgaTVVVVTHDLELV 182
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
321-499 |
3.43e-21 |
|
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: 91.93 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIG-TRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI-------HCGTKLEVAYFdqhrA 392
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpiKAKERRKSIGY----V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 393 TLDPD-----KTVMDNLAEGKQEvmVNGRPRHVLGYLQDF-LFPPKRAMtPvRALSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:cd03226 77 MQDVDyqlftDSVREELLLGLKE--LDAGNEQAETVLKDLdLYALKERH-P-LSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1437745527 467 PTNDLDVETLELLEELVD--AYQG-TVLLVSHDREF 499
Cdd:cd03226 153 PTSGLDYKNMERVGELIRelAAQGkAVIVITHDYEF 188
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
19-231 |
3.97e-21 |
|
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: 91.87 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVcLVGRNGAGKSTLLRVLAKEQPLDDGQVvyEQDLVTARLQQDPPRDIEGtifdFVAQGVAEDAQYi 98
Cdd:cd03264 16 LDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTI--RIDGQDVLKQPQKLRRRIG----YLPQEFGVYPNF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 99 teyhrvskvietdPSEKNLNRLAQLQEVLDNRnlwlLDSRIAEVLEKLGLNGEAE--LSSLSGGWLRKAALGRALVSAPK 176
Cdd:cd03264 88 -------------TVREFLDYIAWLKGIPSKE----VKARVDEVLELVNLGDRAKkkIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 177 VLFLDEPTNHLDIETILWLEKFLKDF-QGSIVFIS-HDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELgEDRIVILStHIVEDVESLCNQVAVLNKGKL 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-231 |
4.17e-21 |
|
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: 97.53 E-value: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDA--PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVY---------EQDL--VT 68
Cdd:COG4987 332 PSLELEDVSFRYPGAgrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLggvdlrdldEDDLrrRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 69 ARLQQDPPrdiegtIFDfvaQGVAEdaqyiteyhrvskvietdpsekNLnRLA-------QLQEVLDnrnlwllDSRIAE 141
Cdd:COG4987 412 AVVPQRPH------LFD---TTLRE----------------------NL-RLArpdatdeELWAALE-------RVGLGD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 142 VLEKL--GLN---GEAElSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETIlwlEKFLKDFQG-----SIVFISH 211
Cdd:COG4987 453 WLAALpdGLDtwlGEGG-RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATE---QALLADLLEalagrTVLLITH 528
|
250 260
....*....|....*....|
gi 1437745527 212 DRSFIRNMaTRIIDLDRGKL 231
Cdd:COG4987 529 RLAGLERM-DRILVLEDGRI 547
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-231 |
4.28e-21 |
|
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: 97.52 E-value: 4.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 15 DAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQV-VYEQDLVTARLQ----------QDPpRDIEGTI 83
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlINGVDLSDLDPAswrrqiawvpQNP-YLFAGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 84 FDFVAQGvAEDAqyiteyhrvskvieTDpseknlnrlAQLQEVLDnrnlwllDSRIAEVLEKL--GLN---GEAElSSLS 158
Cdd:COG4988 428 RENLRLG-RPDA--------------SD---------EELEAALE-------AAGLDEFVAALpdGLDtplGEGG-RGLS 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 159 GGWLRKAALGRALVSAPKVLFLDEPTNHLDIETilwlEKFLKD-----FQGSIV-FISHDRSFIRNmATRIIDLDRGKL 231
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAET----EAEILQalrrlAKGRTViLITHRLALLAQ-ADRILVLDDGRI 549
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
17-231 |
4.99e-21 |
|
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: 91.78 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLVT---ARLQQDPPRDIeGTIFDFvaqgva 92
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgTDISKlseKELAAFRRRHI-GFVFQS------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 93 edaqyiteYHRvskvietdpseknLNRLAQLQEV-----LDNRNLWLLDSRIAEVLEKLGLNGEAEL--SSLSGGWLRKA 165
Cdd:cd03255 91 --------FNL-------------LPDLTALENVelpllLAGVPKKERRERAEELLERVGLGDRLNHypSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 166 ALGRALVSAPKVLFLDEPTNHLDIET---IL-WLEKFLKDFQGSIVFISHDRSFIRnMATRIIDLDRGKL 231
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETgkeVMeLLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-230 |
5.57e-21 |
|
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: 90.52 E-value: 5.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 14 SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQV-VYEQDLvtarlqqdppRDIEgtifdfvaqgva 92
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlIDGVDL----------RDLD------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 93 edaqyITEYHRVSKVIETDPseknlnrlaqlqevldnrnlWLLDSRIAEVLeklglngeaelssLSGGWLRKAALGRALV 172
Cdd:cd03228 71 -----LESLRKNIAYVPQDP--------------------FLFSGTIRENI-------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 173 SAPKVLFLDEPTNHLDIET-ILWLEKFLKDFQG-SIVFISHDRSFIRnMATRIIDLDRGK 230
Cdd:cd03228 113 RDPPILILDEATSALDPETeALILEALRALAKGkTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-473 |
5.91e-21 |
|
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: 96.68 E-value: 5.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDA----PLLDNTDLFIDENERVCLVGRNGAGKS----TLLRVLAKEQPLDDGQVVYE-QDLVTA-- 69
Cdd:COG4172 4 MPLLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDgQDLLGLse 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 70 -RLQQDPPRDIeGTIFdfvaqgvaedaQyiteyhrvskvietDP--SeknLNRL----AQLQEVL------DNRNLWlld 136
Cdd:COG4172 84 rELRRIRGNRI-AMIF-----------Q--------------EPmtS---LNPLhtigKQIAEVLrlhrglSGAAAR--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 137 SRIAEVLEKLGL-NGEAELSS----LSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIET---ILWLekfLKDFQG---- 204
Cdd:COG4172 132 ARALELLERVGIpDPERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVqaqILDL---LKDLQRelgm 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 205 SIVFISHDRSFIRNMATRIIDLDRGKLsswpgnydkyleskeealrVEEQQNAE-FDrklAQEEAWIRQGIKARRTRNEG 283
Cdd:COG4172 209 ALLLITHDLGVVRRFADRVAVMRQGEI-------------------VEQGPTAElFA---APQHPYTRKLLAAEPRGDPR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 284 RVRAlkalrversERREVLGSARMQVEEATRSG---KIVFELedvnysigtrRLVRDFSAKVQRGDKIALVGPNGCGKTT 360
Cdd:COG4172 267 PVPP---------DAPPLLEARDLKVWFPIKRGlfrRTVGHV----------KAVDGVSLTLRRGETLGLVGESGSGKST 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 361 LLKLMLGdLKADSGRIH-CGTKLEVAYFDQHR--------------ATLDPDKTVMDNLAEG---------KQEvmvngR 416
Cdd:COG4172 328 LGLALLR-LIPSEGEIRfDGQDLDGLSRRALRplrrrmqvvfqdpfGSLSPRMTVGQIIAEGlrvhgpglsAAE-----R 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 417 PRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG4172 402 RARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARaLILEPK-LLVLDEPTSALDV 458
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-233 |
7.33e-21 |
|
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: 91.44 E-value: 7.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 11 LAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQV-VYEQDLVTARL------QQ-DPPRDIEGT 82
Cdd:cd03235 7 VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrVFGKPLEKERKrigyvpQRrSIDRDFPIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 83 IFDFVAQGVAedaQYITEYHRVSKvietdpSEKnlnrlaqlqevldnrnlwlldSRIAEVLEKLGLNGEAE--LSSLSGG 160
Cdd:cd03235 87 VRDVVLMGLY---GHKGLFRRLSK------ADK---------------------AKVDEALERVGLSELADrqIGELSGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 161 WLRKAALGRALVSAPKVLFLDEPTNHLDIET---ILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLSS 233
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTqedIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
321-472 |
7.39e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.72 E-value: 7.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKLE------------VAYF 387
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlCGEPVPsrarharqrvgvVPQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 388 DQhratLDPDKTVMDNL-AEGKQEVMVNGRPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:PRK13537 89 DN----LDPDFTVRENLlVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
....*.
gi 1437745527 467 PTNDLD 472
Cdd:PRK13537 165 PTTGLD 170
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-231 |
1.07e-20 |
|
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: 91.49 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 14 SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVL-AKEQPlDDGQVVYE-QDLVTA-----RLQQdppRDIeGTIFD- 85
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInGLERP-TSGSVLVDgTDLTLLsgkelRKAR---RRI-GMIFQh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 86 ---FVAQGVAEDAQYITEYHRVSKvietdpseknlnrlaqlQEVldnrnlwllDSRIAEVLEKLGLNGEAEL--SSLSGG 160
Cdd:cd03258 91 fnlLSSRTVFENVALPLEIAGVPK-----------------AEI---------EERVLELLELVGLEDKADAypAQLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 161 WLRKAALGRALVSAPKVLFLDEPTNHLDIET---ILWLekfLKDFQG----SIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETtqsILAL---LRDINRelglTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
321-496 |
1.14e-20 |
|
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: 91.41 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTK--------------LEVAY 386
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 387 FDQHRATLDpDKTVMDNLA------EGKQEVMVNGRPRHVLGY--LQDF--LFPpkramtpvRALSGGERNRLLLAR-LF 455
Cdd:cd03261 82 LFQSGALFD-SLTVFENVAfplrehTRLSEEEIREIVLEKLEAvgLRGAedLYP--------AELSGGMKKRVALARaLA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1437745527 456 LKPSnLLILDEPTNDLDVETLELLEELV----DAYQGTVLLVSHD 496
Cdd:cd03261 153 LDPE-LLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHD 196
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-231 |
1.15e-20 |
|
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: 90.78 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARlqqdPP--RDIeG 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL----PPkdRDI-A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 82 TIFDFVA----QGVAEDAQYITEYHRVSKViETDPSEKNLNRLAQLQEVLDNRNlwlldsriaevleklglngeaelSSL 157
Cdd:cd03301 76 MVFQNYAlyphMTVYDNIAFGLKLRKVPKD-EIDERVREVAELLQIEHLLDRKP-----------------------KQL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 158 SGGWLRKAALGRALVSAPKVLFLDEPTNHLD----IETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03301 132 SGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
321-498 |
1.47e-20 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 90.27 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKL---------EVAYFDQHR 391
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvpperrNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 392 AtLDPDKTVMDNLAEG--KQEVMVNGRPRHVLGYLQDFLFPPKRAMTPvRALSGGERNRLLLAR-LFLKPSnLLILDEPT 468
Cdd:cd03259 82 A-LFPHLTVAENIAFGlkLRGVPKAEIRARVRELLELVGLEGLLNRYP-HELSGGQQQRVALARaLAREPS-LLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|....
gi 1437745527 469 NDLDVETLELLEELVDAYQG----TVLLVSHDRE 498
Cdd:cd03259 159 SALDAKLREELREELKELQRelgiTTIYVTHDQE 192
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-212 |
1.89e-20 |
|
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: 90.22 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDA----PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTAR-------LQ 72
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPgpdrgyvFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 73 QD---PPRdiegTIFDFVAQGVaedaqyitEYHRVSKvietdpseknlnrlAQLQEvldnrnlwlldsRIAEVLEKLGLN 149
Cdd:cd03293 81 QDallPWL----TVLDNVALGL--------ELQGVPK--------------AEARE------------RAEELLELVGLS 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 150 GEAEL--SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETIL----WLEKFLKDFQGSIVFISHD 212
Cdd:cd03293 123 GFENAypHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREqlqeELLDIWRETGKTVLLVTHD 191
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-231 |
2.35e-20 |
|
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: 89.77 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 15 DAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQV-VYEQDLVTARLQQDP--PRDIeGTIF-DF---V 87
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrVNGQDVSDLRGRAIPylRRKI-GVVFqDFrllP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 88 AQGVAEDAQYITEyhrvskVIETDPSEKNlnrlaqlqevldnrnlwlldSRIAEVLEKLGLNGEAEL--SSLSGGWLRKA 165
Cdd:cd03292 92 DRNVYENVAFALE------VTGVPPREIR--------------------KRVPAALELVGLSHKHRAlpAELSGGEQQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 166 ALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQ---GSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
292-496 |
2.49e-20 |
|
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: 94.73 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 292 RVERSERR--EVLGSARMQVE------EATRSGKIVFELEDVNYSI-GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLL 362
Cdd:TIGR02868 299 RVRAAAERivEVLDAAGPVAEgsapaaGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 363 KLMLGDLKADSGRI-----------HCGTKLEVAYFDQhratlDP---DKTVMDNLAEGK-----QEVMVNGRPRHVLGY 423
Cdd:TIGR02868 379 ATLAGLLDPLQGEVtldgvpvssldQDEVRRRVSVCAQ-----DAhlfDTTVRENLRLARpdatdEELWAALERVGLADW 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 424 LQDFlfpPKRAMTPV----RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELV-DAYQG-TVLLVSHD 496
Cdd:TIGR02868 454 LRAL---PDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLlAALSGrTVVLITHH 529
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
320-472 |
3.81e-20 |
|
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: 88.14 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 320 FELEDVNYSIG--TRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklevaYFDQHratldPD 397
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGV-----PV 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 398 KTVMDNLAegKQEVMVNGRPrhvlgylqdFLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03247 67 SDLEKALS--SLISVLNQRP---------YLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-473 |
4.62e-20 |
|
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: 94.47 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 34 LVGRNGAGKSTLLRVLAKE-QP-LDDGQVVYEQDLVTARLQqdpprdieGTI----FDFVAQG---VAEDAQYIteyHRV 104
Cdd:COG1245 104 ILGPNGIGKSTALKILSGElKPnLGDYDEEPSWDEVLKRFR--------GTElqdyFKKLANGeikVAHKPQYV---DLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 105 SKVIETDPSEknlnrlaqLQEVLDNRNLWLldsriaEVLEKLGLNG--EAELSSLSGGWLRKAALGRALVSAPKVLFLDE 182
Cdd:COG1245 173 PKVFKGTVRE--------LLEKVDERGKLD------ELAEKLGLENilDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 183 PTNHLDIETILWLEKFLKDFQG---SIVFISHDRSfIRNMATRIIDLDRGKlsswPGNY-------------DKYLES-- 244
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEegkYVLVVEHDLA-ILDYLADYVHILYGE----PGVYgvvskpksvrvgiNQYLDGyl 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 245 KEEALRveeqqnaefdrklaqeeawIRQgikarrtrnegrvralKALRVERSERREVLgsarmqveeatrSGKIVFELED 324
Cdd:COG1245 314 PEENVR-------------------IRD----------------EPIEFEVHAPRREK------------EEETLVEYPD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 325 VNYSIGTRRLVRDfSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHcgTKLEVAYFDQHRATlDPDKTVMDNL 404
Cdd:COG1245 347 LTKSYGGFSLEVE-GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKISYKPQYISP-DYDGTVEEFL 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 405 AEGKQEVMVNgrprhvlGYLQDFLFPP---KRAMT-PVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:COG1245 423 RSANTDDFGS-------SYYKTEIIKPlglEKLLDkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-231 |
6.10e-20 |
|
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: 88.47 E-value: 6.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 18 LLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDlvtarlqQDPPRDIEGTIFdFVAQGVaeDAQY 97
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK-------PIKAKERRKSIG-YVMQDV--DYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 98 ITEyhrvSKVIETDPSEKNLNRLAQlqevldnrnlwlldsRIAEVLEKLGLNGEAELS--SLSGGWLRKAALGRALVSAP 175
Cdd:cd03226 85 FTD----SVREELLLGLKELDAGNE---------------QAETVLKDLDLYALKERHplSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 176 KVLFLDEPTNHLDIETILWLEKFLKDFQG---SIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
319-516 |
6.23e-20 |
|
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: 89.76 E-value: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 319 VFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDL-KADSGRIH-CGTKLE------------- 383
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRlFGERRGgedvwelrkrigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 384 VAYFDQHRatLDPDKTVMDNLAEGKQEVMvnGRPRHV----------------LGYLQDflfppkramTPVRALSGGERN 447
Cdd:COG1119 83 VSPALQLR--FPRDETVLDVVLSGFFDSI--GLYREPtdeqrerarellellgLAHLAD---------RPFGTLSQGEQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 448 RLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVD--AYQG--TVLLVSHDREFVDNSVTECWIFEGDGVI 516
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDklAAEGapTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
321-495 |
6.97e-20 |
|
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: 88.43 E-value: 6.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgTKLEVAYFDQHRA-------- 392
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---TFDGKSYQKNIEAlrrigali 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 393 ---TLDPDKTVMDNLAEGKQEVMV-NGRPRHVLGY--LQDflfppkRAMTPVRALSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:cd03268 79 eapGFYPNLTARENLRLLARLLGIrKKRIDEVLDVvgLKD------SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190
....*....|....*....|....*....|..
gi 1437745527 467 PTNDLD---VETLELLEELVDAYQGTVLLVSH 495
Cdd:cd03268 153 PTNGLDpdgIKELRELILSLRDQGITVLISSH 184
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-231 |
9.44e-20 |
|
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: 88.94 E-value: 9.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK-EQPlDDGQVVYEQDLVTARLQQDppRDI-----------E 80
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERP-DSGTILFGGEDATDVPVQE--RNVgfvfqhyalfrH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 GTIFDFVAQGVaedaqyiteyhRVSKVIETDPSEKnlnrlaqlqevldnrnlwlLDSRIAEVLEKLGLNGEAEL--SSLS 158
Cdd:cd03296 89 MTVFDNVAFGL-----------RVKPRSERPPEAE-------------------IRAKVHELLKLVQLDWLADRypAQLS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 159 GGWLRKAALGRALVSAPKVLFLDEPTNHLDI----ETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03296 139 GGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
321-501 |
1.67e-19 |
|
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: 87.55 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVN--YSIGTRRL--VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKL------------- 382
Cdd:cd03255 2 ELKNLSktYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvDGTDIsklsekelaafrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 383 -EVAY-FDQHRatLDPDKTVMDNLA-----EGKQEVMVNGRPRHVLGYLQdfLfpPKRAMTPVRALSGGERNRLLLARLF 455
Cdd:cd03255 82 rHIGFvFQSFN--LLPDLTALENVElplllAGVPKKERRERAEELLERVG--L--GDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1437745527 456 LKPSNLLILDEPTNDLDVETLELL----EELVDAYQGTVLLVSHDREFVD 501
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVmellRELNKEAGTTIVVVTHDPELAE 205
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
322-500 |
2.37e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.86 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 322 LEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQhRATLDPD---- 397
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ-KLYLDTTlplt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 398 -KTVMDNLAEGKQEVMVNGRPRHVLGYLQDFlfppkramtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL 476
Cdd:PRK09544 86 vNRFLRLRPGTKKEDILPALKRVQAGHLIDA---------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|....*...
gi 1437745527 477 ELLEELVDAYQGT----VLLVSHDREFV 500
Cdd:PRK09544 157 VALYDLIDQLRREldcaVLMVSHDLHLV 184
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
316-500 |
3.08e-19 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 87.79 E-value: 3.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 316 GKIVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHcgtklevayFDQHRAT-L 394
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIL---------FDGRDITgL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 DPDK-------------------TVMDNlaegkqeVMVNGRPRHVLGYLQDFLFPPK----------RAM---------- 435
Cdd:COG0411 72 PPHRiarlgiartfqnprlfpelTVLEN-------VLVAAHARLGRGLLAALLRLPRarreereareRAEellervglad 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 436 ---TPVRALSGGERNRLLLAR-LFLKPSnLLILDEPT---NDLDVETLELLEELVDAYQG-TVLLVSHDREFV 500
Cdd:COG0411 145 radEPAGNLSYGQQRRLEIARaLATEPK-LLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLV 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
321-496 |
3.44e-19 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 86.76 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRL----VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH------CGTKLEVAY-FDQ 389
Cdd:cd03293 2 EVRNVSKTYGGGGGavtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYvFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 390 HRatLDPDKTVMDNLAEGkqeVMVNGRPR-----HVLGY-----LQDFL--FPpkramtpvRALSGGERNRLLLAR-LFL 456
Cdd:cd03293 82 DA--LLPWLTVLDNVALG---LELQGVPKaeareRAEELlelvgLSGFEnaYP--------HQLSGGMRQRVALARaLAV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1437745527 457 KPsNLLILDEPTNDLDVETLEL-LEELVDAYQG---TVLLVSHD 496
Cdd:cd03293 149 DP-DVLLLDEPFSALDALTREQlQEELLDIWREtgkTVLLVTHD 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-231 |
4.84e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 88.98 E-value: 4.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK-EQPlDDGQVVY---------EQDLVTARlqqdppRDIeGTIF-DF- 86
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLlERP-TSGSVLVdgvdltalsERELRAAR------RKI-GMIFqHFn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 87 ------VAQGVAedaqYITEYHRVSKvietdpseknlnrlAQLQEvldnrnlwlldsRIAEVLEKLGLNGEAE--LSSLS 158
Cdd:COG1135 93 llssrtVAENVA----LPLEIAGVPK--------------AEIRK------------RVAELLELVGLSDKADayPSQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 159 GGWLRKAALGRALVSAPKVLFLDEPTNHLDIET---ILWLekfLKD----FQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETtrsILDL---LKDinreLGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-233 |
5.11e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 86.25 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDA----PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLVT------AR 70
Cdd:COG1136 3 PLLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgQDISSlserelAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 71 LQQdppRDIeGTIFDFvaqgvaedaqyiteYHrvskVIETDPSEKNLnRLAQLqevLDNRNLWLLDSRIAEVLEKLGLNG 150
Cdd:COG1136 83 LRR---RHI-GFVFQF--------------FN----LLPELTALENV-ALPLL---LAGVSRKERRERARELLERVGLGD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 151 EAEL--SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIET---IL-WLEKFLKDFQGSIVFISHDRsFIRNMATRII 224
Cdd:COG1136 137 RLDHrpSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeeVLeLLRELNRELGTTIVMVTHDP-ELAARADRVI 215
|
....*....
gi 1437745527 225 DLDRGKLSS 233
Cdd:COG1136 216 RLRDGRIVS 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
321-495 |
6.26e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 85.49 E-value: 6.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTK---------LEVAYFDQHR 391
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdepHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 392 ATLDPDKTVMDNLAegkqevmvngRPRHVLGYLQDFLFPPKRAM-------TPVRALSGGERNRLLLARLFLKPSNLLIL 464
Cdd:TIGR01189 82 PGLKPELSALENLH----------FWAAIHGGAQRTIEDALAAVgltgfedLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 1437745527 465 DEPTNDLDVETLELLEELVDAY---QGTVLLVSH 495
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-231 |
6.50e-19 |
|
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: 86.08 E-value: 6.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK------EQPLD-----DGQVVYEQDLVTARL- 71
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndlipGAPDEgevllDGKDIYDLDVDVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 72 -------QQDPPrdIEGTIFDFVAQGVaedaqyiteyhrvskvietdpseknlnrlaQLQEVLDNRNlwlLDSRIAEVLE 144
Cdd:cd03260 81 rrvgmvfQKPNP--FPGSIYDNVAYGL------------------------------RLHGIKLKEE---LDERVEEALR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 145 KLGLNGE----AELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG--SIVFISHDRSFIRN 218
Cdd:cd03260 126 KAALWDEvkdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQQAAR 205
|
250
....*....|...
gi 1437745527 219 MATRIIDLDRGKL 231
Cdd:cd03260 206 VADRTAFLLNGRL 218
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
321-496 |
6.53e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 86.71 E-value: 6.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG-------TKLEVAyfdQHRAT 393
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrplaawSPWELA---RRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 394 LdPDKTVMdNLAEGKQEVMVNGRPRHVLGYLQDFLFPpKRAMTPV----------RALSGGERNRLLLARLFL------- 456
Cdd:COG4559 80 L-PQHSSL-AFPFTVEEVVALGRAPHGSSAAQDRQIV-REALALVglahlagrsyQTLSGGEQQRVQLARVLAqlwepvd 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 457 KPSNLLILDEPTNDLDVetlelleelvdAYQ--------------GTVLLVSHD 496
Cdd:COG4559 157 GGPRWLFLDEPTSALDL-----------AHQhavlrlarqlarrgGGVVAVLHD 199
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
320-498 |
9.82e-19 |
|
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: 84.19 E-value: 9.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 320 FELEDVNYSIG--TRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKLEVAYFDQHRatldp 396
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDPNELG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 397 dktvmdnlaegkqevmvngrpRHVlGYL-QDF-LFPPKRAMTpvrALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03246 76 ---------------------DHV-GYLpQDDeLFSGSIAEN---ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180
....*....|....*....|....*..
gi 1437745527 475 TLELLEELV---DAYQGTVLLVSHDRE 498
Cdd:cd03246 131 GERALNQAIaalKAAGATRIVIAHRPE 157
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-249 |
1.24e-18 |
|
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: 89.61 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 12 AFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLA-KEQPlDDGQVVYEQDLVTARLQQ-----DPPRdiegTIFD 85
Cdd:TIGR03719 331 AFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITgQEQP-DSGTIEIGETVKLAYVDQsrdalDPNK----TVWE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 86 FVAQGvaedaqyiTEYHRVSKVieTDPSEKNLNRLaqlqevldnrNLwlldsriaevlekLGLNGEAELSSLSGGWLRKA 165
Cdd:TIGR03719 406 EISGG--------LDIIKLGKR--EIPSRAYVGRF----------NF-------------KGSDQQKKVGQLSGGERNRV 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 166 ALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLD-RGKLSSWPGNYDKYLES 244
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEYEED 532
|
....*
gi 1437745527 245 KEEAL 249
Cdd:TIGR03719 533 KKRRL 537
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
321-496 |
1.93e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 85.53 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYS----IGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKlEVAYFDQHRA---- 392
Cdd:COG1116 9 ELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-PVTGPGPDRGvvfq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 393 --TLDPDKTVMDNLAEGkqeVMVNGRPR-----HVLGY-----LQDFL--FPpkramtpvRALSGGERNRLLLAR-LFLK 457
Cdd:COG1116 88 epALLPWLTVLDNVALG---LELRGVPKaerreRARELlelvgLAGFEdaYP--------HQLSGGMRQRVAIARaLAND 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1437745527 458 PSnLLILDEPTNDLDVETLELLEELV----DAYQGTVLLVSHD 496
Cdd:COG1116 157 PE-VLLMDEPFGALDALTRERLQDELlrlwQETGKTVLFVTHD 198
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
318-472 |
3.54e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.82 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 318 IVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKL------EVAyfdQH 390
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlNGRPLadwspaELA---RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 391 RATLdPDKTVM--DNLAEgkqEVMVNGRPRHVLGYLQDflfppKR----AMTPV----------RALSGGERNRLLLARL 454
Cdd:PRK13548 78 RAVL-PQHSSLsfPFTVE---EVVAMGRAPHGLSRAED-----DAlvaaALAQVdlahlagrdyPQLSGGEQQRVQLARV 148
|
170 180
....*....|....*....|....
gi 1437745527 455 FL------KPSNLLILDEPTNDLD 472
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALD 172
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-231 |
5.46e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 85.90 E-value: 5.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK-EQPlDDGQVVYEQDLVTARlqqdPP--R 77
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDP-TSGEILIGGRDVTDL----PPkdR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 78 DIEgtifdFVAQG--------VAEDAQYITEYHRVSKvietdpseknlnrlaqlQEVldnrnlwllDSRIAEVLEKLGLn 149
Cdd:COG3839 76 NIA-----MVFQSyalyphmtVYENIAFPLKLRKVPK-----------------AEI---------DRRVREAAELLGL- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 150 geAEL-----SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLD----IETILWLEKFLKDFQGSIVFISHDRSFIRNMA 220
Cdd:COG3839 124 --EDLldrkpKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLA 201
|
250
....*....|.
gi 1437745527 221 TRIIDLDRGKL 231
Cdd:COG3839 202 DRIAVMNDGRI 212
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-231 |
5.54e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 85.97 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK-EQPlDDGQVVY-EQDLVTARLQQDppRDIeG--------- 81
Cdd:COG1118 12 FGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETP-DSGRIVLnGRDLFTNLPPRE--RRV-Gfvfqhyalf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 82 ---TIFDFVAQGVaedaqyiteyhRVSKvietdPSEknlnrlAQLQEvldnrnlwlldsRIAEVLEKLGLNGEAEL--SS 156
Cdd:COG1118 88 phmTVAENIAFGL-----------RVRP-----PSK------AEIRA------------RVEELLELVQLEGLADRypSQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 157 LSGGWLRKAALGRALVSAPKVLFLDEPTNHLD------IETilWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:COG1118 134 LSGGQRQRVALARALAVEPEVLLLDEPFGALDakvrkeLRR--WLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
.
gi 1437745527 231 L 231
Cdd:COG1118 212 I 212
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-231 |
6.61e-18 |
|
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: 82.73 E-value: 6.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFID---ENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLVTARLQQD-PPRDIE-GTIFD----FVA 88
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgTVLFDSRKKINlPPQQRKiGLVFQqyalFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 89 QGVAEDAQYITEYHRVSKvietdpseknlnRLAQLQEVLDNRNL-WLLDSRIAEvleklglngeaelssLSGGWLRKAAL 167
Cdd:cd03297 90 LNVRENLAFGLKRKRNRE------------DRISVDELLDLLGLdHLLNRYPAQ---------------LSGGEKQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 168 GRALVSAPKVLFLDEPTNHLDIETILWLEKFL----KDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03297 143 ARALAAQPELLLLDEPFSALDRALRLQLLPELkqikKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
321-496 |
6.98e-18 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 83.49 E-value: 6.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHcgtklevaYFDQHRATLDPDK-- 398
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIL--------VDGQDITGLSEKEly 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 399 -------------------TVMDNLA----E----GKQEV---------MVNgrprhvlgyLQDF--LFPpkramtpvRA 440
Cdd:COG1127 79 elrrrigmlfqggalfdslTVFENVAfplrEhtdlSEAEIrelvlekleLVG---------LPGAadKMP--------SE 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745527 441 LSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELV----DAYQGTVLLVSHD 496
Cdd:COG1127 142 LSGGMRKRVALARaLALDPE-ILLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHD 201
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-231 |
9.12e-18 |
|
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: 83.70 E-value: 9.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 16 APLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLvtARLQQDPPRDIEGTIfdfvaQGVAED 94
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgQDL--YQLDRKQRRAFRRDV-----QLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 95 AQYITEYHRVSKVIETDPSEkNLNRLAQLQEvldnrnlwllDSRIAEVLEKLGLNGEAEL---SSLSGGWLRKAALGRAL 171
Cdd:TIGR02769 97 SPSAVNPRMTVRQIIGEPLR-HLTSLDESEQ----------KARIAELLDMVGLRSEDADklpRQLSGGQLQRINIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 172 VSAPKVLFLDEPTNHLDI----ETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
315-472 |
9.23e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 87.14 E-value: 9.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 315 SGKIVFEleDVNYSIGTRRLV-RDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklevaYFDQH--- 390
Cdd:COG1132 337 RGEIEFE--NVSFSYPGDRPVlKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI---------LIDGVdir 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 391 ---RATL---------DP---DKTVMDNLAEGK-----QEVmvngrpRHVLG--YLQDFLfppkRAM-----TPV----R 439
Cdd:COG1132 406 dltLESLrrqigvvpqDTflfSGTIRENIRYGRpdatdEEV------EEAAKaaQAHEFI----EALpdgydTVVgergV 475
|
170 180 190
....*....|....*....|....*....|...
gi 1437745527 440 ALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALD 508
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
320-495 |
1.03e-17 |
|
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: 82.25 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 320 FELEDVNYSI-GTRRL-VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklevaYFDQHRAT-LDP 396
Cdd:cd03245 3 IEFRNVSFSYpNQEIPaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV---------LLDGTDIRqLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 397 DK-----------------TVMDNLAEGK-----QEVMVNGRprhvLGYLQDFLFPPKRAM-TPV----RALSGGERNRL 449
Cdd:cd03245 74 ADlrrnigyvpqdvtlfygTLRDNITLGApladdERILRAAE----LAGVTDFVNKHPNGLdLQIgergRGLSGGQRQAV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1437745527 450 LLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQG--TVLLVSH 495
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH 197
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
321-472 |
1.16e-17 |
|
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: 81.92 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLE-----VAYFDQHR 391
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvTDLPpkdrdIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 392 AtLDPDKTVMDNLAEG-----KQEVMVNGRPRHVLGYLQ-DFLFPPKramtpVRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:cd03301 82 A-LYPHMTVYDNIAFGlklrkVPKDEIDERVREVAELLQiEHLLDRK-----PKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
....*..
gi 1437745527 466 EPTNDLD 472
Cdd:cd03301 156 EPLSNLD 162
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-231 |
1.37e-17 |
|
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: 81.87 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 14 SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEqdlvTARLQQDPPRDIEGTIfDFVAQGVAE 93
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLD----GTDIRQLDPADLRRNI-GYVPQDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 94 DAQYITEyhrvskvietdpsekNLNRLAQLQEvldnrnlwllDSRIAEVLEKLGLN--------------GEAElSSLSG 159
Cdd:cd03245 90 FYGTLRD---------------NITLGAPLAD----------DERILRAAELAGVTdfvnkhpngldlqiGERG-RGLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 160 GWLRKAALGRALVSAPKVLFLDEPTNHLDIETilwLEKFLKDFQGSI-----VFISHDRSFIrNMATRIIDLDRGKL 231
Cdd:cd03245 144 GQRQAVALARALLNDPPILLLDEPTSAMDMNS---EERLKERLRQLLgdktlIIITHRPSLL-DLVDRIIVMDSGRI 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
318-472 |
1.37e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.50 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 318 IVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgTKLEVAYFDQHRA----- 392
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI---TVLGVPVPARARLarari 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 393 -------TLDPDKTVMDNL-AEGKQEVMVNGRPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLIL 464
Cdd:PRK13536 117 gvvpqfdNLDLEFTVRENLlVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
....*...
gi 1437745527 465 DEPTNDLD 472
Cdd:PRK13536 197 DEPTTGLD 204
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-231 |
1.40e-17 |
|
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: 82.28 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLvtarLQQDPPRDIEGT 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgKDI----TNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 83 IFD----FVAQGVAEDAQYITEYHRVSKVIetdpseknlnrlaqlqevldnrnlwlLDSRIAEVLEKLGLNGEA--ELSS 156
Cdd:cd03300 77 VFQnyalFPHLTVFENIAFGLRLKKLPKAE--------------------------IKERVAEALDLVQLEGYAnrKPSQ 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 157 LSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGSI----VFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03300 131 LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgitfVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-226 |
1.43e-17 |
|
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: 86.19 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDA-PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVyeqdLVTARLQQDPPRDIEGT 82
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA----VNGVPLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 83 IfDFVAQGVAEDAQYITEYHRVSKVIETDpseknlnrlAQLQEVLDNRNLWLLDSRIAEVLE-KLGLNGeaelSSLSGGW 161
Cdd:TIGR02857 398 I-AWVPQHPFLFAGTIAENIRLARPDASD---------AEIREALERAGLDEFVAALPQGLDtPIGEGG----AGLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 162 LRKAALGRALVSAPKVLFLDEPTNHLDIET-ILWLEKFLKDFQG-SIVFISHDRSFIRNmATRIIDL 226
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETeAEVLEALRALAQGrTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
320-472 |
1.55e-17 |
|
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: 82.23 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 320 FELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGtklEVAYFDQHRATLDPD-- 397
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEG---EVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 398 -----------------KTVMDNLAEG------KQEVMVNGRPRHVL------GYLQDFLFPpkramtpvRALSGGERNR 448
Cdd:cd03260 78 elrrrvgmvfqkpnpfpGSIYDNVAYGlrlhgiKLKEELDERVEEALrkaalwDEVKDRLHA--------LGLSGGQQQR 149
|
170 180
....*....|....*....|....*
gi 1437745527 449 LLLAR-LFLKPSNLLiLDEPTNDLD 472
Cdd:cd03260 150 LCLARaLANEPEVLL-LDEPTSALD 173
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-231 |
2.93e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 82.04 E-value: 2.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK-EQPlDDGQVVYeQDLVTARLQQDPPRDIEGTIfdfvaQGVAEDA-Q 96
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlESP-SQGNVSW-RGEPLAKLNRAQRKAFRRDI-----QMVFQDSiS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 97 YITEYHRVSKVIE------TDPSEKnlNRLAQLQEVLDNRNLwlldsrIAEVLEKLGlngeaelSSLSGGWLRKAALGRA 170
Cdd:PRK10419 101 AVNPRKTVREIIReplrhlLSLDKA--ERLARASEMLRAVDL------DDSVLDKRP-------PQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 171 LVSAPKVLFLDEPTNHLDI----ETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
321-473 |
3.73e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.12 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLEVAYFDQHRATLDP 396
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvEALSARAASRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 397 DKTVMDNLaEGKQEVMVnGRPRHVL---GYLQDFLFPPKRAMT----------PVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:PRK09536 85 DTSLSFEF-DVRQVVEM-GRTPHRSrfdTWTETDRAAVERAMErtgvaqfadrPVTSLSGGERQRVLLARALAQATPVLL 162
|
170
....*....|
gi 1437745527 464 LDEPTNDLDV 473
Cdd:PRK09536 163 LDEPTASLDI 172
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
342-495 |
3.98e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 80.66 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 342 VQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTK--------LEVAYFDqHRATLDPDKTVMDNLAegkqevMV 413
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsRFMAYLG-HLPGLKADLSTLENLH------FL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 414 NG----RPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAY--- 486
Cdd:PRK13543 107 CGlhgrRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHlrg 186
|
....*....
gi 1437745527 487 QGTVLLVSH 495
Cdd:PRK13543 187 GGAALVTTH 195
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-231 |
4.27e-17 |
|
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: 80.63 E-value: 4.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQV-VYEQDLVTARLQQD------PPRDIegtIFDFVaqgV 91
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyINGYSIRTDRKAARqslgycPQFDA---LFDEL---T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 92 AEDAQYIteYHRVskvietdpseKNLNRLAqlqevldnrnlwlLDSRIAEVLEKLGLNGEAEL--SSLSGGWLRKAALGR 169
Cdd:cd03263 92 VREHLRF--YARL----------KGLPKSE-------------IKEEVELLLRVLGLTDKANKraRTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 170 ALVSAPKVLFLDEPTNHLDIET--ILWleKFLKDFQG--SIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASrrAIW--DLILEVRKgrSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
335-500 |
4.61e-17 |
|
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: 80.94 E-value: 4.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 335 VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTklEVAYFDQHR------------ATLDPDKTVM 401
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfDGE--DITGLPPHEiarlgigrtfqiPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 402 DNlaegkqeVMVNGRPRHVLGYLQDFLFPPKRAM------------------TPVRALSGGERNRLLLAR-LFLKPSnLL 462
Cdd:cd03219 94 EN-------VMVAAQARTGSGLLLARARREEREAreraeellervgladladRPAGELSYGQQRRLEIARaLATDPK-LL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1437745527 463 ILDEPT---NDLDVETLELLEELVDAYQGTVLLVSHDREFV 500
Cdd:cd03219 166 LLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVV 206
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-231 |
5.18e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 80.27 E-value: 5.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTarlqqDPPRDIE--- 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-----DDKKNINelr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 ---GTIFdfvaqgvaedaqyiteyhrvskvietdpseKNLNRLAQLqEVLDN-----RNLWLLDSRIAE-----VLEKLG 147
Cdd:cd03262 76 qkvGMVF------------------------------QQFNLFPHL-TVLENitlapIKVKGMSKAEAEeraleLLEKVG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 148 LNGEAEL--SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QG-SIVFISHDRSFIRNMATR 222
Cdd:cd03262 125 LADKADAypAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeEGmTMVVVTHEMGFAREVADR 204
|
....*....
gi 1437745527 223 IIDLDRGKL 231
Cdd:cd03262 205 VIFMDDGRI 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
321-496 |
5.92e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 80.65 E-value: 5.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVnySIGTRrlVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGdLKADSGRIHC-GTKLE---VAYFDQHRATL-- 394
Cdd:COG4138 2 QLNDV--AVAGR--LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLnGRPLSdwsAAELARHRAYLsq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 -DPDKTVMD-------NLAEGKQEVMVNGRPRHVLGYLQ--DFLfppkraMTPVRALSGGERNRLLLARLFLK------- 457
Cdd:COG4138 77 qQSPPFAMPvfqylalHQPAGASSEAVEQLLAQLAEALGleDKL------SRPLTQLSGGEWQRVRLAAVLLQvwptinp 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1437745527 458 PSNLLILDEPTNDLDVETLELLEELVDAY---QGTVLLVSHD 496
Cdd:COG4138 151 EGQLLLLDEPMNSLDVAQQAALDRLLRELcqqGITVVMSSHD 192
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-232 |
7.43e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.52 E-value: 7.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGqvvyeqDLVTARLQQDPPRDIEGTI--------- 83
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG------DLIVDGLKVNDPKVDERLIrqeagmvfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 84 -FDFVAQGVA-EDAQYITEYHRVSkvietdpSEKNLNRLAQlqevldnrnlwlldsriaEVLEKLGLNGEAEL--SSLSG 159
Cdd:PRK09493 85 qFYLFPHLTAlENVMFGPLRVRGA-------SKEEAEKQAR------------------ELLAKVGLAERAHHypSELSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 160 GWLRKAALGRALVSAPKVLFLDEPTNHLDIE---TILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLS 232
Cdd:PRK09493 140 GQQQRVAIARALAVKPKLMLFDEPTSALDPElrhEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-231 |
7.73e-17 |
|
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: 78.24 E-value: 7.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVyeqdlvtarlqqdpprdIEGTI 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL-----------------VDGKE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 84 FDFvaqgvaedaqyiteyhrvskvieTDPSEKnlnrlaqlqevldnrnlwlLDSRIAEVleklglngeaelSSLSGGWLR 163
Cdd:cd03216 64 VSF-----------------------ASPRDA-------------------RRAGIAMV------------YQLSVGERQ 89
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745527 164 KAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QG-SIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03216 90 MVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
251-564 |
7.84e-17 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 84.53 E-value: 7.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 251 VEEQQNAEFDRKLAQEEawiRQgikaRRTRNEGRVRALKALRVerserrevlGSARMQVEEATRSGKIV---FELEDVNY 327
Cdd:PLN03073 122 LSERDLAKIERRKRKEE---RQ----REVQYQAHVAEMEAAKA---------GMPGVYVNHDGNGGGPAikdIHMENFSI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 328 SIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLM---------------------LGD--------LKADSGRihc 378
Cdd:PLN03073 186 SVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMamhaidgipkncqilhveqevVGDdttalqcvLNTDIER--- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 379 gTKL---EVAYFDQHRATLDPDKTVMDNLAE--GKQEVMVNGRPRHVLGYLQ----------------DFLFPPKRAMTP 437
Cdd:PLN03073 263 -TQLleeEAQLVAQQRELEFETETGKGKGANkdGVDKDAVSQRLEEIYKRLElidaytaearaasilaGLSFTPEMQVKA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 438 VRALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETLELLEELVDAYQGTVLLVSHDREFVDNSVTECWIFEGDGvI 516
Cdd:PLN03073 342 TKTFSGGWRMRIALARaLFIEP-DLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQK-L 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 517 NSYVGGYYDAQQQRAQsvSLKNEaNKSRNAPEKTEKET-----KPKQNAKKAT 564
Cdd:PLN03073 420 VTYKGDYDTFERTREE--QLKNQ-QKAFESNERSRSHMqafidKFRYNAKRAS 469
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
335-498 |
8.01e-17 |
|
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: 80.07 E-value: 8.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 335 VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GT--------KLEVAYFDQHRAtLDPDKTVMDNLA 405
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKditnlppeKRDISYVPQNYA-LFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 406 EG--KQEVMVNGRPRHVL---GYLQ-DFLFPPKramtpVRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLEL 478
Cdd:cd03299 94 YGlkKRKVDKKEIERKVLeiaEMLGiDHLLNRK-----PETLSGGEQQRVAIARaLVVNPK-ILLLDEPFSALDVRTKEK 167
|
170 180
....*....|....*....|....
gi 1437745527 479 LEELV----DAYQGTVLLVSHDRE 498
Cdd:cd03299 168 LREELkkirKEFGVTVLHVTHDFE 191
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
15-230 |
1.06e-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: 79.40 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 15 DAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARlqqdPPRDIegtifdfVAQGVAed 94
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGL----PPHER-------ARAGIG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 95 aqYITEYHRVSkvietdPS---EKNL----------NRLAQLQEVLDnrnlwlLDSRIAEVLEKLGlngeaelSSLSGGW 161
Cdd:cd03224 79 --YVPEGRRIF------PEltvEENLllgayarrraKRKARLERVYE------LFPRLKERRKQLA-------GTLSGGE 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 162 LRKAALGRALVSAPKVLFLDEPTNHL------DIETILwleKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:cd03224 138 QQMLAIARALMSRPKLLLLDEPSEGLapkiveEIFEAI---RELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
321-496 |
1.19e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.98 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVnySIGTRRLvrDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGdLKADSGRIHC-GTKLEV----------AYFDQ 389
Cdd:PRK03695 2 QLNDV--AVSTRLG--PLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFaGQPLEAwsaaelarhrAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 390 HRATLdPDKTVMDNLAEGKQEVMVNGRPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLARLFLK------P-SNLL 462
Cdd:PRK03695 77 QQTPP-FAMPVFQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinPaGQLL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1437745527 463 ILDEPTNDLDVETLELLEELVDAY--QG-TVLLVSHD 496
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELcqQGiAVVMSSHD 192
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
321-498 |
1.45e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 81.35 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTklEVAYFD------------ 388
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--RDLFTNlpprerrvgfvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 389 QHRAtLDPDKTVMDNLAEGKQevmVNGRPRH-----VLGYLQDF-L------FPpkramtpvRALSGGERNRLLLAR-LF 455
Cdd:COG1118 82 QHYA-LFPHMTVAENIAFGLR---VRPPSKAeirarVEELLELVqLegladrYP--------SQLSGGQRQRVALARaLA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 456 LKPSnLLILDEPTNDLDVetlelleeLV------------DAYQGTVLLVSHDRE 498
Cdd:COG1118 150 VEPE-VLLLDEPFGALDA--------KVrkelrrwlrrlhDELGGTTVFVTHDQE 195
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
316-472 |
1.73e-16 |
|
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: 82.84 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 316 GKIVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKLE----------V 384
Cdd:TIGR02203 329 GDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdGHDLAdytlaslrrqV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 385 AYFDQHRATLDpdKTVMDNLAEGKQEVMVNGRPRHVL--GYLQDFLFP-PKRAMTPVRA----LSGGERNRLLLARLFLK 457
Cdd:TIGR02203 409 ALVSQDVVLFN--DTIANNIAYGRTEQADRAEIERALaaAYAQDFVDKlPLGLDTPIGEngvlLSGGQRQRLAIARALLK 486
|
170
....*....|....*
gi 1437745527 458 PSNLLILDEPTNDLD 472
Cdd:TIGR02203 487 DAPILILDEATSALD 501
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
321-496 |
1.79e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 79.03 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLvrDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLEVA------YFDQH 390
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqdlTALPPAerpvsmLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 391 raTLDPDKTVMDNLAEG-----------KQEVM-----VNgrprhvLGYLQDFLfppkramtPvRALSGGERNRLLLARL 454
Cdd:COG3840 81 --NLFPHLTVAQNIGLGlrpglkltaeqRAQVEqalerVG------LAGLLDRL--------P-GQLSGGQRQRVALARC 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1437745527 455 FLKPSNLLILDEPTNDLDVETLELLEELVD----AYQGTVLLVSHD 496
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDelcrERGLTVLMVTHD 189
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
335-496 |
1.85e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 79.30 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 335 VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQH----------RATLDPDKTVMDNL 404
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlrrigvvfgqKTQLWWDLPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 405 AEGKQEVMVN-GRPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELV 483
Cdd:cd03267 117 YLLAAIYDLPpARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFL 196
|
170
....*....|....*..
gi 1437745527 484 DAY----QGTVLLVSHD 496
Cdd:cd03267 197 KEYnrerGTTVLLTSHY 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
321-468 |
2.16e-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: 78.63 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGT-----------KLEVAYFD 388
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfDGRditglppheraRAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 389 QHRAtLDPDKTVMDNL---AEGKQEVMVNGRPRHVLGylqdfLFP--PKRAMTPVRALSGGERNRLLLAR-LFLKPSnLL 462
Cdd:cd03224 82 EGRR-IFPELTVEENLllgAYARRRAKRKARLERVYE-----LFPrlKERRKQLAGTLSGGEQQMLAIARaLMSRPK-LL 154
|
....*.
gi 1437745527 463 ILDEPT 468
Cdd:cd03224 155 LLDEPS 160
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
321-498 |
2.36e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 80.91 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLE-----VAYFDQHR 391
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvTGLPpekrnVGMVFQDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 392 AtLDPDKTVMDNLAEG-------KQEV---------MVNgrprhvlgyLQDFLfppKRAmtpVRALSGGERNRLLLAR-L 454
Cdd:COG3842 87 A-LFPHLTVAENVAFGlrmrgvpKAEIrarvaelleLVG---------LEGLA---DRY---PHQLSGGQQQRVALARaL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1437745527 455 FLKPSnLLILDEPTNDLDVETLELLEELVDAYQ----GTVLLVSHDRE 498
Cdd:COG3842 151 APEPR-VLLLDEPLSALDAKLREEMREELRRLQrelgITFIYVTHDQE 197
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
19-230 |
2.51e-16 |
|
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: 78.76 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE----QDLVTARLQQdpPRDIEGTIFDfvaqgvaed 94
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdiNKLKGKALRQ--LRRQIGMIFQ--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 95 aQYiteyhrvskvietdpsekNL-NRLAQLQEVL----DNRNLW--------LLDSRIA-EVLEKLGLNGEAEL--SSLS 158
Cdd:cd03256 86 -QF------------------NLiERLSVLENVLsgrlGRRSTWrslfglfpKEEKQRAlAALERVGLLDKAYQraDQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 159 GGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF---QGSIVFIS-HDRSFIRNMATRIIDLDRGK 230
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDLAREYADRIVGLKDGR 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-247 |
4.26e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.42 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK-----------EQPLDDGQVVYEQDLVTA 69
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielypearvsGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 70 RLQ-----QDPPRDIEGTIFDFVAQGVaedaqyiteyhrvskvietdpsekNLNRLAQLQEVLDNRNLWLLDSriAEVLE 144
Cdd:PRK14247 81 RRRvqmvfQIPNPIPNLSIFENVALGL------------------------KLNRLVKSKKELQERVRWALEK--AQLWD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 145 KLGLNGEAELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG--SIVFISHdrsfIRNMATR 222
Cdd:PRK14247 135 EVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH----FPQQAAR 210
|
250 260
....*....|....*....|....*....
gi 1437745527 223 IID----LDRGKLSSWPGNYDKYLESKEE 247
Cdd:PRK14247 211 ISDyvafLYKGQIVEWGPTREVFTNPRHE 239
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
319-473 |
5.03e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.22 E-value: 5.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 319 VFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI-HCGTKLEV-AYFDQ-----HR 391
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkLDGGDIDDpDVAEAchylgHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 392 ATLDPDKTVMDNLaEGKQEVMvNGRPRHVLGYLQDFLFPPKrAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
Cdd:PRK13539 82 NAMKPALTVAENL-EFWAAFL-GGEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
..
gi 1437745527 472 DV 473
Cdd:PRK13539 159 DA 160
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
321-498 |
5.06e-16 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 77.41 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHcgtkleVAYFDQHR--------- 391
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT------VAGHDVVReprevrrri 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 392 ------ATLDPDKTVMDNLA-EGKQEVMVNGRPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLIL 464
Cdd:cd03265 76 givfqdLSVDDELTGWENLYiHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1437745527 465 DEPTNDLDVETLELLEELVDAYQG----TVLLVSHDRE 498
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEefgmTILLTTHYME 193
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-224 |
5.94e-16 |
|
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: 79.33 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRV---LAKEQPLDDGQVVYE-QDLVTA-----------RLQ---QDP----- 75
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAilgLLPPPGITSGEILFDgEDLLKLsekelrkirgrEIQmifQDPmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 76 PRDiegTIFDFVAQGVaedaqyitEYHR-VSKvietdpseknlnrlAQLQEvldnrnlwlldsRIAEVLEKLGLNGEAE- 153
Cdd:COG0444 101 PVM---TVGDQIAEPL--------RIHGgLSK--------------AEARE------------RAIELLERVGLPDPERr 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 154 LSS----LSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIET---ILWLekfLKDFQ---G-SIVFISHDRSFIRNMATR 222
Cdd:COG0444 144 LDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIqaqILNL---LKDLQrelGlAILFITHDLGVVAEIADR 220
|
..
gi 1437745527 223 II 224
Cdd:COG0444 221 VA 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
321-500 |
6.52e-16 |
|
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: 76.94 E-value: 6.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-------CGTKLEVAYFDQHRAt 393
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldIAARNRIGYLPEERG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 394 LDPDKTVMDNL---AE----GKQEVMvngrpRHVLGYLQDFLFPPKRAmTPVRALSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:cd03269 81 LYPKMKVIDQLvylAQlkglKKEEAR-----RRIDEWLERLELSEYAN-KRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1437745527 467 PTNDLDVETLELLEELVDAYQG---TVLLVSHDREFV 500
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARagkTVILSTHQMELV 191
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-311 |
6.53e-16 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 81.37 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKE-QPLddgqvvyeqdlvtarlqqdpprdiE 80
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGElAPV------------------------S 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 GTIfdFVAQGVAED--AQYITEYHRvskvietdPSEKNLNRLAQL--QEvldnrnlwlLDSRIAEVLEKLGLNGEA---E 153
Cdd:PRK10636 367 GEI--GLAKGIKLGyfAQHQLEFLR--------ADESPLQHLARLapQE---------LEQKLRDYLGGFGFQGDKvteE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 154 LSSLSGGwlRKAALGRALV--SAPKVLFLDEPTNHLDIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK10636 428 TRRFSGG--EKARLVLALIvwQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 232 SSWPGNYDKYLESKEEALRVEEQQNAEfDRKLAQEEAWIRQGIKARRTRNEGRVRALKAlRVERSERR-EVLGSARMQVE 310
Cdd:PRK10636 506 EPFDGDLEDYQQWLSDVQKQENQTDEA-PKENNANSAQARKDQKRREAELRTQTQPLRK-EIARLEKEmEKLNAQLAQAE 583
|
.
gi 1437745527 311 E 311
Cdd:PRK10636 584 E 584
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
569-638 |
6.58e-16 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 72.50 E-value: 6.58e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 569 KLSYHLIRELEQLPAKLERLEEELGCLQEEVAAADFFTRpHEETEKVLKALADKENELETAFDRWQELEM 638
Cdd:pfam16326 1 KLSYKEQRELEELEAEIEKLEEEIAELEAQLADPELYSD-YEKLQELSAELEELEAELEELYERWEELEE 69
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
317-498 |
6.77e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 77.39 E-value: 6.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 317 KIVFELEDVNYSIGT----RRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKL------EVA 385
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLiDGQDIsslserELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 386 YFdqhRAT----------LDPDKTVMDNLA-----EGKQEVMVNGRPRHVLGYLQdfLfpPKRAMTPVRALSGGERNRLL 450
Cdd:COG1136 82 RL---RRRhigfvfqffnLLPELTALENVAlplllAGVSRKERRERARELLERVG--L--GDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 451 LAR-LFLKPSnLLILDEPTNDLDVETLELL----EELVDAYQGTVLLVSHDRE 498
Cdd:COG1136 155 IARaLVNRPK-LILADEPTGNLDSKTGEEVlellRELNRELGTTIVMVTHDPE 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-191 |
9.51e-16 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 80.48 E-value: 9.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 15 DAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVyeqdlvtarLQQDPPRDIEGTIFDFVAQGVAED 94
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT---------LDGVPVSSLDQDEVRRRVSVCAQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 95 AqyiteyHrvskVIETDPSEkNLnRLAQlQEVLDNRNLWLLDS-RIAEVLEKL--GLN---GEAElSSLSGGWLRKAALG 168
Cdd:TIGR02868 418 A------H----LFDTTVRE-NL-RLAR-PDATDEELWAALERvGLADWLRALpdGLDtvlGEGG-ARLSGGERQRLALA 483
|
170 180
....*....|....*....|...
gi 1437745527 169 RALVSAPKVLFLDEPTNHLDIET 191
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAET 506
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
321-473 |
1.22e-15 |
|
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: 76.89 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLV-RDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLEVAYFDQHRATLD 395
Cdd:cd03253 2 EFENVTFAYDPGRPVlKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdiREVTLDSLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 396 PD-----KTVMDNLAEGK-----QEVMVNGRPRHVLGYLQDFlfpPKRAMTPV--RA--LSGGERNRLLLARLFLKPSNL 461
Cdd:cd03253 82 QDtvlfnDTIGYNIRYGRpdatdEEVIEAAKAAQIHDKIMRF---PDGYDTIVgeRGlkLSGGEKQRVAIARAILKNPPI 158
|
170
....*....|..
gi 1437745527 462 LILDEPTNDLDV 473
Cdd:cd03253 159 LLLDEATSALDT 170
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-472 |
1.23e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.13 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDA----PLLDNTDLFIDENERVCLVGRNGAGKS-TLLRVLakeQPLDDGQVVYEQ-DLVTA---RL 71
Cdd:PRK15134 3 QPLLAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL---RLLPSPPVVYPSgDIRFHgesLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 72 QQDPP--RDIEGTIFDFVAQgvaEDAQYITEYHRVSKvietdpseknlnrlaQLQEVLD-NRNLWLLDSR--IAEVLEKL 146
Cdd:PRK15134 80 HASEQtlRGVRGNKIAMIFQ---EPMVSLNPLHTLEK---------------QLYEVLSlHRGMRREAARgeILNCLDRV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 147 GL-NGEAELS----SLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIET---ILWLEKFLK-DFQGSIVFISHDRSFIR 217
Cdd:PRK15134 142 GIrQAAKRLTdyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVqaqILQLLRELQqELNMGLLFITHNLSIVR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 218 NMATRIIDLDRGklsswpgnydkyleskeealRVEEQQNAefdRKL--AQEEAWIRQGIKARrtrNEGRVRALKA----- 290
Cdd:PRK15134 222 KLADRVAVMQNG--------------------RCVEQNRA---ATLfsAPTHPYTQKLLNSE---PSGDPVPLPEpaspl 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 291 LRVERserrevlgsarMQVEEATRSGKIvfeledvNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTT----LLKLML 366
Cdd:PRK15134 276 LDVEQ-----------LQVAFPIRKGIL-------KRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 367 --GDLKADSGRIHCGT---------KLEVAYFDQHRAtLDPDKTVMDNLAEGKQ----EVMVNGRPRHVLGYLQDF-LFP 430
Cdd:PRK15134 338 sqGEIWFDGQPLHNLNrrqllpvrhRIQVVFQDPNSS-LNPRLNVLQIIEEGLRvhqpTLSAAQREQQVIAVMEEVgLDP 416
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1437745527 431 PKRAMTPVrALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLD 472
Cdd:PRK15134 417 ETRHRYPA-EFSGGQRQRIAIARaLILKPS-LIILDEPTSSLD 457
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-230 |
1.30e-15 |
|
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: 76.56 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARlqqdPPRDIe 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL----PPHRI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 gtifdfVAQGVAedaqYITEYHRV----SkVIEtdpsekNLnRLAQLQevldNRNLWLLDSRIAEVLE---KLG--LNGE 151
Cdd:COG0410 76 ------ARLGIG----YVPEGRRIfpslT-VEE------NL-LLGAYA----RRDRAEVRADLERVYElfpRLKerRRQR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 152 AelSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHL------DIETILwleKFLKDfQG-SIVFISHDRSFIRNMATRII 224
Cdd:COG0410 134 A--GTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLapliveEIFEII---RRLNR-EGvTILLVEQNARFALEIADRAY 207
|
....*.
gi 1437745527 225 DLDRGK 230
Cdd:COG0410 208 VLERGR 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
321-472 |
1.33e-15 |
|
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: 76.08 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGdKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklevaYFDQHRATLDPDKTv 400
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI---------RIDGQDVLKQPQKL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 401 mdnlaegkqevmvngrpRHVLGYL-QDFLFPPK------------------------------------RAMTPVRALSG 443
Cdd:cd03264 71 -----------------RRRIGYLpQEFGVYPNftvrefldyiawlkgipskevkarvdevlelvnlgdRAKKKIGSLSG 133
|
170 180
....*....|....*....|....*....
gi 1437745527 444 GERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03264 134 GMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
321-472 |
1.46e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 78.58 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLE-----VAY-FdQH 390
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGgrdvTDLPpkdrnIAMvF-QS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 391 RAtLDPDKTVMDNLAEG-------KQEvmVNGRPRHVLGYLQ--DFLfppKRamtPVRALSGGERNRLLLARLFLKPSNL 461
Cdd:COG3839 84 YA-LYPHMTVYENIAFPlklrkvpKAE--IDRRVREAAELLGleDLL---DR---KPKQLSGGQRQRVALGRALVREPKV 154
|
170
....*....|.
gi 1437745527 462 LILDEPTNDLD 472
Cdd:COG3839 155 FLLDEPLSNLD 165
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
17-231 |
1.62e-15 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 76.78 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLVT----------ARLQQDPPRDIEGTIFD 85
Cdd:TIGR03873 15 LIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAgVDLHGlsrrararrvALVEQDSDTAVPLTVRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 86 FVAQGvaedaqyiteyhRVSkvietdpseknlnrlaqlqevldNRNLWLLDSR-----IAEVLEKLGLNGEAE--LSSLS 158
Cdd:TIGR03873 95 VVALG------------RIP-----------------------HRSLWAGDSPhdaavVDRALARTELSHLADrdMSTLS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 159 GGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG---SIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:TIGR03873 140 GGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVLDGGRV 215
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-233 |
1.68e-15 |
|
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: 78.23 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 23 DLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLV---TARLQQDPPRDIEGTIFD----FVAQGVAEDA 95
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsRKGIFLPPEKRRIGYVFQearlFPHLSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 96 QYiteyhrvsKVIETDPSEKNLnrlaqlqevldnrnlwlldsRIAEVLEKLGLNG--EAELSSLSGGWLRKAALGRALVS 173
Cdd:TIGR02142 97 RY--------GMKRARPSERRI--------------------SFERVIELLGIGHllGRLPGRLSGGEKQRVAIGRALLS 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 174 APKVLFLDEPTNHLDI----ETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLSS 233
Cdd:TIGR02142 149 SPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
13-231 |
1.70e-15 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 77.43 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQV-VYEQDLVTArlqqdpPRDIEGTIfDFVAQGV 91
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTArVAGYDVVRE------PRKVRRSI-GIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 92 AEDaqyiteyhrvskviETDPSEKNLNRLAQLQEVldnrNLWLLDSRIAEVLEKLGLNGEAE--LSSLSGGWLRKAALGR 169
Cdd:TIGR01188 76 SVD--------------EDLTGRENLEMMGRLYGL----PKDEAEERAEELLELFELGEAADrpVGTYSGGMRRRLDIAA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 170 ALVSAPKVLFLDEPTNHLDIET--ILW-LEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:TIGR01188 138 SLIHQPDVLFLDEPTTGLDPRTrrAIWdYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRI 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-520 |
1.74e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 79.29 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQvvYEQDLVT-ARL---QQdpp 76
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE--RQSQFSHiTRLsfeQL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 77 rdiegtifdfvaQGVAEDaqyitEYHRVSkvieTD---PSEKNLNRLAQ---LQEVLDNrnlwlldSRIAEVLEKLGLng 150
Cdd:PRK10938 76 ------------QKLVSD-----EWQRNN----TDmlsPGEDDTGRTTAeiiQDEVKDP-------ARCEQLAQQFGI-- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 151 EAELSS----LSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGS---IVFISHDRSFIRNMATRI 223
Cdd:PRK10938 126 TALLDRrfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSgitLVLVLNRFDEIPDFVQFA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 224 IDLDrgklsswpgnydkyleskeealrveeqqnaefDRKLaqeeawIRQGikarrTRNEGRVRALKAlRVERSERREVL- 302
Cdd:PRK10938 206 GVLA--------------------------------DCTL------AETG-----EREEILQQALVA-QLAHSEQLEGVq 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 303 --GSARMQVEEATRSGKIVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDlkadsgriHC-G 379
Cdd:PRK10938 242 lpEPDEPSARHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD--------HPqG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 380 TKLEVAYFDQHRATldpDKTVMDNlaegKQ-----------EVMVNGRPRHVL--GYL------------QDFL------ 428
Cdd:PRK10938 314 YSNDLTLFGRRRGS---GETIWDI----KKhigyvssslhlDYRVSTSVRNVIlsGFFdsigiyqavsdrQQKLaqqwld 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 429 ---FPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQG---TVLL-VSHDREFVD 501
Cdd:PRK10938 387 ilgIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISegeTQLLfVSHHAEDAP 466
|
570
....*....|....*....
gi 1437745527 502 NSVTECWIFEGDGVINSYV 520
Cdd:PRK10938 467 ACITHRLEFVPDGDIYRYV 485
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-231 |
1.82e-15 |
|
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: 75.87 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQ-VVYEQDLVTArlqqdpPRDIEGTIfDFVAQGV 91
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVVRE------PREVRRRI-GIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 92 AEDAQyITEYhrvskvietdpseKNLNRLAQLQEVLDNRnlwlLDSRIAEVLEKLGLnGEAE---LSSLSGGWLRKAALG 168
Cdd:cd03265 83 SVDDE-LTGW-------------ENLYIHARLYGVPGAE----RRERIDELLDFVGL-LEAAdrlVKTYSGGMRRRLEIA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 169 RALVSAPKVLFLDEPTNHLDIETI--LW--LEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRahVWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
317-531 |
1.99e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.91 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 317 KIVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklevaYFDQHR-ATLD 395
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL---------LFEGEDiSTLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 396 PDK-----------------TVMDNLAEGKQEVMVNGRPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLARLFLKP 458
Cdd:PRK10247 76 PEIyrqqvsycaqtptlfgdTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 459 SNLLILDEPTNDLDVETLELLEELVDAY----QGTVLLVSHDRefvdNSVTECwifegDGVI--NSYVGGYYDAQQQRA 531
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYvreqNIAVLWVTHDK----DEINHA-----DKVItlQPHAGEMQEARYELA 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-495 |
2.01e-15 |
|
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: 74.00 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 320 FELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHcgtklevayfdqhratldpdkt 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 400 vmdnlaegkqevmVNGRPRHVLGylqdflfpPKRAM----TPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03216 59 -------------VDGKEVSFAS--------PRDARragiAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180
....*....|....*....|...
gi 1437745527 476 LELLEELVD--AYQG-TVLLVSH 495
Cdd:cd03216 118 VERLFKVIRrlRAQGvAVIFISH 140
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
337-498 |
2.03e-15 |
|
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: 75.41 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 337 DFSAKVQ---RGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGtklEVAYFD---------QHR--------ATLDP 396
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN---GTVLFDsrkkinlppQQRkiglvfqqYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 397 DKTVMDNLAEG---KQEVMVNGRPRHVLGYLQdfLFPPKRAmtPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03297 89 HLNVRENLAFGlkrKRNREDRISVDELLDLLG--LDHLLNR--YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180
....*....|....*....|....*....
gi 1437745527 474 ETLELLEELVDA----YQGTVLLVSHDRE 498
Cdd:cd03297 165 ALRLQLLPELKQikknLNIPVIFVTHDLS 193
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
320-495 |
2.72e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 73.73 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 320 FELEDVNYSIGT-RRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKlMLGDL-KADSGRIHCGTKLEVAYFDQHratldPd 397
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFR-ALAGLwPWGSGRIGMPEGEDLLFLPQR-----P- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 398 ktvmdnlaegkqeVMVNGRPRHVLGYLQDflfppkramtpvRALSGGERNRLLLARLFL-KPSnLLILDEPTNDLDVETL 476
Cdd:cd03223 74 -------------YLPLGTLREQLIYPWD------------DVLSGGEQQRLAFARLLLhKPK-FVFLDEATSALDEESE 127
|
170
....*....|....*....
gi 1437745527 477 ELLEELVDAYQGTVLLVSH 495
Cdd:cd03223 128 DRLYQLLKELGITVISVGH 146
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
330-473 |
3.07e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.84 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 330 GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKLE---VAYFDQ-----HRATLDPDKTV 400
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwQGEPIRrqrDEYHQDllylgHQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 401 MDNLA-------EGKQEVMVNGRPRHVLGylqdflfppKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13538 92 LENLRfyqrlhgPGDDEALWEALAQVGLA---------GFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-231 |
3.31e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 75.92 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQdlvtARLQQDPPRDI---------EGTI-FDF 86
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG----RPLAAWSPWELarrravlpqHSSLaFPF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 87 vaqgvaedaqyiteyhRVSKVIEtdpseknLNRLAQLQEVLDNRNLwlldsrIAEVLEKLGLNGEAELS--SLSGGWLRK 164
Cdd:COG4559 91 ----------------TVEEVVA-------LGRAPHGSSAAQDRQI------VREALALVGLAHLAGRSyqTLSGGEQQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 165 AALGRALV-------SAPKVLFLDEPTNHLDI---ETILWLEKFLKDFQGSIVFISHDrsfiRNMAT----RIIDLDRGK 230
Cdd:COG4559 142 VQLARVLAqlwepvdGGPRWLFLDEPTSALDLahqHAVLRLARQLARRGGGVVAVLHD----LNLAAqyadRILLLHQGR 217
|
.
gi 1437745527 231 L 231
Cdd:COG4559 218 L 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
321-502 |
3.52e-15 |
|
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: 74.75 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVN--YSIGTRRLvRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKL------EVAYFDQHR 391
Cdd:cd03292 2 EFINVTktYPNGTAAL-DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 392 AT------LDPDKTVMDNLAEGKQEVMVNGR--PRHVLGYLQDF-LFPPKRAMTpvRALSGGERNRLLLARLFLKPSNLL 462
Cdd:cd03292 81 GVvfqdfrLLPDRNVYENVAFALEVTGVPPReiRKRVPAALELVgLSHKHRALP--AELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1437745527 463 ILDEPTNDLDVETLELLEE---LVDAYQGTVLLVSHDREFVDN 502
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNllkKINKAGTTVVVATHAKELVDT 201
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-232 |
4.39e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.38 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGqvvyeqDLVTA--RLQQDPP-- 76
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG------DLFIGekRMNDVPPae 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 77 RDIeGTIFDFVA----QGVAEDAQYITEYHRVSKvIETDPSEKNLNRLAQLQEVLDNRNlwlldsriaevleklglngea 152
Cdd:PRK11000 75 RGV-GMVFQSYAlyphLSVAENMSFGLKLAGAKK-EEINQRVNQVAEVLQLAHLLDRKP--------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 153 elSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLD--------IEtilwLEKFLKDFQGSIVFISHDRSFIRNMATRII 224
Cdd:PRK11000 132 --KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmrIE----ISRLHKRLGRTMIYVTHDQVEAMTLADKIV 205
|
....*...
gi 1437745527 225 DLDRGKLS 232
Cdd:PRK11000 206 VLDAGRVA 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
321-498 |
6.00e-15 |
|
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: 74.68 E-value: 6.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTK---------LEVAYFDQHR 391
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqeRNVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 392 AtLDPDKTVMDNLAEGKQEVMVNGRP---------RHVLGYLQ-DFL---FPPKramtpvraLSGGERNRLLLARLFLKP 458
Cdd:cd03296 84 A-LFRHMTVFDNVAFGLRVKPRSERPpeaeirakvHELLKLVQlDWLadrYPAQ--------LSGGQRQRVALARALAVE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1437745527 459 SNLLILDEPTNDLDVETLELLEELV----DAYQGTVLLVSHDRE 498
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLrrlhDELHVTTVFVTHDQE 198
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
318-472 |
8.02e-15 |
|
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: 74.19 E-value: 8.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 318 IVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH------CGTKL-----EVAY 386
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILidghdvRDYTLaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 387 FDQHraTLDPDKTVMDNLAEGK-----QEVMVNGRPRHVLGYLQDFlfpPKRAMTPV--RA--LSGGERNRLLLARLFLK 457
Cdd:cd03251 81 VSQD--VFLFNDTVAENIAYGRpgatrEEVEEAARAANAHEFIMEL---PEGYDTVIgeRGvkLSGGQRQRIAIARALLK 155
|
170
....*....|....*
gi 1437745527 458 PSNLLILDEPTNDLD 472
Cdd:cd03251 156 DPPILILDEATSALD 170
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
321-468 |
9.94e-15 |
|
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: 73.86 E-value: 9.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLE--------VAYFD 388
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgediTGLPphriarlgIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 389 QHRATLdPDKTVMDNLAEG----KQEVMVNGRPRHVLGylqdfLFPP--KRAMTPVRALSGGERNRLLLAR-LFLKPSnL 461
Cdd:COG0410 85 EGRRIF-PSLTVEENLLLGayarRDRAEVRADLERVYE-----LFPRlkERRRQRAGTLSGGEQQMLAIGRaLMSRPK-L 157
|
....*..
gi 1437745527 462 LILDEPT 468
Cdd:COG0410 158 LLLDEPS 164
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-225 |
1.04e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.42 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDI- 79
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 80 ----EGTI-FDFvaqgvaedaqyiteyhRVSKVIETDPSeKNLNRLAQLQEVldnrnlwllDSRIAE-VLEKLGLNGEAE 153
Cdd:PRK09536 81 svpqDTSLsFEF----------------DVRQVVEMGRT-PHRSRFDTWTET---------DRAAVErAMERTGVAQFAD 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 154 --LSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIE---TILWLEKFLKDFQGSIVFISHDrsfiRNMATRIID 225
Cdd:PRK09536 135 rpVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINhqvRTLELVRRLVDDGKTAVAAIHD----LDLAARYCD 207
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
315-497 |
1.34e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.92 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 315 SGKIVFEleDVNYSI-GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GT---KLEVAYFDQ 389
Cdd:PRK13657 332 KGAVEFD--DVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTdirTVTRASLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 390 HRATL--DP---DKTVMDNLAEGK-----QEVMVNGRPRHVLgylqDFLF-PPKRAMTPV----RALSGGERNRLLLARL 454
Cdd:PRK13657 410 NIAVVfqDAglfNRSIEDNIRVGRpdatdEEMRAAAERAQAH----DFIErKPDGYDTVVgergRQLSGGERQRLAIARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1437745527 455 FLKPSNLLILDEPTNDLDVETLELLEELVDAyqgtvllVSHDR 497
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDE-------LMKGR 521
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
335-500 |
1.58e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.58 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 335 VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTK----LEVAyfdqhrATLDPDKTVMDNlaegkqe 410
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsalLELG------AGFHPELTGREN------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 411 VMVNGRprhVLGY-----------------LQDFLfppkraMTPVRALSGGERNRLLLA-RLFLKPsNLLILDEPtndLD 472
Cdd:COG1134 109 IYLNGR---LLGLsrkeidekfdeivefaeLGDFI------DQPVKTYSSGMRARLAFAvATAVDP-DILLVDEV---LA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1437745527 473 VetlelleelVDAY---------------QGTVLLVSHDREFV 500
Cdd:COG1134 176 V---------GDAAfqkkclarirelresGRTVIFVSHSMGAV 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-467 |
1.74e-14 |
|
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: 73.35 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 320 FELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklevaYFDQHRATLDP--- 396
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKI---------LLDGQDITKLPmhk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 397 -----------------DKTVMDNLAEGKQEVMVNGRPRH-----VLGYLQdflfppkraMTPVR-----ALSGGERNRL 449
Cdd:cd03218 72 rarlgigylpqeasifrKLTVEENILAVLEIRGLSKKEREekleeLLEEFH---------ITHLRkskasSLSGGERRRV 142
|
170
....*....|....*....
gi 1437745527 450 LLAR-LFLKPSNLLiLDEP 467
Cdd:cd03218 143 EIARaLATNPKFLL-LDEP 160
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
288-473 |
1.78e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 76.70 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 288 LKALRVERSERREVL------GSARMQVEEATRSGKIVFEleDVNYSIG-TRRLVRDFSAKVQRGDKIALVGPNGCGKTT 360
Cdd:TIGR01193 438 LQAARVANNRLNEVYlvdsefINKKKRTELNNLNGDIVIN--DVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKST 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 361 LLKLMLGDLKADSGRIHCGTKLeVAYFDQH--RATL-----DP---DKTVMDNLAEGKQEVMVNGRPRHVLGYLQ---DF 427
Cdd:TIGR01193 516 LAKLLVGFFQARSGEILLNGFS-LKDIDRHtlRQFInylpqEPyifSGSILENLLLGAKENVSQDEIWAACEIAEikdDI 594
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1437745527 428 LFPPKRAMTPVRA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR01193 595 ENMPLGYQTELSEegssISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-230 |
1.88e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 73.10 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 3 LISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTarlqqDPPRDIE-- 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-----DSKKDINkl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 ----GTIF-DF-------VAQGVAEdAQYiteyhRVSKVietdpSEKNLNRLAQlqevldnrnlwlldsriaEVLEKLGL 148
Cdd:COG1126 76 rrkvGMVFqQFnlfphltVLENVTL-API-----KVKKM-----SKAEAEERAM------------------ELLERVGL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 149 NGEAEL--SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QG-SIVFISHDRSFIRNMATRI 223
Cdd:COG1126 127 ADKADAypAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLakEGmTMVVVTHEMGFAREVADRV 206
|
....*..
gi 1437745527 224 IDLDRGK 230
Cdd:COG1126 207 VFMDGGR 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-516 |
2.21e-14 |
|
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: 72.56 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 320 FELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKL------------EVAY 386
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdGLKLtddkkninelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 387 FDQHrATLDPDKTVMDNLAEGkqEVMVNGRPR-----HVLGYLQDFLFPPKRAMTPvRALSGGERNRLLLAR-LFLKPSn 460
Cdd:cd03262 81 VFQQ-FNLFPHLTVLENITLA--PIKVKGMSKaeaeeRALELLEKVGLADKADAYP-AQLSGGQQQRVAIARaLAMNPK- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 461 LLILDEPTNDLD---VETLELLEELVdAYQG-TVLLVSHDREFVDnSVTECWIFEGDGVI 516
Cdd:cd03262 156 VMLFDEPTSALDpelVGEVLDVMKDL-AEEGmTMVVVTHEMGFAR-EVADRVIFMDDGRI 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
317-472 |
2.77e-14 |
|
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: 71.81 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 317 KIVFELEDVNYSI------GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMlgdlkadSGRIHCGTKlevayfdqh 390
Cdd:cd03213 1 GVTLSFRNLTVTVksspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAL-------AGRRTGLGV--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 391 ratldpdktvmdnlaegKQEVMVNGRPRH------VLGYLQ--DFLFP---PKRAM---TPVRALSGGERNRLLLAR-LF 455
Cdd:cd03213 65 -----------------SGEVLINGRPLDkrsfrkIIGYVPqdDILHPtltVRETLmfaAKLRGLSGGERKRVSIALeLV 127
|
170
....*....|....*..
gi 1437745527 456 LKPSnLLILDEPTNDLD 472
Cdd:cd03213 128 SNPS-LLFLDEPTSGLD 143
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
322-496 |
3.05e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.17 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 322 LEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQHR-----ATLDP 396
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRlmfqdARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 397 DKTVMDNLAEGkqeVMVNGRPR-----HVLGyLQDflfppkRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
Cdd:PRK11247 95 WKKVIDNVGLG---LKGQWRDAalqalAAVG-LAD------RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180
....*....|....*....|....*....
gi 1437745527 472 DVETLELLEELVDA----YQGTVLLVSHD 496
Cdd:PRK11247 165 DALTRIEMQDLIESlwqqHGFTVLLVTHD 193
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-230 |
3.35e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.60 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTarlqQDPP--RD 78
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT----HVPAenRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 79 IEG-----------TIFDFVAQGVaedaqyiteyhRVSKV--IETDPSEKNLNRLAQLQEvldnrnlwLLDSRIAEvlek 145
Cdd:PRK09452 88 VNTvfqsyalfphmTVFENVAFGL-----------RMQKTpaAEITPRVMEALRMVQLEE--------FAQRKPHQ---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 146 lglngeaelssLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGSI----VFISHDRSFIRNMAT 221
Cdd:PRK09452 145 -----------LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQEEALTMSD 213
|
....*....
gi 1437745527 222 RIIDLDRGK 230
Cdd:PRK09452 214 RIVVMRDGR 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-231 |
4.58e-14 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 72.13 E-value: 4.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAF-SDAPL-LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLVTArlqqDPP---R 77
Cdd:cd03252 1 ITFEHVRFRYkPDGPViLDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDgHDLALA----DPAwlrR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 78 DI-----EGTIFDfvaQGVAEDAQYITEYHRVSKVIETdpseknlNRLAQLQEVLdnrnlwlldSRIAEVLEK-LGLNGe 151
Cdd:cd03252 77 QVgvvlqENVLFN---RSIRDNIALADPGMSMERVIEA-------AKLAGAHDFI---------SELPEGYDTiVGEQG- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 152 aelSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG--SIVFISHDRSFIRNmATRIIDLDRG 229
Cdd:cd03252 137 ---AGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAHRLSTVKN-ADRIIVMEKG 212
|
..
gi 1437745527 230 KL 231
Cdd:cd03252 213 RI 214
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-241 |
4.71e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 75.67 E-value: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDAPLL-DNTDLFIDENERVCLVGRNGAGKSTLLRVLAKE-QPlddgqvvyeqdlvtarlqqdpprdI 79
Cdd:PLN03073 507 PIISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGElQP------------------------S 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 80 EGTIFDFVAQGVAEDAQyiteyHRVskvietDPSEKNLNRLAQLQEVLDNrnlwLLDSRIAEVLEKLGLNGEAELSS--- 156
Cdd:PLN03073 563 SGTVFRSAKVRMAVFSQ-----HHV------DGLDLSSNPLLYMMRCFPG----VPEQKLRAHLGSFGVTGNLALQPmyt 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 157 LSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLSSWPG 236
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHG 707
|
....*
gi 1437745527 237 NYDKY 241
Cdd:PLN03073 708 TFHDY 712
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
330-501 |
5.57e-14 |
|
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: 71.70 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 330 GTRRL--VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHcgtklevaYFDQHRATldpdktvmdNLAEG 407
Cdd:COG4778 20 GGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL--------VRHDGGWV---------DLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 408 KQEVMVNGRpRHVLGYLQDFL--------------------FPPKRAMTPVRAL------------------SGGERNRL 449
Cdd:COG4778 83 SPREILALR-RRTIGYVSQFLrviprvsaldvvaepllergVDREEARARARELlarlnlperlwdlppatfSGGEQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 450 LLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAY--QGTVLL-VSHDREFVD 501
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkaRGTAIIgIFHDEEVRE 216
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-224 |
5.67e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 73.23 E-value: 5.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLVTA----------RLQ---QDP-----PRDi 79
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgQDITGLsgrelrplrrRMQmvfQDPyaslnPRM- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 80 egTIFDFVAQGVaedaqyitEYHRVskvieTDPSEknlnrlaqlqevldnrnlwlLDSRIAEVLEKLGLNGEA------E 153
Cdd:COG4608 113 --TVGDIIAEPL--------RIHGL-----ASKAE--------------------RRERVAELLELVGLRPEHadryphE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 154 LSslsGGWLRKAALGRALVSAPKVLFLDEPTNHLD--IET-ILWLekfLKDFQG----SIVFISHDRSFIRNMATRII 224
Cdd:COG4608 158 FS---GGQRQRIGIARALALNPKLIVCDEPVSALDvsIQAqVLNL---LEDLQDelglTYLFISHDLSVVRHISDRVA 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-231 |
6.44e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 74.82 E-value: 6.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 15 DAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQV-VYEQDLVTARLQ----------QDPPRdIEGTI 83
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlIDGVDIRDLTLEslrrqigvvpQDTFL-FSGTI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 84 FDFVAQGvAEDAqyiTEyHRVSKVIetdpseknlnRLAQLQEVLDNrnlwL---LDSRIAEvleklglNGeaelSSLSGG 160
Cdd:COG1132 431 RENIRYG-RPDA---TD-EEVEEAA----------KAAQAHEFIEA----LpdgYDTVVGE-------RG----VNLSGG 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 161 WLRKAALGRALVSAPKVLFLDEPTNHLDIET-ILWLEKFLKDFQGSIVF-ISHDRSFIRNmATRIIDLDRGKL 231
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETeALIQEALERLMKGRTTIvIAHRLSTIRN-ADRILVLDDGRI 552
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
320-498 |
6.74e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 70.97 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 320 FELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKAD---SGRIhcgtklevaYFDQHRATLDP 396
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEV---------LLNGRRLTALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 397 dktvmdnlAEgkqevmvngrPRHVlGYL--QDFLFP---------------PKRAMTPVRA------------------- 440
Cdd:COG4136 73 --------AE----------QRRI-GILfqDDLLFPhlsvgenlafalpptIGRAQRRARVeqaleeaglagfadrdpat 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 441 LSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLDVETLELLEELV----DAYQGTVLLVSHDRE 498
Cdd:COG4136 134 LSGGQRARVALLRaLLAEPRALL-LDEPFSKLDAALRAQFREFVfeqiRQRGIPALLVTHDEE 195
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-249 |
7.43e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.38 E-value: 7.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 12 AFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLA-KEQPlDDGQVvyeqdlvtarlqqdpprdiegTIFDFVaqg 90
Cdd:PRK11819 333 SFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITgQEQP-DSGTI---------------------KIGETV--- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 91 vaedaqyiteyhRVSKVietDPSEKNLNrlaqlqevlDNRNLWLLDSRIAEVLeKLG---LNGEAELSS----------- 156
Cdd:PRK11819 388 ------------KLAYV---DQSRDALD---------PNKTVWEEISGGLDII-KVGnreIPSRAYVGRfnfkggdqqkk 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 157 ---LSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDL-DRGKLS 232
Cdd:PRK11819 443 vgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFeGDSQVE 522
|
250
....*....|....*..
gi 1437745527 233 SWPGNYDKYLESKEEAL 249
Cdd:PRK11819 523 WFEGNFQEYEEDKKRRL 539
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-245 |
8.52e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 74.78 E-value: 8.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 16 APLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKeqplddgqvVYEQDLVTARLQQDPPRDIEGTIFdfvaqgvaedA 95
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVG---------FFQARSGEILLNGFSLKDIDRHTL----------R 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 96 QYITeYHRVSKVIETDPSEKNLnrLAQLQEVLDNRNLWLLdSRIAEV---LEKLGLNGEAELS----SLSGGWLRKAALG 168
Cdd:TIGR01193 548 QFIN-YLPQEPYIFSGSILENL--LLGAKENVSQDEIWAA-CEIAEIkddIENMPLGYQTELSeegsSISGGQKQRIALA 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 169 RALVSAPKVLFLDEPTNHLDIET---IlwLEKFLKDFQGSIVFISHdRSFIRNMATRIIDLDRGKLSSwPGNYDKYLESK 245
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITekkI--VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIE-QGSHDELLDRN 699
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-231 |
8.96e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 71.73 E-value: 8.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQV-VYEQDlvtarLQQDPPRDIE 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrLNGRP-----LADWSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 GTI----------FDFvaqgvaedaqyiteyhRVSKVIEtdpseknLNRLAQLQEVLDNRNLwlldsrIAEVLEKLGLNG 150
Cdd:PRK13548 76 RRRavlpqhsslsFPF----------------TVEEVVA-------MGRAPHGLSRAEDDAL------VAAALAQVDLAH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 151 EAELS--SLSGGWLRKAALGRALV------SAPKVLFLDEPTNHLDI---ETILWLEK-FLKDFQGSIVFISHDrsfiRN 218
Cdd:PRK13548 127 LAGRDypQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLahqHHVLRLARqLAHERGLAVIVVLHD----LN 202
|
250
....*....|....*..
gi 1437745527 219 MAT----RIIDLDRGKL 231
Cdd:PRK13548 203 LAAryadRIVLLHQGRL 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
29-192 |
1.25e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.29 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 29 NERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEqdlvtarlqqdpPRDIEGTifdfvaqGVAEDAQYITeyHRvskvi 108
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLD------------GGDIDDP-------DVAEACHYLG--HR----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 109 etDPSEKNLNrlaqlqeVLDNRNLW--LL---DSRIAEVLEKLGLNGEAEL--SSLSGGWLRKAALGRALVSAPKVLFLD 181
Cdd:PRK13539 82 --NAMKPALT-------VAENLEFWaaFLggeELDIAAALEAVGLAPLAHLpfGYLSAGQKRRVALARLLVSNRPIWILD 152
|
170
....*....|.
gi 1437745527 182 EPTNHLDIETI 192
Cdd:PRK13539 153 EPTAALDAAAV 163
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-226 |
1.38e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.57 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 12 AFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQ--DPPRDIEGTIFDFVAQ 89
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsEVPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 90 GvaedaqyiteyhrvskvieTDPSEKNLNRLAQlqevlDNRnlwlldSRIAEVLEKLGLNGEAE--LSSLSGGWLRKAAL 167
Cdd:NF040873 81 G-------------------RWARRGLWRRLTR-----DDR------AAVDDALERVGLADLAGrqLGELSGGQRQRALL 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745527 168 GRALVSAPKVLFLDEPTNHLDIET---ILWLEKFLKDFQGSIVFISHDRSFIRNmATRIIDL 226
Cdd:NF040873 131 AQGLAQEADLLLLDEPTTGLDAESrerIIALLAEEHARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
321-467 |
1.58e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.44 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklevaYFDQHRATLDPdktv 400
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI---------FLDGEDITHLP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 401 mdnlaegkqevmVNGRPRHVLGYL-QD------------------FLFPPKRAM-------------TPVR-----ALSG 443
Cdd:COG1137 72 ------------MHKRARLGIGYLpQEasifrkltvednilavleLRKLSKKEReerleelleefgiTHLRkskaySLSG 139
|
170 180
....*....|....*....|....*
gi 1437745527 444 GERNRLLLAR-LFLKPSNLLiLDEP 467
Cdd:COG1137 140 GERRRVEIARaLATNPKFIL-LDEP 163
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-231 |
1.62e-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: 70.09 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 3 LISLTGAYLAFSDAPL----LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQ-DLVTArlqqdpPR 77
Cdd:cd03266 1 MITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKE------PA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 78 DIEGTIfdfvaqGVAEDAQYITEYHRVSKVIETDPSEKNLNRLAQLQevldnrnlwlldsRIAEVLEKLGLNGEAE--LS 155
Cdd:cd03266 75 EARRRL------GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTA-------------RLEELADRLGMEELLDrrVG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 156 SLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDI---ETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03266 136 GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVmatRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
328-500 |
1.76e-13 |
|
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: 70.25 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 328 SIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI--HCGTK--LEVAYFdqhratLDPDKTVMDN 403
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtvRGRVSslLGLGGG------FNPELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 404 laegkqeVMVNGRprhVLGYLQDFLfppkRAM---------------TPVRALSGGERNRLLLA-RLFLKPsNLLILDEP 467
Cdd:cd03220 105 -------IYLNGR---LLGLSRKEI----DEKideiiefselgdfidLPVKTYSSGMKARLAFAiATALEP-DILLIDEV 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 1437745527 468 TNDLDVETLELLEELVDAYQ---GTVLLVSHDREFV 500
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLkqgKTVILVSHDPSSI 205
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
337-512 |
2.21e-13 |
|
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: 70.13 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 337 DFSAKVQRGD-----KIALVGPNGCGKTTLLKLMLGDLKADSGRIhcGTKLE-VAYFDQHrATLDPDKTVMDNLAEG--- 407
Cdd:cd03237 12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--EIELDtVSYKPQY-IKADYEGTVRDLLSSItkd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 408 -------KQEVMvngRPRHVLGYLQdflfppkramTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd03237 89 fythpyfKTEIA---KPLQIEQILD----------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1437745527 481 ELVDAY----QGTVLLVSHDREFVDNSVTECWIFEG 512
Cdd:cd03237 156 KVIRRFaennEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
331-472 |
2.48e-13 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 69.61 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 331 TRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKL---MLGDLKADSGRIHCG--------TKLEVAYFDQHRATLdPDKT 399
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAisgRVEGGGTTSGQILFNgqprkpdqFQKCVAYVRQDDILL-PGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 400 VMDNLA-------------EGKQEVMVNGRPRHVlgylqdflfppkrAMTPVR-----ALSGGERNRLLLARLFLKPSNL 461
Cdd:cd03234 98 VRETLTytailrlprkssdAIRKKRVEDVLLRDL-------------ALTRIGgnlvkGISGGERRRVSIAVQLLWDPKV 164
|
170
....*....|.
gi 1437745527 462 LILDEPTNDLD 472
Cdd:cd03234 165 LILDEPTSGLD 175
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-231 |
2.55e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 71.76 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK-EQPlDDGQVVY---------EQDLVTARlqqdppRDIeGTIFD-F- 86
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLlERP-TSGRVLVdgqdltalsEKELRKAR------RQI-GMIFQhFn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 87 ------VAQGVAEdaqyiteyhrvskvietdPSEknlnrlaqlqevLDNRNLWLLDSRIAEVLEKLGLNGEAEL--SSLS 158
Cdd:PRK11153 93 llssrtVFDNVAL------------------PLE------------LAGTPKAEIKARVTELLELVGLSDKADRypAQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 159 GGWLRKAALGRALVSAPKVLFLDEPTNHLDIET---ILWLekfLKDFQG----SIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATtrsILEL---LKDINRelglTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-231 |
2.76e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.04 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVvyeqdlvtarlqqdpprDIEGTIFDFvaqgvaedaqyi 98
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL-----------------NIAGNHFDF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 99 teyhrvskviETDPSEKNLNRLAQ-LQEVLDNRNLW--------LLDS--------------RIAEVLEKLGLNGEAEL- 154
Cdd:PRK11124 69 ----------SKTPSDKAIRELRRnVGMVFQQYNLWphltvqqnLIEApcrvlglskdqalaRAEKLLERLRLKPYADRf 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 155 -SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGS-I--VFISHDRSFIRNMATRIIDLDRGK 230
Cdd:PRK11124 139 pLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgItqVIVTHEVEVARKTASRVVYMENGH 218
|
.
gi 1437745527 231 L 231
Cdd:PRK11124 219 I 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-230 |
2.92e-13 |
|
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: 69.23 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVyeqdlvtarlqqdpprdIEGTI 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL-----------------FDGKP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 84 FDFVAQgvaEDAQYITE---YHRVSKVIEtdpsekNLNRLAQLqevldnRNLWLLD--SRIAEVLEKLGLNGEAE--LSS 156
Cdd:cd03269 64 LDIAAR---NRIGYLPEergLYPKMKVID------QLVYLAQL------KGLKKEEarRRIDEWLERLELSEYANkrVEE 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 157 LSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG---SIVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:cd03269 129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-234 |
3.59e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.53 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 14 SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDP--PrdiEGTIFDFVA--- 88
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPylP---LGTLREALLypa 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 89 -QGVAEDAQYITEYHRVskvietdpseknlnRLAQLQEVLDNRNLWlldSRIaevleklglngeaelssLSGGWLRKAAL 167
Cdd:COG4178 451 tAEAFSDAELREALEAV--------------GLGHLAERLDEEADW---DQV-----------------LSLGEQQRLAF 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 168 GRALVSAPKVLFLDEPTNHLDIETILWLEKFLKD--FQGSIVFISHdRSFIRNMATRIIDLDRGklSSW 234
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGD--GSW 562
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-231 |
3.73e-13 |
|
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: 72.44 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 15 DAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDI----------EGTIF 84
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQValvsqdvvlfNDTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 85 DFVAQGvaEDAQYITEyhRVSKVIETdpseknlnrlAQLQEVLDNRNLWLlDSRIaevleklGLNGeaelSSLSGGWLRK 164
Cdd:TIGR02203 424 NNIAYG--RTEQADRA--EIERALAA----------AYAQDFVDKLPLGL-DTPI-------GENG----VLLSGGQRQR 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 165 AALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQ---GSIVfISHDRSFIRNmATRIIDLDRGKL 231
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMqgrTTLV-IAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-231 |
3.76e-13 |
|
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: 69.28 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYeQDLVTARLQQDPPRDIeGTIFDFVAQgVA 92
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV-AGLVPWKRRKKFLRRI-GVVFGQKTQ-LW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 93 EDAQYITEYHRVSKVIETDPSEKNlNRLAQLQEVLDnrnlwlldsrIAEVLEKlglngeaELSSLSGGWLRKAALGRALV 172
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPARFK-KRLDELSELLD----------LEELLDT-------PVRQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 173 SAPKVLFLDEPTNHLDIETILWLEKFLKDF----QGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-231 |
3.84e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.78 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLA-KEQPlDDGQV-VYEQDLVTAR---LQQDP 75
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlLEQP-EAGTIrVGDITIDTARslsQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 76 PRDIEGTIfDFVAQGvaedaqYITEYHR--VSKVIETDPSEKNLNRLAQLQevldnrnlwlldsRIAEVLEKLGLNGE-- 151
Cdd:PRK11264 80 IRQLRQHV-GFVFQN------FNLFPHRtvLENIIEGPVIVKGEPKEEATA-------------RARELLAKVGLAGKet 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 152 AELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIE---TILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDR 228
Cdd:PRK11264 140 SYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPElvgEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQ 219
|
...
gi 1437745527 229 GKL 231
Cdd:PRK11264 220 GRI 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-231 |
3.97e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 68.35 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLA--KEQPLDDGQVvyeqdLVTAR-LQQDPPRDIEGtifdFVAQgvaE 93
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEV-----LINGRpLDKRSFRKIIG----YVPQ---D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 94 DAqyiteyhrvskVIETDPSEKNLnrlaqlqevldnrnlwlldsRIAevleklglngeAELSSLSGGWLRKAALGRALVS 173
Cdd:cd03213 91 DI-----------LHPTLTVRETL--------------------MFA-----------AKLRGLSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745527 174 APKVLFLDEPTNHLDIETILWLEKFLKDF--QG-SIVFISHD-RSFIRNMATRIIDLDRGKL 231
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLadTGrTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
335-496 |
4.30e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.50 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 335 VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CG---TKLEVAY-------FDQhRATLDPDKTVMDN 403
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGyvpFKRRKEFarrigvvFGQ-RSQLWWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 404 L-----------AEGKQ--EVMVNgrprhVLGyLQDFLfppkraMTPVRALSGGERNRL-LLARLFLKPSnLLILDEPTN 469
Cdd:COG4586 117 FrllkaiyripdAEYKKrlDELVE-----LLD-LGELL------DTPVRQLSLGQRMRCeLAAALLHRPK-ILFLDEPTI 183
|
170 180 190
....*....|....*....|....*....|.
gi 1437745527 470 DLDVETLELLEELVDAY----QGTVLLVSHD 496
Cdd:COG4586 184 GLDVVSKEAIREFLKEYnrerGTTILLTSHD 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
322-498 |
4.82e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.84 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 322 LEDVNYSIgtRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKlevayfdQHRAT-------- 393
Cdd:PRK10771 4 LTDITWLY--HHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-------DHTTTppsrrpvs 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 394 -------LDPDKTVMDNLAEG---------KQEVMVNGRPRHVlgYLQDFL--FPPkramtpvrALSGGERNRLLLARLF 455
Cdd:PRK10771 75 mlfqennLFSHLTVAQNIGLGlnpglklnaAQREKLHAIARQM--GIEDLLarLPG--------QLSGGQRQRVALARCL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1437745527 456 LKPSNLLILDEPTNDLDVETLELLEELVDAY----QGTVLLVSHDRE 498
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLVSQVcqerQLTLLMVSHSLE 191
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-231 |
5.24e-13 |
|
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: 68.90 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARlqqdPP--RDIEgtifdFVAQGVAedaq 96
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL----PPekRDIS-----YVPQNYA---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 97 yITEYHRVSKVIETDPSEKNLNRLAQLQEVLDnrnlwlldsrIAEVL--EKLgLNGEAElsSLSGGWLRKAALGRALVSA 174
Cdd:cd03299 82 -LFPHMTVYKNIAYGLKKRKVDKKEIERKVLE----------IAEMLgiDHL-LNRKPE--TLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745527 175 PKVLFLDEPTNHLDIET----ILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03299 148 PKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
224-300 |
5.82e-13 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 64.52 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 224 IDLDRGKLSSWPGNYDKYLESKEEALRVEEQQNAEFDRKLAQEEAWI-RQGIKARRTR-NEGRVRALKAL-RVERSERRE 300
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIdRFRAKASKAKqAQSRIKALEKMeRIEKPERDK 80
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
321-498 |
6.69e-13 |
|
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: 68.42 E-value: 6.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKlEVAYFD----------QH 390
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK-DITNLPphkrpvntvfQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 391 RAtLDPDKTVMDNLAEG-----------KQEVMVNGRPRHVLGYLQDFlfppkramtpVRALSGGERNRLLLAR-LFLKP 458
Cdd:cd03300 81 YA-LFPHLTVFENIAFGlrlkklpkaeiKERVAEALDLVQLEGYANRK----------PSQLSGGQQQRVAIARaLVNEP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1437745527 459 SnLLILDEPTNDLDVETLELLEELVDAYQG----TVLLVSHDRE 498
Cdd:cd03300 150 K-VLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQE 192
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-227 |
7.20e-13 |
|
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: 68.97 E-value: 7.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 26 IDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPrDIEGTIFDFVA---QGVAEDAQYITEYh 102
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKA-DYEGTVRDLLSsitKDFYTHPYFKTEI- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 103 rvskvietdpseknLNRLaQLQEVLDNrnlwlldsriaevleklglngeaELSSLSGGWLRKAALGRALVSAPKVLFLDE 182
Cdd:cd03237 100 --------------AKPL-QIEQILDR-----------------------EVPELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1437745527 183 PTNHLDIETILWLEKFLKDF----QGSIVFISHDRSFIRNMATRIIDLD 227
Cdd:cd03237 142 PSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
13-231 |
7.44e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.11 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDL--VTARLQQdpprdiegtiFDFVAQ 89
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgTDVsrLHARDRK----------VGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 90 GVAEdAQYITEYHRVSKVIETDPSEKNLNRLAqlqevldnrnlwlLDSRIAEVLEKLGLNGEAEL--SSLSGGWLRKAAL 167
Cdd:PRK10851 82 HYAL-FRHMTVFDNIAFGLTVLPRRERPNAAA-------------IKAKVTQLLEMVQLAHLADRypAQLSGGQKQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 168 GRALVSAPKVLFLDEPTNHLDI----ETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-231 |
8.05e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.94 E-value: 8.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK-EQPlDDGQVVYEqdlvTARLQQdpPRDIEGTIFdfvaqgv 91
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGlETP-SAGELLAG----TAPLAE--AREDTRLMF------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 92 aEDAqyiteyhrvskvietdpseknlnRLAQLQEVLDNRNL-----WLLDSRiaEVLEKLGLNGEAE--LSSLSGGWLRK 164
Cdd:PRK11247 88 -QDA-----------------------RLLPWKKVIDNVGLglkgqWRDAAL--QALAAVGLADRANewPAALSGGQKQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 165 AALGRALVSAPKVLFLDEPTNHLD----------IETiLWLEkflkdfQG-SIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDaltriemqdlIES-LWQQ------HGfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-230 |
1.03e-12 |
|
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: 68.03 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQV------VYEQDLVTAR-----LQQDPPRdIEGTIFD 85
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlidghdVRDYTLASLRrqiglVSQDVFL-FNDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 86 FVAQGV--AEDAQyiteyhrvskVIETdpseknlNRLAQLQEVLDNRNLWLlDSRIAEvleklglNGeaelSSLSGGWLR 163
Cdd:cd03251 95 NIAYGRpgATREE----------VEEA-------ARAANAHEFIMELPEGY-DTVIGE-------RG----VKLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745527 164 KAALGRALVSAPKVLFLDEPTNHLDIETILW----LEKFLKDfQGSIVfISHDRSFIRNmATRIIDLDRGK 230
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTESERLvqaaLERLMKN-RTTFV-IAHRLSTIEN-ADRIVVLEDGK 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-247 |
1.09e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.54 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 3 LISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDD------------GQVVYEQDLVTAR 70
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdgkvlyfGKDIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 71 LQ-----QDPPRDIEGTIFDFVAQGVAEDAqyITEYHRVSKVIEtdpseknlnrlaqlqEVLDNRNLWlldsriAEVLEK 145
Cdd:PRK14246 90 KEvgmvfQQPNPFPHLSIYDNIAYPLKSHG--IKEKREIKKIVE---------------ECLRKVGLW------KEVYDR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 146 LglngEAELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG--SIVFISHDRSFIRNMATRI 223
Cdd:PRK14246 147 L----NSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV 222
|
250 260
....*....|....*....|....
gi 1437745527 224 IDLDRGKLSSWPGNYDKYLESKEE 247
Cdd:PRK14246 223 AFLYNGELVEWGSSNEIFTSPKNE 246
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
333-496 |
1.11e-12 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 67.06 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 333 RLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKlEVAY----FDQHRATL-----DPDK----- 398
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGE-PLDYsrkgLLERRQRVglvfqDPDDqlfaa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 399 TVMDNLA-----EGKQEVMVNGRPRHVLGYL--QDFlfppkrAMTPVRALSGGERNRLLLA-RLFLKPsNLLILDEPTND 470
Cdd:TIGR01166 85 DVDQDVAfgplnLGLSEAEVERRVREALTAVgaSGL------RERPTHCLSGGEKKRVAIAgAVAMRP-DVLLLDEPTAG 157
|
170 180
....*....|....*....|....*....
gi 1437745527 471 LDVETLELLEELVD---AYQGTVLLVSHD 496
Cdd:TIGR01166 158 LDPAGREQMLAILRrlrAEGMTVVISTHD 186
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
321-496 |
1.12e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 68.19 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGtKLEVAYFdqhratldPDKTV 400
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD-GLDVATT--------PSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 401 MDNLAEGKQEVMVN------------------GRP-----RHV---LGYLQdflfppkraMTPVRA-----LSGGERNRL 449
Cdd:COG4604 74 AKRLAILRQENHINsrltvrelvafgrfpyskGRLtaedrEIIdeaIAYLD---------LEDLADryldeLSGGQRQRA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1437745527 450 LLARLFLKPSNLLILDEPTNDLD----VETLELLEELVDAYQGTVLLVSHD 496
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADELGKTVVIVLHD 195
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-250 |
1.12e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 67.86 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 23 DLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARlqqdPP--RDI-----EGTIFDF--VAQGVAe 93
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL----PPaeRPVsmlfqENNLFPHltVAQNIG- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 94 daqyiteyhrvskvIETDPSEKnLNRLAQlqevldnrnlwlldSRIAEVLEKLGLNG-EAEL-SSLSGGWLRKAALGRAL 171
Cdd:COG3840 94 --------------LGLRPGLK-LTAEQR--------------AQVEQALERVGLAGlLDRLpGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 172 VSAPKVLFLDEPTNHLDI----ETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLsSWPGNYDKYLESK-E 246
Cdd:COG3840 145 VRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRI-AADGPTAALLDGEpP 223
|
....
gi 1437745527 247 EALR 250
Cdd:COG3840 224 PALA 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-231 |
1.32e-12 |
|
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: 66.47 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDA--PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLVTARLQQdpPRDIE 80
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDgADISQWDPNE--LGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 GTifdfvaqgVAEDAQyiteyhrvskvietdpseknlnrlaqlqevldnrnlwLLDSRIAEVLeklglngeaelssLSGG 160
Cdd:cd03246 79 GY--------LPQDDE-------------------------------------LFSGSIAENI-------------LSGG 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 161 WLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQ---GSIVFISHDRSFIRnMATRIIDLDRGKL 231
Cdd:cd03246 101 QRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
335-495 |
1.39e-12 |
|
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: 67.39 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 335 VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklEVAYFDQHRATLD--------PDK-------T 399
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA------TVDGFDVVKEPAEarrrlgfvSDStglydrlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 400 VMDNLA-----EGKQEVMVNGRPRHVLGYLQDFLFPPKRamtpVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03266 95 ARENLEyfaglYGLKGDELTARLEELADRLGMEELLDRR----VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180
....*....|....*....|....
gi 1437745527 475 TLELLEELVDAY---QGTVLLVSH 495
Cdd:cd03266 171 ATRALREFIRQLralGKCILFSTH 194
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-211 |
1.54e-12 |
|
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: 66.61 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVvyeqdlvtaRLQQDPPrdiegtifdfvaqgvaedAQ 96
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV---------RWNGTPL------------------AE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 97 YITEYHRVSKVIetdpseKNLNRLAQLQEVLDNRNLWLLDSR-----IAEVLEKLGLNGEAEL--SSLSGGWLRKAALGR 169
Cdd:TIGR01189 67 QRDEPHENILYL------GHLPGLKPELSALENLHFWAAIHGgaqrtIEDALAAVGLTGFEDLpaAQLSAGQQRRLALAR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1437745527 170 ALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF---QGSIVFISH 211
Cdd:TIGR01189 141 LWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-230 |
1.70e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.48 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK-EQPlDDGQVVYE-QDLVTARLQQDPprd 78
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQP-TAGQIMLDgVDLSHVPPYQRP--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 79 iegtiFDFVAQGVAedaqyITEYHRVSKVIETDPSEKNLNRLAqlqevldnrnlwlLDSRIAEVLEKLGLNGEAELS--S 156
Cdd:PRK11607 93 -----INMMFQSYA-----LFPHMTVEQNIAFGLKQDKLPKAE-------------IASRVNEMLGLVHMQEFAKRKphQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 157 LSGGWLRKAALGRALVSAPKVLFLDEPTNHLD--IETILWLE--KFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-230 |
1.71e-12 |
|
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: 70.10 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTL----LRVLAKEqplddGQVVYE-QDLVT----------ARLQ---QDP----- 75
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPSE-----GEIRFDgQDLDGlsrralrplrRRMQvvfQDPfgsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 76 PRdieGTIFDFVAQGVAedaqyiteYHRvskvIETDPSEKnlnrlaqlqevldnrnlwllDSRIAEVLEKLGLNGEA--- 152
Cdd:COG4172 377 PR---MTVGQIIAEGLR--------VHG----PGLSAAER--------------------RARVAEALEEVGLDPAArhr 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 153 ---ElssLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIET---ILWLekfLKDFQG----SIVFISHDRSFIRNMATR 222
Cdd:COG4172 422 yphE---FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVqaqILDL---LRDLQRehglAYLFISHDLAVVRALAHR 495
|
....*...
gi 1437745527 223 IIDLDRGK 230
Cdd:COG4172 496 VMVMKDGK 503
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
316-473 |
1.88e-12 |
|
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: 67.25 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 316 GKIVFEleDVNYSIGTRRLV-RDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGtklEVAYFDQHRATL 394
Cdd:cd03254 1 GEIEFE--NVNFSYDEKKPVlKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID---GIDIRDISRKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 ---------DP---DKTVMDNLAEGKQ-----EVMVNGRPRHvlgyLQDFL-FPPKRAMTPVR----ALSGGERNRLLLA 452
Cdd:cd03254 76 rsmigvvlqDTflfSGTIMENIRLGRPnatdeEVIEAAKEAG----AHDFImKLPNGYDTVLGenggNLSQGERQLLAIA 151
|
170 180
....*....|....*....|.
gi 1437745527 453 RLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDT 172
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
17-231 |
1.93e-12 |
|
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: 67.33 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKE-QP-----LDDGQVVYEQDLVTARlqqdppRDIegtifDFVAQG 90
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEPtsgeiFIDGEDIREQDPVELR------RKI-----GYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 91 VAedaqyITEYHRVSKVIETDPseknlnrlaQLQEVLDNRnlwlLDSRIAEVLEKLGLnGEAEL-----SSLSGGWLRKA 165
Cdd:cd03295 84 IG-----LFPHMTVEENIALVP---------KLLKWPKEK----IRERADELLALVGL-DPAEFadrypHELSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 166 ALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQ----GSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
319-498 |
2.10e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.09 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 319 VFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKLE--------VAYFDQ 389
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdGVDLShvppyqrpINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 390 HRAtLDPDKTVMDNLAEG-KQEVM----VNGRPRHVLG--YLQDFlfppkrAMTPVRALSGGERNRLLLARLFLKPSNLL 462
Cdd:PRK11607 99 SYA-LFPHMTVEQNIAFGlKQDKLpkaeIASRVNEMLGlvHMQEF------AKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1437745527 463 ILDEPTNDLDVETLELLEELV----DAYQGTVLLVSHDRE 498
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMQLEVvdilERVGVTCVMVTHDQE 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-231 |
2.80e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.59 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 12 AFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK-EQPlDDGQVVYEQDLVTAR-LQQdppRDIeGTIFD---- 85
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKP-TEGQIFIDGEDVTHRsIQQ---RDI-CMVFQsyal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 86 FVAQGVAEDAQYITEYHRVSKvietdpSEKNlnrlaqlqevldnrnlwlldSRIAEVLEKLGLNGEAE--LSSLSGGWLR 163
Cdd:PRK11432 90 FPHMSLGENVGYGLKMLGVPK------EERK--------------------QRVKEALELVDLAGFEDryVDQISGGQQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 164 KAALGRALVSAPKVLFLDEPTNHLDI-------ETILWLEkflKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK11432 144 RVALARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQ---QQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-231 |
2.82e-12 |
|
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: 66.40 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVvyeqdlvtarlqqdpprDIEGtifdfvaqgvaedaqyi 98
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-----------------TVRG----------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 99 teyhRVSKVIET----DPS---EKNLNRLAQLQEVLDNRnlwlLDSRIAEVLE--KLGLNGEAELSSLSGGwlRKAALGR 169
Cdd:cd03220 84 ----RVSSLLGLgggfNPEltgRENIYLNGRLLGLSRKE----IDEKIDEIIEfsELGDFIDLPVKTYSSG--MKARLAF 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 170 ALVSA--PKVLFLDEPTNHLDIETILWLEKFLKDFQ---GSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03220 154 AIATAlePDILLIDEVLAVGDAAFQEKCQRRLRELLkqgKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
311-498 |
2.85e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 68.82 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 311 EATRSGKIVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH----CGTKL---- 382
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMldgqDITHVpaen 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 383 -EVAYFDQHRAtLDPDKTVMDNLAEG-------KQEVmvngRPRhVLG-----YLQDFlfppkrAMTPVRALSGGERNRL 449
Cdd:PRK09452 86 rHVNTVFQSYA-LFPHMTVFENVAFGlrmqktpAAEI----TPR-VMEalrmvQLEEF------AQRKPHQLSGGQQQRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 450 LLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQG----TVLLVSHDRE 498
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklgiTFVFVTHDQE 206
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
324-472 |
3.84e-12 |
|
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: 66.44 E-value: 3.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 324 DVNYSIGTRRLvRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLEVAYFDQHRA------- 392
Cdd:cd03256 7 SKTYPNGKKAL-KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdiNKLKGKALRQLRRqigmifq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 393 --TLDPDKTVMDNlaegkqeVMVnGRprhvLGYLQDF-----LFPP----------------KRAMTPVRALSGGERNRL 449
Cdd:cd03256 86 qfNLIERLSVLEN-------VLS-GR----LGRRSTWrslfgLFPKeekqralaalervgllDKAYQRADQLSGGQQQRV 153
|
170 180
....*....|....*....|...
gi 1437745527 450 LLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLD 176
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
310-472 |
4.76e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.70 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 310 EEATRSGKIVFELEDVN--YSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYF 387
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSftYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 388 DQH-RATLdpdkTVM------------DNLAEGK----QEVMVngrprHVL---GyLQDFLFPPKRAMTPV----RALSG 443
Cdd:PRK11160 409 EAAlRQAI----SVVsqrvhlfsatlrDNLLLAApnasDEALI-----EVLqqvG-LEKLLEDDKGLNAWLgeggRQLSG 478
|
170 180
....*....|....*....|....*....
gi 1437745527 444 GERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
14-212 |
4.83e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 66.70 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 14 SDAPL-LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDIeGTIF-----DFV 87
Cdd:PRK13648 19 SDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI-GIVFqnpdnQFV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 88 AQGVAEDAQYITEYHRVskvietdPSEKnlnrlaqlqevldnrnlwlLDSRIAEVLEKLGLNGEA--ELSSLSGGWLRKA 165
Cdd:PRK13648 98 GSIVKYDVAFGLENHAV-------PYDE-------------------MHRRVSEALKQVDMLERAdyEPNALSGGQKQRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1437745527 166 ALGRALVSAPKVLFLDEPTNHLDIE---TILWLEKFLK-DFQGSIVFISHD 212
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDarqNLLDLVRKVKsEHNITIISITHD 202
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
336-467 |
5.13e-12 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 65.18 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 336 RDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKleVAY---------------------FDQHR--- 391
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYvsqepwiqngtirenilfgkpFDEERyek 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 392 ----ATLDPDktvMDNLAEGKQ-EVMVNGrprhvlgylqdflfppkramtpvRALSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:cd03250 100 vikaCALEPD---LEILPDGDLtEIGEKG-----------------------INLSGGQKQRISLARAVYSDADIYLLDD 153
|
.
gi 1437745527 467 P 467
Cdd:cd03250 154 P 154
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
324-473 |
5.53e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.19 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 324 DVNYsiGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFD----QHRATLDPDKT 399
Cdd:PRK11231 9 TVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrqlaRRLALLPQHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 400 VmdnlAEG--KQEVMVNGRPRHV--LGYL-QDFLFPPKRAMT----------PVRALSGGERNRLLLARLFLKPSNLLIL 464
Cdd:PRK11231 87 T----PEGitVRELVAYGRSPWLslWGRLsAEDNARVNQAMEqtrinhladrRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
....*....
gi 1437745527 465 DEPTNDLDV 473
Cdd:PRK11231 163 DEPTTYLDI 171
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-233 |
5.70e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.96 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQ-----QDPPRDIeGTIFDFvaqgvae 93
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKkikevKRLRKEI-GLVFQF------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 94 daqyiTEYHRVSKVIETDPSEKNLNRLAQLQEVLdnrnlwlldSRIAEVLEKLGLNGEAELSS---LSGGWLRKAALGRA 170
Cdd:PRK13645 99 -----PEYQLFQETIEKDIAFGPVNLGENKQEAY---------KKVPELLKLVQLPEDYVKRSpfeLSGGQKRRVALAGI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 171 LVSAPKVLFLDEPTNHLDI----ETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLSS 233
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-231 |
6.01e-12 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 64.76 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 14 SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARlqqdPPRDiegtifdFVAQGVAe 93
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR----SPRD-------AIRAGIA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 94 daqYITEyhrvskvietdpseknlNRLAQLqeVLDNRNlwlldsriaeVLEKLGLNgeaelSSLSGGWLRKAALGRALVS 173
Cdd:cd03215 79 ---YVPE-----------------DRKREG--LVLDLS----------VAENIALS-----SLLSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745527 174 APKVLFLDEPTNHLDIETILWLEKFLKDF--QG-SIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELadAGkAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
330-472 |
6.68e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 66.04 E-value: 6.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 330 GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI--------HCGTKLEVAYfdQHRATLdPDKTVM 401
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEItldgvpvtGPGADRGVVF--QKDALL-PWLNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 402 DNLAEGKQevmVNGRPRH-----------VLGyLQDFlfppkrAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:COG4525 95 DNVAFGLR---LRGVPKAerraraeellaLVG-LADF------ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGA 164
|
..
gi 1437745527 471 LD 472
Cdd:COG4525 165 LD 166
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
321-495 |
7.93e-12 |
|
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: 65.21 E-value: 7.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLvrDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLEVA------YFDQH 390
Cdd:cd03298 2 RLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvTAAPPAdrpvsmLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 391 raTLDPDKTVMDNLAEGKQ-EVMVNGRPRH-VLGYLQDFLFPPKRAMTPvRALSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:cd03298 80 --NLFAHLTVEQNVGLGLSpGLKLTAEDRQaIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|.
gi 1437745527 469 NDLDVETLELLEELVDAY----QGTVLLVSH 495
Cdd:cd03298 157 AALDPALRAEMLDLVLDLhaetKMTVLMVTH 187
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-473 |
8.00e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 8.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVyeqdlvtarlqqdpprdIEG 81
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT-----------------INN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 82 TIFDFVAQGVAEDAQYITEYHRVSkVIETDPSEKNL--NRLAQLQ----EVLDNRNlwlLDSRIAEVLEKLGLNGEAE-- 153
Cdd:PRK09700 67 INYNKLDHKLAAQLGIGIIYQELS-VIDELTVLENLyiGRHLTKKvcgvNIIDWRE---MRVRAAMMLLRVGLKVDLDek 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 154 LSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHL---DIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGk 230
Cdd:PRK09700 143 VANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 231 lsswpgnydKYLESKEealrVEEQQNAEFDRKLAQEEawirqgIKARRTRNEGRVRalkalrverserrevlgsarmqve 310
Cdd:PRK09700 222 ---------SSVCSGM----VSDVSNDDIVRLMVGRE------LQNRFNAMKENVS------------------------ 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 311 eaTRSGKIVFELEdvNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKLE------ 383
Cdd:PRK09700 259 --NLAHETVFEVR--NVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLnGKDISprspld 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 384 -----VAYFDQHRAT--LDPDKTVMDNLAEGKQevMVNGRPRHVLGylqdfLFPPK---------RAMTPVRA------- 440
Cdd:PRK09700 335 avkkgMAYITESRRDngFFPNFSIAQNMAISRS--LKDGGYKGAMG-----LFHEVdeqrtaenqRELLALKChsvnqni 407
|
490 500 510
....*....|....*....|....*....|....*
gi 1437745527 441 --LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK09700 408 teLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
318-472 |
8.81e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.98 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 318 IVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGdlkADSGRIHCGTklevayFDQHRATLDPD 397
Cdd:COG2401 29 IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---ALKGTPVAGC------VDVPDNQFGRE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 398 KTVMDNLAEgKQEVMVNGRPRHVLGYLQDFLFppkraMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG2401 100 ASLIDAIGR-KGDFKDAVELLNAVGLSDAVLW-----LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-245 |
8.88e-12 |
|
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: 65.32 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE----QDLVTARL-------QQDPPRdIEGTIFD 85
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDgidiRDISRKSLrsmigvvLQDTFL-FSGTIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 86 FVaqgvaedaqyiteyhRVSKVIETDPSEKNLNRLAQLQEvldnrnlwLLDSRIAEVLEKLGLNGeaelSSLSGGWLRKA 165
Cdd:cd03254 96 NI---------------RLGRPNATDEEVIEAAKEAGAHD--------FIMKLPNGYDTVLGENG----GNLSQGERQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 166 ALGRALVSAPKVLFLDEPTNHLDIETilwlEKFLKD-----FQGSIVF-ISHDRSFIRNmATRIIDLDRGKLSSwPGNYD 239
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTET----EKLIQEaleklMKGRTSIiIAHRLSTIKN-ADKILVLDDGKIIE-EGTHD 222
|
....*.
gi 1437745527 240 KYLESK 245
Cdd:cd03254 223 ELLAKK 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-473 |
1.02e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.74 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARlqqdPPRD-IE---GTIF-DF------- 86
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIR----SPRDaIAlgiGMVHqHFmlvpnlt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 87 VAQGVaedaqyiteyhrvskVIETDPSEKNLNRLAQLQEvldnrnlwlldsRIAEVLEKLGL--NGEAELSSLSGGWLRK 164
Cdd:COG3845 97 VAENI---------------VLGLEPTKGGRLDRKAARA------------RIRELSERYGLdvDPDAKVEDLSVGEQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 165 AALGRALVSAPKVLFLDEPTNHL---DIETILwleKFLKDF--QG-SIVFISHDRSFIRNMATRIIDLDRGKLSswpGNY 238
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLtpqEADELF---EILRRLaaEGkSIIFITHKLREVMAIADRVTVLRRGKVV---GTV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 239 DKYLESKEEaLrveeqqnAE--FDRKLAqeeawirqgikarrtrnegrvralkaLRVERserrevlgsarmqveEATRSG 316
Cdd:COG3845 224 DTAETSEEE-L-------AElmVGREVL--------------------------LRVEK---------------APAEPG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 317 KIVFELEDVNY-SIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKLE----------- 383
Cdd:COG3845 255 EVVLEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRlDGEDITglsprerrrlg 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 384 VAYF--DQHRATLDPDKTVMDNLAEGKQE-------VMVNGRP--RHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLA 452
Cdd:COG3845 335 VAYIpeDRLGRGLVPDMSVAENLILGRYRrppfsrgGFLDRKAirAFAEELIEEFDVRTPGPDTPARSLSGGNQQKVILA 414
|
490 500
....*....|....*....|.
gi 1437745527 453 RLFLKPSNLLILDEPTNDLDV 473
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDV 435
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
316-473 |
1.05e-11 |
|
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: 63.99 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 316 GKIVFELEDvnysIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG------------TKLE 383
Cdd:cd03215 1 GEPVLEVRG----LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkpvtrrsprdaIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 384 VAYF--DQHRATLDPDKTVMDNLAegkqevmvngrprhvLGYLqdflfppkramtpvraLSGGERNRLLLARLFLKPSNL 461
Cdd:cd03215 77 IAYVpeDRKREGLVLDLSVAENIA---------------LSSL----------------LSGGNQQKVVLARWLARDPRV 125
|
170
....*....|..
gi 1437745527 462 LILDEPTNDLDV 473
Cdd:cd03215 126 LILDEPTRGVDV 137
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
19-231 |
1.09e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 65.03 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVvyeqdlvtarlqqdpprDIEGTIFDFvaqgvaedaqyi 98
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL-----------------NIAGHQFDF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 99 teyhrvskviETDPSEKNLNRLAQ-LQEVLDNRNLW----LLDSRIAEVLEKLGLNGEA------------ELSS----- 156
Cdd:COG4161 69 ----------SQKPSEKAIRLLRQkVGMVFQQYNLWphltVMENLIEAPCKVLGLSKEQarekamkllarlRLTDkadrf 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 157 ---LSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGS-I--VFISHDRSFIRNMATRIIDLDRGK 230
Cdd:COG4161 139 plhLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgItqVIVTHEVEFARKVASQVVYMEKGR 218
|
.
gi 1437745527 231 L 231
Cdd:COG4161 219 I 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
319-467 |
1.17e-11 |
|
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: 64.99 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 319 VFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI------------HCGTKLEVAY 386
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIlidgqdithlpmHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 387 FDQhRATLDPDKTVMDNLA---EGKQEVMVNGRPRHVLGYLQDFLFP---PKRAMTpvraLSGGERNRLLLARLFLKPSN 460
Cdd:TIGR04406 81 LPQ-EASIFRKLTVEENIMavlEIRKDLDRAEREERLEALLEEFQIShlrDNKAMS----LSGGERRRVEIARALATNPK 155
|
....*..
gi 1437745527 461 LLILDEP 467
Cdd:TIGR04406 156 FILLDEP 162
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
321-472 |
1.18e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 66.65 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTK---------LEVAYFDQHR 391
Cdd:PRK10851 4 EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardRKVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 392 AtLDPDKTVMDNLAEG---------------KQEV-----MVNgrprhvLGYLQDfLFPPKramtpvraLSGGERNRLLL 451
Cdd:PRK10851 84 A-LFRHMTVFDNIAFGltvlprrerpnaaaiKAKVtqlleMVQ------LAHLAD-RYPAQ--------LSGGQKQRVAL 147
|
170 180
....*....|....*....|..
gi 1437745527 452 AR-LFLKPsNLLILDEPTNDLD 472
Cdd:PRK10851 148 ARaLAVEP-QILLLDEPFGALD 168
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-226 |
1.24e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 64.05 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 18 LLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEqdlvtarlqqdpprdieGTIFDFVAQGVAEDAQY 97
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLN-----------------GGPLDFQRDSIARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 98 ITeyhrvskvietdpsekNLNRLAQLQEVLDNRNLWLL---DSRIAEVLEKLGLNG--EAELSSLSGGWLRKAALGRALV 172
Cdd:cd03231 78 LG----------------HAPGIKTTLSVLENLRFWHAdhsDEQVEEALARVGLNGfeDRPVAQLSAGQQRRVALARLLL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 173 SAPKVLFLDEPTNHLDIETIlwlEKFLKDFQ------GSIVFISHDRSFIRNMATRIIDL 226
Cdd:cd03231 142 SGRPLWILDEPTTALDKAGV---ARFAEAMAghcargGMVVLTTHQDLGLSEAGARELDL 198
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-231 |
1.55e-11 |
|
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: 64.38 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDA--PL--LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK-EQPlDDGQV-VYEQDLvtARLQQDP 75
Cdd:COG4181 7 PIIELRGLTKTVGTGagELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGlDRP-TSGTVrLAGQDL--FALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 76 -----PRDIeGtifdFVAQgvaedaqyitEYHRVSkvietdpsekNLNRL------AQLQEVLDNRnlwlldSRIAEVLE 144
Cdd:COG4181 84 rarlrARHV-G----FVFQ----------SFQLLP----------TLTALenvmlpLELAGRRDAR------ARARALLE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 145 KLGLngeAEL-----SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIET---ILWLEKFLKDFQGS-IVFISHDRSF 215
Cdd:COG4181 133 RVGL---GHRldhypAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqIIDLLFELNRERGTtLVLVTHDPAL 209
|
250
....*....|....*.
gi 1437745527 216 IRnMATRIIDLDRGKL 231
Cdd:COG4181 210 AA-RCDRVLRLRAGRL 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
324-497 |
1.58e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.82 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 324 DVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC---GTKLEVAYFDQ------HRATL 394
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFerqSIKKDLCTYQKqlcfvgHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 DPDKTVMDN------LAEGKQEVMVNGRpRHVLGYLQDFlfppkramtPVRALSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:PRK13540 86 NPYLTLRENclydihFSPGAVGITELCR-LFSLEHLIDY---------PCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|..
gi 1437745527 469 NDLDVETLELLEELVDAYQ---GTVLLVSHDR 497
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
321-496 |
2.09e-11 |
|
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: 66.70 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSI-GTRRLV-RDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtKLEVAYFDQhratLDPDk 398
Cdd:COG4618 332 SVENLTVVPpGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV----RLDGADLSQ----WDRE- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 399 tvmdNLAegkqevmvngrpRHVlGYL-QD-FLFP---------------------PKRA----M---------TPV---- 438
Cdd:COG4618 403 ----ELG------------RHI-GYLpQDvELFDgtiaeniarfgdadpekvvaaAKLAgvheMilrlpdgydTRIgegg 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745527 439 RALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELVD---AYQGTVLLVSHD 496
Cdd:COG4618 466 ARLSGGQRQRIGLARaLYGDPR-LVVLDEPNSNLDDEGEAALAAAIRalkARGATVVVITHR 526
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
335-473 |
2.12e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 65.52 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 335 VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLEVAYFDQHR-----------ATLDPDKT 399
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqdiTGLSGRELRPLRrrmqmvfqdpyASLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 400 VMDNLAEGkqeVMVNGrprhvlgylqdfLFPPKRAMTPVRAL------------------SGGERNRLLLAR-LFLKPSn 460
Cdd:COG4608 114 VGDIIAEP---LRIHG------------LASKAERRERVAELlelvglrpehadryphefSGGQRQRIGIARaLALNPK- 177
|
170
....*....|...
gi 1437745527 461 LLILDEPTNDLDV 473
Cdd:COG4608 178 LIVCDEPVSALDV 190
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-473 |
2.21e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVvyeqdlvtarlqqdpprDIEG 81
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL-----------------EIGG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 82 TIFDFVAQGVAedaqyiteyHRVSkvIETDPSEKNL--NrlaqlQEVLDNRNLWL-----LDSRIAEVLEKLG--LNGEA 152
Cdd:PRK15439 73 NPCARLTPAKA---------HQLG--IYLVPQEPLLfpN-----LSVKENILFGLpkrqaSMQKMKQLLAALGcqLDLDS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 153 ELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHL---DIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRG 229
Cdd:PRK15439 137 SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLtpaETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 230 KLSswpgnydkyLESKEEALRVEEqqnaefdrklaqeeawIRQGIkARRTRNEGRVRALKA-LRVERSERREVLGSARMQ 308
Cdd:PRK15439 217 TIA---------LSGKTADLSTDD----------------IIQAI-TPAAREKSLSASQKLwLELPGNRRQQAAGAPVLT 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 309 VEEATRSGkivfeledvnysigtrrlVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklevaYFD 388
Cdd:PRK15439 271 VEDLTGEG------------------FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI---------MLN 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 389 QHRATLDPDKTVMDN----LAEGKQE---------------VMVN--------GRPRHVL-GYLQDFLFPPKRAMTPVRA 440
Cdd:PRK15439 324 GKEINALSTAQRLARglvyLPEDRQSsglyldaplawnvcaLTHNrrgfwikpARENAVLeRYRRALNIKFNHAEQAART 403
|
490 500 510
....*....|....*....|....*....|...
gi 1437745527 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-231 |
2.29e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.77 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDA--PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVvyeqdlvtaRLQQDPprdi 79
Cdd:PRK11160 337 VSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI---------LLNGQP---- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 80 egtifdfvaqgvaedaqyITEYhrvskvietdpSEKNLNrlaQLQEVLDNR----------NLWLL-----DSRIAEVLE 144
Cdd:PRK11160 404 ------------------IADY-----------SEAALR---QAISVVSQRvhlfsatlrdNLLLAapnasDEALIEVLQ 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 145 KLGL----NGEAELSS--------LSGGWLRKAALGRALVS-APkVLFLDEPTNHLDIET---ILWLekFLKDFQG-SIV 207
Cdd:PRK11160 452 QVGLekllEDDKGLNAwlgeggrqLSGGEQRRLGIARALLHdAP-LLLLDEPTEGLDAETerqILEL--LAEHAQNkTVL 528
|
250 260
....*....|....*....|....
gi 1437745527 208 FISHDRSFIRNMaTRIIDLDRGKL 231
Cdd:PRK11160 529 MITHRLTGLEQF-DRICVMDNGQI 551
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
345-495 |
2.35e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.79 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 345 GDKIALVGPNGCGKTTLLKLMLGDLKAD-SGRIHcGTKLEVAYFDQHRATLD--------PDKTVMDNLAEGKQEvMVNG 415
Cdd:PRK11174 376 GQRIALVGPSGAGKTSLLNALLGFLPYQgSLKIN-GIELRELDPESWRKHLSwvgqnpqlPHGTLRDNVLLGNPD-ASDE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 416 RPRHVL--GYLQDFLfpPKRAM---TPVR----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELV-DA 485
Cdd:PRK11174 454 QLQQALenAWVSEFL--PLLPQgldTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALnAA 531
|
170
....*....|.
gi 1437745527 486 YQG-TVLLVSH 495
Cdd:PRK11174 532 SRRqTTLMVTH 542
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
15-227 |
2.52e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.28 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 15 DAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVY-EQDLVTARlqqdpprdiegtifdfvaqgvae 93
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIRRQR----------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 94 daqyiTEYHRV------SKVIETDPS-EKNLNRLAQLQEVLDNRNLWlldsriaEVLEKLGLNGEAEL--SSLSGGWLRK 164
Cdd:PRK13538 70 -----DEYHQDllylghQPGIKTELTaLENLRFYQRLHGPGDDEALW-------EALAQVGLAGFEDVpvRQLSAGQQRR 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 165 AALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QGSIV-FISHDRSFIRNMATRIIDLD 227
Cdd:PRK13538 138 VALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHaeQGGMViLTTHQDLPVASDKVRKLRLG 203
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
321-472 |
2.78e-11 |
|
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: 64.10 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLV---RDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLEVAYFDQHRAT 393
Cdd:cd03249 2 EFKNVSFRYPSRPDVpilKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDgvdiRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 394 L--DP---DKTVMDNLAEGK---QEVMVNGRPRhvLGYLQDFLFP-PKRAMTPVRA----LSGGERNRLLLARLFLKPSN 460
Cdd:cd03249 82 VsqEPvlfDGTIAENIRYGKpdaTDEEVEEAAK--KANIHDFIMSlPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPK 159
|
170
....*....|..
gi 1437745527 461 LLILDEPTNDLD 472
Cdd:cd03249 160 ILLLDEATSALD 171
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
320-473 |
3.14e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.42 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 320 FELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKL-----------EVAYFD 388
Cdd:PRK10575 12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 389 QHratLDPdktvmdnlAEGK--QEVMVNGR-PRHvlGYLQDFLFPPKR---------AMTP-----VRALSGGERNRLLL 451
Cdd:PRK10575 92 QQ---LPA--------AEGMtvRELVAIGRyPWH--GALGRFGAADREkveeaislvGLKPlahrlVDSLSGGERQRAWI 158
|
170 180
....*....|....*....|..
gi 1437745527 452 ARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDI 180
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
349-496 |
3.86e-11 |
|
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: 65.13 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 349 ALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GT--------------KLEVAYFDQhRATLDPDKTVMDNLAEGKQEVMV 413
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLnGRtlfdsrkgiflppeKRRIGYVFQ-EARLFPHLSVRGNLRYGMKRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 414 ---NGRPRHV-----LGYLQDflfppkramTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLEL----LEE 481
Cdd:TIGR02142 106 serRISFERViellgIGHLLG---------RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEilpyLER 176
|
170
....*....|....*
gi 1437745527 482 LVDAYQGTVLLVSHD 496
Cdd:TIGR02142 177 LHAEFGIPILYVSHS 191
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-231 |
4.11e-11 |
|
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: 62.33 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 14 SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVyeqdlvtarLQQDPPRDIEGTIfdfvaqgvae 93
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT---------LDGVPVSDLEKAL---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 94 dAQYITeyhrvskvietdpseknlnrlaqlqeVLDNRnLWLLDSRIaevLEKLGLNgeaelssLSGGWLRKAALGRALVS 173
Cdd:cd03247 74 -SSLIS--------------------------VLNQR-PYLFDTTL---RNNLGRR-------FSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745527 174 APKVLFLDEPTNHLDIET---ILWL-EKFLKDfqGSIVFISHDRSFIRNMaTRIIDLDRGKL 231
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITerqLLSLiFEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
321-495 |
4.73e-11 |
|
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: 62.54 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLG--DLKADSGRIhcgtklevaYFDQHRATldpdk 398
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEI---------LFKGEDIT----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 399 tvmdnlaegkqEVMVNGRPRhvLGYLQDFLFPPK----RAMTPVRAL----SGGERNRL-LLARLFLKPSnLLILDEPTN 469
Cdd:cd03217 68 -----------DLPPEERAR--LGIFLAFQYPPEipgvKNADFLRYVnegfSGGEKKRNeILQLLLLEPD-LAILDEPDS 133
|
170 180
....*....|....*....|....*....
gi 1437745527 470 DLDVETLELLEELVDAYQG---TVLLVSH 495
Cdd:cd03217 134 GLDIDALRLVAEVINKLREegkSVLIITH 162
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-230 |
4.90e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.57 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 18 LLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVT-----------ARLQQDPprdiegtifdf 86
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklpeykrakyiGRVFQDP----------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 87 vAQGVAEDAQyITE-----YHRVSKvietdpseKNLnRLAQLQEVLDnrnlwlldsRIAEVLEKLGLNGE----AELSSL 157
Cdd:COG1101 90 -MMGTAPSMT-IEEnlalaYRRGKR--------RGL-RRGLTKKRRE---------LFRELLATLGLGLEnrldTKVGLL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 158 SGGWlRKA-ALGRALVSAPKVLFLDEPTNHLDIET---ILWL-EKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:COG1101 150 SGGQ-RQAlSLLMATLTKPKLLLLDEHTAALDPKTaalVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-230 |
6.67e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.53 E-value: 6.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVL-AKEQPLDDGQVVYEQDLVTARLQQDPPRDIEGTIFdfvaqgvaedaQY 97
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLnGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVF-----------QY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 98 iTEYHRVSKVIETD----PSEKNLNRlaqlQEVLDnrnlwlldsRIAEVLEKLGLNGE--AELS--SLSGGWLRKAALGR 169
Cdd:PRK13637 92 -PEYQLFEETIEKDiafgPINLGLSE----EEIEN---------RVKRAMNIVGLDYEdyKDKSpfELSGGQKRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 170 ALVSAPKVLFLDEPTNHLDI---ETILWLEKFL-KDFQGSIVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPkgrDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-472 |
7.57e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.18 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVN--YSIGT---RRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKlEVAYFDQH-RATL 394
Cdd:COG1101 3 ELKNLSktFNPGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK-DVTKLPEYkRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 ------DP------DKTVMDNLA----EGKQEVMVNGRPRHVLGYLQDFLFP-----PKRAMTPVRALSGGERNRLLLAR 453
Cdd:COG1101 82 igrvfqDPmmgtapSMTIEENLAlayrRGKRRGLRRGLTKKRRELFRELLATlglglENRLDTKVGLLSGGQRQALSLLM 161
|
170
....*....|....*....
gi 1437745527 454 LFLKPSNLLILDEPTNDLD 472
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALD 180
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-231 |
7.70e-11 |
|
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: 62.49 E-value: 7.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 6 LTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVV------------YEQDLVTARLQQ 73
Cdd:cd03248 17 VTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgkpisqyehkYLHSKVSLVGQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 74 dpPRDIEGTIFDFVAQGVAEdaqyiTEYHRVSKVIETDPSEKNLNRLAQlqevldnrNLWlldsriAEVLEKLGLngeae 153
Cdd:cd03248 97 --PVLFARSLQDNIAYGLQS-----CSFECVKEAAQKAHAHSFISELAS--------GYD------TEVGEKGSQ----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 154 lssLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QGSIVFISHDRSFIRNmATRIIDLDRGKL 231
Cdd:cd03248 151 ---LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
321-498 |
8.03e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.79 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC------GTKLEVAYFDQHRATL 394
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpveGPGAERGVVFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 dPDKTVMDNLAEGKQEVMVNGRPRHVLGY----LQDFLFPPKRamtPVRALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:PRK11248 83 -PWRNVQDNVAFGLQLAGVEKMQRLEIAHqmlkKVGLEGAEKR---YIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|..
gi 1437745527 471 LDV-ETLELLEELVDAYQGT---VLLVSHDRE 498
Cdd:PRK11248 159 LDAfTREQMQTLLLKLWQETgkqVLLITHDIE 190
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
316-495 |
9.13e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.13 E-value: 9.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 316 GKIvfELEDVNYSIGTR---RLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLML-------GDLKADSGRIhcgTKLEVA 385
Cdd:TIGR00958 477 GLI--EFQDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQnlyqptgGQVLLDGVPL---VQYDHH 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 386 YFDQHRATLDPD-----KTVMDNLAEG-----KQEVMVNGRPRHVLGYLQDFlfpPKRAMTPV----RALSGGERNRLLL 451
Cdd:TIGR00958 552 YLHRQVALVGQEpvlfsGSVRENIAYGltdtpDEEIMAAAKAANAHDFIMEF---PNGYDTEVgekgSQLSGGQKQRIAI 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1437745527 452 ARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQGTVLLVSH 495
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-229 |
9.20e-11 |
|
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: 62.07 E-value: 9.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVL-AKEQPlDDGQVVYEQ-----DLVTArlqqdPPRDI----EGTIfDF 86
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIyGNYLP-DSGSILVRHdggwvDLAQA-----SPREIlalrRRTI-GY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 87 VAQgvaedaqYITEYHRVSK---VIE------TDPSEknlnrlAQlqevldnrnlwlldSRIAEVLEKLGLngEAELSSL 157
Cdd:COG4778 98 VSQ-------FLRVIPRVSAldvVAEpllergVDREE------AR--------------ARARELLARLNL--PERLWDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 158 -----SGGWLRKAALGRALVSAPKVLFLDEPTNHLD-------IETIlwLEkfLKDfQG-SIVFISHDRSFIRNMATRII 224
Cdd:COG4778 149 ppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDaanravvVELI--EE--AKA-RGtAIIGIFHDEEVREAVADRVV 223
|
....*
gi 1437745527 225 DLDRG 229
Cdd:COG4778 224 DVTPF 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
332-472 |
9.84e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.83 E-value: 9.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 332 RRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQH--------RATL---DPDKTV 400
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRpylplgtlREALlypATAEAF 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 401 MDnlaEGKQEVM--VNgrprhvLGYLQDFLFPPKRAMtpvRALSGGERNRLLLARLFL-KPSnLLILDEPTNDLD 472
Cdd:COG4178 456 SD---AELREALeaVG------LGHLAERLDEEADWD---QVLSLGEQQRLAFARLLLhKPD-WLFLDEATSALD 517
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
337-618 |
1.15e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.97 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 337 DFSakVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHcgTKLEVAYFDQhRATLDPDkTVMDNLAEGKQevMVNGR 416
Cdd:TIGR00957 658 TFS--IPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH--MKGSVAYVPQ-QAWIQND-SLRENILFGKA--LNEKY 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 417 PRHVL---GYLQDFLFPPKRAMTPVRA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQG- 488
Cdd:TIGR00957 730 YQQVLeacALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGv 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 489 ----TVLLVSHDREFV----------DNSVTECW----IFEGDGVINSYVGGYYDAQQQRAqsvsLKNEANKSRNAPekt 550
Cdd:TIGR00957 810 lknkTRILVTHGISYLpqvdviivmsGGKISEMGsyqeLLQRDGAFAEFLRTYAPDEQQGH----LEDSWTALVSGE--- 882
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 551 EKETKPKQNAKKATRSNNKlsyHLIRELEQLPAKLERLEEELGCLQE-EVAAAdfftrpHEETEKVLKA 618
Cdd:TIGR00957 883 GKEAKLIENGMLVTDVVGK---QLQRQLSASSSDSGDQSRHHGSSAElQKAEA------KEETWKLMEA 942
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-231 |
1.20e-10 |
|
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: 61.74 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDAPLldNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVV-YEQDLVTARLQQDPPRDI--E 80
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLiNGVDVTAAPPADRPVSMLfqE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 GTIFDF--VAQGVAedaqyiteyhrvskvIETDPsekNLNRLAQLQEvldnrnlwlldsRIAEVLEKLGLNG-EAELS-S 156
Cdd:cd03298 79 NNLFAHltVEQNVG---------------LGLSP---GLKLTAEDRQ------------AIEVALARVGLAGlEKRLPgE 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 157 LSGGWLRKAALGRALVSAPKVLFLDEPTNHLD----IETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:cd03298 129 LSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
319-472 |
1.38e-10 |
|
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: 61.68 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 319 VFELEDVNYSIGTRR----LVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKLevayfdqhrAT 393
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRlAGQDL---------FA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 394 LDPDktvmdNLAEGkqevmvngRPRHVlGY-LQDF-LFPPKRA----MTPV----------RA----------------- 440
Cdd:COG4181 79 LDED-----ARARL--------RARHV-GFvFQSFqLLPTLTAlenvMLPLelagrrdaraRArallervglghrldhyp 144
|
170 180 190
....*....|....*....|....*....|....
gi 1437745527 441 --LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG4181 145 aqLSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-472 |
1.59e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 62.43 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKLEVAyfdqHRAT------ 393
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwDGEPLDPE----DRRRigylpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 394 ---LDPDKTVMDNL-----------AEGKQEVMVngrprhvlgYLQDF-LfpPKRAMTPVRALSGGERNRL-LLARLFLK 457
Cdd:COG4152 79 ergLYPKMKVGEQLvylarlkglskAEAKRRADE---------WLERLgL--GDRANKKVEELSKGNQQKVqLIAALLHD 147
|
170
....*....|....*
gi 1437745527 458 PSnLLILDEPTNDLD 472
Cdd:COG4152 148 PE-LLILDEPFSGLD 161
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-231 |
1.71e-10 |
|
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: 61.52 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 14 SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDD---GQVVYEQDLVTARLQQDpprdiegtIFDFVAQG 90
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQK--------CVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 91 --------VAEDAQYI----TEYHRVSKVIEtdpseknlnrlaqlQEVLDNRNLWLLDSRIAEVLeklglngeaeLSSLS 158
Cdd:cd03234 90 dillpgltVRETLTYTailrLPRKSSDAIRK--------------KRVEDVLLRDLALTRIGGNL----------VKGIS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 159 GGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QGSIVFIS-HD-RSFIRNMATRIIDLDRGKL 231
Cdd:cd03234 146 GGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLarRNRIVILTiHQpRSDLFRLFDRILLLSSGEI 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
34-230 |
1.73e-10 |
|
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: 63.20 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 34 LVGRNGAGKSTLLRVLAKEQPLDDGQVVY-EQDLVTARLQQD-PP--RDIeGTIFdfvaqgvaedaQyiteyhrvskvie 109
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAGLERPDSGRIRLgGEVLQDSARGIFlPPhrRRI-GYVF-----------Q------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 110 tDPS-------EKNLnRLAQLQEVLDNRNLwlldsRIAEVLEKLGLngeAEL-----SSLSGGWLRKAALGRALVSAPKV 177
Cdd:COG4148 85 -EARlfphlsvRGNL-LYGRKRAPRAERRI-----SFDEVVELLGI---GHLldrrpATLSGGERQRVAIGRALLSSPRL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 178 LFLDEPTNHLDIET---IL-WLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:COG4148 155 LLMDEPLAALDLARkaeILpYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGR 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
330-495 |
1.73e-10 |
|
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: 60.97 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 330 GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI---------HCGTKLEVAYFDQHRATLDPDKTV 400
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggpldfQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 401 MDNL----AEGKQEVMVNGRPRHVLGYLQDflfppkramTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL 476
Cdd:cd03231 91 LENLrfwhADHSDEQVEEALARVGLNGFED---------RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|..
gi 1437745527 477 ELLEELVDAYQ---GTVLLVSH 495
Cdd:cd03231 162 ARFAEAMAGHCargGMVVLTTH 183
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
321-495 |
1.77e-10 |
|
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: 61.33 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTR--RLV-RDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI----HCGTKLEVAYFDQHRAT 393
Cdd:cd03248 13 KFQNVTFAYPTRpdTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgKPISQYEHKYLHSKVSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 394 LDPD-----KTVMDNLAEGKQ-----EVMVNGRPRHVLGYLQDFlfpPKRAMTPV----RALSGGERNRLLLARLFLKPS 459
Cdd:cd03248 93 VGQEpvlfaRSLQDNIAYGLQscsfeCVKEAAQKAHAHSFISEL---ASGYDTEVgekgSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1437745527 460 NLLILDEPTNDLDVETLELLEELVdaYQG----TVLLVSH 495
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQAL--YDWperrTVLVIAH 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
332-472 |
2.41e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.06 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 332 RRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI------------HCGTKLEVAYFDQhRATLDPDKT 399
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplHARARRGIGYLPQ-EASIFRRLS 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 400 VMDNLA---EGKQEVMVNGRPRHVLGYLQDFLFPPKRAMTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK10895 95 VYDNLMavlQIRDDLSAEQREDRANELMEEFHIEHLRDSMG-QSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-212 |
2.55e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.70 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 3 LISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQD---------LVTAR--- 70
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrsrLYTVRkrm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 71 --LQQDPPRDIEGTIFDFVAQGVAEDAQYiteyhrvskvietdPSEknlnrlaqlqevldnrnlwLLDSRIAEVLEKLGL 148
Cdd:PRK11831 87 smLFQSGALFTDMNVFDNVAYPLREHTQL--------------PAP-------------------LLHSTVMMKLEAVGL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 149 NGEAEL--SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGSI----VFISHD 212
Cdd:PRK11831 134 RGAAKLmpSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvtcVVVSHD 203
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
321-496 |
2.59e-10 |
|
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: 61.16 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRR-LVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKlEVAYFDQHR-------- 391
Cdd:cd03295 2 EFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE-DIREQDPVElrrkigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 392 ---ATLDPDKTVMDNLA-----EGKQEVMVNGRPRHVLGYLQdfLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLI 463
Cdd:cd03295 81 iqqIGLFPHMTVEENIAlvpklLKWPKEKIRERADELLALVG--LDPAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1437745527 464 LDEPTNDLDVETLELLEELVDAYQ----GTVLLVSHD 496
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHD 195
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
349-467 |
2.80e-10 |
|
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: 62.43 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 349 ALVGPNGCGKTTLLKLMLGDLKADSGRIHCGtklEVAYFDQ--------HR---------ATLDPDKTVMDNLAEG-KQE 410
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLG---GEVLQDSargiflppHRrrigyvfqeARLFPHLSVRGNLLYGrKRA 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 411 VMVNGRPRH-----VLGyLQDFLfppKRamtPVRALSGGERNRLLLAR-LFLKPSnLLILDEP 467
Cdd:COG4148 106 PRAERRISFdevveLLG-IGHLL---DR---RPATLSGGERQRVAIGRaLLSSPR-LLLMDEP 160
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
327-472 |
2.88e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 60.35 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 327 YSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKAD---SGRIHCGTKLEVAYFDQHRATLdpdktvmdn 403
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEI--------- 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745527 404 laegkqeVMVNGRPRHV--LGYLQDFLFPPK-RAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:cd03233 86 -------IYVSEEDVHFptLTVRETLDFALRcKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
319-472 |
3.11e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 59.95 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 319 VFELEDVNYSI----GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMlgdlkadSGRIHCGTklevayfdqhratl 394
Cdd:cd03232 3 VLTWKNLNYTVpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL-------AGRKTAGV-------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 dpdktvmdnlAEGkqEVMVNGRP-----RHVLGYL--QDFLFP------PKRAMTPVRALSGGERNRLLLA-RLFLKPSn 460
Cdd:cd03232 62 ----------ITG--EILINGRPldknfQRSTGYVeqQDVHSPnltvreALRFSALLRGLSVEQRKRLTIGvELAAKPS- 128
|
170
....*....|..
gi 1437745527 461 LLILDEPTNDLD 472
Cdd:cd03232 129 ILFLDEPTSGLD 140
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-231 |
3.52e-10 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 60.20 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVY-EQDLVTARLQ----------QDPPRdIEGTIfd 85
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdGVDISKIGLHdlrsrisiipQDPVL-FSGTI-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 86 fvaqgvaedaqyiteyhRvskvietdpseKNLNRL-----AQLQEVLDNRNLWlldSRIAEVLEKLGLNGEAELSSLSGG 160
Cdd:cd03244 95 -----------------R-----------SNLDPFgeysdEELWQALERVGLK---EFVESLPGGLDTVVEEGGENLSVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 161 WLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKD-FQGSIVF-ISHdRsfIRNMAT--RIIDLDRGKL 231
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREaFKDCTVLtIAH-R--LDTIIDsdRILVLDKGRV 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
30-230 |
4.61e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.42 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 30 ERVCLVGRNGAGKST----LLRVLAKE-------QPLDdgQVVYEQDL-VTARLQ---QDP-----PR-DIEgtifdfva 88
Cdd:PRK15134 313 ETLGLVGESGSGKSTtglaLLRLINSQgeiwfdgQPLH--NLNRRQLLpVRHRIQvvfQDPnsslnPRlNVL-------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 89 qgvaedaQYITEYHRVSkvietdpsEKNLNRLAQLQEVLdnrnlwlldsriaEVLEKLGLNGEAEL---SSLSGGWLRKA 165
Cdd:PRK15134 383 -------QIIEEGLRVH--------QPTLSAAQREQQVI-------------AVMEEVGLDPETRHrypAEFSGGQRQRI 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 166 ALGRALVSAPKVLFLDEPTNHLDIET---ILWLEKFLK-DFQGSIVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:PRK15134 435 AIARALILKPSLIILDEPTSSLDKTVqaqILALLKSLQqKHQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
321-497 |
4.64e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 61.66 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLEVAYFD-----QHR 391
Cdd:PRK11432 8 VLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgedvTHRSIQQRDicmvfQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 392 AtLDPDKTVMDNLAEG-------KQEvmVNGRPRHVL------GYLQDFlfppkramtpVRALSGGERNRLLLAR-LFLK 457
Cdd:PRK11432 88 A-LFPHMSLGENVGYGlkmlgvpKEE--RKQRVKEALelvdlaGFEDRY----------VDQISGGQQQRVALARaLILK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1437745527 458 PSNLLiLDEPTNDLDVETLELLEELVDAYQG----TVLLVSHDR 497
Cdd:PRK11432 155 PKVLL-FDEPLSNLDANLRRSMREKIRELQQqfniTSLYVTHDQ 197
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
342-516 |
4.70e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.53 E-value: 4.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 342 VQRGDKIALVGPNGCGKTTLLKLM------------LGDLKADSGRIHCGTKLEVAYFDQHRA------TLDPDKTVMDN 403
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARSLSQQKGLIRQLRQHVGfvfqnfNLFPHRTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 404 LAEGKqeVMVNGRPRHVLGYLQDFLFPP-----KRAMTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD---VET 475
Cdd:PRK11264 106 IIEGP--VIVKGEPKEEATARARELLAKvglagKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelVGE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1437745527 476 LELLEELVDAYQGTVLLVSHDREFVDNsVTECWIFEGDGVI 516
Cdd:PRK11264 183 VLNTIRQLAQEKRTMVIVTHEMSFARD-VADRAIFMDQGRI 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
330-500 |
5.26e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.47 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 330 GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKLEVAYFDQHRA--------------TL 394
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWrGEPLAKLNRAQRKAfrrdiqmvfqdsisAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 DPDKTVMDNLAEGKQEVMV---NGRPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
Cdd:PRK10419 103 NPRKTVREIIREPLRHLLSldkAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190
....*....|....*....|....*....|...
gi 1437745527 472 DVETLELLEELVDAYQ---GTV-LLVSHDREFV 500
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQqqfGTAcLFITHDLRLV 215
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-230 |
5.84e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.04 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 6 LTGAYLafSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQV-------------VYEQDLvtARLQ 72
Cdd:PRK10790 346 VSFAYR--DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrplsslshsVLRQGV--AMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 73 QDPPRdIEGTIFDFVAQGvaedaQYITEyHRVSKVIETdpseknlNRLAQLQEVLDNRnlwlLDSRIAEvleklglngea 152
Cdd:PRK10790 422 QDPVV-LADTFLANVTLG-----RDISE-EQVWQALET-------VQLAELARSLPDG----LYTPLGE----------- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 153 ELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QGSIVFISHDRSFIRNmATRIIDLDRGK 230
Cdd:PRK10790 473 QGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLSTIVE-ADTILVLHRGQ 551
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
321-472 |
5.84e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 60.03 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLM-LGDLkADSGRIHCGTklevAYFD-----QHRAT- 393
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLET-PDSGQLNIAG----HQFDfsqkpSEKAIr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 394 --------------LDPDKTVMDNLAEG--------KQEVMvnGRPRHVLGYLQ--DFL--FPpkramtpvRALSGGERN 447
Cdd:COG4161 79 llrqkvgmvfqqynLWPHLTVMENLIEApckvlglsKEQAR--EKAMKLLARLRltDKAdrFP--------LHLSGGQQQ 148
|
170 180
....*....|....*....|....*.
gi 1437745527 448 RLLLAR-LFLKPSNLLiLDEPTNDLD 472
Cdd:COG4161 149 RVAIARaLMMEPQVLL-FDEPTAALD 173
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-227 |
7.02e-10 |
|
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: 58.32 E-value: 7.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 14 SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYeqdlvtarlqqdpPRDieGTIFdFVAQgvae 93
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-------------PEG--EDLL-FLPQ---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 94 dAQYITeyhrvskvietdpseknlnrLAQLQEVLdnRNLWlldSRIaevleklglngeaelssLSGGWLRKAALGRALVS 173
Cdd:cd03223 72 -RPYLP--------------------LGTLREQL--IYPW---DDV-----------------LSGGEQQRLAFARLLLH 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 174 APKVLFLDEPTNHLDIETILWLEKFLKDFQGSIVFISHdRSFIRNMATRIIDLD 227
Cdd:cd03223 109 KPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
9-231 |
8.07e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.50 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 9 AYLAFSDAplLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPP---RDIeGTIFd 85
Cdd:PRK10908 10 AYLGGRQA--LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrRQI-GMIF- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 86 fvaqgvaEDAQYI---TEYHRVS-KVIETDPSEKNLNRlaqlqevldnrnlwlldsRIAEVLEKLGLNGEAE--LSSLSG 159
Cdd:PRK10908 86 -------QDHHLLmdrTVYDNVAiPLIIAGASGDDIRR------------------RVSAALDKVGLLDKAKnfPIQLSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 160 GWLRKAALGRALVSAPKVLFLDEPTNHLD---IETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK10908 141 GEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-231 |
8.23e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 59.71 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQV-VYEQDLVT------AR----LQ 72
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVlVDGLDVATtpsrelAKrlaiLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 73 QDPPRDIEGTIFDFVA-------QGV--AEDAQYITEYhrvskvietdpseknlnrlaqlqevldnrnlwlldsriaevL 143
Cdd:COG4604 82 QENHINSRLTVRELVAfgrfpysKGRltAEDREIIDEA-----------------------------------------I 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 144 EKLGLNGEAE--LSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDI----ETILWLEKFLKDFQGSIVFISHDRSFIR 217
Cdd:COG4604 121 AYLDLEDLADryLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHDINFAS 200
|
250
....*....|....
gi 1437745527 218 NMATRIIDLDRGKL 231
Cdd:COG4604 201 CYADHIVAMKDGRV 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
317-473 |
8.45e-10 |
|
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: 60.45 E-value: 8.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 317 KIVFELEDvnysiGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKA---DSGRI-HCG---TKLEVAYFDQ 389
Cdd:COG0444 8 KVYFPTRR-----GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEIlFDGedlLKLSEKELRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 390 HR------------ATLDPDKTVMDNLAE--------GKQEVMvngrpRHVLGYLQDF-LFPPKRAMtpvRA----LSGG 444
Cdd:COG0444 83 IRgreiqmifqdpmTSLNPVMTVGDQIAEplrihgglSKAEAR-----ERAIELLERVgLPDPERRL---DRypheLSGG 154
|
170 180 190
....*....|....*....|....*....|
gi 1437745527 445 ERNRLLLAR-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG0444 155 MRQRVMIARaLALEPK-LLIADEPTTALDV 183
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
155-233 |
8.64e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 60.66 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 155 SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDI----ETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
...
gi 1437745527 231 LSS 233
Cdd:PRK11144 207 VKA 209
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
30-231 |
1.11e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.47 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 30 ERVCLVGRNGAGKSTLLRVLAKEQPlDDGQVVY-EQDLVT------ARL------QQDPPRDIegTIFdfvaqgvaedaQ 96
Cdd:COG4138 23 ELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLnGRPLSDwsaaelARHraylsqQQSPPFAM--PVF-----------Q 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 97 YITEYhrVSKVIETDPSEKNLNRLAQLqevldnrnLWLLDsriaevleKLGLNgeaeLSSLSGG-W--LRKAA----LGR 169
Cdd:COG4138 89 YLALH--QPAGASSEAVEQLLAQLAEA--------LGLED--------KLSRP----LTQLSGGeWqrVRLAAvllqVWP 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 170 ALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF---QGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:COG4138 147 TINPEGQLLLLDEPMNSLDVAQQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
322-472 |
1.11e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.43 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 322 LEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKL---------EVAYFDQHRA 392
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRmndvppaerGVGMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 393 tLDPDKTVMDNLAEG-------KQEvmVNGRPRHVLGYLQ-DFLFP--PKramtpvrALSGGERNRLLLARLFLKPSNLL 462
Cdd:PRK11000 86 -LYPHLSVAENMSFGlklagakKEE--INQRVNQVAEVLQlAHLLDrkPK-------ALSGGQRQRVAIGRTLVAEPSVF 155
|
170
....*....|
gi 1437745527 463 ILDEPTNDLD 472
Cdd:PRK11000 156 LLDEPLSNLD 165
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-233 |
1.23e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 59.75 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 6 LTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDIeGTIFD 85
Cdd:PRK13650 10 LTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI-GMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 86 -----FVAQGVAEDAQYITEyhrvskvietdpseknlNRLAQLQEvldnrnlwlLDSRIAEVLEKLGLNG--EAELSSLS 158
Cdd:PRK13650 89 npdnqFVGATVEDDVAFGLE-----------------NKGIPHEE---------MKERVNEALELVGMQDfkEREPARLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 159 GGWLRKAALGRALVSAPKVLFLDEPTNHLD----IETILWLEKFLKDFQGSIVFISHDRSFIrNMATRIIDLDRGKLSS 233
Cdd:PRK13650 143 GGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVES 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
326-473 |
1.26e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.46 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 326 NYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI-HCGtklEVAYFDQHRATLdpDKTVMDNL 404
Cdd:TIGR01271 433 NFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIkHSG---RISFSPQTSWIM--PGTIKDNI 507
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 405 AEGKQevMVNGRPRHVLGYLQ---DFLFPPKRAMTPVR----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR01271 508 IFGLS--YDEYRYTSVIKACQleeDIALFPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-212 |
1.27e-09 |
|
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: 59.58 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 21 NTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLvtARLQQDPPRDIEGTIFDFVAQG--------V 91
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgQDI--AAMSRKELRELRRKKISMVFQSfallphrtV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 92 AEDAQYITEYHRVSKvietdpseknLNRLAqlqevldnrnlwlldsRIAEVLEKLGLNGEAE--LSSLSGGWLRKAALGR 169
Cdd:cd03294 120 LENVAFGLEVQGVPR----------AEREE----------------RAAEALELVGLEGWEHkyPDELSGGMQQRVGLAR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1437745527 170 ALVSAPKVLFLDEPTNHLD--I-----ETILWLEkflKDFQGSIVFISHD 212
Cdd:cd03294 174 ALAVDPDILLMDEAFSALDplIrremqDELLRLQ---AELQKTIVFITHD 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
321-472 |
1.35e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.87 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLK-LMLGDLkADSGrihcgtKLEVA--YFDQHRAT---- 393
Cdd:PRK11124 4 QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRvLNLLEM-PRSG------TLNIAgnHFDFSKTPsdka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 394 ----------------LDPDKTVMDNLAE--------GKQEVMvnGRPRHVLGYLQ--DFL--FPPKramtpvraLSGGE 445
Cdd:PRK11124 77 irelrrnvgmvfqqynLWPHLTVQQNLIEapcrvlglSKDQAL--ARAEKLLERLRlkPYAdrFPLH--------LSGGQ 146
|
170 180
....*....|....*....|....*...
gi 1437745527 446 RNRLLLAR-LFLKPSNLLiLDEPTNDLD 472
Cdd:PRK11124 147 QQRVAIARaLMMEPQVLL-FDEPTAALD 173
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
157-473 |
1.81e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 157 LSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIE---TILWLEKFL-KDFQGSIVFISHDRSFIRNMATRIIDLDRGKLS 232
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 233 SwpgnydkyLESKEEALRVEEQqnaEFDRKLAQeeAWIRQGikarRTRNEGRVRALKALRVERSERRE--------VLGS 304
Cdd:PRK10261 249 E--------TGSVEQIFHAPQH---PYTRALLA--AVPQLG----AMKGLDYPRRFPLISLEHPAKQEppieqdtvVDGE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 305 ARMQVEE-ATRsgkivFELEDVNYSIGTRRL--VRDFSAKVQRGDKIALVGPNGCGKTT----LLKLM---LGDLKADSG 374
Cdd:PRK10261 312 PILQVRNlVTR-----FPLRSGLLNRVTREVhaVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVesqGGEIIFNGQ 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 375 RIHC--GTKLEVA------YFDQHRATLDPDKTVMDNLAEG-KQEVMVNGRP--RHVLGYLQDFLFPPKRAMTPVRALSG 443
Cdd:PRK10261 387 RIDTlsPGKLQALrrdiqfIFQDPYASLDPRQTVGDSIMEPlRVHGLLPGKAaaARVAWLLERVGLLPEHAWRYPHEFSG 466
|
330 340 350
....*....|....*....|....*....|.
gi 1437745527 444 GERNRLLLAR-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK10261 467 GQRQRICIARaLALNP-KVIIADEAVSALDV 496
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-473 |
1.95e-09 |
|
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: 60.22 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 3 LISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLD--DGQVVYEQdlvtARLQQDPPRDIE 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSG----SPLKASNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 gtifdfvAQGVAEDAQYITEYHRVSkVIEtdpsekNL---NRLAQLQEVLDNRNLWLldsRIAEVLEKLGL---NGEAEL 154
Cdd:TIGR02633 77 -------RAGIVIIHQELTLVPELS-VAE------NIflgNEITLPGGRMAYNAMYL---RAKNLLRELQLdadNVTRPV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 155 SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHL---DIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKl 231
Cdd:TIGR02633 140 GDYGGGQQQLVEIAKALNKQARLLILDEPSSSLtekETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 232 sswpgnydkyleskeealrveeqqnaefdrklaqeeawiRQGIKARRTRNEGRVRALKALRVERSerrevlgsarMQVEE 311
Cdd:TIGR02633 219 ---------------------------------------HVATKDMSTMSEDDIITMMVGREITS----------LYPHE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 312 ATRSGKIVFELEDVN--YSIGTRR-LVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGdlkADSGRiHCGTklevAYFD 388
Cdd:TIGR02633 250 PHEIGDVILEARNLTcwDVINPHRkRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG---AYPGK-FEGN----VFIN 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 389 QHRATLdpdKTVMDNLAEGKqeVMV-NGRPRH------------VLGYLQDFLFPPK-----------RAMT-------- 436
Cdd:TIGR02633 322 GKPVDI---RNPAQAIRAGI--AMVpEDRKRHgivpilgvgkniTLSVLKSFCFKMRidaaaelqiigSAIQrlkvktas 396
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1437745527 437 ---PVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR02633 397 pflPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
326-473 |
1.96e-09 |
|
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: 59.10 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 326 NYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI-HCGtklEVAYFDQHrATLDPDkTVMDNL 404
Cdd:cd03291 44 NLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkHSG---RISFSSQF-SWIMPG-TIKENI 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 405 AEGKQevMVNGRPRHVLGYLQ---DFLFPPKRAMTPVR----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03291 119 IFGVS--YDEYRYKSVVKACQleeDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
323-473 |
2.02e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.78 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 323 EDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC----GTKLEVA------------- 385
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdGQLRDLYalseaerrrllrt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 386 ---YFDQH-RATLDPDKTVMDNLAEgkqEVMVNGRpRH-------VLGYLQDFLFPPKRAMTPVRALSGGERNRLLLARL 454
Cdd:PRK11701 90 ewgFVHQHpRDGLRMQVSAGGNIGE---RLMAVGA-RHygdiratAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARN 165
|
170
....*....|....*....
gi 1437745527 455 FLKPSNLLILDEPTNDLDV 473
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDV 184
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-231 |
2.22e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.55 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK-EQPlDDGQVVyeqdlVTARLQqdPPrdIE-GTIFDFVAQGvAEDAQ 96
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEP-TSGRVE-----VNGRVS--AL--LElGAGFHPELTG-RENIY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 97 YITEYHRVSKvietdpseknlnrlaqlQEVldnrnlwllDSRIAEVLEKLGLnGEA---ELSSLSGGwlRKAALGRALVS 173
Cdd:COG1134 111 LNGRLLGLSR-----------------KEI---------DEKFDEIVEFAEL-GDFidqPVKTYSSG--MRARLAFAVAT 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 174 A--PKVLFLDEptnhldietilWL-----------EKFLKDFQ---GSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:COG1134 162 AvdPDILLVDE-----------VLavgdaafqkkcLARIRELResgRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-237 |
2.50e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 60.12 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLA-KEQPLDDGQVVYEQDLVTarLQQDPPRDIEGTIFDFVAQgvaedaqy 97
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGcLDKPTSGTYRVAGQDVAT--LDADALAQLRREHFGFIFQ-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 98 itEYHRVSKVietdPSEKNLNRLAQLQEVLDNRNLwlldSRIAEVLEKLGLNGEAEL--SSLSGGWLRKAALGRALVSAP 175
Cdd:PRK10535 94 --RYHLLSHL----TAAQNVEVPAVYAGLERKQRL----LRAQELLQRLGLEDRVEYqpSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 176 KVLFLDEPTNHLDI---ETILWLEKFLKDfQGSIVFI-SHDRSfIRNMATRIIDLDRGKLSSWPGN 237
Cdd:PRK10535 164 QVILADEPTGALDShsgEEVMAILHQLRD-RGHTVIIvTHDPQ-VAAQAERVIEIRDGEIVRNPPA 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
321-545 |
2.54e-09 |
|
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: 60.20 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLG--DLKADSGRI---------------------- 376
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpskvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 377 --HCGTKLE--------------------VAYFDQHRATLDPDKTVMDNLAEGKQEVMVNGRprHVLGYLQDFLFPPK-- 432
Cdd:TIGR03269 82 cpVCGGTLEpeevdfwnlsdklrrrirkrIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGK--EAVGRAVDLIEMVQls 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 433 -RAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL----ELLEELVDAYQGTVLLVSHDREFVDNSVTEC 507
Cdd:TIGR03269 160 hRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1437745527 508 -WIFEG--------DGVINSYVGGYYDAQQQRaqSVSLKNEANKSRN 545
Cdd:TIGR03269 240 iWLENGeikeegtpDEVVAVFMEGVSEVEKEC--EVEVGEPIIKVRN 284
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
32-231 |
3.17e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 58.06 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 32 VCLVGRNGAGKSTLLRVLA-KEQPLDDGQVVYEQDLVTARlqqdpprDIEGTIfdfvaqGVAEDAQYITEYHRVSKVIEt 110
Cdd:PRK10619 34 ISIIGSSGSGKSTFLRCINfLEKPSEGSIVVNGQTINLVR-------DKDGQL------KVADKNQLRLLRTRLTMVFQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 111 dpsEKNL-NRLAQLQEVLDN--RNLWLLDS----RIAEVLEKLGLNGEAEL---SSLSGGWLRKAALGRALVSAPKVLFL 180
Cdd:PRK10619 100 ---HFNLwSHMTVLENVMEApiQVLGLSKQeareRAVKYLAKVGIDERAQGkypVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 181 DEPTNHLDIE---TILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK10619 177 DEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-231 |
3.18e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.28 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 14 SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPpRDIEGTIFDfvaqgvAE 93
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV-RKFVGLVFQ------NP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 94 DAQYIteyhrvSKVIETDPSEKNLNrLAQLQEVLDNRnlwlldsrIAEVLEKLGLNGEAELSS--LSGGWLRKAALGRAL 171
Cdd:PRK13652 88 DDQIF------SPTVEQDIAFGPIN-LGLDEETVAHR--------VSSALHMLGLEELRDRVPhhLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 172 VSAPKVLFLDEPTNHLD----IETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
334-496 |
3.20e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.90 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 334 LVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGR-IHCGTKL--------------EVAYFDQHRATLdPDK 398
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDvIFNGQPMsklssaakaelrnqKLGFIYQFHHLL-PDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 399 TVMDNLAE-----GKQEVMVNGRPRHVLGYLQdflfPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11629 103 TALENVAMplligKKKPAEINSRALEMLAAVG----LEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180
....*....|....*....|....*..
gi 1437745527 474 ETLE---LLEELVDAYQGTV-LLVSHD 496
Cdd:PRK11629 179 RNADsifQLLGELNRLQGTAfLVVTHD 205
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-233 |
3.73e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.21 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDnTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQD---PPRDIEGTIFDFVAQ 89
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikPVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 90 GVAEDAqyiteyhrVSKVIETDPSEKNLNRlaqlQEVldnrnlwllDSRIAEVLEKLGLNGEAELSS---LSGGWLRKAA 166
Cdd:PRK13643 96 QLFEET--------VLKDVAFGPQNFGIPK----EKA---------EKIAAEKLEMVGLADEFWEKSpfeLSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 167 LGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQ---GSIVFISHDRSFIRNMATRIIDLDRGKLSS 233
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHqsgQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-212 |
4.72e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.10 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 18 LLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKeqpLDDGQVvYEQDLVTARLQQdppRDIEGTifdfvAQGVAEDAQY 97
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAG---LDDGSS-GEVSLVGQPLHQ---MDEEAR-----AKLRAKHVGF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 98 ITEYHrvsKVIETDPSEKNLNRLAQLQEVLDNRNlwllDSRIAEVLEKLGLNGEAEL--SSLSGGWLRKAALGRALVSAP 175
Cdd:PRK10584 93 VFQSF---MLIPTLNALENVELPALLRGESSRQS----RNGAKALLEQLGLGKRLDHlpAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1437745527 176 KVLFLDEPTNHLDIETILWLEKFL----KDFQGSIVFISHD 212
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-232 |
5.04e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.88 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARlqqdpprdiegTIFDFVAQGVA 92
Cdd:COG1129 262 LSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR-----------SPRDAIRAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 93 edaqYITEYHRVSKVIETDPSEKNLNrLAQLQEVldnRNLWLLDSR-----IAEVLEKLGL---NGEAELSSLSGGWLRK 164
Cdd:COG1129 331 ----YVPEDRKGEGLVLDLSIRENIT-LASLDRL---SRGGLLDRRreralAEEYIKRLRIktpSPEQPVGNLSGGNQQK 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 165 AALGRALVSAPKVLFLDEPTNHLDIET---ILwleKFLKDF--QG-SIVFISHDRSFIRNMATRIIDLDRGKLS 232
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGIDVGAkaeIY---RLIRELaaEGkAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-224 |
5.42e-09 |
|
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: 59.03 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 26 IDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDlvtarlqqdpprdiegtifdfvaqgVAEDAQYITeyhrvs 105
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-------------------------ISYKPQYIS------ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 106 kvIETDpseknlnrlAQLQEVLDNRNLWLLDSRI--AEVLEKLGLNG--EAELSSLSGGWLRKAALGRALVSAPKVLFLD 181
Cdd:COG1245 412 --PDYD---------GTVEEFLRSANTDDFGSSYykTEIIKPLGLEKllDKNVKDLSGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1437745527 182 EPTNHLDIETILWLEKFLKDF---QGSIVF-ISHDRSFIRNMATRII 224
Cdd:COG1245 481 EPSAHLDVEQRLAVAKAIRRFaenRGKTAMvVDHDIYLIDYISDRLM 527
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
310-472 |
5.55e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 57.35 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 310 EEATRSGKIVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMlgdlkadsGRIH-----CGTKLEV 384
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL--------NRMNdlipgARVEGEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 385 AYFDQ--HRATLDPD-----------------KTVMDNLAEGkqeVMVNG-RPRHVLGYL-QDFLfppKRAM-------- 435
Cdd:COG1117 74 LLDGEdiYDPDVDVVelrrrvgmvfqkpnpfpKSIYDNVAYG---LRLHGiKSKSELDEIvEESL---RKAAlwdevkdr 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1437745527 436 --TPVRALSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLD 472
Cdd:COG1117 148 lkKSALGLSGGQQQRLCIARaLAVEPEVLL-MDEPTSALD 186
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
311-496 |
5.66e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.36 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 311 EATRSGKIVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKleVAYFDQH 390
Cdd:PRK14246 2 EAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK--VLYFGKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 391 RATLD------------------PDKTVMDNLA--------EGKQEV--MVNGRPRHVLGYLQDFlfppKRAMTPVRALS 442
Cdd:PRK14246 80 IFQIDaiklrkevgmvfqqpnpfPHLSIYDNIAyplkshgiKEKREIkkIVEECLRKVGLWKEVY----DRLNSPASQLS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 443 GGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETLELLEELVDAYQG--TVLLVSHD 496
Cdd:PRK14246 156 GGQQQRLTIARaLALKP-KVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
344-501 |
5.68e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 344 RGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHcgtklevayfdqhraTLDPDKTVMDNLAEGKQEVMVNGrprhvlgy 423
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------YIDGEDILEEVLDQLLLIIVGGK-------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 424 lqdflfppkramtpVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQG---------TVLLVS 494
Cdd:smart00382 58 --------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllkseknlTVILTT 123
|
....*..
gi 1437745527 495 HDREFVD 501
Cdd:smart00382 124 NDEKDLG 130
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-231 |
5.71e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.25 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 26 IDENERVCLVGRNGAGKSTLL-----------RVLAKEQPLDDGQVvYEQDLVTARL--QQDPPrdIEGTIFdfvaqgva 92
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLarmagllpgsgSIQFAGQPLEAWSA-AELARHRAYLsqQQTPP--FAMPVF-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 93 edaQYITeYHRVSKViETDPSEKNLNRLAQLqevldnrnLWLLDsriaevleKLGLNgeaeLSSLSGG-W--LRKAA--- 166
Cdd:PRK03695 88 ---QYLT-LHQPDKT-RTEAVASALNEVAEA--------LGLDD--------KLGRS----VNQLSGGeWqrVRLAAvvl 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 167 -LGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QG-SIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK03695 143 qVWPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELcqQGiAVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-231 |
6.08e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 57.72 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDA--PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDI 79
Cdd:PRK13635 4 EIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 80 eGTIFD-----FVAQGVAEDAQYITEYHRVskvietdPSEKNLNRLAQ-LQEVldnrnlwlldsRIAEVLEKlglngeaE 153
Cdd:PRK13635 84 -GMVFQnpdnqFVGATVQDDVAFGLENIGV-------PREEMVERVDQaLRQV-----------GMEDFLNR-------E 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 154 LSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLD-------IETIlwleKFLKDFQGSIVF-ISHDRSFIRNmATRIID 225
Cdd:PRK13635 138 PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETV----RQLKEQKGITVLsITHDLDEAAQ-ADRVIV 212
|
....*.
gi 1437745527 226 LDRGKL 231
Cdd:PRK13635 213 MNKGEI 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-473 |
6.34e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.86 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTArlqqDPPRDieg 81
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTF----NGPKS--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 82 tifdfvaqgvAEDAQyITEYHrvskvietdpseKNLNRLAQLQeVLDN------------RNLW-LLDSRIAEVLEKLGL 148
Cdd:PRK10762 76 ----------SQEAG-IGIIH------------QELNLIPQLT-IAENiflgrefvnrfgRIDWkKMYAEADKLLARLNL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 149 NGEAE--LSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHL-DIET--ILWLEKFLKDFQGSIVFISHDRSFIRNMATRI 223
Cdd:PRK10762 132 RFSSDklVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETesLFRVIRELKSQGRGIVYISHRLKEIFEICDDV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 224 IDLDRGKLsswpgnydkyleskeealrVEEQQNAEFDrklaqEEAWIRQGIkarrtrneGRVRALKALRVERserreVLG 303
Cdd:PRK10762 212 TVFRDGQF-------------------IAEREVADLT-----EDSLIEMMV--------GRKLEDQYPRLDK-----APG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 304 SARMQVEEATRSGkivfeledvnysigtrrlVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI------- 376
Cdd:PRK10762 255 EVRLKVDNLSGPG------------------VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVtldghev 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 377 -----HCGTKLEVAYF--DQHRATLDPDKTVMDNLA--------------EGKQEVMVNGrprhvlgylqDF--LFPPKr 433
Cdd:PRK10762 317 vtrspQDGLANGIVYIseDRKRDGLVLGMSVKENMSltalryfsraggslKHADEQQAVS----------DFirLFNIK- 385
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1437745527 434 amTPVRA-----LSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK10762 386 --TPSMEqaiglLSGGNQQKVAIARgLMTRP-KVLILDEPTRGVDV 428
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-232 |
6.79e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 15 DAPLLDNTDL----FIDEN------ERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARlqqdpprdiegTIF 84
Cdd:PRK15439 265 GAPVLTVEDLtgegFRNISlevragEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAL-----------STA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 85 DFVAQGVAedaqYITEYHRVSKVIETDPSEKNLNRLAQlqevlDNRNLWLLDSRIAEVLEK----LGL---NGEAELSSL 157
Cdd:PRK15439 334 QRLARGLV----YLPEDRQSSGLYLDAPLAWNVCALTH-----NRRGFWIKPARENAVLERyrraLNIkfnHAEQAARTL 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 158 SGGWLRKAALGRALVSAPKVLFLDEPTNHLDIET---ILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKLS 232
Cdd:PRK15439 405 SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSArndIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-231 |
8.68e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 56.92 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 3 LISLTGAYLAFSDA-PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVvyeqdLVTARLQQDPP----- 76
Cdd:PRK13644 1 MIRLENVSYSYPDGtPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV-----LVSGIDTGDFSklqgi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 77 RDIEGTIFD-----FVAQGVAEDAQYITEyhrvskvietdpseknlnrlaqlqevldnrNLWL----LDSRIAEVLEKLG 147
Cdd:PRK13644 76 RKLVGIVFQnpetqFVGRTVEEDLAFGPE------------------------------NLCLppieIRKRVDRALAEIG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 148 LNGEAELS--SLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIE---TILWLEKFLKDFQGSIVFISHDRSFIRNmATR 222
Cdd:PRK13644 126 LEKYRHRSpkTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDsgiAVLERIKKLHEKGKTIVYITHNLEELHD-ADR 204
|
....*....
gi 1437745527 223 IIDLDRGKL 231
Cdd:PRK13644 205 IIVMDRGKI 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-276 |
8.85e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 56.79 E-value: 8.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAF----SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTA----R-- 70
Cdd:COG4525 1 MSMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpgadRgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 71 -LQQD---PPRD-IEGTIFDFVAQGVAEDAqyiteyhrvskvietdpseknlnRLAqlqevldnrnlwlldsRIAEVLEK 145
Cdd:COG4525 81 vFQKDallPWLNvLDNVAFGLRLRGVPKAE-----------------------RRA----------------RAEELLAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 146 LGLNGEAE--LSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDI---ETI------LWlekflKDFQGSIVFISHDRS 214
Cdd:COG4525 122 VGLADFARrrIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAltrEQMqellldVW-----QRTGKGVFLITHSVE 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745527 215 FIRNMATRIIdldrgKLSSWPGnydkyleskeealRVEEQQNAEFDRKLAQEEAwIRQgIKA 276
Cdd:COG4525 197 EALFLATRLV-----VMSPGPG-------------RIVERLELDFSRRFLAGED-ARA-IKS 238
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-225 |
8.91e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.72 E-value: 8.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 31 RVC-LVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVT-------ARL-----QQDPPrdIEG-TIFDFVAQGvaedaQ 96
Cdd:PRK10575 38 KVTgLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswsskafARKvaylpQQLPA--AEGmTVRELVAIG-----R 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 97 YiteyhrvskvietdPSEKNLNRLAQlqevlDNRnlwlldSRIAEVLEKLGLNGEAE--LSSLSGGWLRKAALGRALVSA 174
Cdd:PRK10575 111 Y--------------PWHGALGRFGA-----ADR------EKVEEAISLVGLKPLAHrlVDSLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 175 PKVLFLDEPTNHLDIE---TILWLEKFLKDFQG-SIVFISHDrsfiRNMATRIID 225
Cdd:PRK10575 166 SRCLLLDEPTSALDIAhqvDVLALVHRLSQERGlTVIAVLHD----INMAARYCD 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-231 |
9.59e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 56.56 E-value: 9.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 10 YLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQV-VYEQDL--VTAR--------LQQDPPrd 78
Cdd:PRK11231 9 TVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVfLGDKPIsmLSSRqlarrlalLPQHHL-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 79 iegtifdfVAQGVAedAQYITEYHRvskvietDPSEKNLNRLAQLQEvldnrnlwlldSRIAEVLEKLGLNGEAE--LSS 156
Cdd:PRK11231 87 --------TPEGIT--VRELVAYGR-------SPWLSLWGRLSAEDN-----------ARVNQAMEQTRINHLADrrLTD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 157 LSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG---SIVFISHDrsfiRNMATRIID----LDRG 229
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTqgkTVVTVLHD----LNQASRYCDhlvvLANG 214
|
..
gi 1437745527 230 KL 231
Cdd:PRK11231 215 HV 216
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-226 |
1.02e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDD-----------GQVVYEQDLVTA 69
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrvegrveffNQNIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 70 RLQQD------PPRDIEGTIFDFVAQGVaedaqyiteyhrvsKVIETDPsekNLNRLAQLQEVLDNRNLWlldSRIAEVL 143
Cdd:PRK14258 85 RLRRQvsmvhpKPNLFPMSVYDNVAYGV--------------KIVGWRP---KLEIDDIVESALKDADLW---DEIKHKI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 144 EKLGLNgeaelssLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF----QGSIVFISHDRSFIrnm 219
Cdd:PRK14258 145 HKSALD-------LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHNLHQV--- 214
|
....*..
gi 1437745527 220 aTRIIDL 226
Cdd:PRK14258 215 -SRLSDF 220
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
1.18e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 56.54 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAF--SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLA---KEQPLD---DGQVVYEQDLVTARlqq 73
Cdd:PRK13632 6 VMIKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTgllKPQSGEikiDGITISKENLKEIR--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 74 dppRDIeGTIF-----DFVAQGVAEDAQYITEYHRVskvietDPSEknlnrlaqlqevldnrnlwlLDSRIAEVLEKLGL 148
Cdd:PRK13632 83 ---KKI-GIIFqnpdnQFIGATVEDDIAFGLENKKV------PPKK--------------------MKDIIDDLAKKVGM 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 149 NG--EAELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG----SIVFISHDRSFIRNmATR 222
Cdd:PRK13632 133 EDylDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrkkTLISITHDMDEAIL-ADK 211
|
....*....
gi 1437745527 223 IIDLDRGKL 231
Cdd:PRK13632 212 VIVFSEGKL 220
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
312-472 |
1.24e-08 |
|
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: 57.91 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 312 ATRSGKIVFEleDVNYSIGTRR-LVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKL-EVAyfd 388
Cdd:COG5265 352 VVGGGEVRFE--NVSFGYDPERpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIdGQDIrDVT--- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 389 QH--RATLD--PDKTVM------DNLAEGK-----QEVMVNGRprhvLGYLQDF---LfpPKRAMTPV--RA--LSGGER 446
Cdd:COG5265 427 QAslRAAIGivPQDTVLfndtiaYNIAYGRpdaseEEVEAAAR----AAQIHDFiesL--PDGYDTRVgeRGlkLSGGEK 500
|
170 180
....*....|....*....|....*.
gi 1437745527 447 NRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALD 526
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-225 |
1.31e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.32 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLD-----DGQVVYE--------QDLVT 68
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNghniysprTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 69 AR------LQQdpPRDIEGTIFDFVAQGVAEDAqyITEYHRVSKVIetdpsEKNLNRLAQLQEVLDNrnlwLLDSRIAev 142
Cdd:PRK14239 84 LRkeigmvFQQ--PNPFPMSIYENVVYGLRLKG--IKDKQVLDEAV-----EKSLKGASIWDEVKDR----LHDSALG-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 143 leklglngeaelssLSGGWLRKAALGRALVSAPKVLFLDEPTNHLD------IETILWLekfLKDfQGSIVFISHdrsfi 216
Cdd:PRK14239 149 --------------LSGGQQQRVCIARVLATSPKIILLDEPTSALDpisagkIEETLLG---LKD-DYTMLLVTR----- 205
|
250
....*....|.
gi 1437745527 217 rNM--ATRIID 225
Cdd:PRK14239 206 -SMqqASRISD 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
318-472 |
1.32e-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: 55.96 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 318 IVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKLEVAYFDQHRATLDP 396
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 397 --------DKTVMDNLAEGKQevmvnGRPRHVLGYL------QDFLFP-PKRAMTPV----RALSGGERNRLLLARLFLK 457
Cdd:cd03252 81 vlqenvlfNRSIRDNIALADP-----GMSMERVIEAaklagaHDFISElPEGYDTIVgeqgAGLSGGQRQRIAIARALIH 155
|
170
....*....|....*
gi 1437745527 458 PSNLLILDEPTNDLD 472
Cdd:cd03252 156 NPRILIFDEATSALD 170
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
138-228 |
1.33e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 55.57 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 138 RIAEVLEKLGLNGEAE--LSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKF----LKDFQGSIVFISH 211
Cdd:COG4136 113 RVEQALEEAGLAGFADrdPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTH 192
|
90
....*....|....*..
gi 1437745527 212 DRSFIRNmATRIIDLDR 228
Cdd:COG4136 193 DEEDAPA-AGRVLDLGN 208
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-231 |
1.35e-08 |
|
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: 56.08 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVL------AKEQPLDDGQVVYEQDLVTARLQ-----QDPPrdiegtIFD 85
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvSSGSILIDGQDIREVTLDSLRRAigvvpQDTV------LFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 86 fvaqgvaEDAQYITEYHRVskvietDPSEKNLNRLAQLqevldnrnlwlldSRIAEVLEKL--GLN---GEAELSsLSGG 160
Cdd:cd03253 89 -------DTIGYNIRYGRP------DATDEEVIEAAKA-------------AQIHDKIMRFpdGYDtivGERGLK-LSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 161 WLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKD-FQG-SIVFISHDRSFIRNmATRIIDLDRGKL 231
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDvSKGrTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
323-473 |
1.40e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.15 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 323 EDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLK----LML---GDLKADSGRIHCGTKLEVAY---FDQHRA 392
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRtlsrLMTpahGHVWLDGEHIQHYASKEVARrigLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 393 TLDPDKTVMDNLAEGK---QEVMVNGRPRHvlgylQDFLFPPKRAM-------TPVRALSGGERNRLLLARLFLKPSNLL 462
Cdd:PRK10253 91 TTPGDITVQELVARGRyphQPLFTRWRKED-----EEAVTKAMQATgithladQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170
....*....|.
gi 1437745527 463 ILDEPTNDLDV 473
Cdd:PRK10253 166 LLDEPTTWLDI 176
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
30-231 |
1.51e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 57.66 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 30 ERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE----QDLVTARLQqdppRDIeGTIFdfvaqgvaEDA----QYITEY 101
Cdd:PRK13657 362 QTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDgtdiRTVTRASLR----RNI-AVVF--------QDAglfnRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 102 HRVSKvieTDPSEKNLNRLAQLQEVLD--NRNLWLLDSRIAEvleklglNGeaelSSLSGGWLRKAALGRALVSAPKVLF 179
Cdd:PRK13657 429 IRVGR---PDATDEEMRAAAERAQAHDfiERKPDGYDTVVGE-------RG----RQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 180 LDEPTNHLDIETilwlEKFLKD-----FQGSIVF-ISHDRSFIRNmATRIIDLDRGKL 231
Cdd:PRK13657 495 LDEATSALDVET----EAKVKAaldelMKGRTTFiIAHRLSTVRN-ADRILVFDNGRV 547
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-234 |
1.79e-08 |
|
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: 55.11 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVL------AKEQPLDDGQVVYEQDLVTAR-----LQQDPprdiegTIFd 85
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALfrfleaEEGKIEIDGIDISTIPLEDLRssltiIPQDP------TLF- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 86 fvaqgvaedaqyiteyhrvSKVIETDPSEKNLNRLAQLQEVLdnrnlwlldsRIAEVleklGLNgeaelssLSGGWLRKA 165
Cdd:cd03369 95 -------------------SGTIRSNLDPFDEYSDEEIYGAL----------RVSEG----GLN-------LSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745527 166 ALGRALVSAPKVLFLDEPTNHLDIETILWLEKFL-KDFQGS-IVFISHDRSFIRNMAtRIIDLDRGKLSSW 234
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIrEEFTNStILTIAHRLRTIIDYD-KILVMDAGEVKEY 204
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
319-472 |
1.80e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 56.18 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 319 VFELEDVNYSI--GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKLEVAYFDQHRATL- 394
Cdd:PRK13635 5 IIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVgGMVLSEETVWDVRRQVg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 ----DPDK-----TVMDNLAEGKQEvmvNGRPR-----------HVLGyLQDFL-FPPKRamtpvraLSGGERNRLLLAR 453
Cdd:PRK13635 85 mvfqNPDNqfvgaTVQDDVAFGLEN---IGVPReemvervdqalRQVG-MEDFLnREPHR-------LSGGQKQRVAIAG 153
|
170 180
....*....|....*....|
gi 1437745527 454 -LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13635 154 vLALQPD-IIILDEATSMLD 172
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-229 |
1.80e-08 |
|
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: 55.55 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAK-EQPlDDGQVVYEQDLVTArlqQDPPRDIEGTIFDFVAQGVAEDAQY 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQP-TSGGVILEGKQITE---PGPDRMVVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 98 ITeyhrVSKVIETDPSEKNlnrlaqlQEVLDnrnlwlldsriaEVLEKLGLNGEAE--LSSLSGGWLRKAALGRALVSAP 175
Cdd:TIGR01184 77 LA----VDRVLPDLSKSER-------RAIVE------------EHIALVGLTEAADkrPGQLSGGMKQRVAIARALSIRP 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 176 KVLFLDEPTNHLDIETILWL-EKFLKDFQGS---IVFISHDRSFIRNMATRIIDLDRG 229
Cdd:TIGR01184 134 KVLLLDEPFGALDALTRGNLqEELMQIWEEHrvtVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-224 |
1.81e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.64 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 20 DNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVY-EQDL----------VTARLQ---QDP-----PRdie 80
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlGKDLlgmkddewraVRSDIQmifQDPlaslnPR--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 GTIFDFVAQGVaedaqyITEYHRVSKvietdpseknlnrlaqlQEVLDnrnlwlldsRIAEVLEKLGLngeaeLSSL--- 157
Cdd:PRK15079 115 MTIGEIIAEPL------RTYHPKLSR-----------------QEVKD---------RVKAMMLKVGL-----LPNLinr 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 158 -----SGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG----SIVFISHDRSFIRNMATRII 224
Cdd:PRK15079 158 yphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemglSLIFIAHDLAVVKHISDRVL 233
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
321-376 |
1.88e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.93 E-value: 1.88e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI 376
Cdd:PRK11831 9 DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-231 |
1.90e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 55.94 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDIE---GTIFDFVAQGVAEDA 95
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRkriGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 96 qyiteyhrVSKVIETDPSEKNLNrlaqLQEVLDnrnlwlldsRIAEVLEKLGLNGEAELSS---LSGGWLRKAALGRALV 172
Cdd:PRK13646 103 --------VEREIIFGPKNFKMN----LDEVKN---------YAHRLLMDLGFSRDVMSQSpfqMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 173 SAPKVLFLDEPTNHLDIETILWLEKFLKDFQ----GSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
316-473 |
1.91e-08 |
|
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: 55.11 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 316 GKIVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHcgtklevayFDQHRATLD 395
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE---------IDGIDISTI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 396 PDKTVMDNLAEGKQE-VMVNGRPRHVLG----YLQDFLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:cd03369 76 PLEDLRSSLTIIPQDpTLFSGTIRSNLDpfdeYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
...
gi 1437745527 471 LDV 473
Cdd:cd03369 156 IDY 158
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-188 |
2.17e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.16 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 11 LAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQP-----LDDGQVVYEQDLVTARLQ-----QDPpRDIE 80
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslKINGIELRELDPESWRKHlswvgQNP-QLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 GTIFDFVAQGvaedAQYITEyhrvskvietdpseknlnrlAQLQEVLDNrnlwlldSRIAEVLEKL--GLN---GEAElS 155
Cdd:PRK11174 437 GTLRDNVLLG----NPDASD--------------------EQLQQALEN-------AWVSEFLPLLpqGLDtpiGDQA-A 484
|
170 180 190
....*....|....*....|....*....|...
gi 1437745527 156 SLSGGWLRKAALGRALVSAPKVLFLDEPTNHLD 188
Cdd:PRK11174 485 GLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-231 |
2.69e-08 |
|
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: 56.73 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVvyeqdlvTARLQQDPprdIEGTIFDFVAQGVAEdaQYI 98
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV-------NVRVGDEW---VDMTKPGPDGRGRAK--RYI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 99 ----TEY----HR-----VSKVIETD-PSEknlnrLAQLQEVLDNRNLWLLDSRIAEVLEKLGlngeaelSSLSGGWLRK 164
Cdd:TIGR03269 368 gilhQEYdlypHRtvldnLTEAIGLElPDE-----LARMKAVITLKMVGFDEEKAEEILDKYP-------DELSEGERHR 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 165 AALGRALVSAPKVLFLDEPTNHLD-------IETILwleKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDpitkvdvTHSIL---KAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
322-500 |
2.85e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.44 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 322 LEDVNYSIgtrrlvrdfsakvQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklevaYFDQHRATldpDKTVm 401
Cdd:PRK13637 23 LDNVNIEI-------------EDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI---------IIDGVDIT---DKKV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 402 dNLAEGKQEV-MVNGRPRHVL---GYLQDFLFPP--------------KRAMTPVR------------ALSGGERNRLLL 451
Cdd:PRK13637 77 -KLSDIRKKVgLVFQYPEYQLfeeTIEKDIAFGPinlglseeeienrvKRAMNIVGldyedykdkspfELSGGQKRRVAI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 452 ARLF-LKPSnLLILDEPTNDLDVETLELLEELV----DAYQGTVLLVSHDREFV 500
Cdd:PRK13637 156 AGVVaMEPK-ILILDEPTAGLDPKGRDEILNKIkelhKEYNMTIILVSHSMEDV 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-231 |
2.94e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.61 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDIE---GTIFDFvaqgvaEDA 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRkkvSLVFQF------PEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 96 QYITEyhRVSKVIETDPseknLNRLAQLQEVLDNRNLWLldsriaevlEKLGLNGEAELSS---LSGGWLRKAALGRALV 172
Cdd:PRK13641 97 QLFEN--TVLKDVEFGP----KNFGFSEDEAKEKALKWL---------KKVGLSEDLISKSpfeLSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745527 173 SAPKVLFLDEPTNHLDIETILWLEKFLKDFQG---SIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
337-473 |
3.19e-08 |
|
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: 54.64 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 337 DFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLE---------------VAYFDQHRATLDpdKTVM 401
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKPWLLN--ATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 402 DNLAEG----KQevmvngRPRHVLG--YLQ-DFLFPPKRAMTPVRA----LSGGERNRLLLARLFLKPSNLLILDEPTND 470
Cdd:cd03290 97 ENITFGspfnKQ------RYKAVTDacSLQpDIDLLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
...
gi 1437745527 471 LDV 473
Cdd:cd03290 171 LDI 173
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
317-468 |
3.30e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.89 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 317 KIVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLEVAYFDQHRA 392
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkdiTDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 393 TLDPD-------KTVMDNLAEG---KQEVMVNGRPRHVLGylqdfLFPPKRAMTPVRA--LSGGERNRLLLARLFLKPSN 460
Cdd:PRK11614 83 AIVPEgrrvfsrMTVEENLAMGgffAERDQFQERIKWVYE-----LFPRLHERRIQRAgtMSGGEQQMLAIGRALMSQPR 157
|
....*...
gi 1437745527 461 LLILDEPT 468
Cdd:PRK11614 158 LLLLDEPS 165
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-231 |
3.42e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.19 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 14 SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVL-AKEQPLDDGQVVYEQDLVTarLQQDPPRDIE---GTIFD---- 85
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLInGLLLPDDNPNSKITVDGIT--LTAKTVWDIRekvGIVFQnpdn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 86 -FVAQGVAEDAQYITEyhrvskvietdpseknlNRLAQLQEVLdnrnlwlldSRIAEVLEKLGLNG--EAELSSLSGGWL 162
Cdd:PRK13640 96 qFVGATVGDDVAFGLE-----------------NRAVPRPEMI---------KIVRDVLADVGMLDyiDSEPANLSGGQK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 163 RKAALGRALVSAPKVLFLDEPTNHLDI---ETILWL-EKFLKDFQGSIVFISHDRSFIrNMATRIIDLDRGKL 231
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPagkEQILKLiRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKL 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
335-496 |
3.56e-08 |
|
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: 54.39 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 335 VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLG-DLKADSGRIHCGTKLEVAYFDQ----HRATLDPDKTVMDNLAEGKQ 409
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGGVILEGKQITEPGPDRmvvfQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 410 EVMVN---GRPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEEL--- 482
Cdd:TIGR01184 81 RVLPDlskSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARaLSIRPK-VLLLDEPFGALDALTRGNLQEElmq 159
|
170
....*....|....*
gi 1437745527 483 -VDAYQGTVLLVSHD 496
Cdd:TIGR01184 160 iWEEHRVTVLMVTHD 174
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-212 |
4.14e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLR-VLAKEQPlDDGQVVYEQDLVTArlqqdpprdi 79
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRvVLGLVAP-DEGVIKRNGKLRIG---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 80 egtifdFVAQGVAEDAqyiTEYHRVSKVIETDPSEKNLNRLAQLQEVldnrnlwlldsRIAEVLEklglngeAELSSLSG 159
Cdd:PRK09544 71 ------YVPQKLYLDT---TLPLTVNRFLRLRPGTKKEDILPALKRV-----------QAGHLID-------APMQKLSG 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 160 GWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWL----EKFLKDFQGSIVFISHD 212
Cdd:PRK09544 124 GETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHD 180
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-184 |
4.65e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.50 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLV---TARLQQdpp 76
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgKDITdwqTAKIMR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 77 rdiegtifdfvaqgvaEDAQYITEYHRVSKVIETdpsEKNLN------RLAQLQEVLDnrnlwlldsRIAEVLEKLGLNG 150
Cdd:PRK11614 80 ----------------EAVAIVPEGRRVFSRMTV---EENLAmggffaERDQFQERIK---------WVYELFPRLHERR 131
|
170 180 190
....*....|....*....|....*....|....
gi 1437745527 151 EAELSSLSGGWLRKAALGRALVSAPKVLFLDEPT 184
Cdd:PRK11614 132 IQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
319-500 |
5.02e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 54.85 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 319 VFELEDV--NYSIGTRRLvRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKlEVAYFDQHRATL-- 394
Cdd:PRK13636 5 ILKVEELnyNYSDGTHAL-KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYSRKGLMKLre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 -------DPDKTVMD------------NLAEGKQEvmVNGRPRHVL-----GYLQDflfppkramTPVRALSGGERNRLL 450
Cdd:PRK13636 83 svgmvfqDPDNQLFSasvyqdvsfgavNLKLPEDE--VRKRVDNALkrtgiEHLKD---------KPTHCLSFGQKKRVA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 451 LARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQG----TVLLVSHDREFV 500
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelglTIIIATHDIDIV 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
329-500 |
5.76e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.73 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 329 IGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI----HCGTKL---EVAY--------FDQHRAT 393
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsgHDITRLknrEVPFlrrqigmiFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 394 LDpdKTVMDNLAegkQEVMVNGRP-----RHVLGYLQDFLFPPKRAMTPVRaLSGGERNRLLLARLFLKPSNLLILDEPT 468
Cdd:PRK10908 92 MD--RTVYDNVA---IPLIIAGASgddirRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190
....*....|....*....|....*....|....*
gi 1437745527 469 NDLDVETLELLEELVDAYQG---TVLLVSHDREFV 500
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLI 200
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-216 |
6.07e-08 |
|
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: 53.70 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVT-------AR-----LQQDPprdiegTIF 84
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITklpmhkrARlgigyLPQEA------SIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 85 DFVAqgVAEDAQYITEYHRVSKVIetdpseknlnRLAQLQEVLDnrnlwllDSRIAEVLEKLGlngeaelSSLSGGWLRK 164
Cdd:cd03218 88 RKLT--VEENILAVLEIRGLSKKE----------REEKLEELLE-------EFHITHLRKSKA-------SSLSGGERRR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 165 AALGRALVSAPKVLFLDEPTNHLD---IETILWLEKFLKDFQGSIVFISH---------DRSFI 216
Cdd:cd03218 142 VEIARALATNPKFLLLDEPFAGVDpiaVQDIQKIIKILKDRGIGVLITDHnvretlsitDRAYI 205
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-231 |
6.23e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 54.71 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLL--------------RVLakeqplddGQVVYEQDLVTAR-----------LQQ 73
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIkmltgilvptsgevRVL--------GYVPFKRRKEFARrigvvfgqrsqLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 74 D-PPRD---IEGTIFDFvaqgvaEDAQYiteyhrvskvietdpsEKNLNRLAqlqEVLDnrnlwlldsrIAEVLE----K 145
Cdd:COG4586 110 DlPAIDsfrLLKAIYRI------PDAEY----------------KKRLDELV---ELLD----------LGELLDtpvrQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 146 LGLnGE---AELsslsggwlrkAAlgrALVSAPKVLFLDEPTNHLDIETILWLEKFLKD----FQGSIVFISHDRSFIRN 218
Cdd:COG4586 155 LSL-GQrmrCEL----------AA---ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynreRGTTILLTSHDMDDIEA 220
|
250
....*....|...
gi 1437745527 219 MATRIIDLDRGKL 231
Cdd:COG4586 221 LCDRVIVIDHGRI 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-230 |
6.75e-08 |
|
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: 53.70 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 15 DAPLLDNTDLFIDENERVCLVGRNGAGKST----LLR---VLAKEQPLDdGQVVYEQDLVTARLQ-----QDPPRdIEGT 82
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTvvslLERfydPTSGEILLD-GVDIRDLNLRWLRSQiglvsQEPVL-FDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 83 IFDFVAQGvAEDAqyiteyhrvskvieTDPSEKNLNRLAQLQEVLDNrnlwLLDSRIAEVleklGLNGeaelSSLSGGWL 162
Cdd:cd03249 93 IAENIRYG-KPDA--------------TDEEVEEAAKKANIHDFIMS----LPDGYDTLV----GERG----SQLSGGQK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745527 163 RKAALGRALVSAPKVLFLDEPTNHLDIETILW----LEKFLKDFqgSIVFISHDRSFIRNmATRIIDLDRGK 230
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLvqeaLDRAMKGR--TTIVIAHRLSTIRN-ADLIAVLQNGQ 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
337-542 |
7.03e-08 |
|
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: 54.04 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 337 DFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLEVAYFDQHRATL-----------DPDKTVM 401
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqdlYQLDRKQRRAFRRDVqlvfqdspsavNPRMTVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 402 DNLAEGKQEVM---VNGRPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETLE 477
Cdd:TIGR02769 109 QIIGEPLRHLTsldESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARaLAVKP-KLIVLDEAVSNLDMVLQA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 478 LLEELVDAYQ---GTV-LLVSHDREFVDNSVTECWIFEGDGVINsyvggyydaQQQRAQSVSLKNEANK 542
Cdd:TIGR02769 188 VILELLRKLQqafGTAyLFITHDLRLVQSFCQRVAVMDKGQIVE---------ECDVAQLLSFKHPAGR 247
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-211 |
7.36e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.08 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDD-----------GQVVYEQDLVTARLQ-------QD 74
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearvegevrlfGRNIYSPDVDPIEVRrevgmvfQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 75 PPRDIEGTIFDFVAQGVaedaqyiteyhrvskvietdpsekNLNRLAQLQEVLDNRNLWLLDSRIAEVLEKLGLNGEAel 154
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGV------------------------KLNGLVKSKKELDERVEWALKKAALWDEVKDRLNDYP-- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 155 SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG--SIVFISH 211
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
9-231 |
9.02e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.50 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 9 AYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKST---LL---------RVLAKEQPLDDGQVVYEQDLVTARLQQdpP 76
Cdd:TIGR00958 487 SYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLqnlyqptggQVLLDGVPLVQYDHHYLHRQVALVGQE--P 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 77 RDIEGTIFDFVAQGVaedaqyiteyhrvskvietDPSEKNLNRLAQLQEVLDNRNLWLLDSRIAEVLEKLglngeaelSS 156
Cdd:TIGR00958 565 VLFSGSVRENIAYGL-------------------TDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKG--------SQ 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 157 LSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKfLKDFQG-SIVFISHDRSFIRNmATRIIDLDRGKL 231
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE-SRSRASrTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-230 |
9.93e-08 |
|
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: 52.86 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSD-----APLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-------QdlvTARL 71
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPgsiayvsQ---EPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 72 QQdpprdieGTIFDFVAQGVAEDAQyiteyhRVSKVIetdpseknlnRLAQLQEVLDNrnlwLLDSRIAEVLEKlGLNge 151
Cdd:cd03250 78 QN-------GTIRENILFGKPFDEE------RYEKVI----------KACALEPDLEI----LPDGDLTEIGEK-GIN-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 152 aelssLSGGwlRKA--ALGRALVSAPKVLFLDEPTNHLDIETILWL-----EKFLKDfQGSIVFISHDRSFIRNmATRII 224
Cdd:cd03250 128 -----LSGG--QKQriSLARAVYSDADIYLLDDPLSAVDAHVGRHIfenciLGLLLN-NKTRILVTHQLQLLPH-ADQIV 198
|
....*.
gi 1437745527 225 DLDRGK 230
Cdd:cd03250 199 VLDNGR 204
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-231 |
1.02e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.02 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 15 DAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE----QDLVTARLQQDpprdiegtiFDFVAQG 90
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDghdlRDYTLASLRNQ---------VALVSQN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 91 V-------AEDAQYITEYHRVSKVIEtdpsekNLNRLAQLQEV---LDNRnlwlLDSRIAEvleklglNGeaelSSLSGG 160
Cdd:PRK11176 426 VhlfndtiANNIAYARTEQYSREQIE------EAARMAYAMDFinkMDNG----LDTVIGE-------NG----VLLSGG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 161 WLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG---SIVfISHDRSFIRNmATRIIDLDRGKL 231
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrtSLV-IAHRLSTIEK-ADEILVVEDGEI 556
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
34-473 |
1.17e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.53 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 34 LVGRNGAGKSTLLRVLAKEQPLDDGQVVY---EQDLVTARlqqdpprdiegtifDFVAQGVAEDAQyitEYHRVSK--VI 108
Cdd:PRK11288 35 LMGENGAGKSTLLKILSGNYQPDAGSILIdgqEMRFASTT--------------AALAAGVAIIYQ---ELHLVPEmtVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 109 EtdpsekNLnRLAQLQE---VLDNRnlwLLDSRIAEVLEKLGLN--GEAELSSLSGGWLRKAALGRALVSAPKVLFLDEP 183
Cdd:PRK11288 98 E------NL-YLGQLPHkggIVNRR---LLNYEAREQLEHLGVDidPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 184 TNHL---DIETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKlsswpgnydkYLESKEEAlrveeqqnAEFD 260
Cdd:PRK11288 168 TSSLsarEIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGR----------YVATFDDM--------AQVD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 261 RKlaqeeawirQGIKARRTRNEGRVRALKAlrverserREvLGSARMQVEEatrsgkivfeledvnysIGTRRLVRDFSA 340
Cdd:PRK11288 230 RD---------QLVQAMVGREIGDIYGYRP--------RP-LGEVRLRLDG-----------------LKGPGLREPISF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 341 KVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKLEVAY-FDQHRA--TLDPD----------KTVMDNLAe 406
Cdd:PRK11288 275 SVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYlDGKPIDIRSpRDAIRAgiMLCPEdrkaegiipvHSVADNIN- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 407 gkqevmVNGRPRHVLG---------------YLQDFLFPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
Cdd:PRK11288 354 ------ISARRHHLRAgclinnrweaenadrFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
..
gi 1437745527 472 DV 473
Cdd:PRK11288 428 DV 429
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-188 |
1.49e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 53.68 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDIEGTI 83
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 84 FDFVAQ--GVAEDAQYITEYHRVS--KVIETDPSeknLNRLAQLQEVLDNRnlwlldsriaevleklglngeaeLSSLSG 159
Cdd:PRK13536 122 FDNLDLefTVRENLLVFGRYFGMStrEIEAVIPS---LLEFARLESKADAR-----------------------VSDLSG 175
|
170 180
....*....|....*....|....*....
gi 1437745527 160 GWLRKAALGRALVSAPKVLFLDEPTNHLD 188
Cdd:PRK13536 176 GMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
331-473 |
1.62e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 53.56 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 331 TRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKLEVAYFDQHR--------------ATLD 395
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLGMKDDEWRavrsdiqmifqdplASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 396 PDKTVMDNLAE---------GKQEVM---------VNGRPRHVLGYLQDFlfppkramtpvralSGGERNRLLLAR-LFL 456
Cdd:PRK15079 113 PRMTIGEIIAEplrtyhpklSRQEVKdrvkammlkVGLLPNLINRYPHEF--------------SGGQCQRIGIARaLIL 178
|
170
....*....|....*..
gi 1437745527 457 KPsNLLILDEPTNDLDV 473
Cdd:PRK15079 179 EP-KLIICDEPVSALDV 194
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
321-472 |
1.70e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 52.79 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLK------------LMLGDLKADSGRIH-CGTKLEVAY- 386
Cdd:PRK09493 3 EFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdLIVDGLKVNDPKVDeRLIRQEAGMv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 387 FDQHraTLDPDKTVMDNLAEGkqevmvngrPRHVLGY-----------LQDFLFPPKRAMTPVRALSGGERNRLLLAR-L 454
Cdd:PRK09493 83 FQQF--YLFPHLTALENVMFG---------PLRVRGAskeeaekqareLLAKVGLAERAHHYPSELSGGQQQRVAIARaL 151
|
170
....*....|....*...
gi 1437745527 455 FLKPsNLLILDEPTNDLD 472
Cdd:PRK09493 152 AVKP-KLMLFDEPTSALD 168
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
349-501 |
1.71e-07 |
|
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: 52.22 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 349 ALVGPNGCGKTTLlklmlgdlkadsgrIHCgtkLEVAYFDQHRATLDPDKTVMDNLAEGKQEVMV-------NGRPRHVL 421
Cdd:cd03240 26 LIVGQNGAGKTTI--------------IEA---LKYALTGELPPNSKGGAHDPKLIREGEVRAQVklafenaNGKKYTIT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 422 GYLQDFL---FPP-----KRAMTPVRALSGGERN------RLLLARLFLKPSNLLILDEPTNDLDVETLELL-EELVDAY 486
Cdd:cd03240 89 RSLAILEnviFCHqgesnWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESlAEIIEER 168
|
170
....*....|....*....
gi 1437745527 487 QGT----VLLVSHDREFVD 501
Cdd:cd03240 169 KSQknfqLIVITHDEELVD 187
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
30-231 |
2.05e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 30 ERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQ---DLVTARLQQDPPRDIEGTIFDFVA-----QGVAEDaqyITEY 101
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqriDTLSPGKLQALRRDIQFIFQDPYAsldprQTVGDS---IMEP 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 102 HRVSKVIETDPSEKnlnrlaqlqevldnrnlwlldsRIAEVLEKLGLNGEAELS---SLSGGWLRKAALGRALVSAPKVL 178
Cdd:PRK10261 428 LRVHGLLPGKAAAA----------------------RVAWLLERVGLLPEHAWRyphEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 179 FLDEPTNHLDI----ETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK10261 486 IADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
335-500 |
2.06e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.81 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 335 VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklevaYFDQHRATLD---------------PDK- 398
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI---------IIDGDLLTEEnvwdirhkigmvfqnPDNq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 399 ----TVMDNLAEGKQ------EVMVNgRPRHVLGY--LQDFlfppkRAMTPVRaLSGGERNRLLLARLFLKPSNLLILDE 466
Cdd:PRK13650 94 fvgaTVEDDVAFGLEnkgiphEEMKE-RVNEALELvgMQDF-----KEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 1437745527 467 PTNDLDVETLELLEELV----DAYQGTVLLVSHDREFV 500
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIkgirDDYQMTVISITHDLDEV 204
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
339-499 |
2.07e-07 |
|
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: 51.97 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 339 SAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQHRATLD--------------PDKTVMDNL 404
Cdd:TIGR02211 25 SLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRnkklgfiyqfhhllPDFTALENV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 405 AE----GKQEVMVNGRPRHVLgyLQDFLFPPKRAMTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLEL-- 478
Cdd:TIGR02211 105 AMplliGKKSVKEAKERAYEM--LEKVGLEHRINHRP-SELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIif 181
|
170 180
....*....|....*....|...
gi 1437745527 479 -LEELVDAYQGT-VLLVSHDREF 499
Cdd:TIGR02211 182 dLMLELNRELNTsFLVVTHDLEL 204
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-224 |
2.16e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 25 FIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDL------VTArlqqdpprDIEGTIFDFVAQgVAEDaqYI 98
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKIsykpqyIKP--------DYDGTVEDLLRS-ITDD--LG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 99 TEYHRVskvietdpseknlnrlaqlqevldnrnlwlldsriaEVLEKLGLNG--EAELSSLSGGWLRKAALGRALVSAPK 176
Cdd:PRK13409 430 SSYYKS------------------------------------EIIKPLQLERllDKNVKDLSGGELQRVAIAACLSRDAD 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1437745527 177 VLFLDEPTNHLDIETILWLEKFLKDF----QGSIVFISHDRSFIRNMATRII 224
Cdd:PRK13409 474 LYLLDEPSAHLDVEQRLAVAKAIRRIaeerEATALVVDHDIYMIDYISDRLM 525
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-211 |
2.40e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.78 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLD--DGQVVYEQDLVTARlqqdpprd 78
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQAS-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 79 iegTIFDFVAQGVAEDAQYITEYHRVSkVIEtdpsekNLNRLAQLQE--VLDNRNLWLldsRIAEVLEKLGL--NGEAEL 154
Cdd:PRK13549 75 ---NIRDTERAGIAIIHQELALVKELS-VLE------NIFLGNEITPggIMDYDAMYL---RAQKLLAQLKLdiNPATPV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 155 SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHL---DIETILWLEKFLKDFQGSIVFISH 211
Cdd:PRK13549 142 GNLGLGQQQLVEIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKAHGIACIYISH 201
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
13-257 |
2.42e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 52.71 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKeqpLDDGQVVYEQ--DLVTARLQQdpprdiEGTIFDFVAQG 90
Cdd:PRK09984 14 FNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSG---LITGDKSAGShiELLGRTVQR------EGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 91 VAEDAQYITEYHRVskvietdpseknlNRLAQLQEVL----DNRNLW---------LLDSRIAEVLEKLGLNGEA--ELS 155
Cdd:PRK09984 85 RANTGYIFQQFNLV-------------NRLSVLENVLigalGSTPFWrtcfswftrEQKQRALQALTRVGMVHFAhqRVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 156 SLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG----SIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVALRQGHV 231
|
250 260 270
....*....|....*....|....*....|
gi 1437745527 232 ----SSWPGNYDKYLESKEEALRVEEQQNA 257
Cdd:PRK09984 232 fydgSSQQFDNERFDHLYRSINRVEENAKA 261
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-231 |
2.79e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.93 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLlrvlakeqplddgqVVYEQDLVTARLQQDPPRDIE-GTIFDFVAQGVAEDAQY 97
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTL--------------VTHFNGLIKSKYGTIQVGDIYiGDKKNNHELITNPYSKK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 98 ITEYHRVSKVIE-----------TDPSEKNL--NRLAQLQEVLDNRNlwlldsRIAEVLEKLGLNG---EAELSSLSGGW 161
Cdd:PRK13631 108 IKNFKELRRRVSmvfqfpeyqlfKDTIEKDImfGPVALGVKKSEAKK------LAKFYLNKMGLDDsylERSPFGLSGGQ 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 162 LRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QGSIVF-ISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK13631 182 KRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkaNNKTVFvITHTMEHVLEVADEVIVMDKGKI 254
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-231 |
2.94e-07 |
|
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: 53.60 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 14 SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVvyeqdlvtaRL------QQDP----------PR 77
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV---------RLdgadlsQWDReelgrhigylPQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 78 DIE---GTIFDFVAQ-GVAEDAqyiteyhrvsKVIETdpseknlnrlAQLQEVLDnrnlWLL------DSRIAEvleklg 147
Cdd:COG4618 414 DVElfdGTIAENIARfGDADPE----------KVVAA----------AKLAGVHE----MILrlpdgyDTRIGE------ 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 148 lNGeaelSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLD-------IETIlwleKFLKDFQGSIVFISHDRSFIrNMA 220
Cdd:COG4618 464 -GG----ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAI----RALKARGATVVVITHRPSLL-AAV 533
|
250
....*....|.
gi 1437745527 221 TRIIDLDRGKL 231
Cdd:COG4618 534 DKLLVLRDGRV 544
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-226 |
3.08e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVvyeqdlvtarlqqdpprDIEG 81
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI-----------------QIDG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 82 TifdfvAQGVAEDAQYITEYHRVSKVIETDPSEKNLNRLAQLQEVLDNRNlwlldsrIAEVLEKLGLNGEAE--LSSLSG 159
Cdd:PRK13543 73 K-----TATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQM-------PGSALAIVGLAGYEDtlVRQLSA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 160 GWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF---QGSIVFISHDRSFIRNMATRIIDL 226
Cdd:PRK13543 141 GQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-231 |
3.15e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVvyeqdLVTARlqqdpprDIEgTIFDFVAQGVAEDAQ 96
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTV-----LVGGK-------DIE-TNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 97 YITEYHRVSKVietdpseKNLNRLAQLQevldNRNLWLLDSRIAEVLEKLGLNGE--AELSSLSGGWLRKAALGRALVSA 174
Cdd:TIGR01257 1011 HNILFHHLTVA-------EHILFYAQLK----GRSWEEAQLEMEAMLEDTGLHHKrnEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 175 PKVLFLDEPTNHLDIET--ILWlEKFLKDFQG-SIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSrrSIW-DLLLKYRSGrTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
337-495 |
3.27e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 337 DFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKlEVAyFDQHRATLD-------------PDKTVMDN 403
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-EMR-FASTTAALAagvaiiyqelhlvPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 404 LAEGK--------QEVMVNGRPRHVLGYLQDFLFPPkramTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
Cdd:PRK11288 100 LYLGQlphkggivNRRLLNYEAREQLEHLGVDIDPD----TPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSARE 175
|
170 180
....*....|....*....|...
gi 1437745527 476 LELLEELVDAY--QGTVLL-VSH 495
Cdd:PRK11288 176 IEQLFRVIRELraEGRVILyVSH 198
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-500 |
3.35e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 52.04 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKlEVAYFDQHR--------- 391
Cdd:COG4674 12 YVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT-DLTGLDEHEiarlgigrk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 392 ---ATLDPDKTVMDNLaegkqEVMVNG--RPRHVLGY------------------LQDflfppkRAMTPVRALSGGERNR 448
Cdd:COG4674 91 fqkPTVFEELTVFENL-----ELALKGdrGVFASLFArltaeerdrieevletigLTD------KADRLAGLLSHGQKQW 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 449 LLLARLFLKPSNLLILDEPT---------------NDLdvetlelleelvdAYQGTVLLVSHDREFV 500
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVagmtdaetertaellKSL-------------AGKHSVVVVEHDMEFV 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-228 |
3.38e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 10 YLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPL-DDGQVVYEQ----DLVTARLQQDPPRDIEG--T 82
Cdd:PTZ00265 1175 YISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkNDHHIVFKNehtnDMTNEQDYQGDEEQNVGmkN 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 83 IFDFVAQGVAEDAQYITEYHRVSKVI--ETDPSEKNLNRLAQL-----QE-VLDNRNLW--------------------- 133
Cdd:PTZ00265 1255 VNEFSLTKEGGSGEDSTVFKNSGKILldGVDICDYNLKDLRNLfsivsQEpMLFNMSIYenikfgkedatredvkrackf 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 134 -LLDSRIAEVLEKLGLNGEAELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGSIvfishD 212
Cdd:PTZ00265 1335 aAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA-----D 1409
|
250
....*....|....*.
gi 1437745527 213 RSFIrNMATRIIDLDR 228
Cdd:PTZ00265 1410 KTII-TIAHRIASIKR 1424
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
35-220 |
3.64e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 52.66 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 35 VGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLVTA----------RLQ---QDP-----PRDIEGTIfdfvaqgVAEDA 95
Cdd:PRK11308 47 VGESGCGKSTLARLLTMIETPTGGELYYQgQDLLKAdpeaqkllrqKIQivfQNPygslnPRKKVGQI-------LEEPL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 96 QyiteyhrvskvIETDpseknLNRlAQLQEvldnrnlwlldsRIAEVLEKLGLNGEAELS---SLSGGWLRKAALGRALV 172
Cdd:PRK11308 120 L-----------INTS-----LSA-AERRE------------KALAMMAKVGLRPEHYDRyphMFSGGQRQRIAIARALM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1437745527 173 SAPKVLFLDEPTNHLDIET---ILWLEKFL-KDFQGSIVFISHDRSFIRNMA 220
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVqaqVLNLMMDLqQELGLSYVFISHDLSVVEHIA 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-231 |
3.66e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 52.33 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 23 DLFIDENERVCLVGRNGAGKSTLLRVL-AKEQPlDDGQVVYEQDLVTARLQQD---PPRDIEGTIFDFvaqgvaEDAQYI 98
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLnGLLQP-TSGTVTIGERVITAGKKNKklkPLRKKVGIVFQF------PEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 99 TEyhRVSKVIETDP-----SEKNLNRLAqlqevldnrnlwlldsriAEVLEKLGLNGEAELSS---LSGGWLRKAALGRA 170
Cdd:PRK13634 100 EE--TVEKDICFGPmnfgvSEEDAKQKA------------------REMIELVGLPEELLARSpfeLSGGQMRRVAIAGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 171 LVSAPKVLFLDEPTNHLD----IETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-188 |
3.67e-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: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 18 LLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQP---------LDDGQVV--YEQDLVTARLQQDpprDIegtifdF 86
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvkgsgsvLLNGMPIdaKEMRAISAYVQQD---DL------F 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 87 VAQGVAEDAQYITEYHRVSkvietdpseknlNRLAQLQEVLdnrnlwlldsRIAEVLEKLGLNGEA--------ELSSLS 158
Cdd:TIGR00955 111 IPTLTVREHLMFQAHLRMP------------RRVTKKEKRE----------RVDEVLQALGLRKCAntrigvpgRVKGLS 168
|
170 180 190
....*....|....*....|....*....|
gi 1437745527 159 GGWLRKAALGRALVSAPKVLFLDEPTNHLD 188
Cdd:TIGR00955 169 GGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
311-472 |
3.99e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.06 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 311 EATRSGKIVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklevaYFDQH 390
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI---------FYNNQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 391 RATLD---------------PDK-----TVMDNLAEGKQEVMVNGRPRH--VLGYLQDFLFPPKRAMTPvRALSGGERNR 448
Cdd:PRK13648 72 AITDDnfeklrkhigivfqnPDNqfvgsIVKYDVAFGLENHAVPYDEMHrrVSEALKQVDMLERADYEP-NALSGGQKQR 150
|
170 180
....*....|....*....|....*
gi 1437745527 449 LLLAR-LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13648 151 VAIAGvLALNPS-VIILDEATSMLD 174
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
337-472 |
4.20e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 337 DFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLK--ADSGRIHCGTkleVAYFDQHRATLdpDKTVMDNLAEG-KQEVMV 413
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShaETSSVVIRGS---VAYVPQVSWIF--NATVRENILFGsDFESER 709
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 414 NGRPRHVLGYLQDFLFPPKRAMTPVRA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PLN03232 710 YWRAIDVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-226 |
4.27e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 51.71 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 8 GAYLAfsdaplLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPL-----DDGQVVY-EQDLVTARLqqDP------ 75
Cdd:PRK14243 21 GSFLA------VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFhGKNLYAPDV--DPvevrrr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 76 -------PRDIEGTIFDFVAQGVAedaqyITEYhrvsKVIETDPSEKNLNRLAqlqevldnrnLWlldsriAEVLEKLGL 148
Cdd:PRK14243 93 igmvfqkPNPFPKSIYDNIAYGAR-----INGY----KGDMDELVERSLRQAA----------LW------DEVKDKLKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 149 NGeaelSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QGSIVFISHdrsfirNM--ATRII 224
Cdd:PRK14243 148 SG----LSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTH------NMqqAARVS 217
|
..
gi 1437745527 225 DL 226
Cdd:PRK14243 218 DM 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-230 |
4.89e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 51.66 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQ-----------QDPPRDI-EGTIFDF 86
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkwvrskvglvfQDPDDQVfSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 87 VAQGVAEdaqyiteyhrvskvIETDPSEknlnrlaqlqevldnrnlwlLDSRIAEVLEKLGLNGEAELSS--LSGGWLRK 164
Cdd:PRK13647 101 VAFGPVN--------------MGLDKDE--------------------VERRVEEALKAVRMWDFRDKPPyhLSYGQKKR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 165 AALGRALVSAPKVLFLDEPTNHLD------IETILW-LEKflkdfQGSIVFIS-HDRSFIRNMATRIIDLDRGK 230
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDprgqetLMEILDrLHN-----QGKTVIVAtHDVDLAAEWADQVIVLKEGR 215
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-200 |
4.99e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 50.32 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 14 SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQplDDGqvvyeqdlvtarlqqdpprDIEGTIFdfvaqgvae 93
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK--TAG-------------------VITGEIL--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 94 daqyiteyhrvskvIETDPSEKNLNRLAQLQEVLDnrnlwlLDSRIAEVLEKLGLNgeAELSSLSGGWLRKAALGRALVS 173
Cdd:cd03232 68 --------------INGRPLDKNFQRSTGYVEQQD------VHSPNLTVREALRFS--ALLRGLSVEQRKRLTIGVELAA 125
|
170 180
....*....|....*....|....*..
gi 1437745527 174 APKVLFLDEPTNHLDIETILWLEKFLK 200
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-231 |
5.85e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 51.63 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVY--------------EQDLVTARLQQDPPRDIE---- 80
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkekEKVLEKLVIQKTRFKKIKkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 -----GTIFDFvaqgvaedaqyiTEYHRVSKVIETDPSEKNLNRLAQLQEVLDnrnlwlldsRIAEVLEKLGLNGEAELS 155
Cdd:PRK13651 103 irrrvGVVFQF------------AEYQLFEQTIEKDIIFGPVSMGVSKEEAKK---------RAAKYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 156 S---LSGGWLRKAALGRALVSAPKVLFLDEPTNHLD---IETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRG 229
Cdd:PRK13651 162 SpfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
..
gi 1437745527 230 KL 231
Cdd:PRK13651 242 KI 243
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-189 |
6.48e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.21 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 34 LVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVT-------ARLQQDPPRDIEGTIfdfvaqGVAEDAQYITEYHRVSK 106
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEildefrgSELQNYFTKLLEGDV------KVIVKPQYVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 107 vietdpseknlNRLAQLQEVLDNRNLwlLDsriaEVLEKLGLNG--EAELSSLSGGWLRKAALGRALVSAPKVLFLDEPT 184
Cdd:cd03236 105 -----------GKVGELLKKKDERGK--LD----ELVDQLELRHvlDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
....*
gi 1437745527 185 NHLDI 189
Cdd:cd03236 168 SYLDI 172
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-231 |
8.65e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 50.90 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 15 DAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTArlqQDPPRDIE------GTIFDF-- 86
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS---TSKNKDIKqirkkvGLVFQFpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 87 ---VAQGVAEDAQYITEYHRVSKvIETDPSEKNLNRLAQLQEVLDNRNLWlldsriaevleklglngeaelsSLSGGWLR 163
Cdd:PRK13649 96 sqlFEETVLKDVAFGPQNFGVSQ-EEAEALAREKLALVGISESLFEKNPF----------------------ELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745527 164 KAALGRALVSAPKVLFLDEPTNHLDI---ETILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPkgrKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-210 |
8.79e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 49.95 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 13 FSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKeqplddgqvvyeqdlvtarlQQDPPRDIEGTI-FDfvaqgv 91
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN--------------------RTEGNVSVEGDIhYN------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 92 AEDAQYITEYHR--VSKVIETDpseknlNRLAQL--QEVLDNRnlwlldsriaevlekLGLNGEAELSSLSGGWLRKAAL 167
Cdd:cd03233 71 GIPYKEFAEKYPgeIIYVSEED------VHFPTLtvRETLDFA---------------LRCKGNEFVRGISGGERKRVSI 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1437745527 168 GRALVSAPKVLFLDEPTNHLDIETILWLEKFLK---DFQGSIVFIS 210
Cdd:cd03233 130 AEALVSRASVLCWDNSTRGLDSSTALEILKCIRtmaDVLKTTTFVS 175
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
311-495 |
8.99e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.94 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 311 EATRS-GKIVFEleDVNYSIGTRRL--VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKLE--- 383
Cdd:PRK11176 334 VIERAkGDIEFR--NVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdGHDLRdyt 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 384 -------VAYFDQ--HratLDPDkTVMDNLAEGKQEVMVNGRPRHV--LGYLQDFLFPPKRAMTPV-----RALSGGERN 447
Cdd:PRK11176 412 laslrnqVALVSQnvH---LFND-TIANNIAYARTEQYSREQIEEAarMAYAMDFINKMDNGLDTVigengVLLSGGQRQ 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1437745527 448 RLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQG--TVLLVSH 495
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH 537
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
335-472 |
1.24e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.00 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 335 VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLEVAYFD-----QHRAtLDPDKTVMDNLA 405
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGgrvvNELEPADRDiamvfQNYA-LYPHMSVRENMA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 406 EG-------KQEvmVNGRPRHVLGYL--QDFLfppKRamTPvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11650 99 YGlkirgmpKAE--IEERVAEAARILelEPLL---DR--KP-RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
19-183 |
1.38e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 50.03 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVT-------AR-----LQQDPprdiegTIFdf 86
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIThlpmhkrARlgigyLPQEA------SIF-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 87 vaQG--VAEDAQYITEYHRVSKvietdpsEKNLNRLAQLqevldnrnlwLLDSRIAEVLEKLGlngeaelSSLSGGWLRK 164
Cdd:COG1137 91 --RKltVEDNILAVLELRKLSK-------KEREERLEEL----------LEEFGITHLRKSKA-------YSLSGGERRR 144
|
170
....*....|....*....
gi 1437745527 165 AALGRALVSAPKVLFLDEP 183
Cdd:COG1137 145 VEIARALATNPKFILLDEP 163
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
300-472 |
1.58e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 51.26 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 300 EVLGSARMQVEEATR---SGKIvfELEDVNYSIGTRRLV-RDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGR 375
Cdd:PRK10790 320 ELMDGPRQQYGNDDRplqSGRI--DIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 376 IHCGTK----LEVAYFDQHRATLDPDKTVM-----DNLAEGKQ--EVMVngrpRHVLGYLQdfLFPPKRAM-----TPV- 438
Cdd:PRK10790 398 IRLDGRplssLSHSVLRQGVAMVQQDPVVLadtflANVTLGRDisEEQV----WQALETVQ--LAELARSLpdglyTPLg 471
|
170 180 190
....*....|....*....|....*....|....*..
gi 1437745527 439 ---RALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK10790 472 eqgNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-188 |
1.60e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 50.19 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPR---- 77
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRvgvv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 78 -DIEGTIFDFVaqgVAEDAQYITEYHRVSKvietdpseknlnrlAQLQEvldnrnlwlldsRIAEVLE--KLGLNGEAEL 154
Cdd:PRK13537 86 pQFDNLDPDFT---VRENLLVFGRYFGLSA--------------AAARA------------LVPPLLEfaKLENKADAKV 136
|
170 180 190
....*....|....*....|....*....|....
gi 1437745527 155 SSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLD 188
Cdd:PRK13537 137 GELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
330-472 |
1.63e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.20 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 330 GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLM----LGDLKADSGRIHCGTKLEV-------AYFDQH-----RAT 393
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrsPKGVKGSGSVLLNGMPIDAkemraisAYVQQDdlfipTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 394 LDPDKTVMDNLAEGKQEVMVNGRPRhVLGYLQDfLFPPKRAMT------PVRALSGGERNRLLLARLFLKPSNLLILDEP 467
Cdd:TIGR00955 116 VREHLMFQAHLRMPRRVTKKEKRER-VDEVLQA-LGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
....*
gi 1437745527 468 TNDLD 472
Cdd:TIGR00955 194 TSGLD 198
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
318-472 |
1.65e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.17 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 318 IVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLM--LGDLkADSGRIHCgtklEVAYFDQ--HRAT 393
Cdd:PRK14243 9 TVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDL-IPGFRVEG----KVTFHGKnlYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 394 LDP-----------------DKTVMDNLAEGkqevmvngrPRhVLGYLQDFLFPPKRAM--------------TPVRALS 442
Cdd:PRK14243 84 VDPvevrrrigmvfqkpnpfPKSIYDNIAYG---------AR-INGYKGDMDELVERSLrqaalwdevkdklkQSGLSLS 153
|
170 180 190
....*....|....*....|....*....|
gi 1437745527 443 GGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
321-500 |
1.69e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 50.12 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVN--YSIGTRRLvRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKL---EVAYFDQHRATL- 394
Cdd:PRK13647 6 EVEDLHfrYKDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnaENEKWVRSKVGLv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 --DPD-----KTVMDNLAEGKQEV-----MVNGRPRHVLGYLQDFLFPPKramtPVRALSGGERNRLLLARLFLKPSNLL 462
Cdd:PRK13647 85 fqDPDdqvfsSTVWDDVAFGPVNMgldkdEVERRVEEALKAVRMWDFRDK----PPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1437745527 463 ILDEPTNDLDVETLELLEELVDAY--QG-TVLLVSHDREFV 500
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLhnQGkTVIVATHDVDLA 201
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
316-473 |
1.77e-06 |
|
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: 49.41 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 316 GKIVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLEVAYFDQH- 390
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDgvdiSKIGLHDLRSRi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 391 --------------RATLDP-----DKTVMDNLAEGKQEVMVNGRPrhvlGYLQdflfppkramTPVRA----LSGGERN 447
Cdd:cd03244 81 siipqdpvlfsgtiRSNLDPfgeysDEELWQALERVGLKEFVESLP----GGLD----------TVVEEggenLSVGQRQ 146
|
170 180
....*....|....*....|....*.
gi 1437745527 448 RLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDP 172
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
331-496 |
1.89e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 49.70 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 331 TRRLVRDFSAKVQRGDKIALVGPNGCGKT----TLLKLMLGDLKADSGRIHC-GTKLE--------VAYFDQH-RATLDP 396
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLdGKPVApcalrgrkIATIMQNpRSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 397 DKTVMDNLAEGKQEVMVNGRPRHVLGYLQDF-LFPPKRA--MTPVRaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK10418 95 LHTMHTHARETCLALGKPADDATLTAALEAVgLENAARVlkLYPFE-MSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180
....*....|....*....|....*..
gi 1437745527 474 ETLEL---LEELVDAYQGT-VLLVSHD 496
Cdd:PRK10418 174 VAQARildLLESIVQKRALgMLLVTHD 200
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-205 |
1.99e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.51 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 12 AFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVY-EQDLVTARLQQDPPRDI-----EGTIFd 85
Cdd:PRK10895 12 AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIdDEDISLLPLHARARRGIgylpqEASIF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 86 fvaqgvaedaQYITEYHRVSKVIETdpsEKNLNRlaqlQEVLDNRNLWLLDSRIAEVLEKLGlngeaelSSLSGGWLRKA 165
Cdd:PRK10895 91 ----------RRLSVYDNLMAVLQI---RDDLSA----EQREDRANELMEEFHIEHLRDSMG-------QSLSGGERRRV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1437745527 166 ALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGS 205
Cdd:PRK10895 147 EIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS 186
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
335-473 |
2.01e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.88 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 335 VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQHRATLDPDKTVMD-NLAEGKQEVMV 413
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDwSFPVLVEDVVM 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 414 NGRPRHvLGYLQdflFPPKRAMTPVRA-----------------LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK15056 103 MGRYGH-MGWLR---RAKKRDRQIVTAalarvdmvefrhrqigeLSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
4-216 |
2.05e-06 |
|
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: 49.25 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 4 ISLTGAYLAF-SDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDIEGT 82
Cdd:cd03290 1 VQVTNGYFSWgSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 83 IfDFVAQG-------VAEDAQYITEYH--RVSKVIETdpseknlnrlAQLQEVLDnrnlWLLDSRIAEVLEKlGLNgeae 153
Cdd:cd03290 81 V-AYAAQKpwllnatVEENITFGSPFNkqRYKAVTDA----------CSLQPDID----LLPFGDQTEIGER-GIN---- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745527 154 lssLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDI--------ETILwleKFLKDFQGSIVFISHDRSFI 216
Cdd:cd03290 141 ---LSGGQRQRICVARALYQNTNIVFLDDPFSALDIhlsdhlmqEGIL---KFLQDDKRTLVLVTHKLQYL 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
319-500 |
2.10e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.80 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 319 VFELEDVNYSI-GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKLEVAYFDQHRATL-- 394
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREVRKFVgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 ---DPDKTVMDNLAE----------GKQEVMVNGRPR---HVLGyLQDFlfppkRAMTPvRALSGGERNRLLLARLFLKP 458
Cdd:PRK13652 83 vfqNPDDQIFSPTVEqdiafgpinlGLDEETVAHRVSsalHMLG-LEEL-----RDRVP-HHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1437745527 459 SNLLILDEPTNDLDVETLELLEELVDA----YQGTVLLVSHDREFV 500
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDlpetYGMTVIFSTHQLDLV 201
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-231 |
2.10e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 49.69 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLL------------RVLAKEQPLDdgqvvYE-QDLVTARLQ-----QDPprdiE 80
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFlhfngilkptsgEVLIKGEPIK-----YDkKSLLEVRKTvgivfQNP----D 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 GTIFdfvAQGVAEDAQYiteyhrvskvietDPseknLNRLAQLQEVldnrnlwllDSRIAEVLEKLGLNGEAELSS--LS 158
Cdd:PRK13639 89 DQLF---APTVEEDVAF-------------GP----LNLGLSKEEV---------EKRVKEALKAVGMEGFENKPPhhLS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 159 GGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QGSIVFIS-HDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK13639 140 GGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGITIIIStHDVDLVPVYADKVYVMSDGKI 215
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-191 |
2.13e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.06 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYeqdlvTARLQQDP--PRDIEGTIFDFVAQGVAED 94
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKH-----SGRISFSPqtSWIMPGTIKDNIIFGLSYD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 95 aqyitEYhRVSKVIETdpseknlnrlAQLQEvldnrNLWLLDSRIAEVLEKLGLngeaelsSLSGGWLRKAALGRALVSA 174
Cdd:TIGR01271 515 -----EY-RYTSVIKA----------CQLEE-----DIALFPEKDKTVLGEGGI-------TLSGGQRARISLARAVYKD 566
|
170
....*....|....*..
gi 1437745527 175 PKVLFLDEPTNHLDIET 191
Cdd:TIGR01271 567 ADLYLLDSPFTHLDVVT 583
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
319-517 |
2.18e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 49.73 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 319 VFELEDVNYSIG-----TRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG-------------- 379
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsstskqkeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 380 -TKLEVAYFDQHRATLDPDKTVMDNLAEGKQEVMVN--------GRPRHVLGYLQDFLfppkrAMTPVRaLSGGERNRLL 450
Cdd:PRK13643 81 pVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPkekaekiaAEKLEMVGLADEFW-----EKSPFE-LSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 451 LARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQ---GTVLLVSHDREFVDNSVTECWIFEGDGVIN 517
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHqsgQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
317-472 |
2.23e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 49.60 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 317 KIVFELEDV--NYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKLEVAYFDQHRAT 393
Cdd:PRK13632 5 SVMIKVENVsfSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 394 L-----DPDK-----TVMDNLAEGKQEVMVNGR--PRHVLGYLQ-----DFL-FPPKRamtpvraLSGGERNRLLLAR-L 454
Cdd:PRK13632 85 IgiifqNPDNqfigaTVEDDIAFGLENKKVPPKkmKDIIDDLAKkvgmeDYLdKEPQN-------LSGGQKQRVAIASvL 157
|
170
....*....|....*...
gi 1437745527 455 FLKPSnLLILDEPTNDLD 472
Cdd:PRK13632 158 ALNPE-IIIFDESTSMLD 174
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-213 |
2.26e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.06 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDApLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAkeqplddgqvvyeqdlvtaRLQqdpprDIE 80
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-------------------RLL-----STE 1272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 GTIfdfVAQGVAEDAQYITEYHRVSKVIE------TDPSEKNLNRLAQLQEvldnRNLWL------LDSRIAEVLEKLGL 148
Cdd:TIGR01271 1273 GEI---QIDGVSWNSVTLQTWRKAFGVIPqkvfifSGTFRKNLDPYEQWSD----EEIWKvaeevgLKSVIEQFPDKLDF 1345
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 149 NGEAELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKD-FQGSIVFISHDR 213
Cdd:TIGR01271 1346 VLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQsFSNCTVILSEHR 1411
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
157-232 |
3.02e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.00 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 157 LSGGWLRKAALGRALVSAPKVLFLDEPTNHLDI----ETILWLEKFLKDfqG-SIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVgakkEIYQLINQFKAE--GlSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
.
gi 1437745527 232 S 232
Cdd:PRK10762 474 S 474
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
339-473 |
3.07e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 339 SAKVQRGDKIALVGPNGCGKTTLLKLML-------GDLKADSGRIHCGTKLEVA--------YFDQHRATLDPDKTVMDN 403
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTmietptgGELYYQGQDLLKADPEAQKllrqkiqiVFQNPYGSLNPRKKVGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 404 LAE--------GKQE-------VM--VNGRPRHVLGYLQDFlfppkramtpvralSGGERNRLLLAR-LFLKPsNLLILD 465
Cdd:PRK11308 115 LEEpllintslSAAErrekalaMMakVGLRPEHYDRYPHMF--------------SGGQRQRIAIARaLMLDP-DVVVAD 179
|
....*...
gi 1437745527 466 EPTNDLDV 473
Cdd:PRK11308 180 EPVSALDV 187
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
343-473 |
3.22e-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: 50.17 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 343 QRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKLEVayFDQHRAT-LdpdKTVMDNLAEGKQEV-----MVNG 415
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEePSWDEV--LKRFRGTeL---QDYFKKLANGEIKVahkpqYVDL 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 416 RPRHVLGYLQDFLfppKRA--------------MTP-----VRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:COG1245 172 IPKVFKGTVRELL---EKVdergkldelaeklgLENildrdISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
342-513 |
3.27e-06 |
|
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: 47.95 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 342 VQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHcgtklevayFDQHRATLDPDKTvmdnlaegkqevmvngrprhvl 421
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE---------WDGITPVYKPQYI---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 422 gylqdflfppkramtpvrALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAY----QGTVLLVSHDR 497
Cdd:cd03222 71 ------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDL 132
|
170
....*....|....*.
gi 1437745527 498 EFVDNSVTECWIFEGD 513
Cdd:cd03222 133 AVLDYLSDRIHVFEGE 148
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-230 |
3.32e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.83 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQdlvtarlqqdppRDIEG 81
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG------------QHIEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 82 TIFDFVA-QGVAEDAQYITEYHRVSkVIEtdpsekNLnRLAQLQEVldNRNLW--LLDS------------RIAEVLEKL 146
Cdd:PRK11300 72 LPGHQIArMGVVRTFQHVRLFREMT-VIE------NL-LVAQHQQL--KTGLFsgLLKTpafrraesealdRAATWLERV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 147 GL----NGEAelSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLD----IETILWLEKFLKDFQGSIVFISHDRSFIRN 218
Cdd:PRK11300 142 GLlehaNRQA--GNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNpketKELDELIAELRNEHNVTVLLIEHDMKLVMG 219
|
250
....*....|..
gi 1437745527 219 MATRIIDLDRGK 230
Cdd:PRK11300 220 ISDRIYVVNQGT 231
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
332-496 |
3.69e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 332 RRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQHRATLDPD-----KTVMDNLAE 406
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNGEPLAAIDAPrlarlRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 407 -----GKQEVMVNGRPRHVL---------GYLQDFLFPPKRAMTPVR----ALSGGERNRLLLARLFLK---------PS 459
Cdd:PRK13547 94 pafafSAREIVLLGRYPHARragalthrdGEIAWQALALAGATALVGrdvtTLSGGELARVQFARVLAQlwpphdaaqPP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1437745527 460 NLLILDEPTNDLDVETLELLEELVDA----YQGTVLLVSHD 496
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRlardWNLGVLAIVHD 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
319-472 |
3.84e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 48.92 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 319 VFELEDVNYSI--GTRRLvRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKlevayfdqhraTLDP 396
Cdd:PRK13639 1 ILETRDLKYSYpdGTEAL-KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE-----------PIKY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 397 DKTvmdNLAEGKQEV-MVNGRPRHVL---GYLQDFLFPP-----------KRAMTPVRA-------------LSGGERNR 448
Cdd:PRK13639 69 DKK---SLLEVRKTVgIVFQNPDDQLfapTVEEDVAFGPlnlglskeeveKRVKEALKAvgmegfenkpphhLSGGQKKR 145
|
170 180
....*....|....*....|....
gi 1437745527 449 LLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-224 |
4.18e-06 |
|
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: 46.98 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 29 NERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYeqdlvtarlqqdpprdiegtifdfvaqgvaedaqyiteyhrvskvi 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 109 eTDPSEKNLNRLAQLQEVLDNRNlwlldsriaevleKLGLNGEAELsslsggwlrKAALGRALVSAPKVLFLDEPTNHLD 188
Cdd:smart00382 36 -IDGEDILEEVLDQLLLIIVGGK-------------KASGSGELRL---------RLALALARKLKPDVLILDEITSLLD 92
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1437745527 189 IET---------ILWLEKFLKDFQGSIVFISHDRSFIRNMATRII 224
Cdd:smart00382 93 AEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR 137
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-231 |
4.67e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 18 LLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPlddGQVVYEQDLVTAR--LQQDPPRDIEGTIFDFVAQGVAEDA 95
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLT---GGGAPRGARVTGDvtLNGEPLAAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 96 QYITEYhrvskvietdpSEKNLNRLAQLQEVLDNRNLWLLDSRIAEvlEKLGLNGEAEL-----SSLSGGWLRKAALGRA 170
Cdd:PRK13547 93 QPAFAF-----------SAREIVLLGRYPHARRAGALTHRDGEIAW--QALALAGATALvgrdvTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 171 L---------VSAPKVLFLDEPTNHLD-------IETIlwlEKFLKDFQGSIVFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDlahqhrlLDTV---RRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
30-230 |
4.89e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.38 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 30 ERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYeqdlvtarlqqdppRDIEGTIFDFVAQGVAE-------DAQYITEYH 102
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSARLAPDAGEVHY--------------RMRDGQLRDLYALSEAErrrllrtEWGFVHQHP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 103 R------VS---KVIEtdpseknlnRLAqlqeVLDNRNLWLLDSRIAEVLEKLglngEAELSSL-------SGGWLRKAA 166
Cdd:PRK11701 99 RdglrmqVSaggNIGE---------RLM----AVGARHYGDIRATAGDWLERV----EIDAARIddlpttfSGGMQQRLQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 167 LGRALVSAPKVLFLDEPTNHLDIET---ILWLEKFL-KDFQGSIVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVqarLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
151-231 |
5.52e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 151 EAELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QG-SIVFISHDRSFIRNMATRIIDLD 227
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLvqQGvAIIVISSELPEVLGLSDRVLVMH 479
|
....
gi 1437745527 228 RGKL 231
Cdd:PRK13549 480 EGKL 483
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
334-500 |
5.71e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 48.46 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 334 LVRDFSAKVQRGdkiaLVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKLEVA-----YFDQHRATL--DPDKTV----- 400
Cdd:PRK13638 20 LNLDFSLSPVTG----LVGANGCGKSTLFMNLSGLLRPQKGAVLWqGKPLDYSkrgllALRQQVATVfqDPEQQIfytdi 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 401 -------MDNLAEGKQEVMVNGRPRHVLGYLQDFlfppkrAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13638 96 dsdiafsLRNLGVPEAEITRRVDEALTLVDAQHF------RHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190
....*....|....*....|....*....|
gi 1437745527 474 ETLELLEELVD--AYQGT-VLLVSHDREFV 500
Cdd:PRK13638 170 AGRTQMIAIIRriVAQGNhVIISSHDIDLI 199
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-191 |
6.07e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 47.65 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 17 PLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAkeqplddGQVVYEQDLVTARLQQDPPrDIEGTIFDFVAqgvaedaq 96
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA-------GALKGTPVAGCVDVPDNQF-GREASLIDAIG-------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 97 yiteyhrvskvIETDPSEKnlnrlaqlqevldnrnlwlldsriAEVLEKLGLNgEAEL-----SSLSGGWLRKAALGRAL 171
Cdd:COG2401 108 -----------RKGDFKDA------------------------VELLNAVGLS-DAVLwlrrfKELSTGQKFRFRLALLL 151
|
170 180
....*....|....*....|
gi 1437745527 172 VSAPKVLFLDEPTNHLDIET 191
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQT 171
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-231 |
7.12e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.89 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 18 LLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYE-QDLvtARLQQDPPRDIEGTIFDFVAQgvaedaq 96
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgQPM--SKLSSAAKAELRNQKLGFIYQ------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 97 yiteYHRVSkvietdPSEKNLNRLAqLQEVLDNRNLWLLDSRIAEVLEKLGLNGEAE--LSSLSGGWLRKAALGRALVSA 174
Cdd:PRK11629 95 ----FHHLL------PDFTALENVA-MPLLIGKKKPAEINSRALEMLAAVGLEHRANhrPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745527 175 PKVLFLDEPTNHLDI---ETILWLEKFLKDFQGS-IVFISHDRSFIRNMaTRIIDLDRGKL 231
Cdd:PRK11629 164 PRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTaFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
330-516 |
7.52e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.04 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 330 GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKL---------EVAYFDQHRATLDPDK-- 398
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgQLKVADKNQLRLLRTRlt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 399 ------------TVMDNLAEGKQEVM----VNGRPRHVLGYLQDFLFPPKRAMTPVRaLSGGERNRLLLARLFLKPSNLL 462
Cdd:PRK10619 96 mvfqhfnlwshmTVLENVMEAPIQVLglskQEARERAVKYLAKVGIDERAQGKYPVH-LSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 463 ILDEPTNDLD---VETLELLEELVDAYQGTVLLVSHDREFVDNsVTECWIFEGDGVI 516
Cdd:PRK10619 175 LFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARH-VSSHVIFLHQGKI 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
321-472 |
7.71e-06 |
|
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: 47.58 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSIGTRR----LVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKL------------- 382
Cdd:cd03258 3 ELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLtllsgkelrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 383 EVAYFDQHRATLDpDKTVMDNLA-----EGKQEVMVNGRPRHVLGY--LQDflfppKRAMTPvRALSGGERNRLLLAR-L 454
Cdd:cd03258 83 RIGMIFQHFNLLS-SRTVFENVAlpleiAGVPKAEIEERVLELLELvgLED-----KADAYP-AQLSGGQKQRVGIARaL 155
|
170
....*....|....*...
gi 1437745527 455 FLKPSnLLILDEPTNDLD 472
Cdd:cd03258 156 ANNPK-VLLCDEATSALD 172
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
320-472 |
8.57e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.53 E-value: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 320 FELEDVNYSI--GTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLM--LGDLKADSgRIHCGTKL------------- 382
Cdd:PRK14267 3 FAIETVNLRVyyGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEEA-RVEGEVRLfgrniyspdvdpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 383 ----EVAYFDQHRATLdPDKTVMDNLAEGkqeVMVNG--RPRHVLGYLQDFLFPPKRAMTPVR--------ALSGGERNR 448
Cdd:PRK14267 82 evrrEVGMVFQYPNPF-PHLTIYDNVAIG---VKLNGlvKSKKELDERVEWALKKAALWDEVKdrlndypsNLSGGQRQR 157
|
170 180
....*....|....*....|....*
gi 1437745527 449 LLLAR-LFLKPsNLLILDEPTNDLD 472
Cdd:PRK14267 158 LVIARaLAMKP-KILLMDEPTANID 181
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
342-498 |
9.79e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.08 E-value: 9.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 342 VQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQHRATLD--------------PDKTVMDN---- 403
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRakhvgfvfqsfmliPTLNALENvelp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 404 -LAEGKQEVMVNGRPRHVLGYLQdflfPPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEEL 482
Cdd:PRK10584 113 aLLRGESSRQSRNGAKALLEQLG----LGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180
....*....|....*....|
gi 1437745527 483 VDA----YQGTVLLVSHDRE 498
Cdd:PRK10584 189 LFSlnreHGTTLILVTHDLQ 208
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
342-473 |
1.03e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 342 VQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI-HCGTKLEVayFDQHRAT-LdpdKTVMDNLAEGKQEV-----MVN 414
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeEEPSWDEV--LKRFRGTeL---QNYFKKLYNGEIKVvhkpqYVD 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745527 415 GRPRHVLGYLQDFLfppKRA--------------MTPV-----RALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13409 171 LIPKVFKGKVRELL---KKVdergkldevverlgLENIldrdiSELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
335-496 |
1.10e-05 |
|
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: 47.64 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 335 VRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKlEVAYFD----------------QHRATLdPDK 398
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQ-DIAAMSrkelrelrrkkismvfQSFALL-PHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 399 TVMDNLAEGKQevmVNGRPR--------HVL------GYLQDFlfppkramtpVRALSGGERNRLLLAR-LFLKPSnLLI 463
Cdd:cd03294 118 TVLENVAFGLE---VQGVPRaereeraaEALelvgleGWEHKY----------PDELSGGMQQRVGLARaLAVDPD-ILL 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1437745527 464 LDEPTNDLDVETLELLEELVDAYQG----TVLLVSHD 496
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLQAelqkTIVFITHD 220
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
315-503 |
1.11e-05 |
|
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: 46.16 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 315 SGKIVFELEDVNYSIGTRRLVrdfsakvqrgdkiALVGPNGCGKTTLLKlmlgdlkadsgriHCGTKLEVAYFDQHRATL 394
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLV-------------VVTGVSGSGKSTLVN-------------EGLYASGKARLISFLPKF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 DPDKTVM-DNLaegkQEVMVNGrprhvLGYLqdflfPPKRAMTpvrALSGGERNRLLLAR-LFLKPSN-LLILDEPTNDL 471
Cdd:cd03238 58 SRNKLIFiDQL----QFLIDVG-----LGYL-----TLGQKLS---TLSGGELQRVKLASeLFSEPPGtLFILDEPSTGL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 1437745527 472 DVETLELLEELVDAY--QG-TVLLVSHDREFVDNS 503
Cdd:cd03238 121 HQQDINQLLEVIKGLidLGnTVILIEHNLDVLSSA 155
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-213 |
1.68e-05 |
|
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: 47.16 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 1 MPLISLTGAYLAFSDApLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKeqplddgqvvyeqdLVtarlqqdpprDIE 80
Cdd:cd03289 3 MTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLR--------------LL----------NTE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 81 GtifDFVAQGVAEDAQYITEYHRVSKVIetdpSEKNLNRLAQLQEVLDNRNLWLlDSRIAEVLEKLGLN-------GEAE 153
Cdd:cd03289 58 G---DIQIDGVSWNSVPLQKWRKAFGVI----PQKVFIFSGTFRKNLDPYGKWS-DEEIWKVAEEVGLKsvieqfpGQLD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 154 LSSLSGGWL------RKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKD-FQGSIVFISHDR 213
Cdd:cd03289 130 FVLVDGGCVlshghkQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQaFADCTVILSEHR 196
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
331-473 |
2.70e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.01 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 331 TRRLVRDFSAKVQRGDKIALVGPNGCGK--TTLLKLML----------GD--------LKADSGRIHC--GTKLEVAyFD 388
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKsvTALSILRLlpsppvvypsGDirfhgeslLHASEQTLRGvrGNKIAMI-FQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 389 QHRATLDPDKTVMDNLAE-------GKQEV----MVNGRPRhvLGYLQdflfPPKRAMTPVRALSGGERNRLLLARLFLK 457
Cdd:PRK15134 100 EPMVSLNPLHTLEKQLYEvlslhrgMRREAargeILNCLDR--VGIRQ----AAKRLTDYPHQLSGGERQRVMIAMALLT 173
|
170
....*....|....*.
gi 1437745527 458 PSNLLILDEPTNDLDV 473
Cdd:PRK15134 174 RPELLIADEPTTALDV 189
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
318-472 |
3.68e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.17 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 318 IVFELEDVNYSIGT---RRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQhratl 394
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKN----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 dpdktvmDNLAEGKQEV-MVNGRPRHVL---GYLQDFLFPP-----------KRAMTPVR--------------ALSGGE 445
Cdd:PRK13634 78 -------KKLKPLRKKVgIVFQFPEHQLfeeTVEKDICFGPmnfgvseedakQKAREMIElvglpeellarspfELSGGQ 150
|
170 180
....*....|....*....|....*..
gi 1437745527 446 RNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
341-472 |
3.96e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 341 KVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRiHCGTKLEVAYFDQHRATLdpDKTVMDNLAEGKQ-EVMVNGRPRH 419
Cdd:PLN03130 639 DVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA-SVVIRGTVAYVPQVSWIF--NATVRDNILFGSPfDPERYERAID 715
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 420 VLGYLQDFLFPPKRAMTPV--RA--LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PLN03130 716 VTALQHDLDLLPGGDLTEIgeRGvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
258-472 |
4.09e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.03 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 258 EFDRKLAQE-EAWIRQGIKARRTRNEGRVRALKALRVERSE---RREVLGSARM---QVEEATRSGKIVFELEDVNYSIG 330
Cdd:TIGR00956 691 EFNKGAKQKgEILVFRRGSLKRAKKAGETSASNKNDIEAGEvlgSTDLTDESDDvndEKDMEKESGEDIFHWRNLTYEVK 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 331 ----TRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGdlKADSGRIHCGTKL------------EVAYFDQHRATL 394
Cdd:TIGR00956 771 ikkeKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLvngrpldssfqrSIGYVQQQDLHL 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 dPDKTVMDNL---AEGKQ--EVMVNGRPRHVlGYLQDFLFPPKRA----MTPVRALSGGERNRLLLA-RLFLKPSNLLIL 464
Cdd:TIGR00956 849 -PTSTVRESLrfsAYLRQpkSVSKSEKMEYV-EEVIKLLEMESYAdavvGVPGEGLNVEQRKRLTIGvELVAKPKLLLFL 926
|
....*...
gi 1437745527 465 DEPTNDLD 472
Cdd:TIGR00956 927 DEPTSGLD 934
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-268 |
4.52e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 45.46 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 3 LISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTArlqqdpPRDIEGT 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG------PGAERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 83 IFDFVAqgvaedaqyiteyhrvskvietdpseknlnrLAQLQEVLDNRNLWL---------LDSRIAEVLEKLGLNGEAE 153
Cdd:PRK11248 75 VFQNEG-------------------------------LLPWRNVQDNVAFGLqlagvekmqRLEIAHQMLKKVGLEGAEK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 154 --LSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFL----KDFQGSIVFISHDRSFIRNMATRIIDLD 227
Cdd:PRK11248 124 ryIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHDIEEAVFMATELVLLS 203
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1437745527 228 RGklsswPGnydkyleskeealRVEEQQNAEFDRKLAQEEA 268
Cdd:PRK11248 204 PG-----PG-------------RVVERLPLNFARRFVAGES 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-230 |
5.25e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 45.61 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEqdlvtarlqqdpprdieGTIFDFVAQGVAEDAQYI 98
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFD-----------------GKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 99 ------TEYHRVSKVIETDPSEKNLNRLAQLQEVldnrnlwllDSRIAEVLEKLGLN--GEAELSSLSGGWLRKAALGRA 170
Cdd:PRK13636 85 gmvfqdPDNQLFSASVYQDVSFGAVNLKLPEDEV---------RKRVDNALKRTGIEhlKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 171 LVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG----SIVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelglTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-472 |
6.48e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 44.90 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 319 VFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLM------------LGDLKADSGRIHcgtKLEVAY 386
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlielypearvSGEVYLDGQDIF---KMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 387 FDQHRATL------DPDKTVMDNLAEG-------KQEVMVNGRPRHVLGYLQDFLFPPKRAMTPVRALSGGERNRLLLAR 453
Cdd:PRK14247 80 LRRRVQMVfqipnpIPNLSIFENVALGlklnrlvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170
....*....|....*....
gi 1437745527 454 LFLKPSNLLILDEPTNDLD 472
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLD 178
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-258 |
6.88e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 15 DAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVY--EQDLVTARLQ----------QDP------- 75
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndSHNLKDINLKwwrskigvvsQDPllfsnsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 76 PRDIEGTIFDFvaqgvaEDAQYITEYHRVSKVIETDPSEK----------NLNRLAQ------LQEVLDNRNLwLLDSRI 139
Cdd:PTZ00265 477 KNNIKYSLYSL------KDLEALSNYYNEDGNDSQENKNKrnscrakcagDLNDMSNttdsneLIEMRKNYQT-IKDSEV 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 140 AEVLEKLGLNG-------------EAELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQGS- 205
Cdd:PTZ00265 550 VDVSKKVLIHDfvsalpdkyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNe 629
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 206 ---IVFISHDRSFIRNMATRIIDLDRGKLSSWPGNYDKYLESKEEALRVEEQQNAE 258
Cdd:PTZ00265 630 nriTIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNKNNKDD 685
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
151-232 |
7.25e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.79 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 151 EAELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QGS-IVFISHDRSFIRNMATRIIDLD 227
Cdd:COG3845 397 DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELrdAGAaVLLISEDLDEILALSDRIAVMY 476
|
....*
gi 1437745527 228 RGKLS 232
Cdd:COG3845 477 EGRIV 481
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-231 |
9.94e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 45.02 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 3 LISLTGAYLAFSDAPLLdntdlfIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEqDLVTARLQQDPPRDIEGT 82
Cdd:PRK10070 34 ILEKTGLSLGVKDASLA------IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID-GVDIAKISDAELREVRRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 83 IFDFVAQGVAedaqyiteyhrvskvietdpseknlnrLAQLQEVLDNRNLWLLDSRIA---------EVLEKLGLNGEAE 153
Cdd:PRK10070 107 KIAMVFQSFA---------------------------LMPHMTVLDNTAFGMELAGINaeerrekalDALRQVGLENYAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 154 --LSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLD--IETILW--LEKFLKDFQGSIVFISHDRSFIRNMATRIIDLD 227
Cdd:PRK10070 160 syPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplIRTEMQdeLVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
|
....
gi 1437745527 228 RGKL 231
Cdd:PRK10070 240 NGEV 243
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
315-472 |
1.00e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 44.61 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 315 SGKIVfeLEDVNYSIGTR-----RLVRDFSAKVQRGDKIALVGPNGCGKTTLLKL------------MLGDLKADSG--- 374
Cdd:PRK13645 4 SKDII--LDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliisetgqtIVGDYAIPANlkk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 375 -------RIHCGTKLEVAYFDQHRATLDPDKTVMD-NLAEGKQEVMvngrpRHVLGYLQDFLFPPKRAMTPVRALSGGER 446
Cdd:PRK13645 82 ikevkrlRKEIGLVFQFPEYQLFQETIEKDIAFGPvNLGENKQEAY-----KKVPELLKLVQLPEDYVKRSPFELSGGQK 156
|
170 180
....*....|....*....|....*.
gi 1437745527 447 NRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLD 182
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-87 |
1.02e-04 |
|
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: 43.67 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 15 DAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLA--KEQPLDDGQVVYEQDLVT-------ARL-----QQDPPRdIE 80
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITdlppeerARLgiflaFQYPPE-IP 90
|
....*...
gi 1437745527 81 G-TIFDFV 87
Cdd:cd03217 91 GvKNADFL 98
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
32-210 |
1.21e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.61 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 32 VCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDIEGTiFDFVAQGVAEDAQYITEYHRVSKVIETD 111
Cdd:COG3593 26 TVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELT-FGSLLSRLLRLLLKEEDKEELEEALEEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 112 PSEKNlNRLAQLQEVLDNR----------NLWLLDSRIAEVLEKLGL----NGEAELSSLSGG--WLRKAALGRALVSA- 174
Cdd:COG3593 105 NEELK-EALKALNELLSEYlkelldgldlELELSLDELEDLLKSLSLriedGKELPLDRLGSGfqRLILLALLSALAELk 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1437745527 175 ----PKVLFLDEPTNHLDIETILWLEKFLKDFQGSI--VFIS 210
Cdd:COG3593 184 rapaNPILLIEEPEAHLHPQAQRRLLKLLKELSEKPnqVIIT 225
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
338-376 |
1.24e-04 |
|
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: 45.17 E-value: 1.24e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1437745527 338 FSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRI 376
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
324-472 |
1.48e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.87 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 324 DVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADS--------GRIHCGTKLEVAYFDQHRATLD 395
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftgtilanNRKPTKQILKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 396 PDKTVMDNLAEGKQEVMVNGRPRHVLGYLQDFLFPpKRAMTP----------VRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PLN03211 153 PHLTVRETLVFCSLLRLPKSLTKQEKILVAESVIS-ELGLTKcentiignsfIRGISGGERKRVSIAHEMLINPSLLILD 231
|
....*..
gi 1437745527 466 EPTNDLD 472
Cdd:PLN03211 232 EPTSGLD 238
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
342-472 |
1.54e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.00 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 342 VQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIH-CGTKLEVAYFDQHRAT-LDPDKTVMDNLAEGKQEVMVNGRPRH 419
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATvAGKSILTNISDVHQNMgYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 420 V------------LGYLQDFLFPPKRAMTpvraLSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR01257 2042 VpaeeiekvanwsIQSLGLSLYADRLAGT----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-225 |
1.69e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.93 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 2 PLISLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQP-----------LDDGQVVYE-QDLVTA 69
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyrysgdvLLGGRSIFNyRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 70 R----LQQDPPRDIEGTIFDFVAQGVaedaqyiteyhRVSKVIetdpSEKNLNRLAQLQevLDNRNLW-LLDSRIAEVLE 144
Cdd:PRK14271 100 RrrvgMLFQRPNPFPMSIMDNVLAGV-----------RAHKLV----PRKEFRGVAQAR--LTEVGLWdAVKDRLSDSPF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 145 KLglngeaelsslSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDFQG--SIVFISHDRSfirnMATR 222
Cdd:PRK14271 163 RL-----------SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLA----QAAR 227
|
...
gi 1437745527 223 IID 225
Cdd:PRK14271 228 ISD 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
137-261 |
1.85e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 137 SRIAEVLEKLGLNGEA--ELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETI--LWLE--KFLKDfQGSIVFIS 210
Cdd:NF000106 123 ARADELLERFSLTEAAgrAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRneVWDEvrSMVRD-GATVLLTT 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 211 HDRSFIRNMATRIIDLDRGKLSSwPGNYDKyLESK--EEALRVEEQQNAEFDR 261
Cdd:NF000106 202 QYMEEAEQLAHELTVIDRGRVIA-DGKVDE-LKTKvgGRTLQIRPAHAAELDR 252
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
154-231 |
2.53e-04 |
|
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: 44.05 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 154 LSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF--QG-SIVFISHDRSFIRNMATRIIDLDRGK 230
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaqEGvAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
.
gi 1437745527 231 L 231
Cdd:TIGR02633 481 L 481
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
317-473 |
2.68e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.09 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 317 KIVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGdlkadsgriHCGTKL---EVAYFDQHRAT 393
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG---------HPAYKIlegDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 394 LDPDK-------------------TVMDNL-----AEGKQEVMVNGRPRHVLGYLQDFLfpPKRAMTPV-------RALS 442
Cdd:CHL00131 76 LEPEErahlgiflafqypieipgvSNADFLrlaynSKRKFQGLPELDPLEFLEIINEKL--KLVGMDPSflsrnvnEGFS 153
|
170 180 190
....*....|....*....|....*....|.
gi 1437745527 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDI 184
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
318-496 |
2.95e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 43.28 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 318 IVFELEDVNYSIGT---RRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklEVAYFdqhraTL 394
Cdd:PRK13641 3 IKFENVDYIYSPGTpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI------TIAGY-----HI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 395 DPDkTVMDNLAEGKQEV-MVNGRPRHVL---GYLQDFLFPPK-----------RAMTPVRA--------------LSGGE 445
Cdd:PRK13641 72 TPE-TGNKNLKKLRKKVsLVFQFPEAQLfenTVLKDVEFGPKnfgfsedeakeKALKWLKKvglsedliskspfeLSGGQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 446 RNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVDAYQG---TVLLVSHD 496
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHN 204
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
23-188 |
4.44e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.91 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 23 DLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDppRDI-----------EGTIFDFVAQGV 91
Cdd:PRK11650 24 DLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIamvfqnyalypHMSVRENMAYGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 92 -------AEDAQYITEyhrVSKVIETDPseknlnrlaqlqevldnrnlwLLDSRIAEvleklglngeaelssLSGGWLRK 164
Cdd:PRK11650 102 kirgmpkAEIEERVAE---AARILELEP---------------------LLDRKPRE---------------LSGGQRQR 142
|
170 180
....*....|....*....|....
gi 1437745527 165 AALGRALVSAPKVLFLDEPTNHLD 188
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
293-473 |
4.65e-04 |
|
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: 43.40 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 293 VER-SERREVLGSARMQVEEAT------RSGKIVFELEDVNYSIGTRRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLM 365
Cdd:TIGR00957 1253 VERlKEYSETEKEAPWQIQETAppsgwpPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGL 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 366 LGDLKADSGRIHCgTKLEVAYFDQH--------------------RATLDPDKTVMDnlaegkQEVMVNGRprhvLGYLQ 425
Cdd:TIGR00957 1333 FRINESAEGEIII-DGLNIAKIGLHdlrfkitiipqdpvlfsgslRMNLDPFSQYSD------EEVWWALE----LAHLK 1401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 426 DFL--FPPKRAMTPVRA---LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR00957 1402 TFVsaLPDKLDHECAEGgenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-191 |
5.37e-04 |
|
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: 42.54 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 16 APLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYeqdlvTARLQQDPPRD--IEGTIFDFVAQGVAE 93
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKH-----SGRISFSSQFSwiMPGTIKENIIFGVSY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 94 DaqyitEYhRVSKVIETDPSEKNLNRLAQlqevLDNrnlwlldsriaEVLEKLGLNgeaelssLSGGWLRKAALGRALVS 173
Cdd:cd03291 125 D-----EY-RYKSVVKACQLEEDITKFPE----KDN-----------TVLGEGGIT-------LSGGQRARISLARAVYK 176
|
170
....*....|....*...
gi 1437745527 174 APKVLFLDEPTNHLDIET 191
Cdd:cd03291 177 DADLYLLDSPFGYLDVFT 194
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
158-212 |
5.91e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 42.40 E-value: 5.91e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745527 158 SGGWLRKAALGRALVSAPKVLFLDEPTNHLDIET---ILWLEKFLK-DFQGSIVFISHD 212
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELKrEFNTAIIMITHD 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
322-472 |
6.19e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 42.28 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 322 LEDVNYSI--GTRRLvRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC------------GTKLEVAYF 387
Cdd:PRK13644 4 LENVSYSYpdGTPAL-ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtgdfsklqGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 388 DQHRATLDPDKTVMDNLAEGKQEVM---VNGRPRhVLGYLQDFLFPPKRAMTPvRALSGGERNRLLLARLFLKPSNLLIL 464
Cdd:PRK13644 83 FQNPETQFVGRTVEEDLAFGPENLClppIEIRKR-VDRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEPECLIF 160
|
....*...
gi 1437745527 465 DEPTNDLD 472
Cdd:PRK13644 161 DEVTSMLD 168
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
156-224 |
6.74e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.02 E-value: 6.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437745527 156 SLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIETILWLEKFLKDF----QGSIVFISHDRSFIRNMATRII 224
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSDRIH 143
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
349-473 |
6.79e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 42.17 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 349 ALVGPNGCGKTTLLKLMLGDLKADSGRIHCGT---------------KLEVAY-FDQHRatLDPDKTVMDNLAEGKQEVM 412
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaekgiclppeKRRIGYvFQDAR--LFPHYKVRGNLRYGMAKSM 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 413 VNGRPRHV--LGyLQDFL--FPpkramtpvRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11144 106 VAQFDKIValLG-IEPLLdrYP--------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-212 |
7.68e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 42.00 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 5 SLTGAYLAFSDAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVYEQDLVTARLQQDPPRDIeGTIF 84
Cdd:PRK13642 9 NLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI-GMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 85 -----DFVAQGVAEDAQYITEYHRVskvietdPSEKNLNRlaqLQEVLDNRNLWLLDSRiaevleklglngeaELSSLSG 159
Cdd:PRK13642 88 qnpdnQFVGATVEDDVAFGMENQGI-------PREEMIKR---VDEALLAVNMLDFKTR--------------EPARLSG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745527 160 GWLRKAALGRALVSAPKVLFLDEPTNHLD----IETILWLEKFLKDFQGSIVFISHD 212
Cdd:PRK13642 144 GQKQRVAVAGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
339-496 |
9.68e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 41.62 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 339 SAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKLEVAYFDQHRATL-----DPDK-----TVMDNLAEG 407
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLRRKIgmvfqNPDNqfvgaTVEDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 408 KQEvmvNGRPRH-VLGYLQDFLFPPK----RAMTPVRaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEEL 482
Cdd:PRK13642 107 MEN---QGIPREeMIKRVDEALLAVNmldfKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170
....*....|....*...
gi 1437745527 483 V----DAYQGTVLLVSHD 496
Cdd:PRK13642 183 IheikEKYQLTVLSITHD 200
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
339-526 |
1.24e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 41.23 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 339 SAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIhcgtklEVAYFDQHRAT-LDPDKTVMDNLAEGKQEV----MV 413
Cdd:PRK13651 27 SVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI------EWIFKDEKNKKkTKEKEKVLEKLVIQKTRFkkikKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 414 NGRPRHVLGYLQ-------------DFLFPP-----------KRAMTPVR--------------ALSGGERNRLLLARLF 455
Cdd:PRK13651 101 KEIRRRVGVVFQfaeyqlfeqtiekDIIFGPvsmgvskeeakKRAAKYIElvgldesylqrspfELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745527 456 LKPSNLLILDEPTNDLD---VETLELLEELVDAYQGTVLLVSHDrefVDNSV--TECWIFEGDGVInSYVGGYYDA 526
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD---LDNVLewTKRTIFFKDGKI-IKDGDTYDI 252
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-232 |
1.80e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.44 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 30 ERVCLVGRNGAGKSTLLRVLAKEQPLDDGQVVyeqdLVTARLQQDPPRDIegtifdfVAQGVA---ED--AQYITEYHRV 104
Cdd:PRK11288 280 EIVGLFGLVGAGRSELMKLLYGATRRTAGQVY----LDGKPIDIRSPRDA-------IRAGIMlcpEDrkAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 105 skvietdpsEKNLN-----RLAQLQEVLDNRnlW---LLDSRIAEVLEKLGlNGEAELSSLSGGWLRKAALGRALVSAPK 176
Cdd:PRK11288 349 ---------ADNINisarrHHLRAGCLINNR--WeaeNADRFIRSLNIKTP-SREQLIMNLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745527 177 VLFLDEPTNHLDI-------ETILWLEKflkdfQG-SIVFISHDRSFIRNMATRIIDLDRGKLS 232
Cdd:PRK11288 417 VILLDEPTRGIDVgakheiyNVIYELAA-----QGvAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
321-472 |
2.14e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 40.50 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 321 ELEDVNYSI--GT---RRLVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKL------------- 382
Cdd:PRK13649 4 NLQNVSYTYqaGTpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 383 --EVAYFDQHRATLDPDKTVMDNLAEGKQEVMVN-------GRPRHVLGYLQDFLFppkrAMTPVRaLSGGERNRLLLAR 453
Cdd:PRK13649 84 rkKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSqeeaealAREKLALVGISESLF----EKNPFE-LSGGQMRRVAIAG 158
|
170
....*....|....*....
gi 1437745527 454 LFLKPSNLLILDEPTNDLD 472
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLD 177
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
154-251 |
2.19e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 154 LSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDI-------ETILWLEKflKDfqGSIVFISHDRSFIRNMATRIIDL 226
Cdd:PRK10982 389 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVgakfeiyQLIAELAK--KD--KGIIIISSEMPELLGITDRILVM 464
|
90 100
....*....|....*....|....*
gi 1437745527 227 DRGKLSswpGNYDKYLESKEEALRV 251
Cdd:PRK10982 465 SNGLVA---GIVDTKTTTQNEILRL 486
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
150-230 |
2.21e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.90 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 150 GEAELSSLSggwLRkAALGRALVSAPKVLFLDEPTNHLD-------IETILWLEKFLKDFQgsIVFISHDRSFIRNMAT- 221
Cdd:cd03240 119 GEKVLASLI---IR-LALAETFGSNCGILALDEPTTNLDeenieesLAEIIEERKSQKNFQ--LIVITHDEELVDAADHi 192
|
90
....*....|
gi 1437745527 222 -RIIDLDRGK 230
Cdd:cd03240 193 yRVEKDGRQK 202
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-228 |
2.27e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 19 LDNTDLFIDENERV-CLVGRNGAGKSTLLRVLA---------------KEQPLDDGQVVYEQDLV----TARLQQDPPRD 78
Cdd:COG3950 14 FEDLEIDFDNPPRLtVLVGENGSGKTTLLEAIAlalsgllsrlddvkfRKLLIRNGEFGDSAKLIlyygTSRLLLDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 79 IEGTIFDFVAQGVA-------EDA------QYITEYHrvsKVIETDPSEKNLNRLAQLQEVL-----DNRNLWLLDSRIA 140
Cdd:COG3950 94 KLERLKEEYFSRLDgydslldEDSnlreflEWLREYL---EDLENKLSDELDEKLEAVREALnkllpDFKDIRIDRDPGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 141 EVLEKLGlNGEAELSSLSGG--------------WLRKAALGRALVSAPKVLFLDEPTNHLDIE---TIL-WLEKFLKDF 202
Cdd:COG3950 171 LVILDKN-GEELPLNQLSDGersllalvgdlarrLAELNPALENPLEGEGIVLIDEIDLHLHPKwqrRILpDLRKIFPNI 249
|
250 260
....*....|....*....|....*..
gi 1437745527 203 QgsIVFISHDRSFIRNMATR-IIDLDR 228
Cdd:COG3950 250 Q--FIVTTHSPLILSSLEDEeVIVLER 274
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
342-500 |
3.05e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 39.97 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 342 VQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHC-GTKLE------------VAYFDQHRatLDPDKTVMDNLaegk 408
Cdd:PRK11300 28 VREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLrGQHIEglpghqiarmgvVRTFQHVR--LFREMTVIENL---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 409 qevMVnGRPRHV-LGYLQDFLFPP----------KRAMT-------------PVRALSGGERNRLLLARLFLKPSNLLIL 464
Cdd:PRK11300 102 ---LV-AQHQQLkTGLFSGLLKTPafrraesealDRAATwlervgllehanrQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1437745527 465 DEP--------TNDLDvetlELLEELVDAYQGTVLLVSHDREFV 500
Cdd:PRK11300 178 DEPaaglnpkeTKELD----ELIAELRNEHNVTVLLIEHDMKLV 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-63 |
3.14e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 3.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1437745527 19 LDNTDLFIDENERVCLVGRNGAGKSTLLRVLAKEQPLD--DGQVVYE 63
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFD 63
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
151-245 |
3.65e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.15 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 151 EAELSSLSGGWLRKAALGRALVSAPKVLFLDEPTNHLDIET---ILWLEKFLKDFQGSIVFISHDRSFIRNMATRIIDLD 227
Cdd:PRK09700 404 NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAkaeIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFC 483
|
90
....*....|....*...
gi 1437745527 228 RGKLSSWPGNYDKYLESK 245
Cdd:PRK09700 484 EGRLTQILTNRDDMSEEE 501
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
347-368 |
3.76e-03 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 38.24 E-value: 3.76e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
437-500 |
4.05e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 4.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745527 437 PVRALSGGERNRLLLARLFLKPS---NLLILDEPTNDL---DVETLELLEELVdAYQG-TVLLVSHDREFV 500
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAYELLAPSkkpTLYVLDEPTTGLhthDIKALIYVLQSL-THQGhTVVIIEHNMHVV 875
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
352-472 |
4.23e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.08 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 352 GPNGCGKTTLLKLMLGDLKADSGRIH---CGT----KLEVAYFDqHRATLDPDKTVMDNL---AEGKQEVMVNGRPRHVL 421
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYyknCNInniaKPYCTYIG-HNLGLKLEMTVFENLkfwSEIYNSAETLYAAIHYF 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1437745527 422 GyLQDFLfppkraMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13541 112 K-LHDLL------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
350-406 |
4.71e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.21 E-value: 4.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745527 350 LVGPNGCGKTTLLKLM----------LGDLKADSGRIHCGTKLE----VAYFDQHRATLDPDKTVMDNLAE 406
Cdd:COG3950 30 LVGENGSGKTTLLEAIalalsgllsrLDDVKFRKLLIRNGEFGDsaklILYYGTSRLLLDGPLKKLERLKE 100
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
157-224 |
4.96e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 39.34 E-value: 4.96e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745527 157 LSGGWLRKAALGRALVSAPKVLFLDEPTNHLD-------IETILWLEkflKDFQGSIVFISHDRSFIRNMATRII 224
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqaqiIELLLELQ---QKENMALVLITHDLALVAEAAHKII 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
136-231 |
5.09e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 39.30 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 136 DSRIAEVLEKLGL-NGEAELSS----LSGGWLRKAALGRALVSAPKVLFLDEPTNHLDI---ETIL-WLEKFLKDFQGSI 206
Cdd:PRK10418 115 DATLTAALEAVGLeNAARVLKLypfeMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVvaqARILdLLESIVQKRALGM 194
|
90 100
....*....|....*....|....*
gi 1437745527 207 VFISHDRSFIRNMATRIIDLDRGKL 231
Cdd:PRK10418 195 LLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
334-495 |
5.14e-03 |
|
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: 40.12 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 334 LVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCGTKLEVAYFDQH----RATLDPDKTVMDNLAEGKQ 409
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRpymtLGTLRDQIIYPDSSEDMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 410 EVMVNGRPRHVLGYLQ-DFLFPPKRAMTPVR----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELVD 484
Cdd:TIGR00954 547 RGLSDKDLEQILDNVQlTHILEREGGWSAVQdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCR 626
|
170
....*....|.
gi 1437745527 485 AYQGTVLLVSH 495
Cdd:TIGR00954 627 EFGITLFSVSH 637
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
32-217 |
7.76e-03 |
|
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: 39.35 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 32 VCLVGRNGAGKSTLLRVLAKEQPLDDGqvvyeqdlvtaRLQQDPPrdieGTIFdFVAQgvaedAQYITEYHRVSKVIETD 111
Cdd:TIGR00954 481 LLICGPNGCGKSSLFRILGELWPVYGG-----------RLTKPAK----GKLF-YVPQ-----RPYMTLGTLRDQIIYPD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 112 PSEKNLNR---LAQLQEVLDNRNLWLLdsriaeVLEKLGLNGEAELSS-LSGGWLRKAALGRALVSAPKVLFLDEPTNHL 187
Cdd:TIGR00954 540 SSEDMKRRglsDKDLEQILDNVQLTHI------LEREGGWSAVQDWMDvLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180 190
....*....|....*....|....*....|
gi 1437745527 188 DIETILWLEKFLKDFQGSIVFISHDRSFIR 217
Cdd:TIGR00954 614 SVDVEGYMYRLCREFGITLFSVSHRKSLWK 643
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
322-496 |
8.37e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 38.86 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 322 LEDVNYSIGtrrlVRDFSAKVQRGDKIALVGPNGCGKTTLLKLMLGDLKADSGRIHCG----TKLEVAYFDQHRA----- 392
Cdd:PRK10070 35 LEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiAKISDAELREVRRkkiam 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745527 393 -----TLDPDKTVMDNLAEGKQEVMVNGRPRH--VLGYLQDFLFPPKRAMTPvRALSGGERNRLLLARLFLKPSNLLILD 465
Cdd:PRK10070 111 vfqsfALMPHMTVLDNTAFGMELAGINAEERRekALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190
....*....|....*....|....*....|....*
gi 1437745527 466 EPTNDLDVETLELLEELV----DAYQGTVLLVSHD 496
Cdd:PRK10070 190 EAFSALDPLIRTEMQDELvklqAKHQRTIVFISHD 224
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
437-471 |
9.03e-03 |
|
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: 39.23 E-value: 9.03e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1437745527 437 PVRALSGGERNRLLLARLFLKPSN---LLILDEPTNDL 471
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGL 863
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
439-472 |
9.26e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.24 E-value: 9.26e-03
10 20 30
....*....|....*....|....*....|....
gi 1437745527 439 RALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
15-50 |
9.99e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.08 E-value: 9.99e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1437745527 15 DAPLLDNTDLFIDENERVCLVGRNGAGKSTLLRVLA 50
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA 54
|
|
| |
