|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-552 |
0e+00 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 1152.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 1 MAQYIYTMNRVSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGIKIGYLEQEPPL 80
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 81 DPTKDVRGNVEDGVREALDALERLDQVFAEYADPDADFDALAKEQEKLESIIHAWDAHNLNNQLEIAADALNLPAWDADV 160
Cdd:PRK11819 82 DPEKTVRENVEEGVAEVKAALDRFNEIYAAYAEPDADFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPWDAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 161 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGHGIPY 240
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 241 QGNYSSWLEQKNARLEQEQKQEESFAKALKKELEWVRSNAKGQQKKNKARMERFEELNSKEFQQRNETSEIYIPPGPRLG 320
Cdd:PRK11819 242 EGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYEELLSEEYQKRNETNEIFIPPGPRLG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 321 NKVVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQIRDTLDN 400
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 401 NKTVWEEVSGGLDILKVGDYEIASRAYIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETL 480
Cdd:PRK11819 402 NKTVWEEISGGLDIIKVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETL 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 481 RALEDAILVFPGTVMVVSHDRWFLDRIATHILSFENE-QPEFYTGNYAEYEAYRQSRLGEDAVQ-KRTKYKKIS 552
Cdd:PRK11819 482 RALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDsQVEWFEGNFQEYEEDKKRRLGADAARpHRIKYKKLT 555
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-551 |
0e+00 |
|
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: 1108.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 2 AQYIYTMNRVSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGIKIGYLEQEPPLD 81
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 82 PTKDVRGNVEDGVREALDALERLDQVFAEYADPDADFDALAKEQEKLESIIHAWDAHNLNNQLEIAADALNLPAWDADVT 161
Cdd:TIGR03719 81 PTKTVRENVEEGVAEIKDALDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDADVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGHGIPYQ 241
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 242 GNYSSWLEQKNARLEQEQKQEESFAKALKKELEWVRSNAKGQQKKNKARMERFEELNSKEFQQRNETSEIYIPPGPRLGN 321
Cdd:TIGR03719 241 GNYSSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRNETAEIYIPPGPRLGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 322 KVVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQIRDTLDNN 401
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 402 KTVWEEVSGGLDILKVGDYEIASRAYIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLR 481
Cdd:TIGR03719 401 KTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLR 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 482 ALEDAILVFPGTVMVVSHDRWFLDRIATHILSFENE-QPEFYTGNYAEYEAYRQSRLGEDAVQ-KRTKYKKI 551
Cdd:TIGR03719 481 ALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDsHVEWFEGNFSEYEEDKKRRLGEDADQpHRIKYKKL 552
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-532 |
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: 729.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 8 MNRVSKMVPpKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGIKIGYLEQEPPLDPTKDVR 87
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNVEDGVREALDALERLDQVFAEYADPDADFDALAKEQEKLESIihawDAHNLNNQLEIAADALNLPA--WDADVTKLSG 165
Cdd:COG0488 80 DTVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEAL----GGWEAEARAEEILSGLGFPEedLDRPVSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 166 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGHGIPYQGNYS 245
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 246 SWLEQKNARLEQEQKQEESFAKALKKELEWVRSN-AKGQQ-KKNKARMERFEELNSKEFQQRNETSEIYIPPGPRLGNKV 323
Cdd:COG0488 236 AYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFrAKARKaKQAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQIRDTLDNNKT 403
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 404 VWEEVSGGLDilkvGDYEIASRAYIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRAL 483
Cdd:COG0488 396 VLDELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 491208697 484 EDAILVFPGTVMVVSHDRWFLDRIATHILSFENEQPEFYTGNYAEYEAY 532
Cdd:COG0488 472 EEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-549 |
5.10e-115 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 354.64 E-value: 5.10e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 31 PGAKIGVLGLNGAGKSTLLRIMAG-VDKDfSGEARAQPGIKIGYLEQEPPldptKDVRGNVED----GVREALDALER-- 103
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNGeVLLD-DGRIIYEQDLIVARLQQDPP----RNVEGTVYDfvaeGIEEQAEYLKRyh 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 104 --LDQVFAEYADpdADFDALAKEQEKLEsiiHAwDAHNLNNQLEIAADALNLPAwDADVTKLSGGERRRVALCRLLLSKP 181
Cdd:PRK11147 103 diSHLVETDPSE--KNLNELAKLQEQLD---HH-NLWQLENRINEVLAQLGLDP-DAALSSLSGGWLRKAALGRALVSNP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 182 DMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGHGIPYQGNYSSWLEQKNARLEQEQKQ 261
Cdd:PRK11147 176 DVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALRVEELQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 262 EESFAKALKKELEWVRSNAKGQQKKNKARMERFEELNSKEFQQRNE--TSEIYIPPGPRLGNKVVEVEGISKSFDGRVLY 339
Cdd:PRK11147 256 NAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVmgTAKMQVEEASRSGKIVFEMENVNYQIDGKQLV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 340 ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQIRDTLDNNKTVWEEVSGGLDILKVGD 419
Cdd:PRK11147 336 KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNLAEGKQEVMVNG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 420 YEIASRAYIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAILVFPGTVMVVSH 499
Cdd:PRK11147 416 RPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSH 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 491208697 500 DRWFLDRIATHILSFE-NEQPEFYTGNYaeyeayrqsrlgEDAVQKRTKYK 549
Cdd:PRK11147 496 DRQFVDNTVTECWIFEgNGKIGRYVGGY------------HDARQQQAQYL 534
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-529 |
2.38e-82 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 266.37 E-value: 2.38e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 25 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGIKIGYL-------EQEPPLD----------PTKDVR 87
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLrqdqfafEEFTVLDtvimghtelwEVKQER 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNV--------EDGVREAldaleRLDQVFAEYadpDAdFDALAKEQEKLESIIHAWDAHNLNNQlEIAadalnlPAWdad 159
Cdd:PRK15064 100 DRIyalpemseEDGMKVA-----DLEVKFAEM---DG-YTAEARAGELLLGVGIPEEQHYGLMS-EVA------PGW--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 160 vtKLsggerrRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGHGIP 239
Cdd:PRK15064 161 --KL------RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 240 YQGNYSSWLEQknARLEQEQKQ-EESFAKALKKEL-EWVR---SNA-KGQQKKNKAR-MER--FEELNSKEFQqrneTSE 310
Cdd:PRK15064 233 YPGNYDEYMTA--ATQARERLLaDNAKKKAQIAELqSFVSrfsANAsKAKQATSRAKqIDKikLEEVKPSSRQ----NPF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 311 IYIPPGPRLGNKVVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAY 390
Cdd:PRK15064 307 IRFEQDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 391 VGQirDT---LDNNKTVWEEVSgglDILKVGDYEIASRAYIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVIL 467
Cdd:PRK15064 387 YAQ--DHaydFENDLTLFDWMS---QWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 468 LDEPSNDLDIETLRALEDAILVFPGTVMVVSHDRWFLDRIATHILSFENEQPEFYTGNYAEY 529
Cdd:PRK15064 462 MDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-532 |
1.55e-72 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 243.54 E-value: 1.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGIKIGYLEQE-PPLD-PTKDVrgnVEDGVRE 96
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQEtPALPqPALEY---VIDGDRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 97 ALDALERLDQvfaeyADPDADFDALAKEQEKLESIiHAWD----AHNLNNQLEIAADALNLPawdadVTKLSGGERRRVA 172
Cdd:PRK10636 91 YRQLEAQLHD-----ANERNDGHAIATIHGKLDAI-DAWTirsrAASLLHGLGFSNEQLERP-----VSDFSGGWRMRLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 173 LCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGHGIPYQGNYSSWLEQKN 252
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 253 ARLEQEQ----KQEESFAKaLKKELEWVRSNA-KGQQKKNKARM-ERFEEL------NSKEFQQRNETSeiyippgprLG 320
Cdd:PRK10636 240 TRLAQQQamyeSQQERVAH-LQSYIDRFRAKAtKAKQAQSRIKMlERMELIapahvdNPFHFSFRAPES---------LP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 321 NKVVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQIR-DTLD 399
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQlEFLR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 400 NNKTVWEEVSGgldiLKVGDYEIASRAYIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIET 479
Cdd:PRK10636 390 ADESPLQHLAR----LAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 491208697 480 LRALEDAILVFPGTVMVVSHDRWFLDRIATHILSFENEQPEFYTGNYAEYEAY 532
Cdd:PRK10636 466 RQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQW 518
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
326-537 |
3.41e-69 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 231.49 E-value: 3.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 326 VEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQiRDTLDNNKTVW 405
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQ-EPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 406 EEVSGGLDILK--------------------------------VGDYEIASRA--YIGRFNFKGQDQQKRVGELSGGERN 451
Cdd:COG0488 80 DTVLDGDAELRaleaeleeleaklaepdedlerlaelqeefeaLGGWEAEARAeeILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 452 RLQLAKILQQGANVILLDEPSNDLDIETLRALEDAILVFPGTVMVVSHDRWFLDRIATHILSFENEQPEFYTGNYAEYEA 531
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLE 239
|
....*.
gi 491208697 532 YRQSRL 537
Cdd:COG0488 240 QRAERL 245
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
324-516 |
5.52e-56 |
|
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: 184.57 E-value: 5.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQirdtldnnkt 403
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 404 vweevsggldilkvgdyeiasrayigrfnfkgqdqqkrvgeLSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRAL 483
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|...
gi 491208697 484 EDAILVFPGTVMVVSHDRWFLDRIATHILSFEN 516
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELED 142
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-500 |
2.47e-55 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 198.55 E-value: 2.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAgvdkdfsgeARAQPGI----KIGYLEQEPPLDPTKDVRGNVEDGV 94
Cdd:PLN03073 190 RDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA---------MHAIDGIpkncQILHVEQEVVGDDTTALQCVLNTDI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 95 rEALDALERLDQVFAEYADPD---------------ADFDALAKEQEKLESIIHAWDAHNLNNQleiAADALNLPAWDAD 159
Cdd:PLN03073 261 -ERTQLLEEEAQLVAQQRELEfetetgkgkgankdgVDKDAVSQRLEEIYKRLELIDAYTAEAR---AASILAGLSFTPE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 160 VTK-----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDR 234
Cdd:PLN03073 337 MQVkatktFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 235 GHGIPYQGNYSSWLEQKNARLEQEQKQEESFAKA---LKKELEWVRSNAKGQ---QKKNKA--RMERFEE-LNSKEFQQR 305
Cdd:PLN03073 417 QKLVTYKGDYDTFERTREEQLKNQQKAFESNERSrshMQAFIDKFRYNAKRAslvQSRIKAldRLGHVDAvVNDPDYKFE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 306 NETseiyipPGPRLGNKVVEVEGISKSF-DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGE 384
Cdd:PLN03073 497 FPT------PDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 385 SVKVAYVGQIR-DTLDNNKTVWeevsggLDILKV--GDYEIASRAYIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQ 461
Cdd:PLN03073 571 KVRMAVFSQHHvDGLDLSSNPL------LYMMRCfpGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFK 644
|
490 500 510
....*....|....*....|....*....|....*....
gi 491208697 462 GANVILLDEPSNDLDIETLRALEDAILVFPGTVMVVSHD 500
Cdd:PLN03073 645 KPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHD 683
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
18-236 |
1.61e-52 |
|
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: 175.33 E-value: 1.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGIKIGYLEQeppldptkdvrgnvedgvrea 97
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 98 ldalerldqvfaeyadpdadfdalakeqeklesiihawdahnlnnqleiaadalnlpawdadvtkLSGGERRRVALCRLL 177
Cdd:cd03221 71 -----------------------------------------------------------------LSGGEKMRLALAKLL 85
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 178 LSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGH 236
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-512 |
2.93e-43 |
|
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: 161.22 E-value: 2.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV--------------DKDFSGEARAQPGIKIGYLEQEPP--LDP 82
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphggrisgevlldGRDLLELSEALRGRRIGMVFQDPMtqLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 83 TKdvrgnVEDGVREALDALERldqvfaeyadPDADFDALAKEqeklesiihawdahnlnnqleiAADALNLPA-WDADVT 161
Cdd:COG1123 99 VT-----VGDQIAEALENLGL----------SRAEARARVLE----------------------LLEAVGLERrLDRYPH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGhg 237
Cdd:COG1123 142 QLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDG-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 238 ipyqgnysswleqknaRLEQEQKQEESFAkalkkelewvrsnakgqqkkNKARMERFEELNSKEFQQrnetseiyiPPGP 317
Cdd:COG1123 220 ----------------RIVEDGPPEEILA--------------------APQALAAVPRLGAARGRA---------APAA 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 318 RLGNKVVEVEGISKSFDGR------VLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV---- 386
Cdd:COG1123 255 AAAEPLLEVRNLSKRYPVRgkggvrAV-DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdGKDLtkls 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 387 ---------KVAYVGQIRDT-LDNNKTVWEEVSGGLDILKVGDY-EIASRAY--IGRFNFKGQDQQKRVGELSGGERNRL 453
Cdd:COG1123 334 rrslrelrrRVQMVFQDPYSsLNPRMTVGDIIAEPLRLHGLLSRaERRERVAelLERVGLPPDLADRYPHELSGGQRQRV 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 454 QLAKILQQGANVILLDEPSNDLD-------IETLRALEDAilvFPGTVMVVSHDRWFLDRIATHIL 512
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDvsvqaqiLNLLRDLQRE---LGLTYLFISHDLAVVRYIADRVA 476
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
323-512 |
1.02e-37 |
|
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: 139.41 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV----------KVAYV 391
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 392 GQIRDTLDNNkTVWEEVS-------GGLDILKVGDYEIASRAyIGRFN---FKgqdqQKRVGELSGGERNRLQLAKILQQ 461
Cdd:COG1120 81 PQEPPAPFGL-TVRELVAlgryphlGLFGRPSAEDREAVEEA-LERTGlehLA----DRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 462 GANVILLDEPSNDLDI----ETLRALEDAILVFPGTVMVVSHDrwfLD---RIATHIL 512
Cdd:COG1120 155 EPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD---LNlaaRYADRLV 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-231 |
1.97e-37 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 137.23 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARaqpgikigyLEQEPPLDPTKDVRGNV-----EDG 93
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVL---------WNGEPIRDAREDYRRRLaylghADG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 94 VREALDALERLDQVFAEYADPDADFDALAkeqeklesiihawdahnlnnqleiAADALNL-PAWDADVTKLSGGERRRVA 172
Cdd:COG4133 86 LKPELTVRENLRFWAALYGLRADREAIDE------------------------ALEAVGLaGLADLPVRQLSAGQKRRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 173 LCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFP---GTIVAITHDRYFLDNVAEWILE 231
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAARVLDLG 203
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
321-512 |
3.47e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.91 E-value: 3.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 321 NKVVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV-----KVAYVGQi 394
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPrrarrRIGYVPQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 RDTLDNNK--TVWEEVSGGLD-------ILKVGDYEIASRA--------YIGRfnfkgqdqqkRVGELSGGERNRLQLAK 457
Cdd:COG1121 83 RAEVDWDFpiTVRDVVLMGRYgrrglfrRPSRADREAVDEAlervgledLADR----------PIGELSGGQQQRVLLAR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 458 ILQQGANVILLDEPSNDLDIETLRALEDAI--LVFPG-TVMVVSHDRWFLDRIATHIL 512
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLreLRREGkTILVVTHDLGAVREYFDRVL 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
19-236 |
7.32e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.71 E-value: 7.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR-------AQPGI----KIGYLEQEPPLdptkdvr 87
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsAMPPPewrrQVAYVPQEPAL------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 gnVEDGVRealDALERLDQVFAEYADPDADFDALAkeqeklesiihawdahnlnnQLEIAADALnlpawDADVTKLSGGE 167
Cdd:COG4619 86 --WGGTVR---DNLPFPFQLRERKFDRERALELLE--------------------RLGLPPDIL-----DKPVERLSGGE 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491208697 168 RRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGH 236
Cdd:COG4619 136 RQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
325-517 |
8.94e-36 |
|
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: 133.04 E-value: 8.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV-----KVAYVGQIRDTL 398
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLekerkRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 399 -DNNKTVWEEVS-------GGLDILKVGDYEIASRA--YIGRFNFKgqdqQKRVGELSGGERNRLQLAKILQQGANVILL 468
Cdd:cd03235 81 rDFPISVRDVVLmglyghkGLFRRLSKADKAKVDEAleRVGLSELA----DRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491208697 469 DEPSNDLDIETLRALEDAI--LVFPG-TVMVVSHDRWFLDRIATHILSFENE 517
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLreLRREGmTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
325-512 |
1.06e-35 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 133.83 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV---------KVAYVGQI 394
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdGEDVrkeprearrQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 RDtLDNNKTVWEEVSGGLDILKVGDYEIASRA--YIGRFNFkGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPS 472
Cdd:COG4555 83 RG-LYDRLTVRENIRYFAELYGLFDEELKKRIeeLIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491208697 473 NDLDIETLRALEDAILVF---PGTVMVVSHDRWFLDRIATHIL 512
Cdd:COG4555 161 NGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVV 203
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
324-512 |
2.93e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 132.11 E-value: 2.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVT-LGESV---------KVAYVGQ 393
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVardpaevrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 394 iRDTLDNNKTVWE--EVSGGLdiLKVGDYEIASRA--YIGRFNFKGqDQQKRVGELSGGERNRLQLAKILQQGANVILLD 469
Cdd:COG1131 81 -EPALYPDLTVREnlRFFARL--YGLPRKEARERIdeLLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491208697 470 EPSNDLDIETLRALEDAI--LVFPG-TVMVVSHDRWFLDRIATHIL 512
Cdd:COG1131 157 EPTSGLDPEARRELWELLreLAAEGkTVLLSTHYLEEAERLCDRVA 202
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
325-516 |
5.89e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 130.71 E-value: 5.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV----------KVAYVGQ 393
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPLsampppewrrQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 394 ----IRDTL-DNNKTVWEEVSGGLDILKVgdyeiasRAYIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILL 468
Cdd:COG4619 82 epalWGGTVrDNLPFPFQLRERKFDRERA-------LELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491208697 469 DEPSNDLDIETLRALEDAILVFP----GTVMVVSHDRWFLDRIATHILSFEN 516
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-517 |
4.71e-34 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 136.09 E-value: 4.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 31 PGAKIGVLGLNGAGKSTLLRIMAG------------VDKD-----FSG-----------EARAQPGIKIGYLEQEPpldp 82
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGelipnlgdyeeePSWDevlkrFRGtelqnyfkklyNGEIKVVHKPQYVDLIP---- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 83 tKDVRGNVEDgvrealdALERLDqvfaeyadpdadfdalakEQEKLESIIhawdahnlnnqleiaaDALNL-PAWDADVT 161
Cdd:PRK13409 174 -KVFKGKVRE-------LLKKVD------------------ERGKLDEVV----------------ERLGLeNILDRDIS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsvswlERF-----LKDF-PG-TIVAITHDRYFLDNVAEWIleldr 234
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR-----QRLnvarlIRELaEGkYVLVVEHDLAVLDYLADNV----- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 235 gH---GIPyqGNYSSWLEQKNARleqeqkqeesfakalkkelewVRSNA--KGQQKKNKARMeRFEELnskEFQQRNETS 309
Cdd:PRK13409 282 -HiayGEP--GAYGVVSKPKGVR---------------------VGINEylKGYLPEENMRI-RPEPI---EFEERPPRD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 310 EiyiPPGPRLgnkvVEVEGISKSfdgrvlYENLSFTVPPTAI-----VGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLge 384
Cdd:PRK13409 334 E---SERETL----VEYPDLTKK------LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 385 SVKVAYV---------GQIRDTLDNNKT------VWEEVSGGLDILKVGDyeiasrayigrfnfkgqdqqKRVGELSGGE 449
Cdd:PRK13409 399 ELKISYKpqyikpdydGTVEDLLRSITDdlgssyYKSEIIKPLQLERLLD--------------------KNVKDLSGGE 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 450 RNRLQLAKILQQGANVILLDEPSNDLDIE----TLRALEDAILVFPGTVMVVSHDRWFLDRIATHILSFENE 517
Cdd:PRK13409 459 LQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEGE 530
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-191 |
1.88e-33 |
|
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: 124.30 E-value: 1.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFSGEARAQPGIKIGYLEQEPPLDPTKDVRGNV 90
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLlsptegtilldGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 91 EDGVRealdalerldqvfaeyadpdadfdalakeqeklesiIHAWDAHNLNNQLEIAADALNLPAWDADV-----TKLSG 165
Cdd:pfam00005 81 RLGLL------------------------------------LKGLSKREKDARAEEALEKLGLGDLADRPvgerpGTLSG 124
|
170 180
....*....|....*....|....*.
gi 491208697 166 GERRRVALCRLLLSKPDMLLLDEPTN 191
Cdd:pfam00005 125 GQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-236 |
3.08e-33 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 126.04 E-value: 3.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEaraqpgikIGYLEQEPPLDPTKDVRGNVedGVrea 97
Cdd:cd03225 13 ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGE--------VLVDGKDLTKLSLKELRRKV--GL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 98 ldalerldqVFAeyaDPDADF-------D-ALAKEQEKLesiihawDAHNLNNQLEIAADALNLPAW-DADVTKLSGGER 168
Cdd:cd03225 80 ---------VFQ---NPDDQFfgptveeEvAFGLENLGL-------PEEEIEERVEEALELVGLEGLrDRSPFTLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491208697 169 RRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHDRYFLDNVAEWILELDRGH 236
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
325-512 |
6.40e-33 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 124.08 E-value: 6.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV----------KVAYVGQ 393
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLdGKDLaslspkelarKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 394 IrdtldnnktvweevsggLDILKVGDYEiasrayigrfnfkgqdqQKRVGELSGGERNRLQLAKILQQGANVILLDEPSN 473
Cdd:cd03214 81 A-----------------LELLGLAHLA-----------------DRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491208697 474 DLDI-------ETLRALEDAilvFPGTVMVVSHDRWFLDRIATHIL 512
Cdd:cd03214 127 HLDIahqiellELLRRLARE---RGKTVVMVLHDLNLAARYADRVI 169
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
325-516 |
9.45e-33 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 124.50 E-value: 9.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGR---VLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVKVAYVGQIRDT--- 397
Cdd:cd03225 1 ELKNLSFSYPDGarpAL-DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLTKLSLKELRRKvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 -LDN------NKTVWEEVSGGLDILKVGDYEIASRA--YIGRFNFKGQdQQKRVGELSGGERNRLQLAKILQQGANVILL 468
Cdd:cd03225 80 vFQNpddqffGPTVEEEVAFGLENLGLPEEEIEERVeeALELVGLEGL-RDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491208697 469 DEPSNDLDIETLRALEDAILVFPG---TVMVVSHDRWFLDRIATHILSFEN 516
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
323-500 |
2.51e-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: 123.36 E-value: 2.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK---------VAYVG 392
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWnGEPIRdaredyrrrLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 393 QiRDTLDNNKTVWEEVSGGLDILKVGDYEIASRAYIGRFNFKGQdQQKRVGELSGGERNRLQLAKILQQGANVILLDEPS 472
Cdd:COG4133 82 H-ADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|.
gi 491208697 473 NDLDIETLRALEDAILVFP---GTVMVVSHD 500
Cdd:COG4133 160 TALDAAGVALLAELIAAHLargGAVLLTTHQ 190
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-274 |
2.60e-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: 124.20 E-value: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGI-----------KIGYLEQEPPLDPTKDV 86
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID-GEdvrkeprearrQIGVLPDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 RGNVEdgvrealdalerldqVFAE-YADPDADFdalakeQEKLESIIHAwdahnlnNQLEIAADALnlpawdadVTKLSG 165
Cdd:COG4555 92 RENIR---------------YFAElYGLFDEEL------KKRIEELIEL-------LGLEEFLDRR--------VGELST 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 166 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDF---PGTIVAITHDRYFLDNVAEWILELDRGHgIPYQG 242
Cdd:COG4555 136 GMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGK-VVAQG 214
|
250 260 270
....*....|....*....|....*....|..
gi 491208697 243 NYSSWLEQKNarleqEQKQEESFAKALKKELE 274
Cdd:COG4555 215 SLDELREEIG-----EENLEDAFVALIGSEEG 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-517 |
5.50e-32 |
|
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: 130.29 E-value: 5.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 31 PGAKIGVLGLNGAGKSTLLRIMAG------------VDKD-----FSG-----------EARAQPGIKIGYLEQEPpldp 82
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGelkpnlgdydeePSWDevlkrFRGtelqdyfkklaNGEIKVAHKPQYVDLIP---- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 83 tKDVRGNVEDgvrealdALERLDqvfaeyadpdadfdalakEQEKLESIIhawdahnlnnqleiaaDALNL-PAWDADVT 161
Cdd:COG1245 174 -KVFKGTVRE-------LLEKVD------------------ERGKLDELA----------------EKLGLeNILDRDIS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVSWLERFLKDFPGTIVAITHDRYFLDNVAEWIleldrgH-- 236
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYqrlNVARLIRELAEEGKYVLVVEHDLAILDYLADYV------Hil 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 237 -------GI---PYQ-----GNY-SSWLEQKNARleqeqkqeesfakalkkelewVRSNAKgqqkknkarmeRFEELNSK 300
Cdd:COG1245 286 ygepgvyGVvskPKSvrvgiNQYlDGYLPEENVR---------------------IRDEPI-----------EFEVHAPR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 301 EFQQRNEtseiyippgprlgnkVVEVEGISKSFDGRVLyenlsfTVPPTAI-----VGIVGPNGAGKTTLFRMMTGEQQP 375
Cdd:COG1245 334 REKEEET---------------LVEYPDLTKSYGGFSL------EVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 376 DTGTVTlgESVKVAYVGQ-IRDtlDNNKTVwEEVSGGLDILKVGD----YEIASRAYIGRFnfkgqdQQKRVGELSGGER 450
Cdd:COG1245 393 DEGEVD--EDLKISYKPQyISP--DYDGTV-EEFLRSANTDDFGSsyykTEIIKPLGLEKL------LDKNVKDLSGGEL 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491208697 451 NRLQLAKILQQGANVILLDEPSNDLDIE----TLRALEDAILVFPGTVMVVSHDRWFLDRIATHILSFENE 517
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEGE 532
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
339-473 |
1.19e-31 |
|
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: 119.29 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 339 YENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLG-----------ESVKVAYVGQiRDTLDNNKTVWEE 407
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQ-DPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491208697 408 VSGGLDILKVGDYEIASRAYIGRFNFKGQDQQKRV-----GELSGGERNRLQLAKILQQGANVILLDEPSN 473
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
19-253 |
2.80e-31 |
|
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: 127.96 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD-KDFSGEARAQpgiKIGYLEQEPPL-DPT 83
Cdd:COG4987 348 RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLrfldpqsgsitlgGVDlRDLDEDDLRR---RIAVVPQRPHLfDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 84 kdVRGNVedgvrealdaleRLdqvfaeyADPDADFDALakeqeklesiihaWDAhnLNnQLEIAADALNLPA-WDADV-- 160
Cdd:COG4987 425 --LRENL------------RL-------ARPDATDEEL-------------WAA--LE-RVGLGDWLAALPDgLDTWLge 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 161 --TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV-SWLERFLKDFPG-TIVAITHDRYFLDNVAEwILELDRGH 236
Cdd:COG4987 468 ggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEqALLADLLEALAGrTVLLITHRLAGLERMDR-ILVLEDGR 546
|
250
....*....|....*..
gi 491208697 237 GIPyQGNYSSWLEQKNA 253
Cdd:COG4987 547 IVE-QGTHEELLAQNGR 562
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
324-512 |
3.77e-31 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 118.65 E-value: 3.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVT-LGESV---------KVAYVGQ 393
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvLGKDIkkepeevkrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 394 IrDTLDNNKTVWEevsggldilkvgdyeiasraYIgrfnfkgqdqqkrvgELSGGERNRLQLAKILQQGANVILLDEPSN 473
Cdd:cd03230 81 E-PSLYENLTVRE--------------------NL---------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491208697 474 DLDIETLRALEDAI--LVFPG-TVMVVSHDRWFLDRIATHIL 512
Cdd:cd03230 125 GLDPESRREFWELLreLKKEGkTILLSSHILEEAERLCDRVA 166
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-236 |
1.67e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.42 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR------AQPGIKIGYLEQEPPLDPT-----KDV 86
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQRAEVDWDfpitvRDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 rgnVEDGVREALDALERLDQvfaeyADPDADFDALAkeqeklesiihawdahnlnnQLEIAADAlnlpawDADVTKLSGG 166
Cdd:COG1121 98 ---VLMGRYGRRGLFRRPSR-----ADREAVDEALE--------------------RVGLEDLA------DRPIGELSGG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491208697 167 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHDRYFLDNVAEWILELDRGH 236
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGL 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
324-508 |
2.00e-30 |
|
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: 118.01 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV--------KVAYVGQi 394
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVtgvpperrNIGMVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 RDTLDNNKTVWEEVSGGLDILKVGDYEIASRA--YIGRFNFKGQdQQKRVGELSGGERNRLQLAKILQQGANVILLDEPS 472
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVreLLELVGLEGL-LNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491208697 473 NDLDIET---LRALEDAILVFPG-TVMVVSHDR----WFLDRIA 508
Cdd:cd03259 159 SALDAKLreeLREELKELQRELGiTTIYVTHDQeealALADRIA 202
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
17-218 |
2.05e-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: 119.38 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------------ARAQpgiKIGYLEQEPPLDP 82
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvlldgrdlaslsrrELAR---RIAYVPQEPPAPF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 83 TKDVRGNVEDGVREALDALERLDQvfaeyADPDADFDALAkeqeklesiihawdahnlnnQLEIAADAlnlpawDADVTK 162
Cdd:COG1120 89 GLTVRELVALGRYPHLGLFGRPSA-----EDREAVEEALE--------------------RTGLEHLA------DRPVDE 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 163 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHD 218
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARERGRTVVMVLHD 197
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-236 |
2.93e-30 |
|
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: 118.20 E-value: 2.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIGYleqepplDPTKDVRGNVedGVr 95
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-GKDITK-------KNLRELRRKV--GL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 96 ealdalerldqVFAeyaDPDADF-------D------ALAKEQEKLESIIHAwdahnlnnqleiAADALNLPAW-DADVT 161
Cdd:COG1122 80 -----------VFQ---NPDDQLfaptveeDvafgpeNLGLPREEIRERVEE------------ALELVGLEHLaDRPPH 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHDRYFLDNVAEWILELDRGH 236
Cdd:COG1122 134 ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
325-516 |
5.17e-30 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 115.03 E-value: 5.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLgesvkvayvgqirdtldnnktv 404
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 405 weevsGGLDILKVGDYEIasRAYIGrfnfkgqdqqkRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALE 484
Cdd:cd00267 59 -----DGKDIAKLPLEEL--RRRIG-----------YVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 491208697 485 DAI--LVFPG-TVMVVSHDRWFLDRIATHILSFEN 516
Cdd:cd00267 121 ELLreLAEEGrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
324-516 |
1.83e-29 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 115.89 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSF-DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVKVAYVGQIRDTL--- 398
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDITKKNLRELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 399 ----DN---NKTVWEEVSGGLDILKVGDYEIASRA--YIGRFNFKGQdQQKRVGELSGGERNRLQLAKILQQGANVILLD 469
Cdd:COG1122 81 fqnpDDqlfAPTVEEDVAFGPENLGLPREEIRERVeeALELVGLEHL-ADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491208697 470 EPSNDLDIETLRALEDAILVFPG---TVMVVSHDRWFLDRIATHILSFEN 516
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
336-539 |
5.98e-29 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 121.43 E-value: 5.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 336 RVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQIRDTLD---------------- 399
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPqpaleyvidgdreyrq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 400 -----------NNKTVWEEVSGGLDILKVgdYEIASRA--YIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVI 466
Cdd:PRK10636 94 leaqlhdanerNDGHAIATIHGKLDAIDA--WTIRSRAasLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491208697 467 LLDEPSNDLDIETLRALEDAILVFPGTVMVVSHDRWFLDRIATHILSFENEQPEFYTGNYAEYEAYRQSRLGE 539
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQ 244
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-236 |
7.44e-29 |
|
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: 112.49 E-value: 7.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEA--------RAQPGIK--IGYLEQEPPLDPTKDVR 87
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdikKEPEEVKrrIGYLPEEPSLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNVedgvrealdalerldqvfaeyadpdadfdalakeqeklesiihawdahnlnnqleiaadalnlpawdadvtKLSGGE 167
Cdd:cd03230 92 ENL-----------------------------------------------------------------------KLSGGM 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 168 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDF---PGTIVAITHDRYFLDNVAEWILELDRGH 236
Cdd:cd03230 101 KQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
18-236 |
8.06e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 114.39 E-value: 8.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR--------AQPGIK--IGYLEQEPPLDP--Tkd 85
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvarDPAEVRrrIGYVPQEPALYPdlT-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 86 vrgnvedgVREALDALERLdqvfaeYADPDADFDALAKEqeklesiihawdahnlnnqleiAADALNL-PAWDADVTKLS 164
Cdd:COG1131 90 --------VRENLRFFARL------YGLPRKEARERIDE----------------------LLELFGLtDAADRKVGTLS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 165 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHDRYFLDNVAEWILELDRGH 236
Cdd:COG1131 134 GGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-259 |
3.21e-28 |
|
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: 119.55 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEA---------------RAQpgikIGYLEQEPPL 80
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqidpaslRRQ----IGVVLQDVFL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 81 dptkdVRGNVEDGVRealdalerldqvfaeYADPDADFDAlakeqeklesIIHAwdahnlnnqLEIAA---DALNLPA-W 156
Cdd:COG2274 561 -----FSGTIRENIT---------------LGDPDATDEE----------IIEA---------ARLAGlhdFIEALPMgY 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 157 DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG--TIVAITHDRYFLDNvAEWIL 230
Cdd:COG2274 602 DTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-ADRII 680
|
250 260 270
....*....|....*....|....*....|.
gi 491208697 231 ELDRGHgIPYQGNYSSWLEQKN--ARLEQEQ 259
Cdd:COG2274 681 VLDKGR-IVEDGTHEELLARKGlyAELVQQQ 710
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-508 |
4.32e-28 |
|
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: 117.98 E-value: 4.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVD--KDFSGEARAQPGI--KIGYLE-QEPPLDPTKDVRGNVEdgv 94
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHVALceKCGYVErPSKVGEPCPVCGGTLE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 95 REALDALERLDQVFAEYADPDA-----DFdALAKEQEKLESIIHAWD--AHNLNNQLEIAADALNLPAWDADVT----KL 163
Cdd:TIGR03269 91 PEEVDFWNLSDKLRRRIRKRIAimlqrTF-ALYGDDTVLDNVLEALEeiGYEGKEAVGRAVDLIEMVQLSHRIThiarDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 164 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV----SWLERFLKDFPGTIVAITHDRYFLDNVAEwileldrghgip 239
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSD------------ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 240 yqgnYSSWLEqkNARLEQEQKQEESFAKAlkkelewvrsnakgqqkknkarMERFEELnskefqQRNETSEIyippgprl 319
Cdd:TIGR03269 238 ----KAIWLE--NGEIKEEGTPDEVVAVF----------------------MEGVSEV------EKECEVEV-------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 320 GNKVVEVEGISK---SFDGRVL--YENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTV-------------- 380
Cdd:TIGR03269 276 GEPIIKVRNVSKryiSVDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkp 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 381 -TLGESVKVAYVGQIRD--TLDNNKTVWEEVSG--GLDILKvgdyEIASRAYIGRFNFKGQDQQKRVG-------ELSGG 448
Cdd:TIGR03269 356 gPDGRGRAKRYIGILHQeyDLYPHRTVLDNLTEaiGLELPD----ELARMKAVITLKMVGFDEEKAEEildkypdELSEG 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 449 ERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAIL----VFPGTVMVVSHDRWFL----DRIA 508
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkareEMEQTFIIVSHDMDFVldvcDRAA 499
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
332-500 |
5.47e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.79 E-value: 5.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 332 SFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQ---IRDTLDnnKTVWEEV 408
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrseVPDSLP--LTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 409 S-------GGLDILKVGDYEIASRAY--IGRFNFKGQdqqkRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIET 479
Cdd:NF040873 79 AmgrwarrGLWRRLTRDDRAAVDDALerVGLADLAGR----QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180
....*....|....*....|....
gi 491208697 480 LRALEDAILVFPG---TVMVVSHD 500
Cdd:NF040873 155 RERIIALLAEEHArgaTVVVVTHD 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
324-500 |
9.09e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 111.02 E-value: 9.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGR-----VLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK-----VAYVG 392
Cdd:cd03293 1 LEVRNVSKTYGGGggavtAL-EDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdGEPVTgpgpdRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 393 QiRDTLDNNKTVWEEVSGGLDILKVGDYEIASRA--YIGRFNFKGQdQQKRVGELSGGERNRLQLAKILQQGANVILLDE 470
Cdd:cd03293 80 Q-QDALLPWLTVLDNVALGLELQGVPKAEARERAeeLLELVGLSGF-ENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190
....*....|....*....|....*....|....
gi 491208697 471 PSNDLDIETLRALEDAILV----FPGTVMVVSHD 500
Cdd:cd03293 158 PFSALDALTREQLQEELLDiwreTGKTVLLVTHD 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
17-218 |
1.26e-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: 109.06 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------------ARAQpgiKIGYLEQeppldp 82
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEilldgkdlaslspkELAR---KIAYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 83 tkdvrgnvedgvrealdALERLDqvfaeyadpdadFDALAkeqeklesiihawdahnlnnqleiaadalnlpawDADVTK 162
Cdd:cd03214 81 -----------------ALELLG------------LAHLA----------------------------------DRPFNE 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 163 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHD 218
Cdd:cd03214 98 LSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIELLELLRRLARERGKTVVMVLHD 157
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
324-511 |
2.05e-27 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 109.90 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLY--ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK---------VAYV 391
Cdd:cd03263 1 LQIRNLTKTYKKGTKPavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYInGYSIRtdrkaarqsLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 392 GQiRDTLDNNKTVWE--EVSGGLDILKVGDYEIASRAYIGRFNFKgQDQQKRVGELSGGERNRLQLAKILQQGANVILLD 469
Cdd:cd03263 81 PQ-FDALFDELTVREhlRFYARLKGLPKSEIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491208697 470 EPSNDLDIETLRALEDAIL-VFPG-TVMVVSHDRWFLDRIATHI 511
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILeVRKGrSIILTTHSMDEAEALCDRI 202
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-235 |
2.63e-27 |
|
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: 109.55 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR------AQPGIKIGYLEQEPPLDPtkDVRGNVED 92
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSIDR--DFPISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 93 GVREALDALERLdqvfaeyadpdadFDALAKEQEKLesIIHAwdahnlnnqLEiAADALNLpaWDADVTKLSGGERRRVA 172
Cdd:cd03235 90 VVLMGLYGHKGL-------------FRRLSKADKAK--VDEA---------LE-RVGLSEL--ADRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 173 LCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHDRYFLDNVAEWILELDRG 235
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
17-236 |
3.13e-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: 107.33 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARaqpgikigYLEQEPPLDPTKDVRGNVedgvre 96
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL--------IDGKDIAKLPLEELRRRI------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 97 aldalerldqvfaeyadpdadfdalakeqekleSIIHawdahnlnnQLeiaadalnlpawdadvtklSGGERRRVALCRL 176
Cdd:cd00267 76 ---------------------------------GYVP---------QL-------------------SGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491208697 177 LLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHDRYFLDNVAEWILELDRGH 236
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
19-218 |
1.56e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 108.64 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR------AQPGIKIGYLEQEPPLDPTKDVRGNVED 92
Cdd:COG1116 24 VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvTGPGPDRGVVFQEPALLPWLTVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 93 GVREA-LDALERLDQVfAEYadpdadfdalakeqekLESIihawdahnlnnQLEIAADAlnLPAwdadvtKLSGGERRRV 171
Cdd:COG1116 104 GLELRgVPKAERRERA-REL----------------LELV-----------GLAGFEDA--YPH------QLSGGMRQRV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491208697 172 ALCRLLLSKPDMLLLDEPTNHLDA---ESV-SWLERFLKDFPGTIVAITHD 218
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDAltrERLqDELLRLWQETGKTVLFVTHD 198
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
325-500 |
3.46e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.51 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGesvkvayvGQIRDTLDNNK-- 402
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLN--------GRPLAAWSPWEla 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 403 ----------------TVWEEVSGGLdilkvgdyeiasrayIGRFNFKGQDQQ------KRVG----------ELSGGER 450
Cdd:COG4559 75 rrravlpqhsslafpfTVEEVVALGR---------------APHGSSAAQDRQivrealALVGlahlagrsyqTLSGGEQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 451 NRLQLAKILQQ-------GANVILLDEPSNDLDI-------ETLRALEDAilvfPGTVMVVSHD 500
Cdd:COG4559 140 QRVQLARVLAQlwepvdgGPRWLFLDEPTSALDLahqhavlRLARQLARR----GGGVVAVLHD 199
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
323-500 |
3.50e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 107.48 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSF----DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK-----VAYVG 392
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdGKPVTgpgpdRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 393 QiRDTLDNNKTVWEEVSGGLDILKVGDYEIASRA--YIGRFNFKGqDQQKRVGELSGGERNRLQLAKILQQGANVILLDE 470
Cdd:COG1116 87 Q-EPALLPWLTVLDNVALGLELRGVPKAERRERAreLLELVGLAG-FEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190
....*....|....*....|....*....|....
gi 491208697 471 PSNDLDIETLRALEDAIL----VFPGTVMVVSHD 500
Cdd:COG1116 165 PFGALDALTRERLQDELLrlwqETGKTVLFVTHD 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-311 |
4.55e-26 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 112.35 E-value: 4.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGIKIGYLEQ-EPPLDPTKDVRGNVEDGvr 95
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQhRAELDPEKTVMDNLAEG-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 96 ealdalerldqvfaeyadpdadfdalakeqeKLESIIHAWDAHNLnNQLEiaaDALNLPAWD-ADVTKLSGGERRRVALC 174
Cdd:PRK11147 408 -------------------------------KQEVMVNGRPRHVL-GYLQ---DFLFHPKRAmTPVKALSGGERNRLLLA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 175 RLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITHDRYFLDNVAE--WILELDrGHGIPYQGNYSSWLEQKN 252
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTecWIFEGN-GKIGRYVGGYHDARQQQA 531
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 253 ARLEQEQK-QEESFAKALKKELEWVRSNAKGQQKKNK------ARMERFE--------ELNSKEF--QQRNETSEI 311
Cdd:PRK11147 532 QYLALKQPaVKKKEEAAAPKAETVKRSSKKLSYKLQReleqlpQLLEDLEaeiealqaQVADADFfsQPHEQTQKV 607
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-251 |
5.26e-26 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 111.52 E-value: 5.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGIKIGYLEQeppldptkdvrgnvedgvrea 97
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQ--------------------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 98 ldalerldqvfaeyaDPDADFDalakEQEKLESIIHAWDAHNLNNQ--------LEIAADALNLPawdadVTKLSGGERR 169
Cdd:PRK15064 390 ---------------DHAYDFE----NDLTLFDWMSQWRQEGDDEQavrgtlgrLLFSQDDIKKS-----VKVLSGGEKG 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 170 RVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGHGIPYQGNYSSWLE 249
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLR 525
|
..
gi 491208697 250 QK 251
Cdd:PRK15064 526 SQ 527
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
325-512 |
5.98e-26 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 106.37 E-value: 5.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV------KVAYVGQIRdT 397
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFdGEDItglpphEIARLGIGR-T 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 LDNNK-----TVWEEV--------SGGLDILKVGDYEIASRAYIGRF-NFKG-QDQQKR-VGELSGGERNRLQLAKILQQ 461
Cdd:cd03219 81 FQIPRlfpelTVLENVmvaaqartGSGLLLARARREEREARERAEELlERVGlADLADRpAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 462 GANVILLDEP--------SNDLdIETLRALEDAILvfpgTVMVVSHDRWFLDRIATHIL 512
Cdd:cd03219 161 DPKLLLLDEPaaglnpeeTEEL-AELIRELRERGI----TVLLVEHDMDVVMSLADRVT 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
325-512 |
6.98e-26 |
|
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: 106.66 E-value: 6.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV------KVAYVGQIRdT 397
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFdGRDItglpphRIARLGIAR-T 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 LDNNK-----TVWEEV-------------SGGLDILKVGDYEIASRA----YIGRFNFKGQdQQKRVGELSGGERNRLQL 455
Cdd:COG0411 85 FQNPRlfpelTVLENVlvaaharlgrgllAALLRLPRARREEREAREraeeLLERVGLADR-ADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 456 AKILQQGANVILLDEP--------SNDLdIETLRALEDAILVfpgTVMVVSHDRWFLDRIATHIL 512
Cdd:COG0411 164 ARALATEPKLLLLDEPaaglnpeeTEEL-AELIRRLRDERGI---TILLIEHDMDLVMGLADRIV 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
294-528 |
2.59e-25 |
|
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: 109.85 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 294 FEELNSKEFQQRNETSEIyippgPRLGNKVVEVEGISKSF-DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGE 372
Cdd:COG4988 312 FALLDAPEPAAPAGTAPL-----PAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 373 QQPDTGTVTL-GESV----------KVAYVGQ--------IRD--TLDNNKTVWEEVsggldilkvgdYEIASRAYIGRF 431
Cdd:COG4988 387 LPPYSGSILInGVDLsdldpaswrrQIAWVPQnpylfagtIREnlRLGRPDASDEEL-----------EAALEAAGLDEF 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 432 nFKGQDQ--QKRVGE----LSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAIL-VFPG-TVMVVSHdRWF 503
Cdd:COG4988 456 -VAALPDglDTPLGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRrLAKGrTVILITH-RLA 533
|
250 260
....*....|....*....|....*
gi 491208697 504 LDRIATHILSFENEQPEFyTGNYAE 528
Cdd:COG4988 534 LLAQADRILVLDDGRIVE-QGTHEE 557
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-251 |
3.94e-25 |
|
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: 109.46 E-value: 3.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE-----------ARAQPGIKIGYLEQEPPLdPTK 84
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSilingvdlsdlDPASWRRQIAWVPQNPYL-FAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 85 DVRGNVedgvrealdaleRLdqvfaeyADPDADFDALAK--EQEKLESIIHAwdahnLNNQLE--IAADALNLpawdadv 160
Cdd:COG4988 426 TIRENL------------RL-------GRPDASDEELEAalEAAGLDEFVAA-----LPDGLDtpLGEGGRGL------- 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 161 tklSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG--TIVAITHDRYFLDNvAEWILELDRGHgI 238
Cdd:COG4988 475 ---SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALLAQ-ADRILVLDDGR-I 549
|
250
....*....|...
gi 491208697 239 PYQGNYSSWLEQK 251
Cdd:COG4988 550 VEQGTHEELLAKN 562
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
323-508 |
8.02e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.70 E-value: 8.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLG----ESVKVAYVGQIRDTL 398
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNgrplADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 399 DNNK------TVWEEVSGGLDIL----------------KVGDYEIASRAYIgrfnfkgqdqqkrvgELSGGERNRLQLA 456
Cdd:PRK13548 82 PQHSslsfpfTVEEVVAMGRAPHglsraeddalvaaalaQVDLAHLAGRDYP---------------QLSGGEQQRVQLA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 457 KILQQ------GANVILLDEPSNDLDI----ETLRALEDAILVFPGTVMVVSHD-----RWfLDRIA 508
Cdd:PRK13548 147 RVLAQlwepdgPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHDlnlaaRY-ADRIV 212
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
19-235 |
8.25e-25 |
|
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: 103.74 E-value: 8.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------DFSGE--------ARAQpgiKIGYLEQEPPLDPTK 84
Cdd:TIGR03873 14 RLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRpdagtvDLAGVdlhglsrrARAR---RVALVEQDSDTAVPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 85 DVRGNVedgvrealdALERLDQVFAEYADPDADfDALAKEQeklesiihawdahnlnnqleIAADALNLPAwDADVTKLS 164
Cdd:TIGR03873 91 TVRDVV---------ALGRIPHRSLWAGDSPHD-AAVVDRA--------------------LARTELSHLA-DRDMSTLS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 165 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHDRYFLDNVAEWILELDRG 235
Cdd:TIGR03873 140 GGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVLDGG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
323-511 |
8.55e-25 |
|
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: 103.14 E-value: 8.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVT-LGESVkvayVGQIRDTLD-- 399
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvDGQDI----TGLSEKELYel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 400 --------------NNKTVWEEVSGGLDIL-KVGDYEIASRA--YIGRFNFKGqDQQKRVGELSGGERNRLQLAK--ILQ 460
Cdd:COG1127 81 rrrigmlfqggalfDSLTVFENVAFPLREHtDLSEAEIRELVleKLELVGLPG-AADKMPSELSGGMRKRVALARalALD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 461 qgANVILLDEPSNDLDIETLRALEDAIL----VFPGTVMVVSHDRWFLDRIATHI 511
Cdd:COG1127 160 --PEILLYDEPTAGLDPITSAVIDELIRelrdELGLTSVVVTHDLDSAFAIADRV 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
18-236 |
9.42e-25 |
|
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: 102.18 E-value: 9.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEA------------------RAQpgiKIGYLEQEPP 79
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklsekelaafRRR---HIGFVFQSFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 80 LDPTKDVRGNVEdgvrealdalerLDQVFAEyadpdaDFDALAKEQeklesiihawdAHNLNNQLEIAADALNLPAwdad 159
Cdd:cd03255 93 LLPDLTALENVE------------LPLLLAG------VPKKERRER-----------AEELLERVGLGDRLNHYPS---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 160 vtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDFPGTIVAITHDRyFLDNVAEWILELDRG 235
Cdd:cd03255 140 --ELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDG 216
|
.
gi 491208697 236 H 236
Cdd:cd03255 217 K 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-236 |
1.01e-24 |
|
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: 102.96 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEaraqpgikIGYLEQEPPLDPTKDVRGNVE----DG 93
Cdd:COG1124 17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGE--------VTFDGRPVTRRRRKAFRRRVQmvfqDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 94 vREALDALERLDQVFAEyadpdadfdALAkeqeklesiihawdAHNLNNQLEIAADALNLPAWDADVTK-----LSGGER 168
Cdd:COG1124 89 -YASLHPRHTVDRILAE---------PLR--------------IHGLPDREERIAELLEQVGLPPSFLDryphqLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 169 RRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGH 236
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDvsvqAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGR 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
324-516 |
1.09e-24 |
|
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: 100.54 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGR---VLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLG---------ESV--KVA 389
Cdd:cd03228 1 IEFKNVSFSYPGRpkpVL-KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDgvdlrdldlESLrkNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 390 YVGQirDTLDNNKTVWEEVsggldilkvgdyeiasrayigrfnfkgqdqqkrvgeLSGGERNRLQLAKILQQGANVILLD 469
Cdd:cd03228 80 YVPQ--DPFLFSGTIRENI------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491208697 470 EPSNDLDIETLRALEDAILVFPG--TVMVVSHdRWFLDRIATHILSFEN 516
Cdd:cd03228 122 EATSALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDD 169
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
325-518 |
1.12e-24 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 101.56 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSF-DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV--------KVAYVGQIR 395
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikakerrkSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 396 DTLDNNKTVWEEVSGGLDILkvGDYEIASRAYIGRFN-FKGQDQQKRvgELSGGERNRLQLAKILQQGANVILLDEPSND 474
Cdd:cd03226 81 DYQLFTDSVREELLLGLKEL--DAGNEQAETVLKDLDlYALKERHPL--SLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491208697 475 LDIETLRALEDAILVFPG---TVMVVSHDRWFLDRIATHILSFENEQ 518
Cdd:cd03226 157 LDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
324-511 |
1.62e-24 |
|
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: 101.52 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVT-LGESVK-----VAYVGQIRD- 396
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfDGKSYQknieaLRRIGALIEa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 397 -TLDNNKTVWEEVSGGLDILKVGDYEIASraYIGRFNFKgQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDL 475
Cdd:cd03268 81 pGFYPNLTARENLRLLARLLGIRKKRIDE--VLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 491208697 476 DIETLRALEDAILVFP---GTVMVVSHDRWFLDRIATHI 511
Cdd:cd03268 158 DPDGIKELRELILSLRdqgITVLISSHLLSEIQKVADRI 196
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
20-218 |
5.17e-24 |
|
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: 100.24 E-value: 5.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR------AQPGIKIGYLEQEPPLDPTKDVRGNVEDG 93
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYVFQQDALLPWLTVLDNVALG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 94 VR----EALDALERLDQVFAEYadpdadfdalakeqeKLESIIHAWdahnlnnqleiaadalnlPAwdadvtKLSGGERR 169
Cdd:cd03293 98 LElqgvPKAEARERAEELLELV---------------GLSGFENAY------------------PH------QLSGGMRQ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491208697 170 RVALCRLLLSKPDMLLLDEPTNHLDA---ESV-SWLERFLKDFPGTIVAITHD 218
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDAltrEQLqEELLDIWRETGKTVLLVTHD 191
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-236 |
9.72e-24 |
|
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: 97.84 E-value: 9.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGI------------KIGYLEQEPPLdptkdv 86
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID-GVdlrdldleslrkNIAYVPQDPFL------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 rgnvedgvrealdalerldqvfaeyadpdadFDAlakeqekleSIihawdAHNLnnqleiaadalnlpawdadvtkLSGG 166
Cdd:cd03228 88 -------------------------------FSG---------TI-----RENI----------------------LSGG 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 167 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG--TIVAITHdRYFLDNVAEWILELDRGH 236
Cdd:cd03228 101 QRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-237 |
1.17e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.89 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGIKIGYLEQEP--PLdptkdvrGNVedg 93
Cdd:COG4178 373 PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPylPL-------GTL--- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 94 vREALDalerldqvfaeYADPDADFDalakeQEKLESIIHAWDAHNLNNQLEIAADalnlpaWDAdvtKLSGGERRRVAL 173
Cdd:COG4178 443 -REALL-----------YPATAEAFS-----DAELREALEAVGLGHLAERLDEEAD------WDQ---VLSLGEQQRLAF 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 174 CRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKD-FPG-TIVAITHdRYFLDNVAEWILELDRGHG 237
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPGtTVISVGH-RSTLAAFHDRVLELTGDGS 561
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
315-516 |
1.21e-23 |
|
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: 104.85 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 315 PGPRLGNKVVEVEGISKSFDGR---VLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK--- 387
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYPGAgrpVL-DGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLgGVDLRdld 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 388 -------VAYVGQ----IRDTLDNNktvweevsggldiLKVGD--------YEIASRAYIGRFnFKGQDQ--QKRVGE-- 444
Cdd:COG4987 404 eddlrrrIAVVPQrphlFDTTLREN-------------LRLARpdatdeelWAALERVGLGDW-LAALPDglDTWLGEgg 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 445 --LSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAIL-VFPG-TVMVVSHDRWFLDRiATHILSFEN 516
Cdd:COG4987 470 rrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLeALAGrTVLLITHRLAGLER-MDRILVLED 544
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
324-501 |
1.78e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 101.76 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV----------KVAYVGQ 393
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlftnlpprerRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 394 irdtldN-----NKTVWEEVSGGLDILKVGDYEIASRAyigrfnfkgQDQQKRVG----------ELSGGERNRLQLAKI 458
Cdd:COG1118 83 ------HyalfpHMTVAENIAFGLRVRPPSKAEIRARV---------EELLELVQlegladrypsQLSGGQRQRVALARA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491208697 459 LQQGANVILLDEPSNDLDIET-------LRALEDAilvFPGTVMVVSHDR 501
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVrkelrrwLRRLHDE---LGGTTVFVTHDQ 194
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
351-525 |
3.93e-23 |
|
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: 98.63 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 351 IVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLgESVKVAYVGQiRDTLDNNKTVWEEVSGGLDILKVGDY---EIASRAY 427
Cdd:cd03237 27 VIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQ-YIKADYEGTVRDLLSSITKDFYTHPYfktEIAKPLQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 428 IGRFnfkgQDQQkrVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIE----TLRALEDAILVFPGTVMVVSHDRWF 503
Cdd:cd03237 105 IEQI----LDRE--VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKVIRRFAENNEKTAFVVEHDIIM 178
|
170 180
....*....|....*....|..
gi 491208697 504 LDRIATHILSFENEQPEFYTGN 525
Cdd:cd03237 179 IDYLADRLIVFEGEPSVNGVAN 200
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
324-500 |
4.24e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 98.62 E-value: 4.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV----------KVAYVG 392
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVdGLDVattpsrelakRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 393 QirdtlDNNK----TVWEEV-------SGGLdiLKVGDYEIASRAyIGRFNFkgQD-QQKRVGELSGGERNRLQLAKILQ 460
Cdd:COG4604 82 Q-----ENHInsrlTVRELVafgrfpySKGR--LTAEDREIIDEA-IAYLDL--EDlADRYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491208697 461 QGANVILLDEPSNDLDI----ETLRALEDAILVFPGTVMVVSHD 500
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-235 |
5.99e-23 |
|
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: 96.94 E-value: 5.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------ARAQPGIKIGYLEQEPplDP---TK 84
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSillngkpiKAKERRKSIGYVMQDV--DYqlfTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 85 DVRGNVEDGVREALDALERLDQVFAEYAdpdadfdaLAKEQEKlesiiHAWDahnlnnqleiaadalnlpawdadvtkLS 164
Cdd:cd03226 88 SVREELLLGLKELDAGNEQAETVLKDLD--------LYALKER-----HPLS--------------------------LS 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 165 GGERRRVALCRLLLSKPDMLLLDEPTNHLDA---ESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRG 235
Cdd:cd03226 129 GGQKQRLAIAAALLSGKDLLIFDEPTSGLDYknmERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-292 |
6.59e-23 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 102.94 E-value: 6.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGIKIGYLEQEPpldptkdvrgnvedgvREAL 98
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQ----------------LEFL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 99 DALERLDQVFAEYADpdadfdalaKEQEKlesiihawdahnlnnQLEiaaDALNLPAWDAD-VT----KLSGGERRRVAL 173
Cdd:PRK10636 389 RADESPLQHLARLAP---------QELEQ---------------KLR---DYLGGFGFQGDkVTeetrRFSGGEKARLVL 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 174 CRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGHGIPYQGNysswLEQKNA 253
Cdd:PRK10636 442 ALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGD----LEDYQQ 517
|
250 260 270
....*....|....*....|....*....|....*....
gi 491208697 254 RLEQEQKQEESFAKALKKElewvrSNAKGQQKKNKARME 292
Cdd:PRK10636 518 WLSDVQKQENQTDEAPKEN-----NANSAQARKDQKRRE 551
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
324-512 |
8.45e-23 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 97.19 E-value: 8.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV-------------KVA 389
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdGEDIsglseaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 390 YVGQiRDTLDNNKTVWEEVSGGL-DILKVGDYEIASRA--YIGRFNFKGqDQQKRVGELSGGERNRLQLAKILQQGANVI 466
Cdd:cd03261 81 MLFQ-SGALFDSLTVFENVAFPLrEHTRLSEEEIREIVleKLEAVGLRG-AEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491208697 467 LLDEPSNDLDIETLRALEDAIL----VFPGTVMVVSHDRWFLDRIATHIL 512
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRslkkELGLTSIMVTHDLDTAFAIADRIA 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-218 |
1.42e-22 |
|
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: 95.82 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 30 FPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR--------AQPGI-------KIGYLEQEPPLDPTKDVRGNVEDGV 94
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdSRKKInlppqqrKIGLVFQQYALFPHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 95 REALDAlERLDQVfaeyadpdadfdalakeQEKLesiihawdahnlnnqleiaaDALNL-PAWDADVTKLSGGERRRVAL 173
Cdd:cd03297 101 KRKRNR-EDRISV-----------------DELL--------------------DLLGLdHLLNRYPAQLSGGEKQRVAL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491208697 174 CRLLLSKPDMLLLDEPTNHLDAESVSWLERFL----KDFPGTIVAITHD 218
Cdd:cd03297 143 ARALAAQPELLLLDEPFSALDRALRLQLLPELkqikKNLNIPVIFVTHD 191
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
18-226 |
1.43e-22 |
|
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: 96.42 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------------ARAQPGIKIGYLEQEPP--LD 81
Cdd:cd03257 17 SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSiifdgkdllklsrrLRKIRRKEIQMVFQDPMssLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 82 PTKdvrgNVEDGVREALDALERLDqvfaeyadpdadfdalaKEQEKLESIIhawdahNLNNQLEIAADALN-LPAWdadv 160
Cdd:cd03257 97 PRM----TIGEQIAEPLRIHGKLS-----------------KKEARKEAVL------LLLVGVGLPEEVLNrYPHE---- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 161 tkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKD----FPGTIVAITHD----RYFLDNVA 226
Cdd:cd03257 146 --LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHDlgvvAKIADRVA 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
324-516 |
1.88e-22 |
|
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: 95.63 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDG----RVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV------------ 386
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDIsklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 387 --KVAYVGQiRDTLDNNKTVWEEVSGGLDILKVGDYEIASRAY--IGRFNFkGQDQQKRVGELSGGERNRLQLAKILQQG 462
Cdd:cd03255 81 rrHIGFVFQ-SFNLLPDLTALENVELPLLLAGVPKKERRERAEelLERVGL-GDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 463 ANVILLDEPSNDLDIETLRALEDAILVFPG----TVMVVSHDRwFLDRIATHILSFEN 516
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKeagtTIVVVTHDP-ELAEYADRIIELRD 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
296-499 |
2.60e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 98.36 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 296 ELNSKEFQQRNET-SEIYIPPGPRLGNKVVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQ 374
Cdd:PRK13536 13 RLELSPIERKHQGiSEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 375 PDTGTVT-LGESV---------KVAYVGQIrDTLDNNKTVWEE--VSGGLDILKVGDYE--IASRAYIGRFNFKGqdqQK 440
Cdd:PRK13536 93 PDAGKITvLGVPVpararlaraRIGVVPQF-DNLDLEFTVRENllVFGRYFGMSTREIEavIPSLLEFARLESKA---DA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 441 RVGELSGGERNRLQLAKILQQGANVILLDEPSNDLD-------IETLRALedaiLVFPGTVMVVSH 499
Cdd:PRK13536 169 RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDpharhliWERLRSL----LARGKTILLTTH 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
22-219 |
3.37e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 97.91 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-D-----FSGE---------ARaqpgiKIGYLEQEPPLDPTKDV 86
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETpDsgrivLNGRdlftnlpprER-----RVGFVFQHYALFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 RGNVEDGvreaLDALERldqvfaeyadPDADFDALAKEQekLESIihawdahnlnnQLEIAADALnlPAwdadvtKLSGG 166
Cdd:COG1118 93 AENIAFG----LRVRPP----------SKAEIRARVEEL--LELV-----------QLEGLADRY--PS------QLSGG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 167 ERRRVALCRLLLSKPDMLLLDEPTNHLDAeSV-----SWLERFLKDFPGTIVAITHDR 219
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDA-KVrkelrRWLRRLHDELGGTTVFVTHDQ 194
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
323-488 |
4.74e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 96.72 E-value: 4.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVKVAYVGQI------R 395
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEPLDPEDRRRIgylpeeR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 396 DtLDNNKTVWEEVS--GGLDILKVGDYEIASRAYIGRFNFKGQdQQKRVGELSGGERNRLQLA-------KILqqganvi 466
Cdd:COG4152 81 G-LYPKMKVGEQLVylARLKGLSKAEAKRRADEWLERLGLGDR-ANKKVEELSKGNQQKVQLIaallhdpELL------- 151
|
170 180
....*....|....*....|..
gi 491208697 467 LLDEPSNDLDIETLRALEDAIL 488
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIR 173
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
315-501 |
5.15e-22 |
|
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: 99.67 E-value: 5.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 315 PGPRLGNKVVEVEGISKSFDGR-VLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLG--------ES 385
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNgvpladadAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 386 V---KVAYVGQiRDTLdNNKTVWEEVsgGLDILKVGDYEI---ASRAYIGRF-NFKGQDQQKRVGE----LSGGERNRLQ 454
Cdd:TIGR02857 393 SwrdQIAWVPQ-HPFL-FAGTIAENI--RLARPDASDAEIreaLERAGLDEFvAALPQGLDTPIGEggagLSGGQAQRLA 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491208697 455 LAKILQQGANVILLDEPSNDLDIETLRALEDAILVFPG--TVMVVSHDR 501
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL 517
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
324-487 |
5.76e-22 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 94.36 E-value: 5.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFD---GRVL-YENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLG--ESVKVAYVGQIRDT 397
Cdd:cd03266 2 ITADALTKRFRdvkKTVQaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 LDNNK-------TVWEEVS--GGLDILKVGDYEIASRAYIGRFNFKgQDQQKRVGELSGGERNRLQLAKILQQGANVILL 468
Cdd:cd03266 82 FVSDStglydrlTARENLEyfAGLYGLKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170
....*....|....*....
gi 491208697 469 DEPSNDLDIETLRALEDAI 487
Cdd:cd03266 161 DEPTTGLDVMATRALREFI 179
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-226 |
9.08e-22 |
|
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: 96.71 E-value: 9.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 24 DISLSFfPGAKIGVL-GLNGAGKSTLLRIMAGVDKDFSGEAR--------AQPGI-------KIGYLEQEPPLDPTKDVR 87
Cdd:COG4148 17 DVDFTL-PGRGVTALfGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdSARGIflpphrrRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNVEDGVRealdalerldqvFAEYADPDADFDALAKeqeklesiihawdahnlnnQLEIAAdaLnLpawDADVTKLSGGE 167
Cdd:COG4148 96 GNLLYGRK------------RAPRAERRISFDEVVE-------------------LLGIGH--L-L---DRRPATLSGGE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491208697 168 RRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHDryfLDNVA 226
Cdd:COG4148 139 RQRVAIGRALLSSPRLLLMDEPLAALDlarkAEILPYLERLRDELDIPILYVSHS---LDEVA 198
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-219 |
1.10e-21 |
|
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: 93.35 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 9 NRVSKMVPPKReILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR-------AQPGIK--IGYLEQEPP 79
Cdd:cd03259 4 KGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrdvtGVPPERrnIGMVFQDYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 80 LDPTKDVRGNVEDGVREALDALERLDqvfaeyadpdadfdalAKEQEKLEsiihawdahnlnnQLEIAADAlnlpawDAD 159
Cdd:cd03259 83 LFPHLTVAENIAFGLKLRGVPKAEIR----------------ARVRELLE-------------LVGLEGLL------NRY 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 160 VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDFPGTIVAITHDR 219
Cdd:cd03259 128 PHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLreelREELKELQRELGITTIYVTHDQ 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-218 |
1.24e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.68 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGIKIGYLEQEPPLDPT--KDVRGNVEDGV 94
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSlpLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 95 ---REALDALERLDQVFAEYADPDADFDALAKEQeklesiihawdahnlnnqleiaadalnlpawdadVTKLSGGERRRV 171
Cdd:NF040873 83 warRGLWRRLTRDDRAAVDDALERVGLADLAGRQ----------------------------------LGELSGGQRQRA 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491208697 172 ALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHD 218
Cdd:NF040873 129 LLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
323-499 |
1.30e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.64 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV---------KVAYVG 392
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVpsrarharqRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 393 QIrDTLDNNKTVWEevsgglDILKVGDYEIASRAYIGR-------FNFKGQDQQKRVGELSGGERNRLQLAKILQQGANV 465
Cdd:PRK13537 87 QF-DNLDPDFTVRE------NLLVFGRYFGLSAAAARAlvpplleFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491208697 466 ILLDEPSNDLD-------IETLRALedaiLVFPGTVMVVSH 499
Cdd:PRK13537 160 LVLDEPTTGLDpqarhlmWERLRSL----LARGKTILLTTH 196
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-235 |
1.34e-21 |
|
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: 98.28 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 14 MVPP--KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR-----------AQPGIKIGYLEQEppl 80
Cdd:COG4618 338 VVPPgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgadlsqwdrEELGRHIGYLPQD--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 81 dptkdvrgnVE--DG-VRE--AldaleRLDQvfaeyADPDADFDAlAKeqeklesiihAWDAHNLNNQL------EIAAD 149
Cdd:COG4618 415 ---------VElfDGtIAEniA-----RFGD-----ADPEKVVAA-AK----------LAGVHEMILRLpdgydtRIGEG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 150 ALNLpawdadvtklSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERF---LKDFPGTIVAITHDRYFLdNVA 226
Cdd:COG4618 465 GARL----------SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAiraLKARGATVVVITHRPSLL-AAV 533
|
....*....
gi 491208697 227 EWILELDRG 235
Cdd:COG4618 534 DKLLVLRDG 542
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
17-242 |
1.51e-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: 93.03 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAkIGVLGLNGAGKSTLLRIMAGVDKDFSG-------EARAQPGI---KIGYLEQEPPLDPtkDV 86
Cdd:cd03264 11 GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGtiridgqDVLKQPQKlrrRIGYLPQEFGVYP--NF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 RgnvedgVREALDALERLDQVfaeyadPDADFDALakeqeklesIIHAWDAHNLNNQLeiaadalnlpawDADVTKLSGG 166
Cdd:cd03264 88 T------VREFLDYIAWLKGI------PSKEVKAR---------VDEVLELVNLGDRA------------KKKIGSLSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 167 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAI--THDRYFLDNVAEWILELDRGHgIPYQG 242
Cdd:cd03264 135 MRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGK-LVFEG 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-235 |
1.99e-21 |
|
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: 93.04 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 6 YTMNRVSKMVPP-KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSG---------------EARAQpgi 69
Cdd:cd03245 3 IEFRNVSFSYPNqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGsvlldgtdirqldpaDLRRN--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 70 kIGYLEQEPPLDPTKdVRGNVEDGVREALDalERLDQVfAEYADPDaDFDALakeqeklesiihawdaHNLNNQLEIAAD 149
Cdd:cd03245 80 -IGYVPQDVTLFYGT-LRDNITLGAPLADD--ERILRA-AELAGVT-DFVNK----------------HPNGLDLQIGER 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 150 ALNLpawdadvtklSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG--TIVAITHdRYFLDNVAE 227
Cdd:cd03245 138 GRGL----------SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVD 206
|
....*...
gi 491208697 228 WILELDRG 235
Cdd:cd03245 207 RIIVMDSG 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
324-500 |
2.50e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLG----ESVKVAYVGQIRDTLD 399
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 400 NNKTVWEEVSGGLDIlkvgdyEIASRAYIGRFNFKGQDQQK-------RVG----------ELSGGERNRLQLAKILQQG 462
Cdd:PRK09536 84 QDTSLSFEFDVRQVV------EMGRTPHRSRFDTWTETDRAaverameRTGvaqfadrpvtSLSGGERQRVLLARALAQA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491208697 463 ANVILLDEPSNDLDI-ETLRALEDA-ILVFPG-TVMVVSHD 500
Cdd:PRK09536 158 TPVLLLDEPTASLDInHQVRTLELVrRLVDDGkTAVAAIHD 198
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
324-508 |
2.55e-21 |
|
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: 92.43 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV---------KVAYVGQ 393
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVvreprevrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 394 IRdTLDNNKTVWEEVSGGLDILKVGDYEIASRA-----YIGRFNFKgqdqQKRVGELSGGERNRLQLAKILQQGANVILL 468
Cdd:cd03265 81 DL-SVDDELTGWENLYIHARLYGVPGAERRERIdelldFVGLLEAA----DRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491208697 469 DEPSNDLDIET-------LRALEDAilvFPGTVMVVSHD----RWFLDRIA 508
Cdd:cd03265 156 DEPTIGLDPQTrahvweyIEKLKEE---FGMTILLTTHYmeeaEQLCDRVA 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-471 |
3.56e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.63 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE---------------ARAQpGIKIGYleQEPPLDPTKDV 86
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEilldgepvrfrsprdAQAA-GIAIIH--QELNLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 ------------RGNVEDG--VREALDALERLDqvfaeyadpdadfdalakeqeklesiihawdahnlnnqLEIAADALn 152
Cdd:COG1129 97 aeniflgreprrGGLIDWRamRRRARELLARLG--------------------------------------LDIDPDTP- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 153 lpawdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHdryFLDnvaEwI 229
Cdd:COG1129 138 -------VGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAqgvAIIYISH---RLD---E-V 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 230 LEL-DR------GhgipyqgnysswleqknarleqeqkqeesfakalkkelEWVRSnakgqqkknkarmERFEELNSKEF 302
Cdd:COG1129 204 FEIaDRvtvlrdG--------------------------------------RLVGT-------------GPVAELTEDEL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 303 QQR---NETSEIYIPPGPRLGNKVVEVEGISKsfDGRVlyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGT 379
Cdd:COG1129 233 VRLmvgRELEDLFPKRAAAPGEVVLEVEGLSV--GGVV--RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGE 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 380 VTL-GESVK-----------VAYV-----GQ-------IRD--TLdnnkTVWEEVSGGLDILKVGDYEIASRaYIGRFNF 433
Cdd:COG1129 309 IRLdGKPVRirsprdairagIAYVpedrkGEglvldlsIREniTL----ASLDRLSRGGLLDRRRERALAEE-YIKRLRI 383
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 491208697 434 KGQDQQKRVGELSGGerNrlQ----LAKILQQGANVILLDEP 471
Cdd:COG1129 384 KTPSPEQPVGNLSGG--N--QqkvvLAKWLATDPKVLILDEP 421
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
18-236 |
4.50e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.03 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEA------------------RAQpgiKIGYLEQEPP 79
Cdd:COG1136 20 EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgqdisslserelarlRRR---HIGFVFQFFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 80 LDPTKDVRGNVE-----DGV------REALDALERLDqvfaeyadpdadfdalakeqekLESIIHawdahnlnnqleiaa 148
Cdd:COG1136 97 LLPELTALENVAlplllAGVsrkerrERARELLERVG----------------------LGDRLD--------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 149 dalNLPAwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDFPGTIVAITHDRyfldN 224
Cdd:COG1136 140 ---HRPS------QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDP----E 206
|
250
....*....|....*
gi 491208697 225 VAEW---ILELDRGH 236
Cdd:COG1136 207 LAARadrVIRLRDGR 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
324-500 |
5.22e-21 |
|
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: 91.91 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGesvkvayvGQIRDTLDNNK- 402
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD--------GKDITNLPPHKr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 403 ---------------TVWEEVSGGLDILKVGDYEIASRA--YIGRFNFKGQdQQKRVGELSGGERNRLQLAKILQQGANV 465
Cdd:cd03300 73 pvntvfqnyalfphlTVFENIAFGLRLKKLPKAEIKERVaeALDLVQLEGY-ANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491208697 466 ILLDEPSNDLD--------IEtLRALEDAILVfpgTVMVVSHD 500
Cdd:cd03300 152 LLLDEPLGALDlklrkdmqLE-LKRLQKELGI---TFVFVTHD 190
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
325-499 |
6.36e-21 |
|
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: 89.97 E-value: 6.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDG--RVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLgesvkvayvgqirdtldnnk 402
Cdd:cd03246 2 EVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 403 tvweevsGGLDILKVGDYEIasRAYIGrfnFKGQDQQKRVGE-----LSGGERNRLQLAKILQQGANVILLDEPSNDLDI 477
Cdd:cd03246 62 -------DGADISQWDPNEL--GDHVG---YLPQDDELFSGSiaeniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180
....*....|....*....|....*
gi 491208697 478 ETLRALEDAIL---VFPGTVMVVSH 499
Cdd:cd03246 130 EGERALNQAIAalkAAGATRIVIAH 154
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
324-478 |
6.68e-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: 91.10 E-value: 6.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPtAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK---------VAYVGQ 393
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLkqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 394 ---------IRDTLD--------NNKTVWEEVSGGLDILKVGDYEiasrayigrfnfkgqdqQKRVGELSGGERNRLQLA 456
Cdd:cd03264 80 efgvypnftVREFLDyiawlkgiPSKEVKARVDEVLELVNLGDRA-----------------KKKIGSLSGGMRRRVGIA 142
|
170 180
....*....|....*....|..
gi 491208697 457 KILQQGANVILLDEPSNDLDIE 478
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPE 164
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
332-529 |
9.56e-21 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 96.17 E-value: 9.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 332 SFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQirDTLDNNK-TVWEEVSG 410
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQ--DPPRNVEgTVYDFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 411 GL----DILKvgDYEIASR-----------------------AYIGRFNFK--------GQDQQKRVGELSGGERNRLQL 455
Cdd:PRK11147 90 GIeeqaEYLK--RYHDISHlvetdpseknlnelaklqeqldhHNLWQLENRinevlaqlGLDPDAALSSLSGGWLRKAAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 456 AKILQQGANVILLDEPSNDLDIETLRALEDAILVFPGTVMVVSHDRWFLDRIATHILSFENEQPEFYTGNYAEY 529
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQY 241
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-218 |
9.79e-21 |
|
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: 95.51 E-value: 9.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 10 RVSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFSGEARAQPGIKIGYLEQEP 78
Cdd:TIGR02868 339 DLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLldplqgevtldGVPVSSLDQDEVRRRVSVCAQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 79 PLDPTkDVRGNV----EDGV-REALDALERldqvfAEYADPdadfdaLAKEQEKLESIIHAwdahnlnnqleiaadalnl 153
Cdd:TIGR02868 419 HLFDT-TVRENLrlarPDATdEELWAALER-----VGLADW------LRALPDGLDTVLGE------------------- 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 154 pawdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-SVSWLERFLKDFPG-TIVAITHD 218
Cdd:TIGR02868 468 -----GGARLSGGERQRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLAALSGrTVVLITHH 529
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
324-500 |
1.37e-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: 90.86 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV--------KVAYVGQi 394
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFgGEDAtdvpvqerNVGFVFQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 RDTLDNNKTVWEEVSGGLDILKVGdyEIASRAYIGR-----FNFKGQD--QQKRVGELSGGERNRLQLAKILQQGANVIL 467
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRS--ERPPEAEIRAkvhelLKLVQLDwlADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491208697 468 LDEPSNDLDIET-------LRALEDAILVfpgTVMVVSHD 500
Cdd:cd03296 160 LDEPFGALDAKVrkelrrwLRRLHDELHV---TTVFVTHD 196
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
323-516 |
1.40e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 90.50 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSF-DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV------KVAY---- 390
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQDLsrlkrrEIPYlrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 391 ---VGQirDT-LDNNKTVWEEVSGGLDILKVGDYEIASRAY--IGRFNFKGQdQQKRVGELSGGERNRLQLAKILqqgAN 464
Cdd:COG2884 81 igvVFQ--DFrLLPDRTVYENVALPLRVTGKSRKEIRRRVRevLDLVGLSDK-AKALPHELSGGEQQRVAIARAL---VN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 465 ---VILLDEPSNDLDIET----LRALEDAILVfpG-TVMVVSHDRWFLDRIATHILSFEN 516
Cdd:COG2884 155 rpeLLLADEPTGNLDPETsweiMELLEEINRR--GtTVLIATHDLELVDRMPKRVLELED 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
324-516 |
1.59e-20 |
|
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: 89.17 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV------------KVAY 390
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdGEDLtdledelpplrrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 391 VGQiRDTLDNNKTVWEEVSGGldilkvgdyeiasrayigrfnfkgqdqqkrvgeLSGGERNRLQLAKILQQGANVILLDE 470
Cdd:cd03229 81 VFQ-DFALFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491208697 471 PSNDLDIETLRALEDAI--LV--FPGTVMVVSHDRWFLDRIATHILSFEN 516
Cdd:cd03229 127 PTSALDPITRREVRALLksLQaqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
307-500 |
2.04e-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: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 307 ETSEIYIPPGPRLgnkvvEVEGISKSFDG--RVLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-G 383
Cdd:TIGR02868 323 PAAGAVGLGKPTL-----ELRDLSAGYPGapPVL-DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 384 ESVKVAYVGQIRD--------------TLDNNKTVW------EEVSGGLDILKVGDYeIASRAyigrfnfKGQDQqkRVG 443
Cdd:TIGR02868 397 VPVSSLDQDEVRRrvsvcaqdahlfdtTVRENLRLArpdatdEELWAALERVGLADW-LRALP-------DGLDT--VLG 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491208697 444 E----LSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAIL-VFPG-TVMVVSHD 500
Cdd:TIGR02868 467 EggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLaALSGrTVVLITHH 529
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
325-507 |
3.08e-20 |
|
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: 89.93 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSF-DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV-------------KVA 389
Cdd:cd03256 2 EVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdGTDInklkgkalrqlrrQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 390 YVGQ----I-RDT-LDN-------NKTVW---------EEVSGGLDIL-KVGdyeIASRAYigrfnfkgqdqqKRVGELS 446
Cdd:cd03256 82 MIFQqfnlIeRLSvLENvlsgrlgRRSTWrslfglfpkEEKQRALAALeRVG---LLDKAY------------QRADQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 447 GGERNRLQLAKILQQGANVILLDEPSNDLD-------IETLRAL--EDAIlvfpgTVMVVSHD----RWFLDRI 507
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDpassrqvMDLLKRInrEEGI-----TVIVSLHQvdlaREYADRI 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-226 |
3.31e-20 |
|
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: 93.81 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------------ARAQPGIKIGYLEQEP--P 79
Cdd:COG1123 275 KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSilfdgkdltklsrrSLRELRRRVQMVFQDPysS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 80 LDPtkdvRGNVEDGVREALDALERLdqvfaeyadPDADFDALAKEqeklesiihawdahnlnnqleiAADALNLPAWDAD 159
Cdd:COG1123 355 LNP----RMTVGDIIAEPLRLHGLL---------SRAERRERVAE----------------------LLERVGLPPDLAD 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 160 --VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAeSVSW-----LERFLKDFPGTIVAITHD----RYFLDNVA 226
Cdd:COG1123 400 ryPHELSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAqilnlLRDLQRELGLTYLFISHDlavvRYIADRVA 476
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
306-500 |
3.94e-20 |
|
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: 94.13 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 306 NETSEIYIPPGPRLGNkvVEVEGISKSFDGR---VLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL 382
Cdd:COG2274 458 REEGRSKLSLPRLKGD--IELENVSFRYPGDsppVL-DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 383 G---------ESV--KVAYVGQ----IRDTLDNNKTVWEEvsgGLDILKVgdYEIASRAYIGRF---NFKGQDQQkrVGE 444
Cdd:COG2274 535 DgidlrqidpASLrrQIGVVLQdvflFSGTIRENITLGDP---DATDEEI--IEAARLAGLHDFieaLPMGYDTV--VGE 607
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 445 ----LSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAI--LVFPGTVMVVSHD 500
Cdd:COG2274 608 ggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLrrLLKGRTVIIIAHR 669
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-236 |
4.06e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.08 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD-KDFSGEA-RAQpgikIGYLEQEPPL 80
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLrfydptsgrilidGVDiRDLTLESlRRQ----IGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 81 dptkdVRGNVEDGVRealdalerldqvfaeYADPDADfdalakeqekLESIIHAwdahnlnnqLEIAA---DALNLPA-W 156
Cdd:COG1132 426 -----FSGTIRENIR---------------YGRPDAT----------DEEVEEA---------AKAAQaheFIEALPDgY 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 157 DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSW----LERFLKDfpGTIVAITHdRyfLDNV--A 226
Cdd:COG1132 467 DTVVgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALiqeaLERLMKG--RTTIVIAH-R--LSTIrnA 541
|
250
....*....|
gi 491208697 227 EWILELDRGH 236
Cdd:COG1132 542 DRILVLDDGR 551
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
324-471 |
4.95e-20 |
|
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: 89.14 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK-----------VAYV 391
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLdGQDITklpmhkrarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 392 GQiRDTLDNNKTVWEEVSGGLDILKVGDYEIASR--AYIGRFNFKGQDQQKrVGELSGGERNRLQLAKILQQGANVILLD 469
Cdd:cd03218 81 PQ-EASIFRKLTVEENILAVLEIRGLSKKEREEKleELLEEFHITHLRKSK-ASSLSGGERRRVEIARALATNPKFLLLD 158
|
..
gi 491208697 470 EP 471
Cdd:cd03218 159 EP 160
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
324-500 |
5.02e-20 |
|
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: 89.16 E-value: 5.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTG-----EQQPDTGTVTL-GESV----------- 386
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLdGKDIydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 387 -KVAYVGQIRDTLDnnKTVWEEVSGGL--------DILKVGDYEIASRAYIGRfnfKGQDQQKrVGELSGGERNRLQLAK 457
Cdd:cd03260 81 rRVGMVFQKPNPFP--GSIYDNVAYGLrlhgiklkEELDERVEEALRKAALWD---EVKDRLH-ALGLSGGQQQRLCLAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491208697 458 ILQQGANVILLDEPSNDLDIETLRALEDAILVF--PGTVMVVSHD 500
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
324-499 |
5.87e-20 |
|
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: 87.10 E-value: 5.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVkvayvgQIRDTLDnnk 402
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEV------SFASPRD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 403 tvweevsggldilkvgdyeiASRAYIGrfnfkgqdqqkRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLD------ 476
Cdd:cd03216 72 --------------------ARRAGIA-----------MVYQLSVGERQMVEIARALARNARLLILDEPTAALTpaever 120
|
170 180
....*....|....*....|....*
gi 491208697 477 -IETLRALEDAilvfpG-TVMVVSH 499
Cdd:cd03216 121 lFKVIRRLRAQ-----GvAVIFISH 140
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
325-471 |
8.29e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.55 E-value: 8.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK-----------VAYVG 392
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLdGEDIThlpmhkrarlgIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 393 Q----IRDtLdnnkTVWEEVSGGLDILKVGDYEIASR--AYIGRFNFKGQDQQKRVgELSGGERNRLQLAKILQQGANVI 466
Cdd:COG1137 85 QeasiFRK-L----TVEDNILAVLELRKLSKKEREERleELLEEFGITHLRKSKAY-SLSGGERRRVEIARALATNPKFI 158
|
....*
gi 491208697 467 LLDEP 471
Cdd:COG1137 159 LLDEP 163
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-236 |
8.68e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.19 E-value: 8.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 8 MNRVSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE------------ARAQPGI--KIGY 73
Cdd:COG2884 4 FENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvlvngqdlsrlkRREIPYLrrRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 74 LEQEPPLDPTKDVRGNVedgvreALdALErldqvfaeyadpdadfdALAKEQEKLESIIHAWdahnLNnQLEIAADALNL 153
Cdd:COG2884 84 VFQDFRLLPDRTVYENV------AL-PLR-----------------VTGKSRKEIRRRVREV----LD-LVGLSDKAKAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 154 PAwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDF--PGT--IVAiTHDRYFLDNVAEWI 229
Cdd:COG2884 135 PH------ELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInrRGTtvLIA-THDLELVDRMPKRV 207
|
....*..
gi 491208697 230 LELDRGH 236
Cdd:COG2884 208 LELEDGR 214
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-511 |
8.78e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 89.02 E-value: 8.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 321 NKVVEVEGISKSFDG-RVLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLgesvkvayvgqirdtld 399
Cdd:COG4674 8 GPILYVEDLTVSFDGfKAL-NDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLF----------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 400 nnktvweevsGGLDILKVGDYEIAsRAYIGR-------------------------------FNFKGQDQQKRV------ 442
Cdd:COG4674 70 ----------GGTDLTGLDEHEIA-RLGIGRkfqkptvfeeltvfenlelalkgdrgvfaslFARLTAEERDRIeevlet 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 443 -----------GELSGGERNRLQLAKILQQGANVILLDEPSNDL-DIET------LRALEdailvfpG--TVMVVSHDRW 502
Cdd:COG4674 139 igltdkadrlaGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMtDAETertaelLKSLA-------GkhSVVVVEHDME 211
|
....*....
gi 491208697 503 FLDRIATHI 511
Cdd:COG4674 212 FVRQIARKV 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
18-236 |
1.11e-19 |
|
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: 86.47 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE-------------ARAQPGIKIGYLEQEPPLDPTK 84
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSilidgedltdledELPPLRRRIGMVFQDFALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 85 DVRGNVEDGvrealdalerldqvfaeyadpdadfdalakeqeklesiihawdahnlnnqleiaadalnlpawdadvtkLS 164
Cdd:cd03229 92 TVLENIALG---------------------------------------------------------------------LS 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 165 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKD----FPGTIVAITHDRYFLDNVAEWILELDRGH 236
Cdd:cd03229 103 GGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
323-516 |
1.14e-19 |
|
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: 88.02 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGR----VLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV----------- 386
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLtllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 387 --KVAYVGQIRDTLdNNKTVWEEVSGGLDILKVGDYEIASRAYiGRFNFKGQDQQKRV--GELSGGERNRLQLAKILQQG 462
Cdd:cd03258 81 rrRIGMIFQHFNLL-SSRTVFENVALPLEIAGVPKAEIEERVL-ELLELVGLEDKADAypAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 463 ANVILLDEPSNDLDIET----LRALEDAILVFPGTVMVVSHDRWFLDRIATHILSFEN 516
Cdd:cd03258 159 PKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
323-499 |
1.19e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.01 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVKvayvgqIRDTLDNN 401
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdGKPVR------IRSPRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 402 K----------------TVWEEVSGGLDILKVGDYEIAS-----RAYIGRFNFKgQDQQKRVGELSGGERNRLQLAKILQ 460
Cdd:COG3845 79 AlgigmvhqhfmlvpnlTVAENIVLGLEPTKGGRLDRKAarariRELSERYGLD-VDPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491208697 461 QGANVILLDEP--------SNDLdIETLRALEDAilvfpG-TVMVVSH 499
Cdd:COG3845 158 RGARILILDEPtavltpqeADEL-FEILRRLAAE-----GkSIIFITH 199
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
18-194 |
1.23e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 88.63 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGIKIGYLEQEPPLDPTKDVRGN----VEDG 93
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLTVNrflrLRPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 94 VREAlDALERLDQVFAeyadpdadfdalakeqeklesiihawdAHNLnnqleiaadalnlpawDADVTKLSGGERRRVAL 173
Cdd:PRK09544 96 TKKE-DILPALKRVQA---------------------------GHLI----------------DAPMQKLSGGETQRVLL 131
|
170 180
....*....|....*....|.
gi 491208697 174 CRLLLSKPDMLLLDEPTNHLD 194
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
323-487 |
1.27e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.24 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGES--------VKVAYVGQi 394
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddpdvaEACHYLGH- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 RDTLDNNKTVWEEVSGGLDILKVGDYEIAsrAYIGRFNFKGQdQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSND 474
Cdd:PRK13539 81 RNAMKPALTVAENLEFWAAFLGGEELDIA--AALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170
....*....|...
gi 491208697 475 LDIETLRALEDAI 487
Cdd:PRK13539 158 LDAAAVALFAELI 170
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-236 |
1.38e-19 |
|
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: 87.94 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------ARAQP------GIKIGYLEQEPPLDPTK 84
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEvlidgediSGLSEaelyrlRRRMGMLFQSGALFDSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 85 DVRGNVEDGVREaldalerldqvfaEYADPDADFDALAKEqeKLESIihawdahnlnnQLEIAADALnlPAwdadvtKLS 164
Cdd:cd03261 93 TVFENVAFPLRE-------------HTRLSEEEIREIVLE--KLEAV-----------GLRGAEDLY--PA------ELS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 165 GGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVSWLERFLKDFPG-TIVAITHDRYFLDNVAEWILELDRGH 236
Cdd:cd03261 139 GGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIADRIAVLYDGK 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-243 |
1.67e-19 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 87.60 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------------ARAQPGikIGYLEQEPPLdpt 83
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKilldgqditklpmhKRARLG--IGYLPQEASI--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 84 kdVRG-NVEDGVREALDALERLDqvfaeyadpdadfdalAKEQEKLESIIHAWDAHNLNNQLEIAadalnlpawdadvtk 162
Cdd:cd03218 87 --FRKlTVEENILAVLEIRGLSK----------------KEREEKLEELLEEFHITHLRKSKASS--------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 163 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLE---RFLKDFpGTIVAIT-HdryfldNVAEWILELDRGHgI 238
Cdd:cd03218 134 LSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQkiiKILKDR-GIGVLITdH------NVRETLSITDRAY-I 205
|
....*
gi 491208697 239 PYQGN 243
Cdd:cd03218 206 IYEGK 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
325-499 |
1.71e-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: 86.64 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV----------KVAYVGQi 394
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPlaeqrdepheNILYLGH- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 RDTLDNNKTVWEEVSGGLDILKVGDYEI-ASRAYIGRFNFkgqdQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSN 473
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQRTIeDALAAVGLTGF----EDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 491208697 474 DLD---IETLRALEDAILVFPGTVMVVSH 499
Cdd:TIGR01189 157 ALDkagVALLAGLLRAHLARGGIVLLTTH 185
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-234 |
1.91e-19 |
|
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: 91.58 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 7 TMNRVSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-----------VDKDFSGEARAQPGIKIGYLE 75
Cdd:TIGR02857 323 EFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGfvdptegsiavNGVPLADADADSWRDQIAWVP 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 76 QEPPLdptkdVRGNVEDGVRealdalerldqvfaeYADPDADFDALAKeqeklesIIHAWDAHNLNNQLEiaaDALNLPA 155
Cdd:TIGR02857 403 QHPFL-----FAGTIAENIR---------------LARPDASDAEIRE-------ALERAGLDEFVAALP---QGLDTPI 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 156 wDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES-VSWLERFLKDFPG-TIVAITHDRyfldnvaEWILELD 233
Cdd:TIGR02857 453 -GEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETeAEVLEALRALAQGrTVLLVTHRL-------ALAALAD 524
|
.
gi 491208697 234 R 234
Cdd:TIGR02857 525 R 525
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-217 |
2.60e-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: 86.26 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGikigyleqepPLDPTKDVRGNV------ED 92
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT----------PLAEQRDEPHENilylghLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 93 GVREALDALERLD--QVFAEYADPDAdFDALAkeqeklesiihawdAHNLNnqleiaaDALNLPAwdadvTKLSGGERRR 170
Cdd:TIGR01189 83 GLKPELSALENLHfwAAIHGGAQRTI-EDALA--------------AVGLT-------GFEDLPA-----AQLSAGQQRR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491208697 171 VALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDF---PGTIVAITH 217
Cdd:TIGR01189 136 LALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-238 |
2.92e-19 |
|
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: 84.90 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 7 TMNRVSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGIKIGYLEQEPPLdptkdV 86
Cdd:cd03223 2 ELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYL-----P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 RGNVedgvrealdalerldqvfaeyadpdadfdalaKEQeklesIIHAWDahnlnnqleiaadalnlpawdadvTKLSGG 166
Cdd:cd03223 77 LGTL--------------------------------REQ-----LIYPWD------------------------DVLSGG 95
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 167 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITHdRYFLDNVAEWILELDRGHGI 238
Cdd:cd03223 96 EQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGEGGW 166
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
328-522 |
3.07e-19 |
|
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: 86.58 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 328 GISKSFDGRVLyeNLSFTVPpTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV---------------KVAYVG 392
Cdd:cd03297 5 DIEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 393 QiRDTLDNNKTVWEEVSGGLDILKVGDYEIASRAYIGRFNFkGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPS 472
Cdd:cd03297 82 Q-QYALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491208697 473 NDLDIET----LRALEDAILVFPGTVMVVSHDRWFLDRIATHILSFENEQPEFY 522
Cdd:cd03297 160 SALDRALrlqlLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
321-516 |
4.70e-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: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 321 NKVVEVEGISKSFDG-----RVLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV-------- 386
Cdd:COG1136 2 SPLLELRNLTKSYGTgegevTAL-RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdGQDIsslserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 387 ------KVAYVGQ----IrDTLdnnkTVWEEVSGGLDILKVGDYEIASRA--YIGRFNFKGQdQQKRVGELSGGERNRLQ 454
Cdd:COG1136 81 arlrrrHIGFVFQffnlL-PEL----TALENVALPLLLAGVSRKERRERAreLLERVGLGDR-LDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 455 LAKILQQGANVILLDEPSNDLDIET----LRALEDAILVFPGTVMVVSHDRwFLDRIATHILSFEN 516
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRD 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-217 |
6.76e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 85.24 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGikiGYLEQEPPLDPTKDVRGNvEDGVREAL 98
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG---PLDFQRDSIARGLLYLGH-APGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 99 DALERLdqvfaeyadpdadfdalakeqeklesiiHAWDAHNLNNQLEIAADALNLPAW-DADVTKLSGGERRRVALCRLL 177
Cdd:cd03231 89 SVLENL----------------------------RFWHADHSDEQVEEALARVGLNGFeDRPVAQLSAGQQRRVALARLL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491208697 178 LSKPDMLLLDEPTNHLDAESVSWLERFLKDFP---GTIVAITH 217
Cdd:cd03231 141 LSGRPLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
324-512 |
7.95e-19 |
|
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: 85.02 E-value: 7.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTV-TLGESV------KVAYVGQIRD 396
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlFDGKPLdiaarnRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 397 tLDNNKTVWEEVSGGLDILKVGDYEIASRA--YIGRFNFkGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSND 474
Cdd:cd03269 81 -LYPKMKVIDQLVYLAQLKGLKKEEARRRIdeWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491208697 475 LDIETLRALEDAILVFPG---TVMVVSHDRWFLDRIATHIL 512
Cdd:cd03269 159 LDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVL 199
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
324-476 |
8.46e-19 |
|
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: 85.00 E-value: 8.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVkVAYVG-QIRDT----- 397
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD-VTDLPpKDRDIamvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 ---LDNNKTVWEEVSGGLDILKVGDYEIASR----AYIGRFnfkGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDE 470
Cdd:cd03301 80 nyaLYPHMTVYDNIAFGLKLRKVPKDEIDERvrevAELLQI---EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
....*.
gi 491208697 471 PSNDLD 476
Cdd:cd03301 157 PLSNLD 162
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
286-509 |
8.60e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 89.84 E-value: 8.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 286 KNKARMERFEELnskefqqRNETSEIYIPPGPRLGNKV---VEVEGISKSFDG--RVLyENLSFTVPPTAIVGIVGPNGA 360
Cdd:COG1132 306 RALASAERIFEL-------LDEPPEIPDPPGAVPLPPVrgeIEFENVSFSYPGdrPVL-KDISLTIPPGETVALVGPSGS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 361 GKTTLFRMMTGEQQPDTGTVTLG---------ESV--KVAYVGQirdtlDN---NKTVWEEVSGGLdiLKVGDYEI---A 423
Cdd:COG1132 378 GKSTLVNLLLRFYDPTSGRILIDgvdirdltlESLrrQIGVVPQ-----DTflfSGTIRENIRYGR--PDATDEEVeeaA 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 424 SRAYIGRF--NF-KGQDQQkrVGE----LSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAIL-VFPG-TV 494
Cdd:COG1132 451 KAAQAHEFieALpDGYDTV--VGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALErLMKGrTT 528
|
250
....*....|....*
gi 491208697 495 MVVSHdrwfldRIAT 509
Cdd:COG1132 529 IVIAH------RLST 537
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-236 |
1.18e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.45 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 7 TMNRVSKMVPpKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE------------ARAQpgiKIGYL 74
Cdd:PRK10851 4 EIANIKKSFG-RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHirfhgtdvsrlhARDR---KVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 75 EQEPPLDPTKDVRGNVEDGVReALDALERldqvfaeyadPDADfdALAKEQEKLESIIhawdahnlnnQLEIAADalNLP 154
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLT-VLPRRER----------PNAA--AIKAKVTQLLEMV----------QLAHLAD--RYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 155 AwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWIL 230
Cdd:PRK10851 135 A------QLSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVV 208
|
....*.
gi 491208697 231 ELDRGH 236
Cdd:PRK10851 209 VMSQGN 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-257 |
1.18e-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: 85.42 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------VD-KDF---SGEARAQPGIKIGYLEQEPPL--DP 82
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllrpdsgeilVDgQDItglSEKELYELRRRIGMLFQGGALfdSL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 83 TkdVRGNVEDGVRE--ALDALERLDQVfaeyadpdadfdalakeQEKLESIihawdahNLnnqleiaADALNL-PAwdad 159
Cdd:COG1127 98 T--VFENVAFPLREhtDLSEAEIRELV-----------------LEKLELV-------GL-------PGAADKmPS---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 160 vtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVSWLERFLKD-FPGTIVAITHDRYFLDNVAEWILELDRG 235
Cdd:COG1127 141 --ELSGGMRKRVALARALALDPEILLYDEPTAGLDpitSAVIDELIRELRDeLGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
250 260
....*....|....*....|..
gi 491208697 236 HgIPYQGNYSSWLEQKNARLEQ 257
Cdd:COG1127 219 K-IIAEGTPEELLASDDPWVRQ 239
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-234 |
1.34e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.50 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------ARAQPGIKIGYleQEPPLDPTKDVRGNV 90
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEllagtaplAEAREDTRLMF--QDARLLPWKKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 91 EDGVR-----EALDALERLDqvfaeyadpdadfdalakeqekLESIIHAWdahnlnnqleiaadalnlPAwdadvtKLSG 165
Cdd:PRK11247 103 GLGLKgqwrdAALQALAAVG----------------------LADRANEW------------------PA------ALSG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491208697 166 GERRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVSWLERFLKDFPGTIVAITHDryfldnVAEWILELDR 234
Cdd:PRK11247 137 GQKQRVALARALIHRPGLLLLDEPLGALDAltriEMQDLIESLWQQHGFTVLLVTHD------VSEAVAMADR 203
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-236 |
1.46e-18 |
|
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: 85.08 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------FSGEARAQPGIK---IGYLEQEPPLDPTKDVRGNVED 92
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdsgtilFGGEDATDVPVQernVGFVFQHYALFRHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 93 GVREAlDALERldqvfaeyaDPDADFDALAKEQEKLEsiihawdahnlnnQLEIAADalNLPAwdadvtKLSGGERRRVA 172
Cdd:cd03296 98 GLRVK-PRSER---------PPEAEIRAKVHELLKLV-------------QLDWLAD--RYPA------QLSGGQRQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 173 LCRLLLSKPDMLLLDEPTNHLDA----ESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGH 236
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-218 |
1.77e-18 |
|
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: 84.93 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 9 NRVSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE------------------ARAQpgik 70
Cdd:cd03256 4 ENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSvlidgtdinklkgkalrqLRRQ---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 71 IGYLEQEPPLDPTKDVRGNVEDGvrealdaleRLDQVfaeyadpdADFDALA---KEQEKLESiIHAWDAHNLNNQLEIA 147
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSG---------RLGRR--------STWRSLFglfPKEEKQRA-LAALERVGLLDKAYQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 148 ADalnlpawdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESV-SWLERFLKDFPGTIVAITHD 218
Cdd:cd03256 142 AD------------QLSGGQQQRVAIARALMQQPKLILADEPVASLDpasSRQVmDLLKRINREEGITVIVSLHQ 204
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-217 |
1.89e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.77 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARaqpgikigyLEQEPPLDPtkDVRGNV-----EDG 93
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK---------LDGGDIDDP--DVAEAChylghRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 94 VREALDALERLdQVFAEYADPDadfdalakeqekLESIIHAWDAHNLnnqleiaADALNLPAWDadvtkLSGGERRRVAL 173
Cdd:PRK13539 84 MKPALTVAENL-EFWAAFLGGE------------ELDIAAALEAVGL-------APLAHLPFGY-----LSAGQKRRVAL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491208697 174 CRLLLSKPDMLLLDEPTNHLDAESVswlERFLKDFP------GTIVAITH 217
Cdd:PRK13539 139 ARLLVSNRPIWILDEPTAALDAAAV---ALFAELIRahlaqgGIVIAATH 185
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-217 |
2.15e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 84.75 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------GVDKDFSGEARAQPGI-----KIGYLEQEPPLDPTKDV 86
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgdlpptyGNDVRLFGERRGGEDVwelrkRIGLVSPALQLRFPRDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 RgnVEDGVREAL-DALERldqvfaeYADPDAdfdalakEQEKLesiihawdAHNLNNQLEIAADAlnlpawDADVTKLSG 165
Cdd:COG1119 96 T--VLDVVLSGFfDSIGL-------YREPTD-------EQRER--------ARELLELLGLAHLA------DRPFGTLSQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 166 GERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDFPGTIVAITH 217
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-235 |
2.52e-18 |
|
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: 83.61 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 8 MNRVSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE------------ARAQPGI--KIGY 73
Cdd:cd03292 3 FINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTirvngqdvsdlrGRAIPYLrrKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 74 LEQEPPLDPTKdvrgNVEDGVREALDALERLDQVFAEYAdpdadfdALAKEQEKLESIIHAwdahnlnnqleiaadalnL 153
Cdd:cd03292 83 VFQDFRLLPDR----NVYENVAFALEVTGVPPREIRKRV-------PAALELVGLSHKHRA------------------L 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 154 PAwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFP---GTIVAITHDRYFLDNVAEWIL 230
Cdd:cd03292 134 PA------ELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVI 207
|
....*
gi 491208697 231 ELDRG 235
Cdd:cd03292 208 ALERG 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-218 |
2.95e-18 |
|
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: 83.77 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-----------DFSGEARAQPGI-------KIGYLEQEPP 79
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgapdegevLLDGKDIYDLDVdvlelrrRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 80 LDPtKDVRGNVEDGVRealdalerldqvfaeyadpdadfDALAKEQEKLEsiihawdahnlnnqlEIAADALNLPA-WD- 157
Cdd:cd03260 92 PFP-GSIYDNVAYGLR-----------------------LHGIKLKEELD---------------ERVEEALRKAAlWDe 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 158 ----ADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDF--PGTIVAITHD 218
Cdd:cd03260 133 vkdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
324-499 |
3.18e-18 |
|
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: 83.82 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFD-GRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK----------VAYV 391
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDIRevtldslrraIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 392 GQirDTLDNNKTVWEEVS-GGLDILKVGDYEIASRAYIG----RFNFKgqdQQKRVGE----LSGGERNRLQLAKILQQG 462
Cdd:cd03253 81 PQ--DTVLFNDTIGYNIRyGRPDATDEEVIEAAKAAQIHdkimRFPDG---YDTIVGErglkLSGGEKQRVAIARAILKN 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 491208697 463 ANVILLDEPSNDLDIETLRALEDAIL-VFPG-TVMVVSH 499
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRdVSKGrTTIVIAH 194
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
20-218 |
3.21e-18 |
|
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: 84.02 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------------ARAQ-PGIKIGYLEQEPPLDPTK 84
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTvrlagqdlfaldedARARlRARHVGFVFQSFQLLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 85 DVRGNV-----EDGVREALD-ALERLDQVfaeyadpdadfdALAkeqEKLEsiiHAWdahnlnNQleiaadalnlpawda 158
Cdd:COG4181 106 TALENVmlpleLAGRRDARArARALLERV------------GLG---HRLD---HYP------AQ--------------- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 159 dvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDFPGTIVAITHD 218
Cdd:COG4181 147 ----LSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLVTHD 206
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-218 |
3.42e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 84.88 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkDFSGEARAQpGIKIgyleqeppldpTKDVRGNVEDgvREAL 98
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG---DLTGGGAPR-GARV-----------TGDVTLNGEP--LAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 99 DA--LERLDQVFAEYADPDADFDalAKEQEKLESIIHAWDAHNLNNQ-LEIAADALNLPAWDA----DVTKLSGGERRRV 171
Cdd:PRK13547 77 DAprLARLRAVLPQAAQPAFAFS--AREIVLLGRYPHARRAGALTHRdGEIAWQALALAGATAlvgrDVTTLSGGELARV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 172 ALCRLL---------LSKPDMLLLDEPTNHLD-AESVSWLE---RFLKDFPGTIVAITHD 218
Cdd:PRK13547 155 QFARVLaqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLLDtvrRLARDWNLGVLAIVHD 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
323-508 |
4.10e-18 |
|
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: 83.32 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLY----ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV----------- 386
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdGKDLlklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 387 --KVAYVGQirD---TLDNNKTVWEEVSGGLDILKVGDYEIASRAYIGRFNFK-GQDQQ---KRVGELSGGERNRLQLAK 457
Cdd:cd03257 81 rkEIQMVFQ--DpmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGvGLPEEvlnRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 458 ILQQGANVILLDEPSNDLD-------IETLRALEDAilvFPGTVMVVSHD----RWFLDRIA 508
Cdd:cd03257 159 ALALNPKLLIADEPTSALDvsvqaqiLDLLKKLQEE---LGLTLLFITHDlgvvAKIADRVA 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
323-512 |
4.97e-18 |
|
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: 87.27 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLY--ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPD---TGTVTLGE-----------SV 386
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPavDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGrdllelsealrGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 387 KVAYVGQIRDTLDNNKTVWEEVSGGLDILKVGDYEIASRAyIGRFNFKGQDQ--QKRVGELSGGERNRLQLAKILQQGAN 464
Cdd:COG1123 84 RIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARV-LELLEAVGLERrlDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491208697 465 VILLDEPSNDLD----IETLRALEDAILVFPGTVMVVSHDRWFLDRIATHIL 512
Cdd:COG1123 163 LLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVV 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-189 |
4.99e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.54 E-value: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------------ARAQPGIkiGYLEQEPPLdpt 83
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRifldgedithlpmhKRARLGI--GYLPQEASI--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 84 kdVRG-NVEDGVREALdalerldqvfaEYADPDAdfdalAKEQEKLESIIHAWDAHNLNNQLEIAadalnlpawdadvtk 162
Cdd:COG1137 90 --FRKlTVEDNILAVL-----------ELRKLSK-----KEREERLEELLEEFGITHLRKSKAYS--------------- 136
|
170 180
....*....|....*....|....*..
gi 491208697 163 LSGGERRRVALCRLLLSKPDMLLLDEP 189
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEP 163
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
323-471 |
7.47e-18 |
|
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: 83.09 E-value: 7.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK-----------VAY 390
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIdGQDIThlpmherarlgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 391 VGQ---IRDTLdnnkTVWEEVSGGLDILKVGDY-EIASR--AYIGRFNFKgQDQQKRVGELSGGERNRLQLAKILQQGAN 464
Cdd:TIGR04406 81 LPQeasIFRKL----TVEENIMAVLEIRKDLDRaEREERleALLEEFQIS-HLRDNKAMSLSGGERRRVEIARALATNPK 155
|
....*..
gi 491208697 465 VILLDEP 471
Cdd:TIGR04406 156 FILLDEP 162
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
322-537 |
9.47e-18 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 86.84 E-value: 9.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 322 KVVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTG---------------EQQPDTGTVTLGESV 386
Cdd:PLN03073 176 KDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMhaidgipkncqilhvEQEVVGDDTTALQCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 387 -------------KVAYVGQIRDT----------LDNNKTV--------WEEVSGGLDILKVGDYEIASRAYIGRFNFKG 435
Cdd:PLN03073 256 lntdiertqlleeEAQLVAQQRELefetetgkgkGANKDGVdkdavsqrLEEIYKRLELIDAYTAEARAASILAGLSFTP 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 436 QDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAILVFPGTVMVVSHDRWFLDRIATHILSFE 515
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLH 415
|
250 260
....*....|....*....|..
gi 491208697 516 NEQPEFYTGNYAEYEAYRQSRL 537
Cdd:PLN03073 416 GQKLVTYKGDYDTFERTREEQL 437
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-235 |
1.14e-17 |
|
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: 84.78 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 31 PGAKI-GVLGLNGAGKSTLLRIMAGVDKDFSGE--------ARAQPGI-------KIGYLEQEPPLDPTKDVRGNVEDGV 94
Cdd:TIGR02142 21 PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEivlngrtlFDSRKGIflppekrRIGYVFQEARLFPHLSVRGNLRYGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 95 RealdalerldqvFAEYADPDADFDALAkeqeklesiihawdahnlnnqleiaaDALNL-PAWDADVTKLSGGERRRVAL 173
Cdd:TIGR02142 101 K------------RARPSERRISFERVI--------------------------ELLGIgHLLGRLPGRLSGGEKQRVAI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 174 CRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRG 235
Cdd:TIGR02142 143 GRALLSSPRLLLMDEPLAALDdprkYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDG 208
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-239 |
1.36e-17 |
|
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: 82.46 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 28 SFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAqPGIKIGYLEQEPpldpTKDVRGNVEDGVREALDALERLDQV 107
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYI----KADYEGTVRDLLSSITKDFYTHPYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 108 FAEYADPdadfdalakeqEKLESIIhawdahnlnnqleiaadalnlpawDADVTKLSGGERRRVALCrLLLSKP-DMLLL 186
Cdd:cd03237 96 KTEIAKP-----------LQIEQIL------------------------DREVPELSGGELQRVAIA-ACLSKDaDIYLL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 187 DEPTNHLDAE----SVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDrghGIP 239
Cdd:cd03237 140 DEPSAYLDVEqrlmASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE---GEP 193
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-218 |
1.60e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 81.37 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKDFSG----------------EARaqpgiKIGYLEQEPPLD 81
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAFSAsgevllngrrltalpaEQR-----RIGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 82 PTKDVRGNVEDGVREALDALERLDQVfaeyadpdadfdalakeQEKLESIihawdahnlnnqleiaadalNLPAW-DADV 160
Cdd:COG4136 89 PHLSVGENLAFALPPTIGRAQRRARV-----------------EQALEEA--------------------GLAGFaDRDP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 161 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERF----LKDFPGTIVAITHD 218
Cdd:COG4136 132 ATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHD 193
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
324-515 |
1.81e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 81.04 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV------------KVAY 390
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdGLKLtddkkninelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 391 VGQiRDTLDNNKTVWEEVSGGL-DILKVGDYEIASRA--YIGRFNFKGQdQQKRVGELSGGERNRLQLAKILQQGANVIL 467
Cdd:cd03262 81 VFQ-QFNLFPHLTVLENITLAPiKVKGMSKAEAEERAleLLEKVGLADK-ADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491208697 468 LDEPSNDLDIETLRALEDAI--LVFPGTVMV-VSHDRWFLDRIATHILSFE 515
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMkdLAEEGMTMVvVTHEMGFAREVADRVIFMD 209
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
340-516 |
1.84e-17 |
|
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: 80.98 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 340 ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESvkVAYVGQ----IRDTL-DN-------NKTVWEE 407
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQepwiQNGTIrENilfgkpfDEERYEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 408 V------SGGLDILKVGDyeiasrayigrfnfkgqdqQKRVGE----LSGGERNRLQLAKILQQGANVILLDEPSNDLDI 477
Cdd:cd03250 100 VikacalEPDLEILPDGD-------------------LTEIGEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491208697 478 ETLRAL-EDAI---LVFPGTVMVVSHDRWFLDRiATHILSFEN 516
Cdd:cd03250 161 HVGRHIfENCIlglLLNNKTRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-242 |
2.03e-17 |
|
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: 80.67 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--VDKDFSGEAR--AQPGIK------IGYLEQEPPLDPTkdvr 87
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLinGRPLDKrsfrkiIGYVPQDDILHPT---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 gnveDGVREALDalerldqvfaeyadpdadFDAlakeqeKLESIihawdahnlnnqleiaadalnlpawdadvtklSGGE 167
Cdd:cd03213 97 ----LTVRETLM------------------FAA------KLRGL--------------------------------SGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 168 RRRVALCRLLLSKPDMLLLDEPTNHLD---AESVSWLERFLKDFPGTIVAITHD-RYFLDNVAEWILELDRGHGIpYQG 242
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDsssALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVI-YFG 194
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
326-477 |
2.95e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.76 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 326 VEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV-----------KVAYVGQI 394
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 RDTLDnNKTVWEEVSggldilkVGDYeiASRAYIGRFnfkGQDQQKRVGE-----------------LSGGERNRLQLAK 457
Cdd:PRK10575 94 LPAAE-GMTVRELVA-------IGRY--PWHGALGRF---GAADREKVEEaislvglkplahrlvdsLSGGERQRAWIAM 160
|
170 180
....*....|....*....|
gi 491208697 458 ILQQGANVILLDEPSNDLDI 477
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDI 180
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
323-499 |
3.24e-17 |
|
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: 81.28 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTG-TVTL------GESV-----KVAY 390
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrgGEDVwelrkRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 391 V-GQIRDTLDNNKTVWEEV-SGGLDIL----KVGDYEIA-SRAYIGRFNFkGQDQQKRVGELSGGERNRLQLAKILQQGA 463
Cdd:COG1119 83 VsPALQLRFPRDETVLDVVlSGFFDSIglyrEPTDEQRErARELLELLGL-AHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491208697 464 NVILLDEPSNDLDI---ETLRALEDAILVFPGTVMV-VSH 499
Cdd:COG1119 162 ELLILDEPTAGLDLgarELLLALLDKLAAEGAPTLVlVTH 201
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-211 |
4.00e-17 |
|
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: 79.95 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 7 TMNRVSKMVPpKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR---------AQPGIKIGYLEQE 77
Cdd:cd03268 2 KTNDLTKTYG-KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksyqknIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 78 PPLDPTKDVRGNVEDGVREALDALERLDQVFAEyadpdadfdalakeqeklesiihawdahnlnnqLEIAADAlnlpawD 157
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDEVLDV---------------------------------VGLKDSA------K 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491208697 158 ADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGT 211
Cdd:cd03268 122 KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ 175
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
323-499 |
4.15e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.85 E-value: 4.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK---------VAYVG 392
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIRrqrdeyhqdLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 393 Q---IRDTLdnnkTVWE------EVSGGLDilkvgdyEIASRAYIGRFNFKGQDQQKrVGELSGGERNRLQLAKILQQGA 463
Cdd:PRK13538 81 HqpgIKTEL----TALEnlrfyqRLHGPGD-------DEALWEALAQVGLAGFEDVP-VRQLSAGQQRRVALARLWLTRA 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 491208697 464 NVILLDEPSNDLD---IETLRALEDAILVFPGTVMVVSH 499
Cdd:PRK13538 149 PLWILDEPFTAIDkqgVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
264-516 |
4.59e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.24 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 264 SFAKALKKELEWVRS--NAKGQQKknkARMERFeelnskeFQQRNETSEIYIPPGPRLGNKV---VEVEGISKSFDG-RV 337
Cdd:PRK13657 280 GFATLLIGRLDQVVAfiNQVFMAA---PKLEEF-------FEVEDAVPDVRDPPGAIDLGRVkgaVEFDDVSFSYDNsRQ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 338 LYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVKvayvGQIRDTLDNN-KTVWEEvsGGL--- 412
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIR----TVTRASLRRNiAVVFQD--AGLfnr 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 413 ---DILKVGD--------YEIASRA----YIGRfnfKGQDQQKRVGE----LSGGERNRLQLAKILQQGANVILLDEPSN 473
Cdd:PRK13657 424 sieDNIRVGRpdatdeemRAAAERAqahdFIER---KPDGYDTVVGErgrqLSGGERQRLAIARALLKDPPILILDEATS 500
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 491208697 474 DLDIETLRALEDAI-LVFPG-TVMVVSHdRWFLDRIATHILSFEN 516
Cdd:PRK13657 501 ALDVETEAKVKAALdELMKGrTTFIIAH-RLSTVRNADRILVFDN 544
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
18-197 |
4.89e-17 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 80.41 E-value: 4.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkdfsgeARAQPGikigyleqeppldptkDVRGNVEDGVREA 97
Cdd:TIGR03864 13 ARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRL-------YVAQSG----------------QISVAGHDLRRAP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 98 LDALERLDQVFAEyadPDADFDaLAKEQEKLesiIHAwDAHNL---NNQLEIAA--DALNLPAWDAD-VTKLSGGERRRV 171
Cdd:TIGR03864 70 RAALARLGVVFQQ---PTLDLD-LSVRQNLR---YHA-ALHGLsraEARARIAEllARLGLAERADDkVRELNGGHRRRV 141
|
170 180
....*....|....*....|....*.
gi 491208697 172 ALCRLLLSKPDMLLLDEPTNHLDAES 197
Cdd:TIGR03864 142 EIARALLHRPALLLLDEPTVGLDPAS 167
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
323-511 |
5.69e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.53 E-value: 5.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDG-RVLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVkvayvgQIRDTLD- 399
Cdd:COG1129 4 LLEMRGISKSFGGvKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPV------RFRSPRDa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 400 ---------------NNKTVWEEVSGGLDILKVG--DY---EIASRAYIGRFNFKgQDQQKRVGELSGGERNRLQLAKIL 459
Cdd:COG1129 77 qaagiaiihqelnlvPNLSVAENIFLGREPRRGGliDWramRRRARELLARLGLD-IDPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491208697 460 QQGANVILLDEPS---NDLDIETL----RALEDAilvfpGTVMV-VSHdrwFLD---RIATHI 511
Cdd:COG1129 156 SRDARVLILDEPTaslTEREVERLfriiRRLKAQ-----GVAIIyISH---RLDevfEIADRV 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
21-219 |
6.71e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 82.07 E-value: 6.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFSGEARAQPGIkiGYLEQEPPLDPTKDVRGN 89
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFetpdsgrilldGRDVTGLPPEKRNV--GMVFQDYALFPHLTVAEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 90 VEDGVREA-LDALERLDQVfaeyadpdadfdalakeQEKLEsiihawdahnlnnQLEIAADAlnlpawDADVTKLSGGER 168
Cdd:COG3842 98 VAFGLRMRgVPKAEIRARV-----------------AELLE-------------LVGLEGLA------DRYPHQLSGGQQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 169 RRVALCRLLLSKPDMLLLDEPTNHLDA---ESV-SWLERFLKDFPGTIVAITHDR 219
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAklrEEMrEELRRLQRELGITFIYVTHDQ 196
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
328-483 |
8.32e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.62 E-value: 8.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 328 GISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQ--QPDTGTVTLGEsvkvayvgqirDTLDNNKTVW 405
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD-----------NQFGREASLI 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 406 EEVSGGLDILKVgdYEIASRAYIGR-FNFKgqdqqKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRAL 483
Cdd:COG2401 104 DAIGRKGDFKDA--VELLNAVGLSDaVLWL-----RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
329-536 |
9.38e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 83.02 E-value: 9.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 329 ISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAY------------------ 390
Cdd:PRK15064 7 ITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKlrqdqfafeeftvldtvi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 391 --------VGQIRDTLDNNKTVWEEvsgglDILKVGDYEiasrayiGRF-NFKGQDQQKRVGEL---------------- 445
Cdd:PRK15064 87 mghtelweVKQERDRIYALPEMSEE-----DGMKVADLE-------VKFaEMDGYTAEARAGELllgvgipeeqhyglms 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 446 --SGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAILVFPGTVMVVSHDRWFLDRIATHILSFENEQPEFYT 523
Cdd:PRK15064 155 evAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYP 234
|
250
....*....|....
gi 491208697 524 GNYAEY-EAYRQSR 536
Cdd:PRK15064 235 GNYDEYmTAATQAR 248
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
18-242 |
1.02e-16 |
|
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: 79.63 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------------ARAQPGIkiGYLEQEPPLdpt 83
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKilidgqdithlpmhERARLGI--GYLPQEASI--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 84 kdVRG-NVEDGVREALDALERLDqvfaeyadpdadfdalAKEQEKLesiihawdAHNLNNQLEIAaDALNLPAWDadvtk 162
Cdd:TIGR04406 88 --FRKlTVEENIMAVLEIRKDLD----------------RAEREER--------LEALLEEFQIS-HLRDNKAMS----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 163 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLE---RFLKDFpGTIVAIT-HdryfldNVAEWILELDRGHgI 238
Cdd:TIGR04406 136 LSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVGDIKkiiKHLKER-GIGVLITdH------NVRETLDICDRAY-I 207
|
....
gi 491208697 239 PYQG 242
Cdd:TIGR04406 208 ISDG 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
341-499 |
1.03e-16 |
|
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: 78.12 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 341 NLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQIRDTLdnnkTVWEEvsggldilKVGDY 420
Cdd:cd03247 20 NLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLI----SVLNQ--------RPYLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 421 EIASRAYIGRfnfkgqdqqkrvgELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAILVF--PGTVMVVS 498
Cdd:cd03247 88 DTTLRNNLGR-------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVlkDKTLIWIT 154
|
.
gi 491208697 499 H 499
Cdd:cd03247 155 H 155
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-205 |
1.04e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.69 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 24 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIG-----------YLEQEPpldptkdvrgnved 92
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ-GEPIRrqrdeyhqdllYLGHQP-------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 93 GVREALDALERLD--QVFAEYADPDADFDALAKEqeklesiihawdahNLNNQLEIAADALnlpawdadvtklSGGERRR 170
Cdd:PRK13538 84 GIKTELTALENLRfyQRLHGPGDDEALWEALAQV--------------GLAGFEDVPVRQL------------SAGQQRR 137
|
170 180 190
....*....|....*....|....*....|....*
gi 491208697 171 VALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFL 205
Cdd:PRK13538 138 VALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-270 |
1.22e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 79.67 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGVDKDFSGEARAQPGI----KIGYLEQEPPLDP 82
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdsgqlniAGHQFDFSQKPSEKAIRllrqKVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 83 TKDVRGN-VEDGVREAldalerldqvfaeyadpdadfdALAKEQEKLEsiihawdAHNLNNQLEIAADALNLPAwdadvt 161
Cdd:COG4161 96 HLTVMENlIEAPCKVL----------------------GLSKEQAREK-------AMKLLARLRLTDKADRFPL------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGT-I--VAITHDRYFLDNVAEWILELDRGHgI 238
Cdd:COG4161 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgItqVIVTHEVEFARKVASQVVYMEKGR-I 219
|
250 260 270
....*....|....*....|....*....|..
gi 491208697 239 PYQGNYSSWleqknarleqEQKQEESFAKALK 270
Cdd:COG4161 220 IEQGDASHF----------TQPQTEAFAHYLS 241
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
324-500 |
1.54e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 81.27 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV---------KVAYVGQi 394
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlppkdrNIAMVFQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 rdtldN-----NKTVWEEVSGGLDILKVGDYEIASR-----------AYIGRfnfkgqdqqkRVGELSGGERNRLQLAKI 458
Cdd:COG3839 83 -----SyalypHMTVYENIAFPLKLRKVPKAEIDRRvreaaellgleDLLDR----------KPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491208697 459 LQQGANVILLDEP-SNdLD-------IETLRALEDAIlvfpGTVMV-VSHD 500
Cdd:COG3839 148 LVREPKVFLLDEPlSN-LDaklrvemRAEIKRLHRRL----GTTTIyVTHD 193
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-218 |
1.70e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.67 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSG--------------EARAQPGIK-IGYLEQEPPLDPTKD 85
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGevslvgqplhqmdeEARAKLRAKhVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 86 VRGNVEdgvreaLDALERldqvfaeyadpdADFDALAKEQeklesiihawdAHNLNNQLEIAADALNLPAwdadvtKLSG 165
Cdd:PRK10584 105 ALENVE------LPALLR------------GESSRQSRNG-----------AKALLEQLGLGKRLDHLPA------QLSG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 166 GERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDFPGTIVAITHD 218
Cdd:PRK10584 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkiADLLFSLNREHGTTLILVTHD 206
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
324-508 |
1.73e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 79.41 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGE---------SVKVAYVGQI 394
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 RD---------TLDNNKTVWEEVSGGLDILKVGDYEIA---SRAYIGRFNFKGQDQQ--KRvgeLSGGERNRLQLAKILQ 460
Cdd:PRK11264 84 RQhvgfvfqnfNLFPHRTVLENIIEGPVIVKGEPKEEAtarARELLAKVGLAGKETSypRR---LSGGQQQRVAIARALA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 461 QGANVILLDEPSNDLDIE-------TLRALEDAilvfPGTVMVVSHDRWFLDRIA 508
Cdd:PRK11264 161 MRPEVILFDEPTSALDPElvgevlnTIRQLAQE----KRTMVIVTHEMSFARDVA 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
22-217 |
1.86e-16 |
|
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: 78.56 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkdfsgearaqpgikigyleqeppLDPTKdvrGNVE----DGVREA 97
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL------------------------LEPDA---GFATvdgfDVVKEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 98 LDALERLDQVFaeyaDPDADFDAL-AKEQEKLESIIHAWDAHNLNNQLEIAADALNLPAW-DADVTKLSGGERRRVALCR 175
Cdd:cd03266 74 AEARRRLGFVS----DSTGLYDRLtARENLEYFAGLYGLKGDELTARLEELADRLGMEELlDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491208697 176 LLLSKPDMLLLDEPTNHLDAESVSWLERF---LKDFPGTIVAITH 217
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFirqLRALGKCILFSTH 194
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-242 |
1.92e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 78.91 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARaqpgikigyleqeppldptkdVRGNVEDGVREALd 99
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR---------------------VAGLVPWKRRKKF- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 100 aLERLDQVFAEYAD-----PDADFDALAKEqeklesiIHAWDAHNLNNQLEIAADALNL-PAWDADVTKLSGGERRRVAL 173
Cdd:cd03267 93 -LRRIGVVFGQKTQlwwdlPVIDSFYLLAA-------IYDLPPARFKKRLDELSELLDLeELLDTPVRQLSLGQRMRAEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491208697 174 CRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDF----PGTIVAITHDRYFLDNVAEWILELDRGHgIPYQG 242
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGR-LLYDG 236
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
324-517 |
2.09e-16 |
|
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: 76.81 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGIS-KSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQirdtldnnk 402
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQ--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 403 tvweevsggldilkvgdyeiasRAYIGRFNFKGQ-----DQqkrvgELSGGERNRLQLAKILQQGANVILLDEPSNDLDI 477
Cdd:cd03223 72 ----------------------RPYLPLGTLREQliypwDD-----VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491208697 478 ETLRALEDAILVFPGTVMVVSHdRWFLDRIATHILSFENE 517
Cdd:cd03223 125 ESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGE 163
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-218 |
2.12e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.43 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFSGEARAQPGIKIGYLEQEPPLDPTKDVRGN 89
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTltptagtvlvaGDDVEALSARAASRRVASVPQDTSLSFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 90 VEDGVREALDALERLDqvfaeyadpDADFDALakeqeklESIIhawdahnlnNQLEIAADAlnlpawDADVTKLSGGERR 169
Cdd:PRK09536 98 VEMGRTPHRSRFDTWT---------ETDRAAV-------ERAM---------ERTGVAQFA------DRPVTSLSGGERQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491208697 170 RVALCRLLLSKPDMLLLDEPTNHLDA-ESVSWLE--RFLKDFPGTIVAITHD 218
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDInHQVRTLElvRRLVDDGKTAVAAIHD 198
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-217 |
2.53e-16 |
|
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: 78.39 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 7 TMNRVSKMVPPKR---EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE------------------ARA 65
Cdd:cd03258 3 ELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSvlvdgtdltllsgkelrkARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 66 QpgikIGYLEQEPPLDPTKDVRGNVedgvreALdALErldqvfaeyadpdadfdaLAK-EQEKLESIIHAwdahnLNNQL 144
Cdd:cd03258 83 R----IGMIFQHFNLLSSRTVFENV------AL-PLE------------------IAGvPKAEIEERVLE-----LLELV 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 145 EIAADALNLPAwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKD----FPGTIVAITH 217
Cdd:cd03258 129 GLEDKADAYPA------QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinreLGLTIVLITH 199
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
324-507 |
2.62e-16 |
|
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: 78.02 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDG--RVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK----------VAY 390
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdGTDIRqldpadlrrnIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 391 VGQ----IRDTLDNNKTVWEEVSGGLDILkvgdyEIASRAYIGRF---NFKGQDQQkrVGE----LSGGERNRLQLAKIL 459
Cdd:cd03245 83 VPQdvtlFYGTLRDNITLGAPLADDERIL-----RAAELAGVTDFvnkHPNGLDLQ--IGErgrgLSGGQRQAVALARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491208697 460 QQGANVILLDEPSNDLDIETLRALEDAI--LVFPGTVMVVSHDRWFL---DRI 507
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLrqLLGDKTLIIITHRPSLLdlvDRI 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-217 |
2.81e-16 |
|
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: 76.87 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR-----------AQPGIKIGYLEQEppldptkdv 86
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRldgadisqwdpNELGDHVGYLPQD--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 rgnvedgvrealdalerlDQVFAEyadpdadfdalakeqekleSIihawdAHNLnnqleiaadalnlpawdadvtkLSGG 166
Cdd:cd03246 85 ------------------DELFSG-------------------SI-----AENI----------------------LSGG 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491208697 167 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFP---GTIVAITH 217
Cdd:cd03246 101 QRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAH 154
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-508 |
3.49e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.23 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE---------------ARAQpgiKIGYLEQEPPLDPTKDV 86
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEilidgkpvrirsprdAIAL---GIGMVHQHFMLVPNLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 RGNV----EDGVREALD---ALERLDQVFAEYA---DPDAdfdalakeqeklesiihawdahnlnnqleiaadalnlPAW 156
Cdd:COG3845 98 AENIvlglEPTKGGRLDrkaARARIRELSERYGldvDPDA-------------------------------------KVE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 157 DadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHL-DAESVSWLE--RFLKDFPGTIVAITHDryfLDnvaEwILEL- 232
Cdd:COG3845 141 D-----LSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFEilRRLAAEGKSIIFITHK---LR---E-VMAIa 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 233 DR----------GHGIPyqgnysswleqknarleqeqkQEESfakalKKELewvrsnakgqqkknkARM---ERFEELNS 299
Cdd:COG3845 209 DRvtvlrrgkvvGTVDT---------------------AETS-----EEEL---------------AELmvgREVLLRVE 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 300 KefqqrnetseiyipPGPRLGNKVVEVEGIS-KSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTG 378
Cdd:COG3845 248 K--------------APAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 379 TVTL-GESVKVAYVGQIRDT-------------LDNNKTVWE----------EVSGGLdILKVGDYEIASRAYIGRFNFK 434
Cdd:COG3845 314 SIRLdGEDITGLSPRERRRLgvayipedrlgrgLVPDMSVAEnlilgryrrpPFSRGG-FLDRKAIRAFAEELIEEFDVR 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 435 GQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDI-------ETLRALEDAilvfpGT-VMVVSHDrwfL-- 504
Cdd:COG3845 393 TPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaiefihQRLLELRDA-----GAaVLLISED---Lde 464
|
....*....
gi 491208697 505 -----DRIA 508
Cdd:COG3845 465 ilalsDRIA 473
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
18-236 |
3.87e-16 |
|
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: 77.18 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVDKDFSGEARAQPGIKIGYLEQEPPLDPTK 84
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINlleepdsgtiiidGLKLTDDKKNINELRQKVGMVFQQFNLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 85 DVRGNVEDG---VR-----EALD-ALERLDQVfaeyadpdadfdalakeqeKLESIIHAWDAHnlnnqleiaadalnlpa 155
Cdd:cd03262 92 TVLENITLApikVKgmskaEAEErALELLEKV-------------------GLADKADAYPAQ----------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 156 wdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHDRYFLDNVAEWILEL 232
Cdd:cd03262 136 -------LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVADRVIFM 208
|
....
gi 491208697 233 DRGH 236
Cdd:cd03262 209 DDGR 212
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
324-500 |
3.94e-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: 77.76 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRV---------------LYE------NLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL 382
Cdd:cd03267 1 IEVSNLSKSYRVYSkepgligslkslfkrKYRevealkGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 383 GESV----KVAYVGQIRDTLDNNKTVWeevsggLDILKVGDYEIASRAY-IGRFNFKGQ--------------DQQKRvg 443
Cdd:cd03267 81 AGLVpwkrRKKFLRRIGVVFGQKTQLW------WDLPVIDSFYLLAAIYdLPPARFKKRldelselldleellDTPVR-- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491208697 444 ELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAILVF----PGTVMVVSHD 500
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHY 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
336-512 |
3.94e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.87 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 336 RVLYENL----SFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV--------KVAYVGQirdtlDNN- 401
Cdd:COG3840 8 TYRYGDFplrfDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWnGQDLtalppaerPVSMLFQ-----ENNl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 402 ---KTVWEEVSGGLDI-LKVGDYE------IASRAYIGRFNfkgqdqQKRVGELSGGERNRLQLAKILQQGANVILLDEP 471
Cdd:COG3840 83 fphLTVAQNIGLGLRPgLKLTAEQraqveqALERVGLAGLL------DRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491208697 472 SNDLDI----ETLRALEDAILVFPGTVMVVSHDrwfLD---RIATHIL 512
Cdd:COG3840 157 FSALDPalrqEMLDLVDELCRERGLTVLMVTHD---PEdaaRIADRVL 201
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
324-508 |
4.54e-16 |
|
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: 77.76 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYeNLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV--------KVAYVGQi 394
Cdd:cd03299 1 LKVENLSKDWKEFKLK-NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDItnlppekrDISYVPQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 RDTLDNNKTVWEEVSGGLDILKVGDYEIASRAY-IGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSN 473
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLeIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491208697 474 DLDIET----LRALEDAILVFPGTVMVVSHD----RWFLDRIA 508
Cdd:cd03299 159 ALDVRTkeklREELKKIRKEFGVTVLHVTHDfeeaWALADKVA 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
325-476 |
4.83e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 76.76 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV----------KVAYVGQ- 393
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPldfqrdsiarGLLYLGHa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 394 --IRDTLD--NNKTVW------EEVSGGLDILKVGDYEIASrayigrfnfkgqdqqkrVGELSGGERNRLQLAKILQQGA 463
Cdd:cd03231 82 pgIKTTLSvlENLRFWhadhsdEQVEEALARVGLNGFEDRP-----------------VAQLSAGQQRRVALARLLLSGR 144
|
170
....*....|...
gi 491208697 464 NVILLDEPSNDLD 476
Cdd:cd03231 145 PLWILDEPTTALD 157
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
324-511 |
6.06e-16 |
|
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: 77.34 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSF-DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV----------KVAYV 391
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdGEDIreqdpvelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 392 GQiRDTLDNNKTVWEEVSGGLDILKVGDYEIASRAY-------IGRFNFKgqdqQKRVGELSGGERNRLQLAKILQQGAN 464
Cdd:cd03295 81 IQ-QIGLFPHMTVEENIALVPKLLKWPKEKIRERADellalvgLDPAEFA----DRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491208697 465 VILLDEPSNDLDIETLRALEDAIL----VFPGTVMVVSHDRWFLDRIATHI 511
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKrlqqELGKTIVFVTHDIDEAFRLADRI 206
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-217 |
6.14e-16 |
|
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: 75.54 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEaraqpgIKIgyleqeppldptkdvrgnveDGVRealdal 101
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE------ILV--------------------DGKE------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 102 erldqvfAEYADPdadfdalakeqeklesiihaWDAHNLNnqleIAAdalnlpawdadVTKLSGGERRRVALCRLLLSKP 181
Cdd:cd03216 64 -------VSFASP--------------------RDARRAG----IAM-----------VYQLSVGERQMVEIARALARNA 101
|
170 180 190
....*....|....*....|....*....|....*....
gi 491208697 182 DMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITH 217
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
334-500 |
7.22e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.36 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 334 DGRVLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGE-----------SVKVAYVGQIRDTLDNnK 402
Cdd:PRK11231 14 TKRIL-NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlARRLALLPQHHLTPEG-I 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 403 TVWEEVSGG----LDI---LKVGDYEIASRAYigrfnfkgQDQQ------KRVGELSGGERNRLQLAKILQQGANVILLD 469
Cdd:PRK11231 92 TVRELVAYGrspwLSLwgrLSAEDNARVNQAM--------EQTRinhladRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 491208697 470 EPSNDLDI-------ETLRALEDAilvfpG-TVMVVSHD 500
Cdd:PRK11231 164 EPTTYLDInhqvelmRLMRELNTQ-----GkTVVTVLHD 197
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-218 |
7.78e-16 |
|
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: 76.99 E-value: 7.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQ-------PGIK--IGYLEQEPPLDPTKDVRGNVED 92
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlPPEKrdISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 93 GVREAL-DALERLDQVfaeyadpdadfdalaKEQEKLESIihawdAHNLNNqleiaadalnlpawdaDVTKLSGGERRRV 171
Cdd:cd03299 95 GLKKRKvDKKEIERKV---------------LEIAEMLGI-----DHLLNR----------------KPETLSGGEQQRV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491208697 172 ALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKD----FPGTIVAITHD 218
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKirkeFGVTVLHVTHD 189
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-218 |
8.49e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 78.96 E-value: 8.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFSGEARAQPGIkiGYLEQEPPLDPTKDV 86
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLedptsgeiligGRDVTDLPPKDRNI--AMVFQSYALYPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 RGNVEDGVRealdaLERLdqvfaeyadPDADFDALAKEqeklesiihawdahnlnnqleiAADALNLPAW-DADVTKLSG 165
Cdd:COG3839 93 YENIAFPLK-----LRKV---------PKAEIDRRVRE----------------------AAELLGLEDLlDRKPKQLSG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491208697 166 GERRRVALCRLLLSKPDMLLLDEPTNHLDA--------EsvswLERFLKDFPGTIVAITHD 218
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDAklrvemraE----IKRLHRRLGTTTIYVTHD 193
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
323-507 |
8.54e-16 |
|
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: 76.62 E-value: 8.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSF-DGRVLYE---NLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVT-LGESVKVAYVGQIRDt 397
Cdd:TIGR02211 1 LLKCENLGKRYqEGKLDTRvlkGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLfNGQSLSKLSSNERAK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 LDNNK--------------TVWEEVSGGLDILKVGDYEIASRAY--IGRFNFKGQdQQKRVGELSGGERNRLQLAKILQQ 461
Cdd:TIGR02211 80 LRNKKlgfiyqfhhllpdfTALENVAMPLLIGKKSVKEAKERAYemLEKVGLEHR-INHRPSELSGGERQRVAIARALVN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491208697 462 GANVILLDEPSNDLDIETLRALEDAIL---VFPGT-VMVVSHDRWFLDRI 507
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFDLMLelnRELNTsFLVVTHDLELAKKL 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
323-501 |
9.47e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.11 E-value: 9.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLgESVKVAYVGQIRDTLD--- 399
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLSHVPPYQRPINmmf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 400 ------NNKTVWEEVSGGLDILKVGDYEIASRAYIGRFNFKGQDQQKRV-GELSGGERNRLQLAKILQQGANVILLDEPS 472
Cdd:PRK11607 98 qsyalfPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKpHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190
....*....|....*....|....*....|....
gi 491208697 473 NDLDiETLR---ALE--DAILVFPGTVMVVSHDR 501
Cdd:PRK11607 178 GALD-KKLRdrmQLEvvDILERVGVTCVMVTHDQ 210
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
334-498 |
1.01e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.62 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 334 DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVT-LGESVK-------VAYVGQIRDTLDNNKTVW 405
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISiLGQPTRqalqknlVAYVPQSEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 406 EEV--------SGGLDILKVGDYEIASRAyIGRFNFKgQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDI 477
Cdd:PRK15056 98 EDVvmmgryghMGWLRRAKKRDRQIVTAA-LARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180
....*....|....*....|....*...
gi 491208697 478 ET-------LRALEDAilvfpGTVMVVS 498
Cdd:PRK15056 176 KTeariislLRELRDE-----GKTMLVS 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
163-372 |
1.19e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 79.67 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 163 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAIthdryfldnvaewILELDRGHGIPYQG 242
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITL-------------VLVLNRFDEIPDFV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 243 NYSSWLEqkNARLEQEQKQEESFAKALKKELewvrsnakgqqkknkARMERFEEL---NSKEFQQRNEtseiyIPPG-PR 318
Cdd:PRK10938 203 QFAGVLA--DCTLAETGEREEILQQALVAQL---------------AHSEQLEGVqlpEPDEPSARHA-----LPANePR 260
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 319 --LGNKVVevegiskSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGE 372
Cdd:PRK10938 261 ivLNNGVV-------SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD 309
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
321-501 |
1.22e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.61 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 321 NKVVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVKVAYVgQIRD--- 396
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDVTHRSI-QQRDicm 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 397 -----TLDNNKTVWEEVSGGLDILKVGDYEIASR-----AYIGRFNFkgqdQQKRVGELSGGERNRLQLAKILQQGANVI 466
Cdd:PRK11432 83 vfqsyALFPHMSLGENVGYGLKMLGVPKEERKQRvkealELVDLAGF----EDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 491208697 467 LLDEPSNDLDIETLRALEDAI----LVFPGTVMVVSHDR 501
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIrelqQQFNITSLYVTHDQ 197
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
323-500 |
1.39e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQ---IRDTLD 399
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklyLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 400 NNKTVWEEVSGGL---DILKVgdyeiasrayIGRFNfKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLD 476
Cdd:PRK09544 84 LTVNRFLRLRPGTkkeDILPA----------LKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180
....*....|....*....|....*...
gi 491208697 477 IETLRALEDAI----LVFPGTVMVVSHD 500
Cdd:PRK09544 153 VNGQVALYDLIdqlrRELDCAVLMVSHD 180
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-261 |
1.72e-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: 76.11 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGVD-KDFSGEA-RAQpgikIGYLEQEPPL 80
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvssgsiliDGQDiREVTLDSlRRA----IGVVPQDTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 81 -DPTkdVRGNVEdgvrealdalerldqvfaeYADPDAdfdalaKEQEKLESIIHAwdahnlnnqlEIAADALNLP-AWDA 158
Cdd:cd03253 87 fNDT--IGYNIR-------------------YGRPDA------TDEEVIEAAKAA----------QIHDKIMRFPdGYDT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 159 DV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG--TIVAITHDryfLDNV--AEWIL 230
Cdd:cd03253 130 IVgergLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAHR---LSTIvnADKII 206
|
250 260 270
....*....|....*....|....*....|.
gi 491208697 231 ELDRGhGIPYQGNYSSWLEQKNARLEQEQKQ 261
Cdd:cd03253 207 VLKDG-RIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
325-476 |
1.80e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 76.44 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGR-----VLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL------GESVKVAYVGQ 393
Cdd:COG4525 5 TVRHVSVRYPGGgqpqpAL-QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvtGPGADRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 394 iRDTLDNNKTVWEEVSGGLDILKVGDYEIASRA--YIGRFNFKGQdQQKRVGELSGGERNRLQLAKILQQGANVILLDEP 471
Cdd:COG4525 84 -KDALLPWLNVLDNVAFGLRLRGVPKAERRARAeeLLALVGLADF-ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
....*
gi 491208697 472 SNDLD 476
Cdd:COG4525 162 FGALD 166
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-235 |
2.20e-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: 75.48 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpgikiGYleqeppldptkdvrgnveDGVREALD 99
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVA-----GH------------------DVVREPRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 100 ALERLDQVFAeyaDPDADFDALAKEQEKLESIIHAWDAHNLNNQLEIAADALNL-PAWDADVTKLSGGERRRVALCRLLL 178
Cdd:cd03265 71 VRRRIGIVFQ---DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLlEAADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491208697 179 SKPDMLLLDEPTNHLDAESVS--W--LERFLKDFPGTIVAITHDRYFLDNVAEWILELDRG 235
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-224 |
3.16e-15 |
|
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: 73.89 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 7 TMNRVSKMVPPKRE-ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAraqpgikigYLEQEPPLdptkd 85
Cdd:cd03247 2 SINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVPVS----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 86 vrgNVEDGVREALDALErldqvfaeyadpdadfdalakeQEklesiIHAWDAHNLNNqleiaadaLNLPawdadvtkLSG 165
Cdd:cd03247 68 ---DLEKALSSLISVLN----------------------QR-----PYLFDTTLRNN--------LGRR--------FSG 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 166 GERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDfpGTIVAITH--------DR-YFLDN 224
Cdd:cd03247 102 GERQRLALARILLQDAPIVLLDEPTVGLDPITerqlLSLIFEVLKD--KTLIWITHhltgiehmDKiLFLEN 171
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
325-500 |
3.47e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.51 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLgESVKVAYVGQIRDTLDNN--- 401
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL-DGKPVEGPGAERGVVFQNegl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 402 ---KTVWEEVSGGLDILKVG--DYEIASRAYIGRFNFKGQDqQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLD 476
Cdd:PRK11248 82 lpwRNVQDNVAFGLQLAGVEkmQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180
....*....|....*....|....*...
gi 491208697 477 IETLRALEDAIL-VFPGT---VMVVSHD 500
Cdd:PRK11248 161 AFTREQMQTLLLkLWQETgkqVLLITHD 188
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-234 |
4.37e-15 |
|
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: 74.81 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR------AQPGIKIGYLEQEPPLDPTKDVRGNVEDGVR 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIlegkqiTEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 96 EALDALERLDQvfaeyadpdadfDALAKEQEKLESIIHAWDAHnlnnqleiaadalnlpawdadVTKLSGGERRRVALCR 175
Cdd:TIGR01184 81 RVLPDLSKSER------------RAIVEEHIALVGLTEAADKR---------------------PGQLSGGMKQRVAIAR 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491208697 176 LLLSKPDMLLLDEPTNHLDAESVSWL-ERFLK---DFPGTIVAITHDryfldnVAEWILELDR 234
Cdd:TIGR01184 128 ALSIRPKVLLLDEPFGALDALTRGNLqEELMQiweEHRVTVLMVTHD------VDEALLLSDR 184
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-190 |
4.95e-15 |
|
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: 74.39 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------------ARAQPGikIGYLEQEPPLDPTKD 85
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSirfdgrditglpphERARAG--IGYVPEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 86 VRGNVEDG--VREALDALERLDQVFAEyadpdadFDALaKEQeklesiihawdahnlnnqleiaadalnlpaWDADVTKL 163
Cdd:cd03224 92 VEENLLLGayARRRAKRKARLERVYEL-------FPRL-KER------------------------------RKQLAGTL 133
|
170 180
....*....|....*....|....*..
gi 491208697 164 SGGERRRVALCRLLLSKPDMLLLDEPT 190
Cdd:cd03224 134 SGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
324-499 |
6.11e-15 |
|
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: 77.45 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSF--DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK----------VAY 390
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdGHDLAdytlaslrrqVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 391 VGQirDTLDNNKTVWEEVSGGlDILKVGDYEI---ASRAYIGRF---NFKGQDQQkrVGE----LSGGERNRLQLAKILQ 460
Cdd:TIGR02203 411 VSQ--DVVLFNDTIANNIAYG-RTEQADRAEIeraLAAAYAQDFvdkLPLGLDTP--IGEngvlLSGGQRQRLAIARALL 485
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491208697 461 QGANVILLDEPSNDLDIETLRALEDAI-LVFPG-TVMVVSH 499
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALeRLMQGrTTLVIAH 526
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
325-499 |
6.25e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.26 E-value: 6.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVKVAYVgqiRDTLDnnkt 403
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMRFAST---TAALA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 404 vweevsGGLDILK-----VGDYEIASRAYIGRFNFKG------------QDQQKRVGE----------LSGGERNRLQLA 456
Cdd:PRK11288 79 ------AGVAIIYqelhlVPEMTVAENLYLGQLPHKGgivnrrllnyeaREQLEHLGVdidpdtplkyLSIGQRQMVEIA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491208697 457 KILQQGANVILLDEPSNDL---DIETL----RALEDAilvfpGTVMV-VSH 499
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLsarEIEQLfrviRELRAE-----GRVILyVSH 198
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-477 |
7.07e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.40 E-value: 7.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------ARAQPGI--KIG-YL-EQEPPLDPTKDVR 87
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTleiggnpcARLTPAKahQLGiYLvPQEPLLFPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNVEDGVREALDALERLDQVFAEyadpdadfdalakeqeklesiihawdahnLNNQLEIAADALNLpawdaDVtklsgGE 167
Cdd:PRK15439 105 ENILFGLPKRQASMQKMKQLLAA-----------------------------LGCQLDLDSSAGSL-----EV-----AD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 168 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWL---ERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGHgIPYQGNY 244
Cdd:PRK15439 146 RQIVEILRGLMRDSRILILDEPTASLTPAETERLfsrIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGT-IALSGKT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 245 SSWL----------EQKNARLEQEQKQeesfakalkkeleWVrsnakgqqkknkarmerfeELNSKEFQQRNETseiyip 314
Cdd:PRK15439 225 ADLStddiiqaitpAAREKSLSASQKL-------------WL-------------------ELPGNRRQQAAGA------ 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 315 pgPRLgnKVVEVEGisksfDGrvlYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGE------SVK- 387
Cdd:PRK15439 267 --PVL--TVEDLTG-----EG---FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGkeinalSTAq 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 388 -----VAYVGQIRDT----LD------------NNKTVWEEVSggldilkvgdyeiASRAYIGRF----NFKGQDQQKRV 442
Cdd:PRK15439 335 rlargLVYLPEDRQSsglyLDaplawnvcalthNRRGFWIKPA-------------RENAVLERYrralNIKFNHAEQAA 401
|
490 500 510
....*....|....*....|....*....|....*
gi 491208697 443 GELSGGERNRLQLAKILQQGANVILLDEPSNDLDI 477
Cdd:PRK15439 402 RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-270 |
7.16e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 74.28 E-value: 7.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGVDKDFSGEARAQPGI----KIGYLEQEPPLDP 82
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprsgtlniAGNHFDFSKTPSDKAIRelrrNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 83 TKDVRGN-VEDGVREAldalerldqvfaeyadpdadfdALAKEQEKLESiihawDAHNLNNQLEIAADALNLpawdadvt 161
Cdd:PRK11124 96 HLTVQQNlIEAPCRVL----------------------GLSKDQALARA-----EKLLERLRLKPYADRFPL-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGT-I--VAITHDRYFLDNVAEWILELDRGHgI 238
Cdd:PRK11124 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgItqVIVTHEVEVARKTASRVVYMENGH-I 219
|
250 260 270
....*....|....*....|....*....|..
gi 491208697 239 PYQGNYSSWleqknarleqEQKQEESFAKALK 270
Cdd:PRK11124 220 VEQGDASCF----------TQPQTEAFKNYLS 241
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-253 |
9.70e-15 |
|
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: 73.73 E-value: 9.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKST----LLR---------IMAGVD-KDFSGEA-RAQpgikIGYLEQEPPLD 81
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTvvslLERfydptsgeiLLDGVDiRDLNLRWlRSQ----IGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 82 PTKdVRGNVEdgvrealdalerldqvfaeYADPDAdfdalakEQEKLESIIHAWDAHNLnnqleIAadalNLP-AWDADV 160
Cdd:cd03249 90 DGT-IAENIR-------------------YGKPDA-------TDEEVEEAAKKANIHDF-----IM----SLPdGYDTLV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 161 ----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDFpgTIVAITHdRyfLDNV--AEWIL 230
Cdd:cd03249 134 gergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESeklvQEALDRAMKGR--TTIVIAH-R--LSTIrnADLIA 208
|
250 260
....*....|....*....|...
gi 491208697 231 ELDRGHgIPYQGNYSSWLEQKNA 253
Cdd:cd03249 209 VLQNGQ-VVEQGTHDELMAQKGV 230
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-218 |
9.85e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 74.38 E-value: 9.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR--AQPgikigyLEQEPPLDPTKdVRG------- 88
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlnGRP------LAAWSPWELAR-RRAvlpqhss 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 89 -----NVEDGVREALDAlerldqvfaeYADPDADFDALAkeQEKLEsiihawdahnlnnqleiAADALNLpaWDADVTKL 163
Cdd:COG4559 86 lafpfTVEEVVALGRAP----------HGSSAAQDRQIV--REALA-----------------LVGLAHL--AGRSYQTL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 164 SGGERRRVALCRLL--LSKPDM-----LLLDEPTNHLDaesVSW---LERFLKDF---PGTIVAITHD 218
Cdd:COG4559 135 SGGEQQRVQLARVLaqLWEPVDggprwLFLDEPTSALD---LAHqhaVLRLARQLarrGGGVVAVLHD 199
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-235 |
1.03e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.34 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIGYLE---------------QEPP-- 79
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKLNraqrkafrrdiqmvfQDSIsa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 80 LDPTKDVRgnveDGVREALDALERLDQVfaeyadpdadfDALAKEQEKLEsiihawdahnlnnqleiaadALNLPAWDAD 159
Cdd:PRK10419 102 VNPRKTVR----EIIREPLRHLLSLDKA-----------ERLARASEMLR--------------------AVDLDDSVLD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 160 --VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELD 233
Cdd:PRK10419 147 krPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMD 226
|
..
gi 491208697 234 RG 235
Cdd:PRK10419 227 NG 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-218 |
1.08e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 73.64 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 25 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFSGEARAQPGIKIgyLEQEPPLDPTKDVRGNVEDG 93
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFlppdsgrilwnGQDLTALPPAERPVSM--LFQENNLFPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 94 VREALdaleRLDqvfaeyadpdadfdalAKEQEKLESIIHawdahnlnnQLEIAADALNLPAwdadvtKLSGGERRRVAL 173
Cdd:COG3840 96 LRPGL----KLT----------------AEQRAQVEQALE---------RVGLAGLLDRLPG------QLSGGQRQRVAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491208697 174 CRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHD 218
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-255 |
1.09e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.59 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIgyleqeppLDPTKDVRGnvedgVR-EA- 97
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVD-GLKV--------NDPKVDERL-----IRqEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 98 -----------LDALERLdqVFAeyadPDADFDALAKEQEKLesiihawdAHNLNNQLEIAADALNLPAwdadvtKLSGG 166
Cdd:PRK09493 81 mvfqqfylfphLTALENV--MFG----PLRVRGASKEEAEKQ--------ARELLAKVGLAERAHHYPS------ELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 167 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHDRYFLDNVAEWILELDRGHgIPYQGN 243
Cdd:PRK09493 141 QQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGR-IAEDGD 219
|
250
....*....|...
gi 491208697 244 YSSWLEQK-NARL 255
Cdd:PRK09493 220 PQVLIKNPpSQRL 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-235 |
1.37e-14 |
|
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: 74.07 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIGYLEQEPPLDPTKDV-------------R 87
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFR-GQDLYQLDRKQRRAFRRDVqlvfqdspsavnpR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNVEDGVREALDALERLDqvfaeyadpdadfdalakEQEKLESIIHAWDAHNLNnqleiAADALNLPAwdadvtKLSGGE 167
Cdd:TIGR02769 105 MTVRQIIGEPLRHLTSLD------------------ESEQKARIAELLDMVGLR-----SEDADKLPR------QLSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 168 RRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRG 235
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDmvlqAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
325-489 |
1.45e-14 |
|
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: 72.85 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDG-RVLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK-----------VAYV 391
Cdd:cd03224 2 EVENLNAGYGKsQIL-FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdGRDITglppheraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 392 GQIRDTLDnNKTVWEE-VSGGLDILKVGDYEIASRAYiGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDE 470
Cdd:cd03224 81 PEGRRIFP-ELTVEENlLLGAYARRRAKRKARLERVY-ELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180
....*....|....*....|....*....
gi 491208697 471 PSNDL----------DIETLRALEDAILV 489
Cdd:cd03224 159 PSEGLapkiveeifeAIRELRDEGVTILL 187
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
323-512 |
1.70e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 76.68 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGR----VLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV----------K 387
Cdd:TIGR00958 478 LIEFQDVSFSYPNRpdvpVL-KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLdGVPLvqydhhylhrQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 388 VAYVGQirDTLDNNKTVWEEVSGGLDilKVGDYEIASRA-------YIGRFNfkgQDQQKRVGE----LSGGERNRLQLA 456
Cdd:TIGR00958 557 VALVGQ--EPVLFSGSVRENIAYGLT--DTPDEEIMAAAkaanahdFIMEFP---NGYDTEVGEkgsqLSGGQKQRIAIA 629
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 457 KILQQGANVILLDEPSNDLDIETLRALEDAILVFPGTVMVVSHdRWFLDRIATHIL 512
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH-RLSTVERADQIL 684
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
324-516 |
1.88e-14 |
|
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: 72.44 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVL-YENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV------KVAYVGQ-- 393
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYLRRki 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 394 ---IRDT-LDNNKTVWEEVSGGLDILKVGDYEIASR--AYIGRFNFKGQdQQKRVGELSGGERNRLQLAKILQQGANVIL 467
Cdd:cd03292 81 gvvFQDFrLLPDRNVYENVAFALEVTGVPPREIRKRvpAALELVGLSHK-HRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 468 LDEPSNDLDIETLRALEDailVFPG------TVMVVSHDRWFLDRIATHILSFEN 516
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMN---LLKKinkagtTVVVATHAKELVDTTRHRVIALER 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-235 |
1.92e-14 |
|
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: 72.12 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKDfSGEARAQPGIkiGYLEQEPPLDPTKdVRGNVedgvreald 99
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKL-SGSVSVPGSI--AYVSQEPWIQNGT-IRENI--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 100 alerldqVFAEyadpdaDFDalakeQEKLESIIHAwdahnlnNQLEiaADALNLPawDADVTK-------LSGGERRRVA 172
Cdd:cd03250 87 -------LFGK------PFD-----EERYEKVIKA-------CALE--PDLEILP--DGDLTEigekginLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 173 LCRLLLSKPDMLLLDEPTNHLDAESVSWL-ER----FLKDfPGTIVAITHDRYFLDNvAEWILELDRG 235
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIfENcilgLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-218 |
2.08e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.27 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--------VD------KDFSGEARAQpgiKIGYLEQEPPLD-P 82
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGelspdsgeVRlngrplADWSPAELAR---RRAVLPQHSSLSfP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 83 TkdvrgNVEDGVRealdaLERLDQVFAEYADPDADFDALAkeqeklesiihawdahnlnnqleiAADALNLPawDADVTK 162
Cdd:PRK13548 91 F-----TVEEVVA-----MGRAPHGLSRAEDDALVAAALA------------------------QVDLAHLA--GRDYPQ 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 163 LSGGERRRVALCRLL--LSKPDM----LLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHD 218
Cdd:PRK13548 135 LSGGEQQRVQLARVLaqLWEPDGpprwLLLDEPTSALDlahqHHVLRLARQLAHERGLAVIVVLHD 200
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-235 |
2.10e-14 |
|
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: 72.85 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------------ARAQPGIkiGYLEQEPPLDPTKDVR 87
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSvlfdgeditglpphEIARLGI--GRTFQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNVedgvREALDALERLDQVFAEYADPDADFDALAKEqeklesiihawdahnlnnqleiAADALNL-PAWDADVTKLSGG 166
Cdd:cd03219 94 ENV----MVAAQARTGSGLLLARARREEREARERAEE----------------------LLERVGLaDLADRPAGELSYG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 167 ERRRVALCRLLLSKPDMLLLDEPT---NHLDAESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRG 235
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
334-499 |
2.30e-14 |
|
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: 72.65 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 334 DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV----------KVAYVGQirDTLDNNK 402
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVrdytlaslrrQIGLVSQ--DVFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 403 TVWEEVSGGLDILKVGDYEIASRA-----YIGRFNfKGQDQQkrVGE----LSGGERNRLQLAKILQQGANVILLDEPSN 473
Cdd:cd03251 91 TVAENIAYGRPGATREEVEEAARAanaheFIMELP-EGYDTV--IGErgvkLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180
....*....|....*....|....*...
gi 491208697 474 DLDIETLRALEDAI--LVFPGTVMVVSH 499
Cdd:cd03251 168 ALDTESERLVQAALerLMKNRTTFVIAH 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
323-476 |
2.69e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.60 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLgESVKVAYV-GQIRD----- 396
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML-DGQDITHVpAENRHvntvf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 397 ---TLDNNKTVWEEVSGGLDILKVGDYEIASR-----AYIGRFNFKgqdqQKRVGELSGGERNRLQLAKILQQGANVILL 468
Cdd:PRK09452 93 qsyALFPHMTVFENVAFGLRMQKTPAAEITPRvmealRMVQLEEFA----QRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
....*...
gi 491208697 469 DEPSNDLD 476
Cdd:PRK09452 169 DESLSALD 176
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-235 |
2.75e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 73.30 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEA--RAQPGIKigyleqepplDPTKDVRGNVedgvre 96
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVliRGEPITK----------ENIREVRKFV------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 97 ALDALERLDQVFAEYADPDADFDAlakeqeklesIIHAWDAHNLNNQLEIAADALNLPAWDADVTK-LSGGERRRVALCR 175
Cdd:PRK13652 81 GLVFQNPDDQIFSPTVEQDIAFGP----------INLGLDEETVAHRVSSALHMLGLEELRDRVPHhLSGGEKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 176 LLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG----TIVAITHDRYFLDNVAEWILELDRG 235
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDKG 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
323-487 |
2.81e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.12 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFR----MMTGEQQPDTGTVTLGESVKVA--YVGQIRD 396
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRTVQREgrLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 397 T------------LDNNKTVWEEVSGGL--------DILKVGDYEIASRAY-----IGRFNFKGQdqqkRVGELSGGERN 451
Cdd:PRK09984 84 SrantgyifqqfnLVNRLSVLENVLIGAlgstpfwrTCFSWFTREQKQRALqaltrVGMVHFAHQ----RVSTLSGGQQQ 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 491208697 452 RLQLAKILQQGANVILLDEPSNDLDIETLRALEDAI 487
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTL 195
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-235 |
3.24e-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: 72.08 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDkdfSGE------------ARAQP----GIK---IGYLEQ--- 76
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylPD---SGSilvrhdggwvdlAQASPreilALRrrtIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 77 EPPLDPTKDVrgnvedgVREALDALErldqvfaeyADPDAdfdALAKEQEKLEsiihawdahnlnnqleiaadALNLPA- 155
Cdd:COG4778 104 VIPRVSALDV-------VAEPLLERG---------VDREE---ARARARELLA--------------------RLNLPEr 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 156 -WDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERfLKDFPGTIVAITHDRYFLDNVAEWIL 230
Cdd:COG4778 145 lWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEE-AKARGTAIIGIFHDEEVREAVADRVV 223
|
....*
gi 491208697 231 ELDRG 235
Cdd:COG4778 224 DVTPF 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
327-476 |
3.86e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.23 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 327 EGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGES------------VKVAYVGQi 394
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararRGIGYLPQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 RDTLDNNKTVWEEVSGGLDILK-VGDYEIASRAYIGRFNFKGQDQQKRVGE-LSGGERNRLQLAKILQQGANVILLDEPS 472
Cdd:PRK10895 86 EASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQsLSGGERRRVEIARALAANPKFILLDEPF 165
|
....
gi 491208697 473 NDLD 476
Cdd:PRK10895 166 AGVD 169
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-195 |
3.89e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 72.59 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 7 TMNRVSKMVPPKRE---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR------AQPGIKIGYLEQE 77
Cdd:COG4525 5 TVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITldgvpvTGPGADRGVVFQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 78 PPLDPTKDVRGNVEDGVREA-LDALERLDQVfaeyadpdadfdalakeQEKLESIihawdahnlnnQLEIAADAlnlPAW 156
Cdd:COG4525 85 DALLPWLNVLDNVAFGLRLRgVPKAERRARA-----------------EELLALV-----------GLADFARR---RIW 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 491208697 157 dadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA 195
Cdd:COG4525 134 -----QLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-251 |
3.90e-14 |
|
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: 71.88 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD-KDFS-GEARAQpgikIGYLEQEPPLdp 82
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPrfydvdsgrilidGHDvRDYTlASLRRQ----IGLVSQDVFL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 83 tkdVRGNVEDGVRealdalerldqvfaeYADPDADfdalakeQEKLESIIHAWDAHNLNNQLEiaadalnlPAWDADV-- 160
Cdd:cd03251 88 ---FNDTVAENIA---------------YGRPGAT-------REEVEEAARAANAHEFIMELP--------EGYDTVIge 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 161 --TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDfpGTIVAITHDRYFLDNvAEWILELDR 234
Cdd:cd03251 135 rgVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESerlvQAALERLMKN--RTTFVIAHRLSTIEN-ADRIVVLED 211
|
250
....*....|....*..
gi 491208697 235 GhGIPYQGNYSSWLEQK 251
Cdd:cd03251 212 G-KIVERGTHEELLAQG 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
322-519 |
4.29e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 72.33 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 322 KVVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV------KVAYVGQI 394
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLrGQHIeglpghQIARMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 RdTLDN-----NKTVWE--------EVSGGL--DILKVGDYEIASRAYIGRFNF------KGQDQQKRVGELSGGERNRL 453
Cdd:PRK11300 84 R-TFQHvrlfrEMTVIEnllvaqhqQLKTGLfsGLLKTPAFRRAESEALDRAATwlervgLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 454 QLAKILQQGANVILLDEPSNDLDIETLRALEDAILV----FPGTVMVVSHDRWFLDRIATHILSFENEQP 519
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAElrneHNVTVLLIEHDMKLVMGISDRIYVVNQGTP 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-242 |
5.16e-14 |
|
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: 71.53 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 3 QYIYTMNRVS---KMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD---FSGE--------ARAQPG 68
Cdd:cd03234 1 QRVLPWWDVGlkaKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQilfngqprKPDQFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 69 IKIGYLEQEPPLDPTKDVRGNV------------EDGVREALDALERLDQVfaeyADPDAdfdalakeqeklesiihawd 136
Cdd:cd03234 81 KCVAYVRQDDILLPGLTVRETLtytailrlprksSDAIRKKRVEDVLLRDL----ALTRI-------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 137 AHNLnnqleiaadalnlpawdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFP--GTIVA 214
Cdd:cd03234 137 GGNL-------------------VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLArrNRIVI 197
|
250 260 270
....*....|....*....|....*....|....
gi 491208697 215 IT-H----DRY-FLDNvaewILELDRGhGIPYQG 242
Cdd:cd03234 198 LTiHqprsDLFrLFDR----ILLLSSG-EIVYSG 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
324-499 |
5.40e-14 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 71.49 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFD-GRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL----GESV-------KVAYV 391
Cdd:cd03254 3 IEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgidIRDIsrkslrsMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 392 GQirDTLDNNKTVWEEVSGGLDILKVGDYEIASRA----YIGRFNFKGQDQQkrVGE----LSGGERNRLQLAKILQQGA 463
Cdd:cd03254 83 LQ--DTFLFSGTIMENIRLGRPNATDEEVIEAAKEagahDFIMKLPNGYDTV--LGEnggnLSQGERQLLAIARAMLRDP 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 491208697 464 NVILLDEPSNDLDIETLRALEDAIL-VFPG-TVMVVSH 499
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEkLMKGrTSIIIAH 196
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-252 |
5.59e-14 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 72.48 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 4 YIYTMNrvskmVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEaraqpgIKIG--YLEQEPPLD 81
Cdd:TIGR04521 8 YIYQPG-----TPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGT------VTIDgrDITAKKKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 82 pTKDVRGNV-------EDgvrealdalerldQVFAE--YAD----------PDADFDALAKEqeklesiihawdahnlnn 142
Cdd:TIGR04521 77 -LKDLRKKVglvfqfpEH-------------QLFEEtvYKDiafgpknlglSEEEAEERVKE------------------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 143 qleiAADALNLPA--WDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV----SWLERFLKDFPGTIVAIT 216
Cdd:TIGR04521 125 ----ALELVGLDEeyLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRkeilDLFKRLHKEKGLTVILVT 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 491208697 217 HDryfLDNVAEW---ILELDRG----HGIPYQ-GNYSSWLEQKN 252
Cdd:TIGR04521 201 HS---MEDVAEYadrVIVMHKGkivlDGTPREvFSDVDELEKIG 241
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
24-235 |
5.98e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 73.72 E-value: 5.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 24 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------ARAQPGIK-IGYLEQEPPLDPTKDVRGNVEDGV 94
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQimldgvdlSHVPPYQRpINMMFQSYALFPHMTVEQNIAFGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 95 REalDALERldqvfAEYADPDADFDALAKEQEKLESIIHawdahnlnnqleiaadalnlpawdadvtKLSGGERRRVALC 174
Cdd:PRK11607 117 KQ--DKLPK-----AEIASRVNEMLGLVHMQEFAKRKPH----------------------------QLSGGQRQRVALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 175 RLLLSKPDMLLLDEPTNHLDA--------ESVSWLERflkdFPGTIVAITHDRYFLDNVAEWILELDRG 235
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKklrdrmqlEVVDILER----VGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
18-223 |
7.34e-14 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 71.52 E-value: 7.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK----------------DFSGEARAQPGIKIGYleQEPPld 81
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyevtsgtilfkgqdllELEPDERARAGLFLAF--QYPE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 82 ptkDVRG-NVEDGVREALDALERLDQvfaEYADPDADFDALAKEQEKLESIIHAWDAHNLNnqleiaadalnlpawdadv 160
Cdd:TIGR01978 88 ---EIPGvSNLEFLRSALNARRSARG---EEPLDLLDFEKLLKEKLALLDMDEEFLNRSVN------------------- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 161 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV----SWLERfLKDFPGTIVAITHDRYFLD 223
Cdd:TIGR01978 143 EGFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALkivaEGINR-LREPDRSFLIITHYQRLLN 208
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
22-235 |
7.47e-14 |
|
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: 71.61 E-value: 7.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------------ARAQPGIKIGYleQEPPLDPTKDVR 87
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRilfdgrditglpphRIARLGIARTF--QNPRLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNVEDGV-----REALDALERLDQVFAEYADPDADFDALakeqekLEsiihawdahnlnnQLEIAADAlnlpawDADVTK 162
Cdd:COG0411 98 ENVLVAAharlgRGLLAALLRLPRARREEREARERAEEL------LE-------------RVGLADRA------DEPAGN 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 163 LSGGERRRVALCRLLLSKPDMLLLDEPT---NHLDAESVSWLERFLKDFPG-TIVAITHDRYFLDNVAEWILELDRG 235
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFG 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-236 |
9.02e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.60 E-value: 9.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 37 VLGLNGAGKSTLLRIMAGVDKDFSGEAR--------AQPGI-------KIGYLEQEPPLDPTKDVRGNVEDGVREALDAL 101
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVlngrvlfdAEKGIclppekrRIGYVFQDARLFPHYKVRGNLRYGMAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 102 erldqvfaeyadpdadFDALAKeqekLESIIHAWDahnlnnqleiaadalNLPAwdadvtKLSGGERRRVALCRLLLSKP 181
Cdd:PRK11144 109 ----------------FDKIVA----LLGIEPLLD---------------RYPG------SLSGGEKQRVAIGRALLTAP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 182 DMLLLDEPTNHLDA----ESVSWLERFLKDFPGTIVAITHDryfLDNV---AEWILELDRGH 236
Cdd:PRK11144 148 ELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHS---LDEIlrlADRVVVLEQGK 206
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
342-516 |
9.61e-14 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 70.21 E-value: 9.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 342 LSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGEsVKVAYVGQIRDTL-----DNNK----TVWEEV---- 408
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-VDVTAAPPADRPVsmlfqENNLfahlTVEQNVglgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 409 SGGLDILKVGDYEIASRAyiGRFNFKGQDQqKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDiETLRA-LEDAI 487
Cdd:cd03298 96 SPGLKLTAEDRQAIEVAL--ARVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD-PALRAeMLDLV 171
|
170 180 190
....*....|....*....|....*....|...
gi 491208697 488 LVFPG----TVMVVSHDRWFLDRIATHILSFEN 516
Cdd:cd03298 172 LDLHAetkmTVLMVTHQPEDAKRLAQRVVFLDN 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
21-217 |
9.76e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 70.39 E-value: 9.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR-------AQPGIKIGYLEQEPPLDPtkDVRgnvedg 93
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldIAARNRIGYLPEERGLYP--KMK------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 94 VREALDALERLDQVFAEYADPDADfdalakeqEKLESiihawdahnlnnqLEIAadalnlPAWDADVTKLSGGERRRVAL 173
Cdd:cd03269 87 VIDQLVYLAQLKGLKKEEARRRID--------EWLER-------------LELS------EYANKRVEELSKGNQQKVQF 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491208697 174 CRLLLSKPDMLLLDEPTNHLDAESVSWLE---RFLKDFPGTIVAITH 217
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKdviRELARAGKTVILSTH 186
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-218 |
9.91e-14 |
|
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: 70.36 E-value: 9.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------ARAQPGIK-IGYLEQEPPLDPTKDVR 87
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRiyiggrdvTDLPPKDRdIAMVFQNYALYPHMTVY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNVEDGVRealdaLERLdqvfaeyadPDADFDALAKEQEKLESIIHAWDAHnlnnqleiaadalnlpawdadVTKLSGGE 167
Cdd:cd03301 91 DNIAFGLK-----LRKV---------PKDEIDERVREVAELLQIEHLLDRK---------------------PKQLSGGQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 168 RRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVSWLERFLKDFPGTIVAITHD 218
Cdd:cd03301 136 RQRVALGRAIVREPKVFLMDEPLSNLDAklrvQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
230-297 |
1.17e-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: 66.44 E-value: 1.17e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 230 LELDRGHGIPYQGNYSSWLEQKNARLEQEQKQEESFAKALKKELEWVRSN-AKGQ-QKKNKARMERFEEL 297
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFrAKASkAKQAQSRIKALEKM 70
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
326-500 |
1.35e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.73 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 326 VEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTV-------------TLGESVKV---- 388
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqlrdlyALSEAERRrllr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 389 ---AYVGQ-IRDTLDNNktvweeVSGGLDI----LKVGDyeiasRAYiGRFNFKGQDQQKRV-----------GELSGGE 449
Cdd:PRK11701 89 tewGFVHQhPRDGLRMQ------VSAGGNIgerlMAVGA-----RHY-GDIRATAGDWLERVeidaariddlpTTFSGGM 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 450 RNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAI--LV--FPGTVMVVSHD 500
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVreLGLAVVIVTHD 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-220 |
1.61e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.43 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE------------ARaQPGIKIGYLEQEPPLDPTKD 85
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTvflgdkpismlsSR-QLARRLALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 86 VRGNVEDGVREALDALERLDQvfaeyadpdadfdalaKEQEKLESIIHawdahnlnnQLEIAADAlnlpawDADVTKLSG 165
Cdd:PRK11231 93 VRELVAYGRSPWLSLWGRLSA----------------EDNARVNQAME---------QTRINHLA------DRRLTDLSG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 166 GERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSwLERFLKDFPGTIVAITHD-----RY 220
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDinhqVELMR-LMRELNTQGKTVVTVLHDlnqasRY 204
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
324-501 |
1.98e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 71.65 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV--------KVAYVGQi 394
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhGTDVsrlhardrKVGFVFQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 RDTLDNNKTVWEEVSGGLDILKvgDYEIASRAYIGRFNFKGQD--QQKRVGE-----LSGGERNRLQLAKILQQGANVIL 467
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVLP--RRERPNAAAIKAKVTQLLEmvQLAHLADrypaqLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491208697 468 LDEPSNDLDIET-------LRALEDAiLVFpgTVMVVSHDR 501
Cdd:PRK10851 160 LDEPFGALDAQVrkelrrwLRQLHEE-LKF--TSVFVTHDQ 197
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
319-500 |
2.03e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.81 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 319 LGNKVVEVEGISKSFDGRVLY--ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLG------ESV---- 386
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYalKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlseETVwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 387 -KVAYVGQIRDTLDNNKTVWEEVSGGLDILKVGDYEIASRAyigrfnfkgQDQQKRVG----------ELSGGERNRLQL 455
Cdd:PRK13635 81 rQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERV---------DQALRQVGmedflnrephRLSGGQKQRVAI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491208697 456 AKILQQGANVILLDEPSNDLD-------IETLRALEDAILVfpgTVMVVSHD 500
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDprgrrevLETVRQLKEQKGI---TVLSITHD 200
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
324-479 |
2.07e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 71.65 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGR-----VLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVKVAYVGQIRDT 397
Cdd:COG1135 2 IELENLSKTFPTKggpvtAL-DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 ------------LDNNKTVWEEVSGGLDILKVgdyeiaSRAYIgrfnfkgqdqQKRVGE-----------------LSGG 448
Cdd:COG1135 81 rrkigmifqhfnLLSSRTVAENVALPLEIAGV------PKAEI----------RKRVAEllelvglsdkadaypsqLSGG 144
|
170 180 190
....*....|....*....|....*....|....
gi 491208697 449 ERNRLQLAKILqqgAN---VILLDEPSNDLDIET 479
Cdd:COG1135 145 QKQRVGIARAL---ANnpkVLLCDEATSALDPET 175
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
323-479 |
2.24e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVT-LGESVKV--------AYVGQ 393
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFngpkssqeAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 394 IRDTLD--NNKTVWEEV---------SGGLDILKVgdYEIASRaYIGRFNFKgQDQQKRVGELSGGERNRLQLAKILQQG 462
Cdd:PRK10762 84 IHQELNliPQLTIAENIflgrefvnrFGRIDWKKM--YAEADK-LLARLNLR-FSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170
....*....|....*...
gi 491208697 463 ANVILLDEPSNDL-DIET 479
Cdd:PRK10762 160 SKVIIMDEPTDALtDTET 177
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-217 |
2.38e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.99 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFSGEARaQPGIKIGYLEQEPPLDPTKDVRGN 89
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLthpdagsislcGEPVPSRAR-HARQRVGVVPQFDNLDPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 90 VedgvrealdalerldQVFAEYadpdadFDALAKEQEKLESIIhawdahnlnnqLEIAAdaLNLPAwDADVTKLSGGERR 169
Cdd:PRK13537 101 L---------------LVFGRY------FGLSAAAARALVPPL-----------LEFAK--LENKA-DAKVGELSGGMKR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491208697 170 RVALCRLLLSKPDMLLLDEPTNHLD--AESVSWlERF--LKDFPGTIVAITH 217
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDpqARHLMW-ERLrsLLARGKTILLTTH 196
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
323-515 |
3.12e-13 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 69.04 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGR----VLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV-----------K 387
Cdd:cd03248 11 IVKFQNVTFAYPTRpdtlVL-QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPisqyehkylhsK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 388 VAYVGQirDTLDNNKTVWEEVSGGLDILKVGDY-EIASRAYIGRFNFKGQDQ-QKRVGE----LSGGERNRLQLAKILQQ 461
Cdd:cd03248 90 VSLVGQ--EPVLFARSLQDNIAYGLQSCSFECVkEAAQKAHAHSFISELASGyDTEVGEkgsqLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 462 GANVILLDEPSNDLDIETLRALEDAILVFPG--TVMVVSHDRWFLDRiATHILSFE 515
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAHRLSTVER-ADQILVLD 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
321-501 |
3.17e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.97 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 321 NKVVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV----------KVA 389
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDIstlkpeiyrqQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 390 YVGQ----IRDTL-DNNKTVWEevsggldILKVGDYEIASRAYIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGAN 464
Cdd:PRK10247 85 YCAQtptlFGDTVyDNLIFPWQ-------IRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491208697 465 VILLDEPSNDLDIETLRALEDAI--LVFPGTVMV--VSHDR 501
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIhrYVREQNIAVlwVTHDK 198
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-197 |
3.30e-13 |
|
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: 69.07 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEA----------RAQPGIKIGYLEQEPPLDPTkdvrgnv 90
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdRKAARQSLGYCPQFDALFDE------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 91 edgvreaLDALERLdQVFAEyadpdadFDALAKEQEKLESiihawdahnlnnqlEIAADALNL-PAWDADVTKLSGGERR 169
Cdd:cd03263 90 -------LTVREHL-RFYAR-------LKGLPKSEIKEEV--------------ELLLRVLGLtDKANKRARTLSGGMKR 140
|
170 180
....*....|....*....|....*...
gi 491208697 170 RVALCRLLLSKPDMLLLDEPTNHLDAES 197
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-228 |
3.55e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 69.76 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRimagvdkDFSGEARAQPGiKIGYLEQEPPLDPTKDVRGNVedgvreALD 99
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLL-------HLNGIYLPQRG-RVKVMGREVNAENEKWVRSKV------GLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 100 ALERLDQVFAEYADPDADFDALAKEQEKLEsiihawdahnLNNQLEIAADALNLPAW-DADVTKLSGGERRRVALCRLLL 178
Cdd:PRK13647 85 FQDPDDQVFSSTVWDDVAFGPVNMGLDKDE----------VERRVEEALKAVRMWDFrDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491208697 179 SKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAiTHDryfLDNVAEW 228
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDprgqETLMEILDRLHNQGKTVIVA-THD---VDLAAEW 204
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-477 |
3.90e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.57 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKD-----FSGEARAQPGIK------IGYLEQEPPLDPTKDVRGN 89
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIyTRDagsilYLGKEVTFNGPKssqeagIGIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 90 VEDGvREALDALERLD--QVFAEyadpdADfDALAKeqeklesiihawdahnlnnqleiaadaLNLP-AWDADVTKLSGG 166
Cdd:PRK10762 100 IFLG-REFVNRFGRIDwkKMYAE-----AD-KLLAR---------------------------LNLRfSSDKLVGELSIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 167 ERRRVALCRLLLSKPDMLLLDEPTNHL-DAESVSWLE--RFLKDFPGTIVAITHDRYFLDNVAEWILELDRGHGIPyqgn 243
Cdd:PRK10762 146 EQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRviRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIA---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 244 ysswlEQKNARLEQEQKQEESFAKALKkelewvrsnakgqqkknkarmERFEELNskefqqrnetseiyIPPGPrlgnKV 323
Cdd:PRK10762 222 -----EREVADLTEDSLIEMMVGRKLE---------------------DQYPRLD--------------KAPGE----VR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSfdgRVlyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK-----------VAYV 391
Cdd:PRK10762 258 LKVDNLSGP---GV--NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdGHEVVtrspqdglangIVYI 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 392 GQIR--DTLDNNKTVWEEVS----------GGldILKVGDYEIASRAYIGRFNFKGQDQQKRVGELSGGERNRLQLAKIL 459
Cdd:PRK10762 333 SEDRkrDGLVLGMSVKENMSltalryfsraGG--SLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGL 410
|
490
....*....|....*...
gi 491208697 460 QQGANVILLDEPSNDLDI 477
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDV 428
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
325-472 |
4.01e-13 |
|
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: 68.86 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDG-RVLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK-----------VAYV 391
Cdd:COG0410 5 EVENLHAGYGGiHVL-HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdGEDITglpphriarlgIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 392 GQIRD---TLdnnkTVWEEvsggldiLKVGdyeiasrAYIGRFNFKGQDQQKRV---------------GELSGGERNRL 453
Cdd:COG0410 84 PEGRRifpSL----TVEEN-------LLLG-------AYARRDRAEVRADLERVyelfprlkerrrqraGTLSGGEQQML 145
|
170
....*....|....*....
gi 491208697 454 QLAKILQQGANVILLDEPS 472
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPS 164
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
20-219 |
5.04e-13 |
|
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: 68.53 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------------ARAQ-PGIKIGYLEQEPPLDPTK 84
Cdd:TIGR02211 19 RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEvlfngqslsklssnERAKlRNKKLGFIYQFHHLLPDF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 85 DVRGNVedgvreALDALERLDQVFaeyadpdadfDALAKEQEKLESIihawdahNLNNQLEIAAdalnlpawdadvTKLS 164
Cdd:TIGR02211 99 TALENV------AMPLLIGKKSVK----------EAKERAYEMLEKV-------GLEHRINHRP------------SELS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 165 GGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVSWLERFLKDFPGT-IVAITHDR 219
Cdd:TIGR02211 144 GGERQRVAIARALVNQPSLVLADEPTGNLDnnnAKIIFDLMLELNRELNTsFLVVTHDL 202
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
341-470 |
5.35e-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: 68.33 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 341 NLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLgeSVKVAYVGQIRDTLDNNKTVWEEVSGGLDILKVGDY 420
Cdd:cd03220 40 DVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV--RGRVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRK 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491208697 421 EIASR-AYIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDE 470
Cdd:cd03220 118 EIDEKiDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
321-386 |
6.03e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.57 E-value: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 321 NKVVEVEGISKSF-----DGRVLYE-----------------NLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTG 378
Cdd:COG1134 2 SSMIEVENVSKSYrlyhePSRSLKElllrrrrtrreefwalkDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
....*...
gi 491208697 379 TVTLGESV 386
Cdd:COG1134 82 RVEVNGRV 89
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-252 |
6.61e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.01 E-value: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-GVDKDfSGEARaqpgikigyleqeppLD--PTKDVRgnvEDGVREA 97
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQ-QGEIL---------------LNgqPIADYS---EAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 98 LDALERLDQVFAE-------YADPDADFDALAKEQEKLEsiihawdahnLNNQLEiAADALNlpAWDADVTK-LSGGERR 169
Cdd:PRK11160 416 ISVVSQRVHLFSAtlrdnllLAAPNASDEALIEVLQQVG----------LEKLLE-DDKGLN--AWLGEGGRqLSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 170 RVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDfpGTIVAITHDRYFLDNVAEWILeLDRGHGIPyQGNYS 245
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETerqiLELLAEHAQN--KTVLMITHRLTGLEQFDRICV-MDNGQIIE-QGTHQ 558
|
....*..
gi 491208697 246 SWLEQKN 252
Cdd:PRK11160 559 ELLAQQG 565
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-236 |
7.51e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 67.55 E-value: 7.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK----------------DFSGEARAQPGIKIGYleQEPPld 81
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyevtegeilfkgeditDLPPEERARLGIFLAF--QYPP-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 82 ptkDVRG-NVEDGVRealdalerldqvfaeyadpdadfdalakeqeklesiihawdahNLNnqleiaadalnlpawdadv 160
Cdd:cd03217 88 ---EIPGvKNADFLR-------------------------------------------YVN------------------- 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 161 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDF--PGT-IVAITHDRYFLDNVaewilELDRGH 236
Cdd:cd03217 103 EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreEGKsVLIITHYQRLLDYI-----KPDRVH 176
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
323-516 |
7.89e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 69.06 E-value: 7.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRV-LYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVKVAYVGQIRDTL-- 398
Cdd:PRK13652 3 LIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREVRKFVgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 399 -----DN---NKTVWEEVSGGLDILKVGDYEIASRAYIGRFNFKGQDQQKRV-GELSGGERNRLQLAKILQQGANVILLD 469
Cdd:PRK13652 83 vfqnpDDqifSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVpHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491208697 470 EPSNDLDIETLRALEDAILVFPG----TVMVVSHDRWFLDRIATHILSFEN 516
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDK 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
338-509 |
8.29e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.07 E-value: 8.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 338 LYENL----SFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQIR--------DTLDNNKTVW 405
Cdd:PRK10771 10 LYHHLpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRpvsmlfqeNNLFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 406 EEVSGGLDI-LKVGDY------EIASRAYIgrfnfkgQDQQKRV-GELSGGERNRLQLAKILQQGANVILLDEPSNDLD- 476
Cdd:PRK10771 90 QNIGLGLNPgLKLNAAqreklhAIARQMGI-------EDLLARLpGQLSGGQRQRVALARCLVREQPILLLDEPFSALDp 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 491208697 477 ---IETLRALEDAILVFPGTVMVVSHDrwfLD---RIAT 509
Cdd:PRK10771 163 alrQEMLTLVSQVCQERQLTLLMVSHS---LEdaaRIAP 198
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
324-499 |
8.44e-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: 67.19 E-value: 8.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTG--EQQPDTGTVTL-GESVK-------VAYVGQ 393
Cdd:cd03213 11 VTVKSSPSKSGKQLL-KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLInGRPLDkrsfrkiIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 394 iRDTLDNNKTVWE--EVSGGLdilkvgdyeiasrayigrfnfKGqdqqkrvgeLSGGERNRLQLAKILQQGANVILLDEP 471
Cdd:cd03213 90 -DDILHPTLTVREtlMFAAKL---------------------RG---------LSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 491208697 472 SNDLD-------IETLRALEDAilvfpG-TVMVVSH 499
Cdd:cd03213 139 TSGLDsssalqvMSLLRRLADT-----GrTIICSIH 169
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-64 |
8.62e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.18 E-value: 8.62e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR 64
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
322-475 |
9.11e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.58 E-value: 9.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 322 KVVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV------KVAY---VG 392
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkldhKLAAqlgIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 393 QIRDTLD--NNKTVWEEVS-GGLDILKVG-----DY-EIASRAYI--GRFNFKgQDQQKRVGELSGGERNRLQLAKILQQ 461
Cdd:PRK09700 84 IIYQELSviDELTVLENLYiGRHLTKKVCgvniiDWrEMRVRAAMmlLRVGLK-VDLDEKVANLSISHKQMLEIAKTLML 162
|
170
....*....|....
gi 491208697 462 GANVILLDEPSNDL 475
Cdd:PRK09700 163 DAKVIIMDEPTSSL 176
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-218 |
9.23e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.66 E-value: 9.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 5 IYTMNRVSKMVPpKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEA--RAQP---------GIKIGY 73
Cdd:PRK10575 11 TFALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIllDAQPleswsskafARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 74 LEQEPPLDPTKDVRGNVEDGVREALDALERLDqvfaeyadpdadfdalAKEQEKLESIIHAWDAHNLNNQLeiaadalnl 153
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVAIGRYPWHGALGRFG----------------AADREKVEEAISLVGLKPLAHRL--------- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 154 pawdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHD 218
Cdd:PRK10575 145 ------VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHRLSQERGLTVIAVLHD 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-259 |
1.06e-12 |
|
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: 67.90 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRI------------------MAGVDKDFsgeARAQpgikIGYLEQE 77
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLiqrfyvpengrvlvdghdLALADPAW---LRRQ----VGVVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 78 PPLdPTKDVRGNVedgvrealdalerldqvfaeyadpdadfdALAKEQEKLESIIHAW---DAHNLNNQLEIAADALnlp 154
Cdd:cd03252 85 NVL-FNRSIRDNI-----------------------------ALADPGMSMERVIEAAklaGAHDFISELPEGYDTI--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 155 aWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG--TIVAITHdRYFLDNVAEWILEL 232
Cdd:cd03252 132 -VGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAH-RLSTVKNADRIIVM 209
|
250 260
....*....|....*....|....*....
gi 491208697 233 DRGHgIPYQGNYSSWLEQKN--ARLEQEQ 259
Cdd:cd03252 210 EKGR-IVEQGSHDELLAENGlyAYLYQLQ 237
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-257 |
1.09e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.07 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGearaqpgiKIGYLEQEPPLDPTKDVRGNVEDgvREA 97
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEG--------SIVVNGQTINLVRDKDGQLKVAD--KNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 98 LDALE-RLDQVFAEYAdpdadfdaLAKEQEKLESIIHA-WDAHNLNNQL--EIAADALNLPAWDADV-----TKLSGGER 168
Cdd:PRK10619 87 LRLLRtRLTMVFQHFN--------LWSHMTVLENVMEApIQVLGLSKQEarERAVKYLAKVGIDERAqgkypVHLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 169 RRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFP---GTIVAITHDRYFLDNVAEWILELDRGHgIPYQGNYS 245
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGK-IEEEGAPE 237
|
250
....*....|...
gi 491208697 246 SWLEQ-KNARLEQ 257
Cdd:PRK10619 238 QLFGNpQSPRLQQ 250
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
321-500 |
1.21e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.22 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 321 NKVVEVEGISKSF-DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVT-LGESV----------KV 388
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvMGREVnaenekwvrsKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 389 AYVGQIRDTLDNNKTVWEEVSGGLDILKVGDYEIASRA-----YIGRFNFKgqdqQKRVGELSGGERNRLQLAKILQQGA 463
Cdd:PRK13647 82 GLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVeealkAVRMWDFR----DKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491208697 464 NVILLDEPSNDLD---IETLRALEDAILVFPGTVMVVSHD 500
Cdd:PRK13647 158 DVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-235 |
1.31e-12 |
|
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: 67.13 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMagvdKDFSGEaraqpgIKI-GYLEQEPPLdptKDVRGN------ 89
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGS------ILIdGVDISKIGL---HDLRSRisiipq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 90 ---VEDG-VREALDAlerldqvFAEYADpDADFDALakEQEKLESIIhawDAHNLNNQLEIAADALNLpawdadvtklSG 165
Cdd:cd03244 86 dpvLFSGtIRSNLDP-------FGEYSD-EELWQAL--ERVGLKEFV---ESLPGGLDTVVEEGGENL----------SV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 166 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKD-FPG-TIVAITHdRyfLDNVAEW--ILELDRG 235
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREaFKDcTVLTIAH-R--LDTIIDSdrILVLDKG 213
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
22-236 |
1.41e-12 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 68.10 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVL-GLNGAGKSTLLRIMA----GVDKDFSGEARAQPGIKIGYLEQEPPL----DPTKDVRGNVED 92
Cdd:COG3950 14 FEDLEIDFDNPPRLTVLvGENGSGKTTLLEAIAlalsGLLSRLDDVKFRKLLIRNGEFGDSAKLilyyGTSRLLLDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 93 GVREALDALERLDQVFAEYADPDADFDALAKEQEKLESIIHAWDAHNLNNQLEIAADALN--LPAWDA------------ 158
Cdd:COG3950 94 KLERLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVREALNklLPDFKDiridrdpgrlvi 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 159 --------DVTKLSGGERRRVALC-----RLLLSKPDM---------LLLDEPTNHLdaeSVSWLERFLKD----FPGT- 211
Cdd:COG3950 174 ldkngeelPLNQLSDGERSLLALVgdlarRLAELNPALenplegegiVLIDEIDLHL---HPKWQRRILPDlrkiFPNIq 250
|
250 260
....*....|....*....|....*.
gi 491208697 212 IVAITHDRYFLDNV-AEWILELDRGH 236
Cdd:COG3950 251 FIVTTHSPLILSSLeDEEVIVLERDE 276
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-218 |
1.46e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.56 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKDFSGEA-------RAQPGIKI----GYL--EQEPPLdptkdvrg 88
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEIllngrplSDWSAAELarhrAYLsqQQSPPF-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 89 nvedgvreALDALERLDQVFAEYADPDADFDALAKeqeklesiihawdahnLNNQLEIaADALNLPawdadVTKLSGGER 168
Cdd:COG4138 83 --------AMPVFQYLALHQPAGASSEAVEQLLAQ----------------LAEALGL-EDKLSRP-----LTQLSGGEW 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 169 RRVALCRLLL-----SKPD--MLLLDEPTNHLDAESVSWLERFLKDFP---GTIVAITHD 218
Cdd:COG4138 133 QRVRLAAVLLqvwptINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCqqgITVVMSSHD 192
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
323-476 |
1.55e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 68.18 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSF-DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK------------V 388
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIKydkksllevrktV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 389 AYVGQIRDTLDNNKTVWEEVSGGLDILKVGDYEIASRAyigrfnfkgQDQQKRVG----------ELSGGERNRLQLAKI 458
Cdd:PRK13639 81 GIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRV---------KEALKAVGmegfenkpphHLSGGQKKRVAIAGI 151
|
170
....*....|....*...
gi 491208697 459 LQQGANVILLDEPSNDLD 476
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLD 169
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
351-523 |
1.62e-12 |
|
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: 66.06 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 351 IVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLgESVKVAYVGQirdtldnnktvweevsggldilkvgdyeiasraYIgr 430
Cdd:cd03222 27 VIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVYKPQ---------------------------------YI-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 431 fnfkgqdqqkrvgELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAILVF----PGTVMVVSHDRWFLDR 506
Cdd:cd03222 71 -------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDY 137
|
170
....*....|....*..
gi 491208697 507 IATHILSFENEqPEFYT 523
Cdd:cd03222 138 LSDRIHVFEGE-PGVYG 153
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-217 |
1.85e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.70 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE---------ARAQPG-IKIGYLEQEPPLDPtkdvrgnv 90
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlgvpvpARARLArARIGVVPQFDNLDL-------- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 91 EDGVREALdalerldQVFAEYadpdadFDALAKEqekLESIIHAWdahnlnnqLEIAAdaLNLPAwDADVTKLSGGERRR 170
Cdd:PRK13536 128 EFTVRENL-------LVFGRY------FGMSTRE---IEAVIPSL--------LEFAR--LESKA-DARVSDLSGGMKRR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491208697 171 VALCRLLLSKPDMLLLDEPTNHLD--AESVSWlERF--LKDFPGTIVAITH 217
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDphARHLIW-ERLrsLLARGKTILLTTH 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
326-500 |
3.01e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.01 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 326 VEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGEsvkvAYVGQIRDT-------- 397
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT----APLAEAREDtrlmfqda 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 -LDNNKTVWEEVSGGLDilkvGDYEIASR---AYIGRFNfkgqdqqkRVGE----LSGGERNRLQLAKILQQGANVILLD 469
Cdd:PRK11247 91 rLLPWKKVIDNVGLGLK----GQWRDAALqalAAVGLAD--------RANEwpaaLSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190
....*....|....*....|....*....|....*
gi 491208697 470 EPSNDLD----IETLRALEDAILVFPGTVMVVSHD 500
Cdd:PRK11247 159 EPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
325-512 |
3.34e-12 |
|
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: 65.63 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 325 EVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGeqQPDTgTVTLGEsvkVAYVGQirDTLDnnKTV 404
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKY-EVTEGE---ILFKGE--DITD--LPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 405 WEEVSGGLDI----------LKVGDYEiasrayigRFNFKGqdqqkrvgeLSGGERNRLQLAKILQQGANVILLDEPSND 474
Cdd:cd03217 72 EERARLGIFLafqyppeipgVKNADFL--------RYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491208697 475 LDIETLRALEDAI--LVFPGT-VMVVSHDRWFLDRIAT---HIL 512
Cdd:cd03217 135 LDIDALRLVAEVInkLREEGKsVLIITHYQRLLDYIKPdrvHVL 178
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
327-516 |
3.37e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.93 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 327 EGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV----------KVAYVGQiR 395
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIqhyaskevarRIGLLAQ-N 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 396 DTLDNNKTVWEEVSGG-------LDILKVGDYEIASRAY--IGRFNFKGQDqqkrVGELSGGERNRLQLAKILQQGANVI 466
Cdd:PRK10253 90 ATTPGDITVQELVARGryphqplFTRWRKEDEEAVTKAMqaTGITHLADQS----VDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491208697 467 LLDEPSNDLD----IETLRALEDAILVFPGTVMVVSHDRWFLDRIATHILSFEN 516
Cdd:PRK10253 166 LLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALRE 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
323-500 |
3.69e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.42 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFdgRVL-----------------YE------NLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGT 379
Cdd:COG4586 1 IIEVENLSKTY--RVYekepglkgalkglfrreYReveavdDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 380 VT-LGESV---KVAYVGQI----------------RDTLDNNKTVweevsggldilkvgdYEIASRAY-------IGRFN 432
Cdd:COG4586 79 VRvLGYVPfkrRKEFARRIgvvfgqrsqlwwdlpaIDSFRLLKAI---------------YRIPDAEYkkrldelVELLD 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 433 FKGQ-DQQKRvgELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAIL-------VfpgTVMVVSHD 500
Cdd:COG4586 144 LGELlDTPVR--QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKeynrergT---TILLTSHD 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
288-512 |
4.97e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.30 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 288 KARMER---FEELNSKEFQQRNETSEIYIPPGPRLgnkvvEVEGIS-KSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKT 363
Cdd:COG4178 329 RATVDRlagFEEALEAADALPEAASRIETSEDGAL-----ALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 364 TLFRMMTGEQQPDTGTVTLGESVKVAYVGQ--------IRDTL----DNNKTVWEEVSGGLDILKVGDyeiasraYIGRF 431
Cdd:COG4178 404 TLLRAIAGLWPYGSGRIARPAGARVLFLPQrpylplgtLREALlypaTAEAFSDAELREALEAVGLGH-------LAERL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 432 nfkgqDQQKRVG-ELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAIL-VFPGTVMV-VSHdRWFLDRIA 508
Cdd:COG4178 477 -----DEEADWDqVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLReELPGTTVIsVGH-RSTLAAFH 550
|
....
gi 491208697 509 THIL 512
Cdd:COG4178 551 DRVL 554
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
334-500 |
5.20e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 66.02 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 334 DGRVLyeNLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQqPDTGTVTLGE-----------SVKVAYVGQiRDTLDNNK 402
Cdd:COG4138 9 AGRLG--PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGrplsdwsaaelARHRAYLSQ-QQSPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 403 TVWE----EVSGGLDILKVGD--YEIASRayigrfnFKGQDQQKR-VGELSGGERNRLQLAKILQQ-------GANVILL 468
Cdd:COG4138 85 PVFQylalHQPAGASSEAVEQllAQLAEA-------LGLEDKLSRpLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 491208697 469 DEPSNDLDIETLRALEDAILVFP---GTVMVVSHD 500
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELCqqgITVVMSSHD 192
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-227 |
5.74e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 66.67 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKDfSGEAR-------AQPGIKIGYLEQEPPLDPTKDvrgnvedg 93
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIlAPD-SGEVLwdgepldPEDRRRIGYLPEERGLYPKMK-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 94 VREALDALERLDQVfaeyadPDADfdalAKEQeklesiIHAWdahnlnnqleiaADALNLPAWDAD-VTKLSGGERRRVA 172
Cdd:COG4152 88 VGEQLVYLARLKGL------SKAE----AKRR------ADEW------------LERLGLGDRANKkVEELSKGNQQKVQ 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 173 LCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDF--PGTIVaI--THDryfLDNVAE 227
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGTTV-IfsSHQ---MELVEE 194
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
342-516 |
6.48e-12 |
|
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: 67.06 E-value: 6.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 342 LSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV---------------KVAYVGQiRDTLDNNKTVWE 406
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrRIGYVFQ-EARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 407 EVSGGLDILKVGDYEIASRAYIGRFNFkGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDI----ETLRA 482
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERVIELLGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEILPY 173
|
170 180 190
....*....|....*....|....*....|....
gi 491208697 483 LEDAILVFPGTVMVVSHDRWFLDRIATHILSFEN 516
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLED 207
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-190 |
6.73e-12 |
|
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: 65.39 E-value: 6.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSG--------------EARAQPGIkiGYLEQE----PPLd 81
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsirfdgeditglppHRIARLGI--GYVPEGrrifPSL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 82 pTkdVRGNVEDG---VREALDALERLDQVFAEyadpdadFDALAkeqEKLesiihawdahnlnNQLeiAADalnlpawda 158
Cdd:COG0410 94 -T--VEENLLLGayaRRDRAEVRADLERVYEL-------FPRLK---ERR-------------RQR--AGT--------- 136
|
170 180 190
....*....|....*....|....*....|..
gi 491208697 159 dvtkLSGGERRRVALCRLLLSKPDMLLLDEPT 190
Cdd:COG0410 137 ----LSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-194 |
8.38e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.99 E-value: 8.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 26 SLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR-----------AQPGIKIgyLEQEPPLDPTKDVRGNVEDGV 94
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTlngqdhtttppSRRPVSM--LFQENNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 95 REALdaleRLDqvfaeyadpdadfdalAKEQEKLESIihawdAHN--LNNQLEiaadalNLPAwdadvtKLSGGERRRVA 172
Cdd:PRK10771 97 NPGL----KLN----------------AAQREKLHAI-----ARQmgIEDLLA------RLPG------QLSGGQRQRVA 139
|
170 180
....*....|....*....|..
gi 491208697 173 LCRLLLSKPDMLLLDEPTNHLD 194
Cdd:PRK10771 140 LARCLVREQPILLLDEPFSALD 161
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
17-218 |
8.75e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.49 E-value: 8.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------DFSGEARAQPGIKIGYLEQEPPLDPTKDVRGNV 90
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 91 EDGVREA-LDALERLdqvfaeyadpdadfdALAKEQEKLESIihawdahnlnnqleiaADALNLPAWdadvtKLSGGERR 169
Cdd:PRK11248 92 AFGLQLAgVEKMQRL---------------EIAHQMLKKVGL----------------EGAEKRYIW-----QLSGGQRQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491208697 170 RVALCRLLLSKPDMLLLDEPTNHLDA----ESVSWLERFLKDFPGTIVAITHD 218
Cdd:PRK11248 136 RVGIARALAANPQLLLLDEPFGALDAftreQMQTLLLKLWQETGKQVLLITHD 188
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-241 |
9.75e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 66.41 E-value: 9.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIGyleqePPLDPTKDVRGNVEDGVREALDA 100
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG-DIYIG-----DKKNNHELITNPYSKKIKNFKEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 101 LERLDQVFA--EYA------DPDADFDALAKEQEKLESiiHAWDAHNLNNQleiaadALNLPAWDADVTKLSGGERRRVA 172
Cdd:PRK13631 115 RRRVSMVFQfpEYQlfkdtiEKDIMFGPVALGVKKSEA--KKLAKFYLNKM------GLDDSYLERSPFGLSGGQKRRVA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 173 LCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHDRYFLDNVAEWILELDRG----HGIPYQ 241
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMDKGkilkTGTPYE 262
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
21-218 |
1.02e-11 |
|
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: 64.95 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQ-------PGIK--IGYLEQEPPLDPTKDVRGNVE 91
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkditnlPPHKrpVNTVFQNYALFPHLTVFENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 92 DGVRealdaLERLDQvfaeyadpdADFDALAKEQEKLEsiihawdahnlnnQLEIAADAlnlpawdaDVTKLSGGERRRV 171
Cdd:cd03300 95 FGLR-----LKKLPK---------AEIKERVAEALDLV-------------QLEGYANR--------KPSQLSGGQQQRV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491208697 172 ALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG----TIVAITHD 218
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHD 190
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-228 |
1.14e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.88 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEaraqpgIKIGYlEQEPPLDPTKDVRGNVED--------- 92
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGT------IEWIF-KDEKNKKKTKEKEKVLEKlviqktrfk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 93 GVREALDALERLDQVF--AEYA------DPDADFDALAKEQEKLESiihawdahnlnnqLEIAADALNLPAWDADVTK-- 162
Cdd:PRK13651 96 KIKKIKEIRRRVGVVFqfAEYQlfeqtiEKDIIFGPVSMGVSKEEA-------------KKRAAKYIELVGLDESYLQrs 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 163 ---LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV-SWLERF--LKDFPGTIVAITHDryfLDNVAEW 228
Cdd:PRK13651 163 pfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVkEILEIFdnLNKQGKTIILVTHD---LDNVLEW 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-235 |
1.14e-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: 64.80 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE----ARAQPGIKIGYLE-------QEPPLDpTKD 85
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQvlldGKPISQYEHKYLHskvslvgQEPVLF-ARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 86 VRGNVEdgvrealdalerldqvfaeYADPDADFDALAKEQEKlesiihaWDAHNLNNQLEIAadalnlpaWDADV----T 161
Cdd:cd03248 104 LQDNIA-------------------YGLQSCSFECVKEAAQK-------AHAHSFISELASG--------YDTEVgekgS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG--TIVAITHdRYFLDNVAEWILELDRG 235
Cdd:cd03248 150 QLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH-RLSTVERADQILVLDGG 224
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-206 |
1.22e-11 |
|
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: 63.80 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--VDKDFSGEARA--QPGIK-----IGYLEQEPPLDPTKDvrg 88
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILIngRPLDKnfqrsTGYVEQQDVHSPNLT--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 89 nvedgVREALdalerldqvfaeyadpdaDFDALAKEqeklesiihawdahnlnnqleiaadalnlpawdadvtkLSGGER 168
Cdd:cd03232 96 -----VREAL------------------RFSALLRG--------------------------------------LSVEQR 114
|
170 180 190
....*....|....*....|....*....|....*...
gi 491208697 169 RRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLK 206
Cdd:cd03232 115 KRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-218 |
1.63e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.49 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKREI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAqpgikIGYleqepplDPTKDVRGNVED- 92
Cdd:COG4586 30 REYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV-----LGY-------VPFKRRKEFARRi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 93 ----GVRE-------ALDALERLDQVfaeYADPDADFDALAKEqeklesiihawdahnLNNQLEIaADALNLPawdadVT 161
Cdd:COG4586 98 gvvfGQRSqlwwdlpAIDSFRLLKAI---YRIPDAEYKKRLDE---------------LVELLDL-GELLDTP-----VR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKD----FPGTIVAITHD 218
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynreRGTTILLTSHD 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
324-499 |
1.76e-11 |
|
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: 64.43 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSF--DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVT-----LGESVKVAYVGQI-- 394
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLvdghdLALADPAWLRRQVgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 --RDTLDNNKTVWEEVS---GGLDILKVgdYEIASRAYIGRFNFK---GQDQQkrVGE----LSGGERNRLQLAKILQQG 462
Cdd:cd03252 81 vlQENVLFNRSIRDNIAladPGMSMERV--IEAAKLAGAHDFISElpeGYDTI--VGEqgagLSGGQRQRIAIARALIHN 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 491208697 463 ANVILLDEPSNDLDIETLRALEDAI--LVFPGTVMVVSH 499
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMhdICAGRTVIIIAH 195
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
20-236 |
1.76e-11 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 64.24 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVDKDFSGEARAQPGIKIGYLEQEPPLDPTKDV 86
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINlleepdsgtitvdGEDLTDSKKDINKLRRKVGMVFQQFNLFPHLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 RGNVEDG---VR-----EALD-ALERLDQV-FAEYADpdadfdalakeqeklesiihAWdahnlnnqleiaadalnlPAw 156
Cdd:COG1126 95 LENVTLApikVKkmskaEAEErAMELLERVgLADKAD--------------------AY------------------PA- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 157 dadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHDRYFLDNVAEWILELD 233
Cdd:COG1126 136 -----QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKegmTMVVVTHEMGFAREVADRVVFMD 210
|
...
gi 491208697 234 RGH 236
Cdd:COG1126 211 GGR 213
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-490 |
1.96e-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: 62.83 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 320 GNKVVEVEGISksFDGRVlyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK----------- 387
Cdd:cd03215 1 GEPVLEVRGLS--VKGAV--RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVTrrsprdairag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 388 VAYVGQIRdtldnnktvweeVSGGLdilkVGDYEIASRAYIGRFnfkgqdqqkrvgeLSGGERNRLQLAKILQQGANVIL 467
Cdd:cd03215 77 IAYVPEDR------------KREGL----VLDLSVAENIALSSL-------------LSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190
....*....|....*....|....*....|...
gi 491208697 468 LDEPSNDLDIET-------LRALED---AILVF 490
Cdd:cd03215 128 LDEPTRGVDVGAkaeiyrlIRELADagkAVLLI 160
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-223 |
2.00e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.32 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK----------------DFSGEARAQPGIkiGYLEQEPPldp 82
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyevtsgsilldgedilELSPDERARAGI--FLAFQYPV--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 83 tkDVRG-NVEDGVREALDALerldqvfAEYADPDADFDALAKEqeKLEsiihawdahnlnnQLEIAADALNLPAwdaDVt 161
Cdd:COG0396 88 --EIPGvSVSNFLRTALNAR-------RGEELSAREFLKLLKE--KMK-------------ELGLDEDFLDRYV---NE- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWL----ERFLKDFPGTIVaITHDRYFLD 223
Cdd:COG0396 140 GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVaegvNKLRSPDRGILI-ITHYQRILD 204
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-264 |
2.14e-11 |
|
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: 66.38 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGVD-KDFSGEA-RAQpgikIGYLEQEPPL- 80
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfrfydvtsgriliDGQDiRDVTQASlRAA----IGIVPQDTVLf 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 81 -DptkDVRGNVEdgvrealdalerldqvfaeYADPDADfdalakeQEKLESIIHAwdAHnlnnqleIAADALNLP-AWDA 158
Cdd:COG5265 445 nD---TIAYNIA-------------------YGRPDAS-------EEEVEAAARA--AQ-------IHDFIESLPdGYDT 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 159 DV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDfpGTIVAITHdRyfLDNV--AEW 228
Cdd:COG5265 487 RVgergLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTeraiQAALREVARG--RTTLVIAH-R--LSTIvdADE 561
|
250 260 270
....*....|....*....|....*....|....*...
gi 491208697 229 ILELDRGHgIPYQGNYSSWLEQKN--ARLEQEQKQEES 264
Cdd:COG5265 562 ILVLEAGR-IVERGTHAELLAQGGlyAQMWARQQEEEE 598
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-62 |
2.39e-11 |
|
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: 63.71 E-value: 2.39e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 491208697 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE 62
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT 78
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-242 |
2.57e-11 |
|
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: 63.28 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 24 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------ARAQPGIK-IGYLEQEPPLDPTKDVRGNVEDGV 94
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRvlingvdvTAAPPADRpVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 95 REALdaleRLDQVfaeyadpdadfdalakEQEKLESIIhawdahnlnNQLEIAADALNLPAwdadvtKLSGGERRRVALC 174
Cdd:cd03298 96 SPGL----KLTAE----------------DRQAIEVAL---------ARVGLAGLEKRLPG------ELSGGERQRVALA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 175 RLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGHgIPYQG 242
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR-IAAQG 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-198 |
2.62e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.76 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFSG---EARAQPGIkiGYLEQEPPLDPTK 84
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvprdagniiidDEDISLlplHARARRGI--GYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 85 DVRGNVedgvreaLDALERLDQVFAEyadpdadfdalaKEQEKLESIIHAWDAHNLNNQLEIAadalnlpawdadvtkLS 164
Cdd:PRK10895 94 SVYDNL-------MAVLQIRDDLSAE------------QREDRANELMEEFHIEHLRDSMGQS---------------LS 139
|
170 180 190
....*....|....*....|....*....|....
gi 491208697 165 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV 198
Cdd:PRK10895 140 GGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-239 |
2.76e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.26 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLrimagvdKDFSGEARAQPGikiGYLEQEPPLDPTKdvRGnvedgvreaLD 99
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLF-------MNLSGLLRPQKG---AVLWQGKPLDYSK--RG---------LL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 100 ALERldQVFAEYADPDadfdalakeQEKLESIIHAWDAHNLNN----QLEIAA---DALNLPawDAD------VTKLSGG 166
Cdd:PRK13638 74 ALRQ--QVATVFQDPE---------QQIFYTDIDSDIAFSLRNlgvpEAEITRrvdEALTLV--DAQhfrhqpIQCLSHG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 167 ERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDfpGTIVAI-THDRYFLDNVAEWILELDRG----HG 237
Cdd:PRK13638 141 QKKRVAIAGALVLQARYLLLDEPTAGLDpagrTQMIAIIRRIVAQ--GNHVIIsSHDIDLIYEISDAVYVLRQGqiltHG 218
|
..
gi 491208697 238 IP 239
Cdd:PRK13638 219 AP 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-216 |
3.41e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.84 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLL-----RIMAGVDKDFS----GEARAQPGIKI--GYLEQEPPLDPTKD 85
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKGSGSvllnGMPIDAKEMRAisAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 86 VRgnvedgvrEAL--DALERLDqvfaeyadpdadfDALAKEQ--EKLESIIhawDAHNLNNqleiAADAL-NLPAwdaDV 160
Cdd:TIGR00955 116 VR--------EHLmfQAHLRMP-------------RRVTKKEkrERVDEVL---QALGLRK----CANTRiGVPG---RV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 161 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFP--GTIVAIT 216
Cdd:TIGR00955 165 KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAqkGKTIICT 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-471 |
3.67e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE------------ARAQPGIKIGYLeqepP------ 79
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRvevlggdmadarHRRAVCPRIAYM----Pqglgkn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 80 LDPTKDVRGNVE-----DGvreaLDALERldqvfaeyadpDADFDALAKeqeklesiihawdAHNLnnqleiaADALNLP 154
Cdd:NF033858 89 LYPTLSVFENLDffgrlFG----QDAAER-----------RRRIDELLR-------------ATGL-------APFADRP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 155 AwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVS--W--LERFLKDFPG--TIVAITH----DRYfldn 224
Cdd:NF033858 134 A-----GKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRqfWelIDRIRAERPGmsVLVATAYmeeaERF---- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 225 vaEWILELDRGHgIPYQGNYSSWLEQKNArleqeQKQEESFAKALKKElewvrsnakgqqkknkarmerfeelnskefqQ 304
Cdd:NF033858 205 --DWLVAMDAGR-VLATGTPAELLARTGA-----DTLEAAFIALLPEE-------------------------------K 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 305 RNETSEIYIPPGPRLGNK--VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL 382
Cdd:NF033858 246 RRGHQPVVIPPRPADDDDepAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 383 -GESV---------KVAYVGQ---------IRDTLDnnktvweevsggldiL-----KVGDYEIASR--AYIGRFNFKG- 435
Cdd:NF033858 326 fGQPVdagdiatrrRVGYMSQafslygeltVRQNLE---------------LharlfHLPAAEIAARvaEMLERFDLADv 390
|
490 500 510
....*....|....*....|....*....|....*.
gi 491208697 436 QDQqkRVGELSGGERNRLQLAKILQQGANVILLDEP 471
Cdd:NF033858 391 ADA--LPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
351-511 |
3.77e-11 |
|
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: 63.54 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 351 IVGIVGPNGAGKTTLFRMMTGEQQPDTG------------------------TVTLGESVKVA----YVGQIRDTLDNNK 402
Cdd:cd03236 28 VLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildefrgselqnyfTKLLEGDVKVIvkpqYVDLIPKAVKGKV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 403 tvweevsggLDILKVGDYEIASRAYIGRFNFKGQDQQKrVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIEtlRA 482
Cdd:cd03236 108 ---------GELLKKKDERGKLDELVDQLELRHVLDRN-IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK--QR 175
|
170 180 190
....*....|....*....|....*....|....
gi 491208697 483 LEDAILV-----FPGTVMVVSHDRWFLDRIATHI 511
Cdd:cd03236 176 LNAARLIrelaeDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-238 |
3.78e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.98 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIGYLEQEPPLDPTKDVRGNVEDGVR 95
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG-DIVVSSTSKQKEIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 96 EALDAlerlDQVFAEYADPDADFDALAKEQEKLESiihawdahnlnNQLEIAAdaLNLPAWDADVTKLSGGERRRVALCR 175
Cdd:PRK13643 95 SQLFE----ETVLKDVAFGPQNFGIPKEKAEKIAA-----------EKLEMVG--LADEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 176 LLLSKPDMLLLDEPTNHLDAES-VSWLERF--LKDFPGTIVAITHDRYFLDNVAEWILELDRGHGI 238
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKArIEMMQLFesIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-236 |
4.02e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARaqpgikigyleqeppldptkdVRG-NVEDGVREAL 98
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYR---------------------VAGqDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 99 DALER--LDQVFAEY-----------ADPDADFDALAKEQEKLEsiihawdAHNLNNQLEIAADALNLPAwdadvtKLSG 165
Cdd:PRK10535 81 AQLRRehFGFIFQRYhllshltaaqnVEVPAVYAGLERKQRLLR-------AQELLQRLGLEDRVEYQPS------QLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 166 GERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VSWLERFLKDFPGTIVAITHDRYfLDNVAEWILELDRGH 236
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGE 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
283-490 |
4.24e-11 |
|
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: 65.53 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 283 QQKKNKARM--ERFEE--LNSKEFQQRNETSEIYIPPGPrlgnkvVEVEGISKSFD-GRVLYENLSFTVPPTAIVGIVGP 357
Cdd:TIGR01193 435 QPKLQAARVanNRLNEvyLVDSEFINKKKRTELNNLNGD------IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGM 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 358 NGAGKTTLFRMMTGEQQPDTGTVTL-GESVK----------VAYV--------GQIRDTL---DNNKTVWEEVSGGLDIL 415
Cdd:TIGR01193 509 SGSGKSTLAKLLVGFFQARSGEILLnGFSLKdidrhtlrqfINYLpqepyifsGSILENLllgAKENVSQDEIWAACEIA 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 416 KV-GDYEIASRAYIGRFNFKGqdqqkrvGELSGGERNRLQLAKILQQGANVILLDEPSNDLD-------IETLRALEDAI 487
Cdd:TIGR01193 589 EIkDDIENMPLGYQTELSEEG-------SSISGGQKQRIALARALLTDSKVLILDESTSNLDtitekkiVNNLLNLQDKT 661
|
...
gi 491208697 488 LVF 490
Cdd:TIGR01193 662 IIF 664
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
342-500 |
4.58e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.03 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 342 LSFTVPPTAIVGIVGPNGAGKTTLFRMMTGeQQPDTGTVTLGESVKVAYVG----QIRDTLDNNKT------VWE----- 406
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAaelaRHRAYLSQQQTppfampVFQyltlh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 407 -----EVSGGLDILkvgdYEIASRayigrfnFKGQDQQKR-VGELSGGERNRLQLAKILQQ-------GANVILLDEPSN 473
Cdd:PRK03695 94 qpdktRTEAVASAL----NEVAEA-------LGLDDKLGRsVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMN 162
|
170 180 190
....*....|....*....|....*....|
gi 491208697 474 DLDIETLRALEDAILVFP---GTVMVVSHD 500
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
21-235 |
4.77e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 64.67 E-value: 4.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEaraqpgIKIGyleqeppldptkDVRGN-VEDGVREald 99
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD------LFIG------------EKRMNdVPPAERG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 100 alerLDQVFAEYA-DPDADfdaLAKEQE---KLESIihawDAHNLNNQLEIAADALNLPAW-DADVTKLSGGERRRVALC 174
Cdd:PRK11000 77 ----VGMVFQSYAlYPHLS---VAENMSfglKLAGA----KKEEINQRVNQVAEVLQLAHLlDRKPKALSGGQRQRVAIG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 175 RLLLSKPDMLLLDEPTNHLDAE-------SVSWLERFLKDfpgTIVAITHDRYFLDNVAEWILELDRG 235
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDAAlrvqmriEISRLHKRLGR---TMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
316-499 |
5.58e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 65.23 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 316 GPRLGNKVVEVEGISKSFDGR---VLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAY-- 390
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYPDQpqpVL-KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYse 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 391 ---------VGQiR-----DTLDNN-------------KTVWEEVsgGLDILKVGDyeiasrayigrfnfKGQDQQkrVG 443
Cdd:PRK11160 410 aalrqaisvVSQ-RvhlfsATLRDNlllaapnasdealIEVLQQV--GLEKLLEDD--------------KGLNAW--LG 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 444 E----LSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAILVFPG--TVMVVSH 499
Cdd:PRK11160 471 EggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQnkTVLMITH 532
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-205 |
8.17e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.79 E-value: 8.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 31 PGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------ARAQPGIKIGYLEQEPpldptkdvrgnvedGVREALDALE 102
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVESGQiqidgktaTRGDRSRFMAYLGHLP--------------GLKADLSTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 103 RLDQVFAeyadpdadfdalakeqeklesiIHAWDAHNL-NNQLEIA-----ADALnlpawdadVTKLSGGERRRVALCRL 176
Cdd:PRK13543 102 NLHFLCG----------------------LHGRRAKQMpGSALAIVglagyEDTL--------VRQLSAGQKKRLALARL 151
|
170 180
....*....|....*....|....*....
gi 491208697 177 LLSKPDMLLLDEPTNHLDAESVSWLERFL 205
Cdd:PRK13543 152 WLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-244 |
8.20e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.90 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpgIKIGYLEQEPPLdptkdvrgnvedgvrea 97
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD--VPDNQFGREASL----------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 98 LDALERLDqvfaeyaDPDADFDALAkeqeklesiihawdAHNLNnqleiaaDAlnlPAWDADVTKLSGGERRRVALCRLL 177
Cdd:COG2401 103 IDAIGRKG-------DFKDAVELLN--------------AVGLS-------DA---VLWLRRFKELSTGQKFRFRLALLL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 178 LSKPDMLLLDEPTNHLD---AESVSW-LERFLKDFPGTIVAITHDryflDNVAEWiLELDR----GHGIPYQGNY 244
Cdd:COG2401 152 AERPKLLVIDEFCSHLDrqtAKRVARnLQKLARRAGITLVVATHH----YDVIDD-LQPDLlifvGYGGVPEEKR 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-240 |
8.30e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 61.66 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 9 NRVSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTL-LRIMAGVDKDfSGEARAQpGIKIGYLEQEP--------P 79
Cdd:cd03369 11 NLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLiLALFRFLEAE-EGKIEID-GIDISTIPLEDlrssltiiP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 80 LDPTkdvrgnVEDG-VREALDalerldqVFAEYADpdadfdalakeqeklESIIHAwdahnlnnqLEIAADALNLpawda 158
Cdd:cd03369 89 QDPT------LFSGtIRSNLD-------PFDEYSD---------------EEIYGA---------LRVSEGGLNL----- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 159 dvtklSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFL-KDFPG-TIVAITHDryfLDNVAEW--ILELDR 234
Cdd:cd03369 127 -----SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIrEEFTNsTILTIAHR---LRTIIDYdkILVMDA 198
|
....*.
gi 491208697 235 GHGIPY 240
Cdd:cd03369 199 GEVKEY 204
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
329-508 |
1.07e-10 |
|
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: 62.28 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 329 ISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVKVAYVGQIRD----------- 396
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIdGQDIAAMSRKELRElrrkkismvfq 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 397 --TLDNNKTVWEEVSGGLDILKVGDYEIASRAY--IGRFNFKGqDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPS 472
Cdd:cd03294 110 sfALLPHRTVLENVAFGLEVQGVPRAEREERAAeaLELVGLEG-WEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491208697 473 NDLDIETLRALEDAILV----FPGTVMVVSHDrwfL-------DRIA 508
Cdd:cd03294 189 SALDPLIRREMQDELLRlqaeLQKTIVFITHD---LdealrlgDRIA 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-242 |
1.17e-10 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 62.45 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEaraqpgIKIGYLEqepPLDP--TKDVRGNVedGVr 95
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGK------VTVDGLD---TLDEenLWEIRKKV--GM- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 96 ealdalerldqVFAeyaDPDADFDA-------------LAKEQEKLESIIH-AWDAHNLNNQLEIAadalnlPAwdadvt 161
Cdd:TIGR04520 82 -----------VFQ---NPDNQFVGatveddvafglenLGVPREEMRKRVDeALKLVGMEDFRDRE------PH------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDFPGTIVAITHDryfLDNV--AEWILELDRG 235
Cdd:TIGR04520 136 LLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGrkevLETIRKLNKEEGITVISITHD---MEEAvlADRVIVMNKG 212
|
....*..
gi 491208697 236 HgIPYQG 242
Cdd:TIGR04520 213 K-IVAEG 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-218 |
1.31e-10 |
|
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: 62.28 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILK---------DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkdfsgearaqpgikigyleqeppLDPTkdvR 87
Cdd:cd03294 26 SKEEILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRL------------------------IEPT---S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNVE-DGV------REALDALER--LDQVFAEYAdpdadfdaLAKEQEKLESIIHAWDAHNLNNQ--LEIAADALN---L 153
Cdd:cd03294 79 GKVLiDGQdiaamsRKELRELRRkkISMVFQSFA--------LLPHRTVLENVAFGLEVQGVPRAerEERAAEALElvgL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 154 PAW-DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHD 218
Cdd:cd03294 151 EGWeHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHD 220
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
163-247 |
1.32e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.11 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 163 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGHGIPYQG 242
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHG 707
|
....*
gi 491208697 243 NYSSW 247
Cdd:PLN03073 708 TFHDY 712
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-235 |
1.34e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.34 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGI------------KIGYLEQEPPldpTKD 85
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-GMvlseetvwdvrrQVGMVFQNPD---NQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 86 VRGNVEDGVREAL--------DALERLDQvfaeyadpdadfdalAKEQEKLESIIHAWDAHnlnnqleiaadalnlpawd 157
Cdd:PRK13635 95 VGATVQDDVAFGLenigvpreEMVERVDQ---------------ALRQVGMEDFLNREPHR------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 158 advtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA---ESVSWLERFLKDFPG-TIVAITHDryfLDNVAEW--ILE 231
Cdd:PRK13635 141 -----LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPrgrREVLETVRQLKEQKGiTVLSITHD---LDEAAQAdrVIV 212
|
....
gi 491208697 232 LDRG 235
Cdd:PRK13635 213 MNKG 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-236 |
1.41e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.43 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 10 RVSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIGYLE-QEPPLdptkdvrg 88
Cdd:PRK10908 6 HVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFS-GHDITRLKnREVPF-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 89 nvedgvrealdaLERldQVFAEYADPDADFDALAKEQEKLESIIHAWDAHNLNNQLEIAAD-------ALNLPawdadvT 161
Cdd:PRK10908 77 ------------LRR--QIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDkvglldkAKNFP------I 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHDRYFLDNVAEWILELDRGH 236
Cdd:PRK10908 137 QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-251 |
1.73e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.17 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 1 MAQYIYTMNRVSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAraqpgikigyLEQEPPL 80
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI----------LFDGKPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 81 DPTKdvRGNVEdgVREALDAL--ERLDQVFAEYADPDADFDAL---AKEQEKLESIIHAWDAHNLNnqleiaadalnlPA 155
Cdd:PRK13636 71 DYSR--KGLMK--LRESVGMVfqDPDNQLFSASVYQDVSFGAVnlkLPEDEVRKRVDNALKRTGIE------------HL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 156 WDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVS----WLERFLKDFPGTIVAITHDryfLDNVAEW--- 228
Cdd:PRK13636 135 KDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSeimkLLVEMQKELGLTIIIATHD---IDIVPLYcdn 211
|
250 260
....*....|....*....|...
gi 491208697 229 ILELDRGHGIpYQGNYSSWLEQK 251
Cdd:PRK13636 212 VFVMKEGRVI-LQGNPKEVFAEK 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
324-545 |
1.77e-10 |
|
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: 63.28 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTG--EQQPDTGTVT--LGESVKVAYVG------- 392
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIyhVALCEKCGYVErpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 393 -----------QIRDTLDNNKTVWEEVSGGLDIL-----------KVGDYEIASRAYIGrfnFKGQDQQKRVGE------ 444
Cdd:TIGR03269 81 pcpvcggtlepEEVDFWNLSDKLRRRIRKRIAIMlqrtfalygddTVLDNVLEALEEIG---YEGKEAVGRAVDliemvq 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 445 -----------LSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLR----ALEDAILVFPGTVMVVSHDRWFLDRIAT 509
Cdd:TIGR03269 158 lshrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKlvhnALEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 491208697 510 HILSFEN----------EQPEFYTGNYAEYEAYRQSRLGEDAVQKR 545
Cdd:TIGR03269 238 KAIWLENgeikeegtpdEVVAVFMEGVSEVEKECEVEVGEPIIKVR 283
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
307-487 |
1.85e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 63.30 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 307 ETSEIYIPPGPR---LGNKVVEVEGISKSFDG-RVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL 382
Cdd:COG5265 338 QPPEVADAPDAPplvVGGGEVRFENVSFGYDPeRPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 383 G---------ESVK--VAYVGQirDTLDNNKTVWEEVS-GGLDilkVGDYEI---ASRAYIGRFnFKGQDQ--QKRVGE- 444
Cdd:COG5265 418 DgqdirdvtqASLRaaIGIVPQ--DTVLFNDTIAYNIAyGRPD---ASEEEVeaaARAAQIHDF-IESLPDgyDTRVGEr 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491208697 445 ---LSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAI 487
Cdd:COG5265 492 glkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAAL 537
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-477 |
1.88e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.39 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR--AQP------------GIKIGYleQEPPLDPTKDVR 87
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILidGQEmrfasttaalaaGVAIIY--QELHLVPEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNVEDG--------------VREALDALERLdqvfAEYADPdadfdalakeqeklesiihawdahnlnnqleiaadalnl 153
Cdd:PRK11288 98 ENLYLGqlphkggivnrrllNYEAREQLEHL----GVDIDP--------------------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 154 pawDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERF---LKDFPGTIVAITHdryfldnvaewil 230
Cdd:PRK11288 135 ---DTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVireLRAEGRVILYVSH------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 231 eldrghgipyqgnysswleqknaRLeqeqkqEESFA--KALK--KELEWVRSNAKGQQKKNkarmerfEELNSkEFQQRn 306
Cdd:PRK11288 199 -----------------------RM------EEIFAlcDAITvfKDGRYVATFDDMAQVDR-------DQLVQ-AMVGR- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 307 ETSEIYippG--PR-LGNKVVEVEGISksfdGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL- 382
Cdd:PRK11288 241 EIGDIY---GyrPRpLGEVRLRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLd 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 383 GESVKVAYVGQ-----------------------IRDTLD--------------NNKtvWEEvsggldilkvgdyEIASR 425
Cdd:PRK11288 314 GKPIDIRSPRDairagimlcpedrkaegiipvhsVADNINisarrhhlragcliNNR--WEA-------------ENADR 378
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 491208697 426 aYIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDI 477
Cdd:PRK11288 379 -FIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-251 |
1.93e-10 |
|
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: 63.61 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE-----------ARAQPGIKIGYLEQEPPLDpTKDVR 87
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEillngfslkdiDRHTLRQFINYLPQEPYIF-SGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNVEDGVREALdALERLDQVfAEYADPDADFdalakeqEKLEsiihawdahnLNNQLEIAADALNLpawdadvtklSGGE 167
Cdd:TIGR01193 566 ENLLLGAKENV-SQDEIWAA-CEIAEIKDDI-------ENMP----------LGYQTELSEEGSSI----------SGGQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 168 RRRVALCRLLLSKPDMLLLDEPTNHLDaesvSWLER-------FLKDfpGTIVAITHdRYFLDNVAEWILELDRGhGIPY 240
Cdd:TIGR01193 617 KQRIALARALLTDSKVLILDESTSNLD----TITEKkivnnllNLQD--KTIIFVAH-RLSVAKQSDKIIVLDHG-KIIE 688
|
250
....*....|.
gi 491208697 241 QGNYSSWLEQK 251
Cdd:TIGR01193 689 QGSHDELLDRN 699
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
320-380 |
2.53e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.32 E-value: 2.53e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491208697 320 GNKVVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTV 380
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-234 |
2.82e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 62.84 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 14 MVPPKREIL-KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGIKIGYLEQEPPLDptkdvRGNVED 92
Cdd:TIGR00954 459 LVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMT-----LGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 93 gvrealdalerldQVFaeYADPDADFDALAKEQEKLESIIHAWDAHNL---NNQLEIAADalnlpaWdADVtkLSGGERR 169
Cdd:TIGR00954 534 -------------QII--YPDSSEDMKRRGLSDKDLEQILDNVQLTHIlerEGGWSAVQD------W-MDV--LSGGEKQ 589
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 170 RVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITHdRYFLDNVAEWILELDR 234
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH-RKSLWKYHEYLLYMDG 653
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-218 |
2.95e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.60 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE--------------ARAQ-PGIKIGYLEQEPPLDPtk 84
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDvifngqpmsklssaAKAElRNQKLGFIYQFHHLLP-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 85 dvrgnvedgvrealdalerldqvfaeyadpdaDFDAL--------------AKEQEKlesiihawdAHNLNNQLEIAADA 150
Cdd:PRK11629 101 --------------------------------DFTALenvamplligkkkpAEINSR---------ALEMLAAVGLEHRA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 151 LNLPAwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVSWLERFLKDFPGT-IVAITHD 218
Cdd:PRK11629 140 NHRPS------ELSGGERQRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTaFLVVTHD 205
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-229 |
3.13e-10 |
|
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: 60.84 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 31 PGAKIGVLGLNGAGKSTLLRIMAGvdkdfsgeaRAQPgiKIGYLEQEPPLDPT-KDVRGNvedgvrEALDALERLdqvfa 109
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAG---------KLKP--NLGKFDDPPDWDEIlDEFRGS------ELQNYFTKL----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 110 eyadPDADFDALAKEQE----------KLESIIHAWDAhnlNNQLEIAADALNL-PAWDADVTKLSGGERRRVALCRLLL 178
Cdd:cd03236 83 ----LEGDVKVIVKPQYvdlipkavkgKVGELLKKKDE---RGKLDELVDQLELrHVLDRNIDQLSGGELQRVAIAAALA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491208697 179 SKPDMLLLDEPTNHLDAE---SVSWLERFLKDFPGTIVAITHDRYFLDNVAEWI 229
Cdd:cd03236 156 RDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-218 |
3.49e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.86 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAraqpgikigyLEQEPPLDPTKDVRGNVEDGVR 95
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEV----------LIKGEPIKYDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 96 EALDALErlDQVFAEYADPDADFDALAKEQEKLEsiihawdahnLNNQLEIAADALNLPAWDADVTK-LSGGERRRVALC 174
Cdd:PRK13639 82 IVFQNPD--DQLFAPTVEEDVAFGPLNLGLSKEE----------VEKRVKEALKAVGMEGFENKPPHhLSGGQKKRVAIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491208697 175 RLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHD 218
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHD 196
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
341-507 |
3.73e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.21 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 341 NLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV--------------KVAYVGQIRDTLDNNkTVW 405
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFnGQPMsklssaakaelrnqKLGFIYQFHHLLPDF-TAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 406 EEVSGGLDILKVGDYEIASRAyIGRFNFKGQDQ--QKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETlral 483
Cdd:PRK11629 106 ENVAMPLLIGKKKPAEINSRA-LEMLAAVGLEHraNHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN---- 180
|
170 180 190
....*....|....*....|....*....|..
gi 491208697 484 EDAIL-------VFPGTV-MVVSHDRWFLDRI 507
Cdd:PRK11629 181 ADSIFqllgelnRLQGTAfLVVTHDLQLAKRM 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-235 |
3.86e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.70 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----DKDFSGEA--RAQPGIKIGYLE---------QEPPLDPT 83
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVylDGQDIFKMDVIElrrrvqmvfQIPNPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 84 KDVRGNVEDGVRealdaLERLDQVFAEYAdpdadfdalAKEQEKLESIiHAWDAhnlnnqleiAADALNLPAwdadvTKL 163
Cdd:PRK14247 97 LSIFENVALGLK-----LNRLVKSKKELQ---------ERVRWALEKA-QLWDE---------VKDRLDAPA-----GKL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 164 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFL----KDFpgTIVAITHDRYFLDNVAEWILELDRG 235
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFlelkKDM--TIVLVTHFPQQAARISDYVAFLYKG 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
351-512 |
3.88e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 60.75 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 351 IVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGE-----------SVKVAYVGQIRD------------TLDNNKTVWEE 407
Cdd:PRK10619 33 VISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgQLKVADKNQLRLlrtrltmvfqhfNLWSHMTVLEN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 408 V-SGGLDILKVGDYEIASRA--YIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDI----ETL 480
Cdd:PRK10619 113 VmEAPIQVLGLSKQEARERAvkYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPelvgEVL 192
|
170 180 190
....*....|....*....|....*....|...
gi 491208697 481 RALEDaiLVFPG-TVMVVSHDRWFLDRIATHIL 512
Cdd:PRK10619 193 RIMQQ--LAEEGkTMVVVTHEMGFARHVSSHVI 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-251 |
4.06e-10 |
|
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: 59.93 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE-----------ARAQPGIKIGYLEQEPPLdptkd 85
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQilidgidirdiSRKSLRSMIGVVLQDTFL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 86 VRGNVEDGVRealdalerldqvfaeYADPDADfdalAKEQEKLESIIHAwdaHNLNNQLE-----IAADALNLpawdadv 160
Cdd:cd03254 89 FSGTIMENIR---------------LGRPNAT----DEEVIEAAKEAGA---HDFIMKLPngydtVLGENGGN------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 161 tkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDfpGTIVAITHDRYFLDNvAEWILELDRGH 236
Cdd:cd03254 140 --LSQGERQLLAIARAMLRDPKILILDEATSNIDTETekliQEALEKLMKG--RTSIIIAHRLSTIKN-ADKILVLDDGK 214
|
250
....*....|....*
gi 491208697 237 gIPYQGNYSSWLEQK 251
Cdd:cd03254 215 -IIEEGTHDELLAKK 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
340-500 |
4.32e-10 |
|
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: 60.17 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 340 ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLgESVKVAYVGQIRDTLDNN------KTVWEEVSGGLD 413
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL-EGKQITEPGPDRMVVFQNysllpwLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 414 I----LKVGDYEIASRAYIGRFNFkGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAILV 489
Cdd:TIGR01184 81 RvlpdLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170
....*....|....*
gi 491208697 490 FPG----TVMVVSHD 500
Cdd:TIGR01184 160 IWEehrvTVLMVTHD 174
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
328-478 |
4.45e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.86 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 328 GISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTV-------TLGESVK-VAYVGQI----- 394
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgktaTRGDRSRfMAYLGHLpglka 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 -RDTLDN--------NKTVWEEVSGGLDILKVGDYEiasrayigrfnfkgqdqQKRVGELSGGERNRLQLAKILQQGANV 465
Cdd:PRK13543 96 dLSTLENlhflcglhGRRAKQMPGSALAIVGLAGYE-----------------DTLVRQLSAGQKKRLALARLWLSPAPL 158
|
170
....*....|...
gi 491208697 466 ILLDEPSNDLDIE 478
Cdd:PRK13543 159 WLLDEPYANLDLE 171
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
324-499 |
4.54e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 62.34 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGR--VLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK----------VAY 390
Cdd:PRK11176 342 IEFRNVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdGHDLRdytlaslrnqVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 391 VGQ----IRDTLDNNKTVWEEvsgglDILKVGDYEIASR-AYIGRFNFK---GQDQQkrVGE----LSGGERNRLQLAKI 458
Cdd:PRK11176 422 VSQnvhlFNDTIANNIAYART-----EQYSREQIEEAARmAYAMDFINKmdnGLDTV--IGEngvlLSGGQRQRIAIARA 494
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491208697 459 LQQGANVILLDEPSNDLDIETLRALEDAI--LVFPGTVMVVSH 499
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALdeLQKNRTSLVIAH 537
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-275 |
4.54e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.80 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 4 YIYTMNrvskmVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEaraqpgIKIGYLEQEPPLDPT 83
Cdd:PRK13634 10 HRYQYK-----TPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGT------VTIGERVITAGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 84 --KDVRGNVedGV----REAldalerldQVFAEYADPDADFDAL---AKEQEKLESiihawdahnlnnqleiAADALNLP 154
Cdd:PRK13634 79 klKPLRKKV--GIvfqfPEH--------QLFEETVEKDICFGPMnfgVSEEDAKQK----------------AREMIELV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 155 AWDADVT-----KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVSWLERFLKDFPGTIVAITHDRYFLDNV 225
Cdd:PRK13634 133 GLPEELLarspfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPkgrkEMMEMFYKLHKEKGLTTVLVTHSMEDAARY 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 226 AEWILELDRG----HGIPYQ-GNYSSWLEQKNARLEQEQKqeesFAKALKKELEW 275
Cdd:PRK13634 213 ADQIVVMHKGtvflQGTPREiFADPDELEAIGLDLPETVK----FKRALEEKFGI 263
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-499 |
4.83e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.31 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTG--EQQPD---TGTVTL-GESV---------- 386
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEarvSGEVYLdGQDIfkmdvielrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 387 KVAYVGQIRDTLDNnKTVWEEVSGGLDILKVGDYEIASRAYIGRFNFKGQ--DQQKR-----VGELSGGERNRLQLAKIL 459
Cdd:PRK14247 83 RVQMVFQIPNPIPN-LSIFENVALGLKLNRLVKSKKELQERVRWALEKAQlwDEVKDrldapAGKLSGGQQQRLCIARAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491208697 460 QQGANVILLDEPSNDLDIETLRALEDAILVFPG--TVMVVSH 499
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-235 |
5.15e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.58 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 1 MAQYIYTMNRVSKMVP-PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DKDfsgearaqPGIKIGYLEQ 76
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDN--------PNSKITVDGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 77 EPPLDPTKDVRgnvedgvrealdalERLDQVFAeyaDPDADFDALAKEQEKlesiihawdAHNLNNQ-------LEIAAD 149
Cdd:PRK13640 73 TLTAKTVWDIR--------------EKVGIVFQ---NPDNQFVGATVGDDV---------AFGLENRavprpemIKIVRD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 150 ALN----LPAWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDFPGTIVAITHDryf 221
Cdd:PRK13640 127 VLAdvgmLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGkeqiLKLIRKLKKKNNLTVISITHD--- 203
|
250
....*....|....*.
gi 491208697 222 LD--NVAEWILELDRG 235
Cdd:PRK13640 204 IDeaNMADQVLVLDDG 219
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-217 |
6.29e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 60.97 E-value: 6.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 9 NRVSKMVP-PKREI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE------------------ARAQp 67
Cdd:PRK11153 5 KNISKVFPqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRvlvdgqdltalsekelrkARRQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 68 gikIGYLEQEPPLDPTKDVRGNVedgvreALdALErLDQVfaeyadPDADFDAlaKEQEKLESIihawdahnlnnqlEIA 147
Cdd:PRK11153 84 ---IGMIFQHFNLLSSRTVFDNV------AL-PLE-LAGT------PKAEIKA--RVTELLELV-------------GLS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 148 ADALNLPAwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV-SWLErFLKD----FPGTIVAITH 217
Cdd:PRK11153 132 DKADRYPA------QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTrSILE-LLKDinreLGLTIVLITH 199
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
333-510 |
6.39e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 333 FDGRVLYEnLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV---------------KVAYVGQIRDT 397
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkeikpvrkKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 LDNNKTVWEEVSGGLDILKVGDYEiASRAYIGRFNFKGQDQQ---KRVGELSGGERNRLQLAKILQQGANVILLDEPSND 474
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNFGIPKEK-AEKIAAEKLEMVGLADEfweKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491208697 475 LD----IETLRALEdAILVFPGTVMVVSHdrwFLDRIATH 510
Cdd:PRK13643 175 LDpkarIEMMQLFE-SIHQSGQTVVLVTH---LMDDVADY 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-477 |
6.43e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 1 MAQYIYTMNRVSKMVPPKREiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSG--------------EARAQ 66
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHA-LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGtitinninynkldhKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 67 PGIKIGYleQEPPLdptkdvrgnvedgvreaLDALERLDQVFaeyadpdadfdaLAKEQEKLESIIHAWDAHNLNNQLEI 146
Cdd:PRK09700 80 LGIGIIY--QELSV-----------------IDELTVLENLY------------IGRHLTKKVCGVNIIDWREMRVRAAM 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 147 AADALNLPA-WDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWL---ERFLKDFPGTIVAITHdryfl 222
Cdd:PRK09700 129 MLLRVGLKVdLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISH----- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 223 dNVAEwILEL-DRghgipyqgnYSSwleqknarleqeQKQEESFAKALKKELEwvrsnakgqqKKNKARMERFEELNSKe 301
Cdd:PRK09700 204 -KLAE-IRRIcDR---------YTV------------MKDGSSVCSGMVSDVS----------NDDIVRLMVGRELQNR- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 302 FQQRNETSEiyippgpRLGNKVV-EVEGISKSFDGRVlyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTV 380
Cdd:PRK09700 250 FNAMKENVS-------NLAHETVfEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 381 TLG----------ESVK--VAYVGQIRDtlDN----NKTVWEEVSgGLDILKVGDYEIAsrayIGRFNFK-----GQDQQ 439
Cdd:PRK09700 321 RLNgkdisprsplDAVKkgMAYITESRR--DNgffpNFSIAQNMA-ISRSLKDGGYKGA----MGLFHEVdeqrtAENQR 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 491208697 440 K-----------RVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDI 477
Cdd:PRK09700 394 EllalkchsvnqNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
22-218 |
6.74e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 60.86 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLR-------------IMAGVD-KDFSG----EARAqpgiKIGYLEQEPPLDPT 83
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinllerptsgsvLVDGVDlTALSErelrAARR----KIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 84 KDVRGNVE-----DGVREAldalERLDQVfaeyadpdadfdalakeQEKLESIihawdahnlnnQLEIAADALnlPAwda 158
Cdd:COG1135 97 RTVAENVAlpleiAGVPKA----EIRKRV-----------------AELLELV-----------GLSDKADAY--PS--- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 159 dvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVswLErFLKD----FPGTIVAITHD 218
Cdd:COG1135 140 ---QLSGGQKQRVGIARALANNPKVLLCDEATSALDPEttrSI--LD-LLKDinreLGLTIVLITHE 200
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
19-235 |
7.97e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 59.38 E-value: 7.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEaraqpgIKIGYLEqeppLDPTKDVRGnvEDGVREAL 98
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGT------IRVGDIT----IDTARSLSQ--QKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 99 DalERLDQVFAEYAdpdadfdaLAKEQEKLESIIHAWDAHNLNNQLEIAADALNLPA-------WDADVTKLSGGERRRV 171
Cdd:PRK11264 84 R--QHVGFVFQNFN--------LFPHRTVLENIIEGPVIVKGEPKEEATARARELLAkvglagkETSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 172 ALCRLLLSKPDMLLLDEPTNHLDAESVSWLE---RFLKDFPGTIVAITHDRYFLDNVAEWILELDRG 235
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLntiRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-257 |
8.45e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.68 E-value: 8.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 2 AQYIYTMNRVSKMVPPKrEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPgiKIGYLeqeppld 81
Cdd:PRK14246 7 AEDVFNISRLYLYINDK-AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYF------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 82 pTKDVRgnvedgvreALDALERLDQVFAEYADPDAdFDALAKeqekLESIIHAWDAHNLNNQLEIAA------------- 148
Cdd:PRK14246 77 -GKDIF---------QIDAIKLRKEVGMVFQQPNP-FPHLSI----YDNIAYPLKSHGIKEKREIKKiveeclrkvglwk 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 149 ---DALNLPAwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG--TIVAITHDRYFLD 223
Cdd:PRK14246 142 evyDRLNSPA-----SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVA 216
|
250 260 270
....*....|....*....|....*....|....
gi 491208697 224 NVAEWILELDRGHGIPYQGNYSSWLEQKNARLEQ 257
Cdd:PRK14246 217 RVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-218 |
8.84e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 59.76 E-value: 8.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEaraqpgikIGYLEQEPPLDPTKDVRGNVedGVrealdal 101
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGE--------IFYNNQAITDDNFEKLRKHI--GI------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 102 erldqVFAeyaDPDADFdalakeqekLESIIHAWDAHNLNNQL-------EIAADALN----LPAWDADVTKLSGGERRR 170
Cdd:PRK13648 88 -----VFQ---NPDNQF---------VGSIVKYDVAFGLENHAvpydemhRRVSEALKqvdmLERADYEPNALSGGQKQR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491208697 171 VALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG----TIVAITHD 218
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHD 202
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
341-483 |
9.28e-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: 58.82 E-value: 9.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 341 NLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPD---TGTVTL-GESVK-------VAYVGQ---------IRDTL-- 398
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFnGQPRKpdqfqkcVAYVRQddillpgltVRETLty 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 399 -----------DNNKTVWEEVSGGLDilkVGDYEIASrayigrfnfkgqdqqKRVGELSGGERNRLQLAKILQQGANVIL 467
Cdd:cd03234 105 tailrlprkssDAIRKKRVEDVLLRD---LALTRIGG---------------NLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180
....*....|....*....|...
gi 491208697 468 LDEPSNDLD-------IETLRAL 483
Cdd:cd03234 167 LDEPTSGLDsftalnlVSTLSQL 189
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-235 |
9.92e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 59.62 E-value: 9.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 8 MNRVSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIGyleqepplDPTKdvr 87
Cdd:PRK13644 4 LENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVS-GIDTG--------DFSK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 gnvEDGVREALDALerldqvfaeYADPDADFDALAKEQEKlesiihAWDAHNL-------NNQLEIAADALNLPAWDADV 160
Cdd:PRK13644 72 ---LQGIRKLVGIV---------FQNPETQFVGRTVEEDL------AFGPENLclppieiRKRVDRALAEIGLEKYRHRS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 161 TK-LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES-VSWLERF--LKDFPGTIVAITHDRYFLdNVAEWILELDRG 235
Cdd:PRK13644 134 PKtLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIkkLHEKGKTIVYITHNLEEL-HDADRIIVMDRG 211
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
329-506 |
1.16e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 329 ISKSFD--GRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK---VAYVGQI-----RDT 397
Cdd:PRK13540 5 IELDFDyhDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKkdlCTYQKQLcfvghRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 LDNNKTVWEEVSggLDI-LKVGDYEIASRAYIgrfnFK-GQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDL 475
Cdd:PRK13540 85 INPYLTLRENCL--YDIhFSPGAVGITELCRL----FSlEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180 190
....*....|....*....|....*....|....
gi 491208697 476 D---IETLRALEDAILVFPGTVMVVSHDRWFLDR 506
Cdd:PRK13540 159 DelsLLTIITKIQEHRAKGGAVLLTSHQDLPLNK 192
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
324-499 |
1.22e-09 |
|
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: 58.71 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGR---VLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK----------VA 389
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRdlnlrwlrsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 390 YVGQ--------IRDTL---DNNKTVWEEVsggldilkvgdyEIASRAYIGRFNFKGQDQ-QKRVGE----LSGGERNRL 453
Cdd:cd03249 81 LVSQepvlfdgtIAENIrygKPDATDEEVE------------EAAKKANIHDFIMSLPDGyDTLVGErgsqLSGGQKQRI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491208697 454 QLAKILQQGANVILLDEPSNDLDIETLR----ALEDAILVFpgTVMVVSH 499
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKlvqeALDRAMKGR--TTIVIAH 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
314-499 |
1.49e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.48 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 314 PPGPRLGNKVVEVEGISKSFDGRVLYE-----NLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKV 388
Cdd:PRK13631 12 VPNPLSDDIILRVKNLYCVFDEKQENElvalnNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 389 AYVGQIRDTLDNNK---------------------------TVWEEVSGGLDILKVGDYEIASRA--YIGRFNFKGQDQQ 439
Cdd:PRK13631 92 DKKNNHELITNPYSkkiknfkelrrrvsmvfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAkfYLNKMGLDDSYLE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491208697 440 KRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAILVFPG---TVMVVSH 499
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITH 234
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
329-499 |
1.50e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 57.96 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 329 ISKSFDGRVLYeNLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGES-------VKVAYVG-----QIRD 396
Cdd:PRK13541 7 LQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCninniakPYCTYIGhnlglKLEM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 397 TLDNNKTVWEEVsggldilkvgdYEIASRAYIGRFNFKGQD-QQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDL 475
Cdd:PRK13541 86 TVFENLKFWSEI-----------YNSAETLYAAIHYFKLHDlLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
|
170 180
....*....|....*....|....*..
gi 491208697 476 DIETLRALEDAILVFP---GTVMVVSH 499
Cdd:PRK13541 155 SKENRDLLNNLIVMKAnsgGIVLLSSH 181
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-218 |
1.61e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.41 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 25 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKDFSGEAR-----------AQPGIKIGYLEQE--PPLdptkdvrgnve 91
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQfagqpleawsaAELARHRAYLSQQqtPPF----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 92 dgvreALDALERLDQVFAEYADPDADFDALakeqeklesiihawdaHNLNNQLEIAaDALNLPawdadVTKLSGGERRRV 171
Cdd:PRK03695 83 -----AMPVFQYLTLHQPDKTRTEAVASAL----------------NEVAEALGLD-DKLGRS-----VNQLSGGEWQRV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 172 ALCRLLL-----SKPD--MLLLDEPTNHLDAESVSWLERFLKDFP---GTIVAITHD 218
Cdd:PRK03695 136 RLAAVVLqvwpdINPAgqLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
342-476 |
1.81e-09 |
|
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: 60.73 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 342 LSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESvkVAYVGQ----IRDTLDNN------------KTVW 405
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQqawiQNDSLRENilfgkalnekyyQQVL 734
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491208697 406 EEVS--GGLDILKVGDyeiasRAYIGRfnfKGQDqqkrvgeLSGGERNRLQLAKILQQGANVILLDEPSNDLD 476
Cdd:TIGR00957 735 EACAllPDLEILPSGD-----RTEIGE---KGVN-------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
323-487 |
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 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDT--GTVTLGESVKVAyvGQIRDT--- 397
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKA--SNIRDTera 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 ----------LDNNKTVWEEVSGGLDILKVG---DYEIASR---AYIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQ 461
Cdd:TIGR02633 79 giviihqeltLVPELSVAENIFLGNEITLPGgrmAYNAMYLrakNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNK 158
|
170 180
....*....|....*....|....*.
gi 491208697 462 GANVILLDEPSNDLDIETLRALEDAI 487
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDII 184
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
297-486 |
2.18e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.86 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 297 LNSKEFQQRNETSEIyippgprLGNKVVEVEG---ISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGeQ 373
Cdd:PRK11174 328 LETPLAHPQQGEKEL-------ASNDPVTIEAedlEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-F 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 374 QPDTGTVT-----LGESV------KVAYVGQ--------IRD--TLDNNKTVWEEVSGGLDilkvgdyeiasRAYIGRF- 431
Cdd:PRK11174 400 LPYQGSLKingieLRELDpeswrkHLSWVGQnpqlphgtLRDnvLLGNPDASDEQLQQALE-----------NAWVSEFl 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 432 --NFKGQDQQkrVGE----LSGGERNRLQLAKILQQGANVILLDEPSNDLDIET----LRALEDA 486
Cdd:PRK11174 469 plLPQGLDTP--IGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSeqlvMQALNAA 531
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
337-514 |
2.19e-09 |
|
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: 57.89 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 337 VLyENLSFTVPPTAIVGIVGPNGAGKTT----LFRMMtgeqQPDTGTVTL-GESVK------------------VAYVGQ 393
Cdd:cd03244 19 VL-KNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIdGVDISkiglhdlrsrisiipqdpVLFSGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 394 IRDTLD-----NNKTVWEevsggldILKvgdyEIASRAYIGRFNFKGQDQQKRVGE-LSGGERNRLQLAKILQQGANVIL 467
Cdd:cd03244 94 IRSNLDpfgeySDEELWQ-------ALE----RVGLKEFVESLPGGLDTVVEEGGEnLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491208697 468 LDEPSNDLDIETLRALEDAI-LVFPG-TVMVVSHdrwfldRIAThILSF 514
Cdd:cd03244 163 LDEATASVDPETDALIQKTIrEAFKDcTVLTIAH------RLDT-IIDS 204
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
341-504 |
2.29e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 57.73 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 341 NLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVK---------------VAYVGQIRDTLdnNKTVW 405
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKPWLL--NATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 406 EEVSGG--------------------LDILKVGDyeiasrayigrfnfkgqdqQKRVGE----LSGGERNRLQLAKILQQ 461
Cdd:cd03290 97 ENITFGspfnkqrykavtdacslqpdIDLLPFGD-------------------QTEIGErginLSGGQRQRICVARALYQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491208697 462 GANVILLDEPSNDLDIE-TLRALEDAILVF----PGTVMVVSHDRWFL 504
Cdd:cd03290 158 NTNIVFLDDPFSALDIHlSDHLMQEGILKFlqddKRTLVLVTHKLQYL 205
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-217 |
2.39e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 60.12 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEA--RAQPGI---------KIGYLEQEPPLdPTKD 85
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVllDGVPLVqydhhylhrQVALVGQEPVL-FSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 86 VRGNVEDGVREAldalerldqvfaeyadPDADFDALAKEQeklesiihawDAHNLNNQLEIAADALNLPAWdadvTKLSG 165
Cdd:TIGR00958 571 VRENIAYGLTDT----------------PDEEIMAAAKAA----------NAHDFIMEFPNGYDTEVGEKG----SQLSG 620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491208697 166 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITH 217
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-252 |
2.55e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 58.46 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIGYleqepplDPTKDVRGNVedGVr 95
Cdd:PRK13632 19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKID-GITISK-------ENLKEIRKKI--GI- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 96 ealdalerldqVFaeyADPDADFDALAKE-------------QEKLESII-HAWDAHNLNNQLeiaadalnlpawDADVT 161
Cdd:PRK13632 88 -----------IF---QNPDNQFIGATVEddiafglenkkvpPKKMKDIIdDLAKKVGMEDYL------------DKEPQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDF----PGTIVAITHDryfLDNV--AEWILELDRG 235
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITHD---MDEAilADKVIVFSEG 218
|
250
....*....|....*..
gi 491208697 236 HGIpYQGNYSSWLEQKN 252
Cdd:PRK13632 219 KLI-AQGKPKEILNNKE 234
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-218 |
2.73e-09 |
|
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: 57.70 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 10 RVSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE-------ARAQPGI----KIGYLEQEP 78
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEifidgedIREQDPVelrrKIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 79 PLDPTKDVRGNVEdgvreALDALERLdqvfaeyadPDADFDALAKEQEKLESiihawdahnlnnqLEIAADALNLPAwda 158
Cdd:cd03295 85 GLFPHMTVEENIA-----LVPKLLKW---------PKEKIRERADELLALVG-------------LDPAEFADRYPH--- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 159 dvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLE----RFLKDFPGTIVAITHD 218
Cdd:cd03295 135 ---ELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQeefkRLQQELGKTIVFVTHD 195
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-238 |
2.94e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 58.30 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 4 YIYtmnrvSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEaraqpgIKI-GY-LEQEPPLD 81
Cdd:PRK13641 10 YIY-----SPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGT------ITIaGYhITPETGNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 82 PTKDVRGNVedgvreALDALERLDQVFAEYADPDADFDAL---AKEQEKLESIIHaWdahnlNNQLEIAADALNLPAWDa 158
Cdd:PRK13641 79 NLKKLRKKV------SLVFQFPEAQLFENTVLKDVEFGPKnfgFSEDEAKEKALK-W-----LKKVGLSEDLISKSPFE- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 159 dvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHDryfLDNVAEW---ILEL 232
Cdd:PRK13641 146 ----LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHN---MDDVAEYaddVLVL 218
|
....*.
gi 491208697 233 DRGHGI 238
Cdd:PRK13641 219 EHGKLI 224
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
336-500 |
3.25e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 56.21 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 336 RVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRmmtgeqqpDTGTVTLGESVKVAYVGQIrdtldnnktvweevsggldil 415
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILD--------AIGLALGGAQSATRRRSGV--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 416 KVGDYEIASRAyigRFNFkgqdqqkRVGELSGGERNRLQLAKILQ----QGANVILLDEPSNDLDIETLRALEDAI---L 488
Cdd:cd03227 59 KAGCIVAAVSA---ELIF-------TRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAIlehL 128
|
170
....*....|..
gi 491208697 489 VFPGTVMVVSHD 500
Cdd:cd03227 129 VKGAQVIVITHL 140
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
324-476 |
3.30e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.89 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGES----VKVAY--VGQIRDT 397
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndVPPAErgVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 --LDNNKTVWEEVSGGLDILKVGDYEIASR----AYIGRFnfkGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEP 471
Cdd:PRK11000 84 yaLYPHLSVAENMSFGLKLAGAKKEEINQRvnqvAEVLQL---AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
....*
gi 491208697 472 SNDLD 476
Cdd:PRK11000 161 LSNLD 165
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-235 |
3.34e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.22 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAraqpgikigYLEQEPpldptkdvrgnVEDGVREALDAL 101
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI---------LLDGKP-----------VTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 102 erLDQVFAEYADpdadFDALAKEQ--EKLESIIHAWDAH-NLNNQLEIAADALNLpawdadvTKLSGGERRRVALCRLLL 178
Cdd:PRK10522 399 --FSAVFTDFHL----FDQLLGPEgkPANPALVEKWLERlKMAHKLELEDGRISN-------LKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491208697 179 SKPDMLLLDE------PtnHLDAESVSWLERFLKDFPGTIVAITHDRYFLDNvAEWILELDRG 235
Cdd:PRK10522 466 EERDILLLDEwaadqdP--HFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNG 525
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-217 |
3.65e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.48 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-----------DFSGEARAQPGI-------KIGYLEQEPP 79
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevtitgsiVYNGHNIYSPRTdtvdlrkEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 80 LDPTKdVRGNVEDGVR-EALDALERLDQVfaeyadpdadfdalAKEQEKLESIihaWDahNLNNQLEIAADALnlpawda 158
Cdd:PRK14239 97 PFPMS-IYENVVYGLRlKGIKDKQVLDEA--------------VEKSLKGASI---WD--EVKDRLHDSALGL------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491208697 159 dvtklSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFL----KDFpgTIVAITH 217
Cdd:PRK14239 150 -----SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLlglkDDY--TMLLVTR 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
323-514 |
3.93e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.19 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSF-DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLG-------ESVKVAY---- 390
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghditrlKNREVPFlrrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 391 VGQIRDT--LDNNKTVWEEVSGGLDILKVGDYEIASRAYIGRFNFKGQDQQKRVG-ELSGGERNRLQLAKILQQGANVIL 467
Cdd:PRK10908 81 IGMIFQDhhLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPiQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491208697 468 LDEPSNDLDietlRALEDAIL-VFPG------TVMVVSHDRWFLDRIATHILSF 514
Cdd:PRK10908 161 ADEPTGNLD----DALSEGILrLFEEfnrvgvTVLMATHDIGLISRRSYRMLTL 210
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
324-512 |
3.97e-09 |
|
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: 56.85 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGIsKSFDGRvlyENLSFTVPPTAIVGivgPNGAGKTTLFRMM----TGEQQPDTGTVTLGESV--KVAYVGQIRDT 397
Cdd:cd03240 4 LSIRNI-RSFHER---SEIEFFSPLTLIVG---QNGAGKTTIIEALkyalTGELPPNSKGGAHDPKLirEGEVRAQVKLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 LDNNKTVWEEVSGGLDILkvgDYEIASRayigrfnfkgQDQQKR-----VGELSGGERN------RLQLAKILQQGANVI 466
Cdd:cd03240 77 FENANGKKYTITRSLAIL---ENVIFCH----------QGESNWplldmRGRCSGGEKVlasliiRLALAETFGSNCGIL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491208697 467 LLDEPSNDLDIETLR-ALEDAI------LVFpgTVMVVSHDRWFLDRiATHIL 512
Cdd:cd03240 144 ALDEPTTNLDEENIEeSLAEIIeerksqKNF--QLIVITHDEELVDA-ADHIY 193
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-206 |
4.43e-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: 59.54 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkdfsgearaqpgIKIGYLEQEPPLDptkdvrGNVEDGV---- 94
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL----------------LRLLSTEGEIQID------GVSWNSVtlqt 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 95 -REALDALER----LDQVFAEYADPdadfdalaKEQEKLESIIHAWDAHNLNNQLEIAADALNLPAWDADVTkLSGGERR 169
Cdd:TIGR01271 1290 wRKAFGVIPQkvfiFSGTFRKNLDP--------YEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYV-LSNGHKQ 1360
|
170 180 190
....*....|....*....|....*....|....*..
gi 491208697 170 RVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLK 206
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLK 1397
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
323-516 |
4.76e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.02 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK--VAYVGQIRD--- 396
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdGLKVNdpKVDERLIRQeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 397 ------TLDNNKTVWEEVSGG----------------LDIL-KVGdyeIASRAYigrfnfkgqdqqKRVGELSGGERNRL 453
Cdd:PRK09493 81 mvfqqfYLFPHLTALENVMFGplrvrgaskeeaekqaRELLaKVG---LAERAH------------HYPSELSGGQQQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 454 QLAKILQQGANVILLDEPSNDLDI----ETLRALEDaiLVFPGTVMV-VSHDRWFLDRIATHILSFEN 516
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPelrhEVLKVMQD--LAEEGMTMViVTHEIGFAEKVASRLIFIDK 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-229 |
4.78e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.16 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKDFSGEARAQPGIKI-GYLEQEPPLDPTkDVRgnvedgvreal 98
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRL-LELNEEARVEGEVRLfGRNIYSPDVDPI-EVR----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 99 dalERLDQVFaEYADP------------DADFDALAKEQEKLESIIHaWDAHNLNNQLEIAADALNLPAwdadvtKLSGG 166
Cdd:PRK14267 85 ---REVGMVF-QYPNPfphltiydnvaiGVKLNGLVKSKKELDERVE-WALKKAALWDEVKDRLNDYPS------NLSGG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 167 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFL----KDFpgTIVAITHDRYFLDNVAEWI 229
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLfelkKEY--TIVLVTHSPAQAARVSDYV 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-232 |
4.88e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.48 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 4 YIYtmnrvSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIGYLEQEPPLDPT 83
Cdd:PRK13646 10 YTY-----QKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDKYIRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 84 KDVRGNV----EDGVREalDALERldqvfaEYADPDADFDALAKEQEKlesiihawDAHNLNNQLEIAADALNLPAWdad 159
Cdd:PRK13646 84 RKRIGMVfqfpESQLFE--DTVER------EIIFGPKNFKMNLDEVKN--------YAHRLLMDLGFSRDVMSQSPF--- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 160 vtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFP----GTIVAITHDryfLDNVAEWILEL 232
Cdd:PRK13646 145 --QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHD---MNEVARYADEV 216
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
341-506 |
5.13e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 55.79 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 341 NLSFTVPPTAIVGIVGPNGAGKTTLFR--MMTGEQQPDTGTVTLGESVKVAYVGQIRDTLDNnktvweevsgGLDILKVG 418
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVNegLYASGKARLISFLPKFSRNKLIFIDQLQFLIDV----------GLGYLTLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 419 dyeiasrayigrfnfkgqdqqKRVGELSGGERNRLQLAKILQQGA--NVILLDEPSNDLDIETLRALEDAI--LVFPG-T 493
Cdd:cd03238 83 ---------------------QKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIkgLIDLGnT 141
|
170
....*....|...
gi 491208697 494 VMVVSHDRWFLDR 506
Cdd:cd03238 142 VILIEHNLDVLSS 154
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
334-483 |
6.56e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.14 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 334 DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGE----QQPD----TGTVTL-GE---SVKVAYVGQIRDTLDNN 401
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltggGAPRgarvTGDVTLnGEplaAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 402 K------TVWEEVSGGL-------DILKVGDYEIASRAY--IGRFNFKGQDqqkrVGELSGGERNRLQLAKILQQ----- 461
Cdd:PRK13547 92 AqpafafSAREIVLLGRypharraGALTHRDGEIAWQALalAGATALVGRD----VTTLSGGELARVQFARVLAQlwpph 167
|
170 180 190
....*....|....*....|....*....|...
gi 491208697 462 ----GANVILLDEPSNDLD-------IETLRAL 483
Cdd:PRK13547 168 daaqPPRYLLLDEPTAALDlahqhrlLDTVRRL 200
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
343-512 |
7.03e-09 |
|
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: 57.80 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 343 SFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV---------------KVAYVGQ---------IRDTL 398
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrRIGYVFQearlfphlsVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 399 D---------NNKTVWEEVsggLDILKVGDyeIASRayigrfnfkgqdqqkRVGELSGGERNRLQLAKILQQGANVILLD 469
Cdd:COG4148 99 LygrkrapraERRISFDEV---VELLGIGH--LLDR---------------RPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491208697 470 EPSNDLD----------IETLRAlEDAIlvfPgtVMVVSHDRWFLDRIATHIL 512
Cdd:COG4148 159 EPLAALDlarkaeilpyLERLRD-ELDI---P--ILYVSHSLDEVARLADHVV 205
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-218 |
7.09e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.02 E-value: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFSGEA---RAQpgiKIGYLEQepplDPTK 84
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSlppdsgsilidGKDVTKLPeykRAK---YIGRVFQ----DPMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 85 DVRGN--VED------------GVREALDALERldqvfAEYadpdadfdalakeQEKLESiihawdahnLNNQLEiaaDA 150
Cdd:COG1101 92 GTAPSmtIEEnlalayrrgkrrGLRRGLTKKRR-----ELF-------------RELLAT---------LGLGLE---NR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 151 LnlpawDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVSWL-ERFLKDFPGTIVAITHD 218
Cdd:COG1101 142 L-----DTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktAALVLELtEKIVEENNLTTLMVTHN 208
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-218 |
7.28e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.03 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPGI-----------------KIGYLEQEPPLD 81
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLlggrsifnyrdvlefrrRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 82 PTKdVRGNVEDGVRealdalerldqvfAEYADPDADFDALAkeQEKLESIiHAWDAhnlnnqleiAADALNLPAWdadvt 161
Cdd:PRK14271 114 PMS-IMDNVLAGVR-------------AHKLVPRKEFRGVA--QARLTEV-GLWDA---------VKDRLSDSPF----- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG--TIVAITHD 218
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
340-508 |
7.92e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.15 E-value: 7.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 340 ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV--------------KVAYVGQIRDTLDNNKTV 404
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHItpetgnknlkklrkKVSLVFQFPEAQLFENTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 405 WEEVSGGLDILKVGDYEIASRA--YIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRA 482
Cdd:PRK13641 104 LKDVEFGPKNFGFSEDEAKEKAlkWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180
....*....|....*....|....*....
gi 491208697 483 LEDAILVFPG---TVMVVSHDrwfLDRIA 508
Cdd:PRK13641 184 MMQLFKDYQKaghTVILVTHN---MDDVA 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-476 |
8.10e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.18 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKS-TLLRIM----------AGVDKDFSGEA---------RAQPGIKIGYLEQEP 78
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvyPSGDIRFHGESllhaseqtlRGVRGNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 79 --PLDPTKdvrgNVEDGVREALdALERldqvfaeyadpdadfdALAKEQEKLEsIIHAWDAHNLNNqleiAADALN-LPA 155
Cdd:PRK15134 102 mvSLNPLH----TLEKQLYEVL-SLHR----------------GMRREAARGE-ILNCLDRVGIRQ----AAKRLTdYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 156 wdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHD----RYFLDNVAe 227
Cdd:PRK15134 156 ------QLSGGERQRVMIAMALLTRPELLIADEPTTALDvsvqAQILQLLRELQQELNMGLLFITHNlsivRKLADRVA- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 228 wileldrghgipyqgnysswlEQKNARLEQEQKQEESFAKAlkkelewvrSNAKGQQKknkarmerfeeLNSKefqqrne 307
Cdd:PRK15134 229 ---------------------VMQNGRCVEQNRAATLFSAP---------THPYTQKL-----------LNSE------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 308 tSEIYIPPGPRLGNKVVEVEGISKSFDGR-----------VLYENLSFTVPPTAIVGIVGPNGAGKTT----LFRMMTGE 372
Cdd:PRK15134 261 -PSGDPVPLPEPASPLLDVEQLQVAFPIRkgilkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 373 ------QQPdtgTVTLGESVKVAYVGQIR-------DTLDNNKTVWEEVSGGLDI----LKVGDYEIASRAYIGRFNFKG 435
Cdd:PRK15134 340 geiwfdGQP---LHNLNRRQLLPVRHRIQvvfqdpnSSLNPRLNVLQIIEEGLRVhqptLSAAQREQQVIAVMEEVGLDP 416
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 491208697 436 QDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLD 476
Cdd:PRK15134 417 ETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
324-529 |
8.41e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 56.17 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV----------------- 386
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkpsekairllrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 387 KVAYVGQiRDTLDNNKTVWEE-VSGGLDILKVGDYEIASRA-----------YIGRFNFkgqdqqkrvgELSGGERNRLQ 454
Cdd:COG4161 83 KVGMVFQ-QYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAmkllarlrltdKADRFPL----------HLSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 455 LAKILQQGANVILLDEPSNDLDIETLRALEDAILVFPG---TVMVVSHDRWFLDRIATHILSFEN------------EQP 519
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIVTHEVEFARKVASQVVYMEKgriieqgdashfTQP 231
|
250
....*....|
gi 491208697 520 EfyTGNYAEY 529
Cdd:COG4161 232 Q--TEAFAHY 239
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
162-508 |
9.65e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 9.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGHG 237
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 238 IpyqgnysswleqKNARLEQE-QKQEESFAKALKKELEWVRSnAKGQQKKNKARMERFEELNSKEFQQRNETseiYIPpg 316
Cdd:PRK10261 248 V------------ETGSVEQIfHAPQHPYTRALLAAVPQLGA-MKGLDYPRRFPLISLEHPAKQEPPIEQDT---VVD-- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 317 prlGNKVVEVEGISKSFDGRV-----------LYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GE 384
Cdd:PRK10261 310 ---GEPILQVRNLVTRFPLRSgllnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFnGQ 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 385 SVKVAYVGQIRDTLDNNKTVWEEVSGGLDILKVGDYEIASRAYIGRFnFKGQDQQKRVG------------------ELS 446
Cdd:PRK10261 387 RIDTLSPGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGL-LPGKAAAARVAwllervgllpehawryphEFS 465
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 447 GGERNRLQLAKILQQGANVILLDEPSNDLDIeTLRA-----LEDAILVFPGTVMVVSHDRWFLDRIA 508
Cdd:PRK10261 466 GGQRQRICIARALALNPKVIIADEAVSALDV-SIRGqiinlLLDLQRDFGIAYLFISHDMAVVERIS 531
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
340-508 |
9.70e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.66 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 340 ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVKVAYVGQIRDTL-------DNN---KTVWEEV 408
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVWDIRHKIgmvfqnpDNQfvgATVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 409 SGGLDILKVGDYEIASR-----AYIGRFNFKgqdqQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLD------- 476
Cdd:PRK13650 104 AFGLENKGIPHEEMKERvnealELVGMQDFK----EREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrlel 179
|
170 180 190
....*....|....*....|....*....|..
gi 491208697 477 IETLRALEDAilvFPGTVMVVSHDrwfLDRIA 508
Cdd:PRK13650 180 IKTIKGIRDD---YQMTVISITHD---LDEVA 205
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-216 |
9.85e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 9.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPG------------IKIGYLEQEPPLdptkdVR 87
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrSKIGVVSQDPLL-----FS 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNVEDGVREALDALERLDQV--------FAEYADPDADFDALAKEQEKLESIIHAWDAHNL-----NNQLEIAADALN-- 152
Cdd:PTZ00265 474 NSIKNNIKYSLYSLKDLEALsnyynedgNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELiemrkNYQTIKDSEVVDvs 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 153 -----------LP-AWD----ADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAIT 216
Cdd:PTZ00265 554 kkvlihdfvsaLPdKYEtlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-262 |
9.96e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.93 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKdFSGEARAQpGI------------KIGYLEQEPPLdPTKDVRG 88
Cdd:PRK11174 365 LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKIN-GIelreldpeswrkHLSWVGQNPQL-PHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 89 NVedgvrealdALerldqvfaeyADPDADfdalakeQEKLESIIHAWDAHNLNNQLeiaADALNLPAWDADVTkLSGGER 168
Cdd:PRK11174 442 NV---------LL----------GNPDAS-------DEQLQQALENAWVSEFLPLL---PQGLDTPIGDQAAG-LSVGQA 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 169 RRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDfpGTIVAITHDryfLDNVAEW--ILELDRGhGIPYQG 242
Cdd:PRK11174 492 QRLALARALLQPCQLLLLDEPTASLDAHSeqlvMQALNAASRR--QTTLMVTHQ---LEDLAQWdqIWVMQDG-QIVQQG 565
|
250 260
....*....|....*....|..
gi 491208697 243 NYSSWLEQKN--ARLEQEQKQE 262
Cdd:PRK11174 566 DYAELSQAGGlfATLLAHRQEE 587
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-477 |
1.22e-08 |
|
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: 57.53 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV--------DKDFSGEARAQPGIK------IGYLEQEPPLDPTKDVR 87
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwdgEIYWSGSPLKASNIRdteragIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNVEDGVREALDALErldqvfaeyadpdADFDALAKEqeklesiihawdAHNLNNQLEIAADALNLPawdadVTKLSGGE 167
Cdd:TIGR02633 97 ENIFLGNEITLPGGR-------------MAYNAMYLR------------AKNLLRELQLDADNVTRP-----VGDYGGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 168 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVAITHDRYFLDNVaewileldrghgipyqgnyssw 247
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEV---------------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 248 leqknarleqeqkqeesfaKALKKELEWVRSnakGQQKKNKArMERFEELNSKEFQQRNETSEIYiPPGPR-LGNKVVEV 326
Cdd:TIGR02633 205 -------------------KAVCDTICVIRD---GQHVATKD-MSTMSEDDIITMMVGREITSLY-PHEPHeIGDVILEA 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 327 EGIS-----KSFDGRVlyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTG-------------EQQPDTGTVTLGESVKV 388
Cdd:TIGR02633 261 RNLTcwdviNPHRKRV--DDVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvfinGKPVDIRNPAQAIRAGI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 389 AYVGQIRDT--------LDNNKT--VWEEVSGGLDILKVGDYEIASRAyIGRFNFKGQDQQKRVGELSGGERNRLQLAKI 458
Cdd:TIGR02633 339 AMVPEDRKRhgivpilgVGKNITlsVLKSFCFKMRIDAAAELQIIGSA-IQRLKVKTASPFLPIGRLSGGNQQKAVLAKM 417
|
490
....*....|....*....
gi 491208697 459 LQQGANVILLDEPSNDLDI 477
Cdd:TIGR02633 418 LLTNPRVLILDEPTRGVDV 436
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
323-480 |
1.30e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDT--GTVTLGESVKVAYvgQIRDT--- 397
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQAS--NIRDTera 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 ----------LDNNKTVWEEVSGGLDILKVG--DY-EIASRAY--IGRFNFkGQDQQKRVGELSGGERNRLQLAKILQQG 462
Cdd:PRK13549 83 giaiihqelaLVKELSVLENIFLGNEITPGGimDYdAMYLRAQklLAQLKL-DINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180
....*....|....*....|.
gi 491208697 463 ANVILLDEPSNDL---DIETL 480
Cdd:PRK13549 162 ARLLILDEPTASLtesETAVL 182
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-217 |
1.55e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.93 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 15 VPPKR-EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG------VDKD--FSGEARAQPGI-KI-GYLEQEPPLDPt 83
Cdd:PLN03140 888 VTEDRlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGrktggyIEGDirISGFPKKQETFaRIsGYCEQNDIHSP- 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 84 kdvrgnvEDGVREALdalerldqVFAEyadpdadFDALAKEQEKLESIIHAWDAHNLnNQLEIAADAL-NLPAwdadVTK 162
Cdd:PLN03140 967 -------QVTVRESL--------IYSA-------FLRLPKEVSKEEKMMFVDEVMEL-VELDNLKDAIvGLPG----VTG 1019
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 163 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLK---DFPGTIVAITH 217
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRntvDTGRTVVCTIH 1077
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-190 |
1.67e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.95 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR--------AQPG--IK--IGYLeqeppldpTKDV 86
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvriRSPRdaIRagIAYV--------PEDR 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 RGN---VEDGVRE-----ALDALER---LDQvfaeyadpdadfdalAKEQEKLESIIHawdahnlnnQLEIAAdalnlPA 155
Cdd:COG1129 337 KGEglvLDLSIREnitlaSLDRLSRgglLDR---------------RRERALAEEYIK---------RLRIKT-----PS 387
|
170 180 190
....*....|....*....|....*....|....*
gi 491208697 156 WDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPT 190
Cdd:COG1129 388 PEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
323-383 |
1.76e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 1.76e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLG 383
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
334-483 |
2.02e-08 |
|
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: 57.23 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 334 DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTL----FRMMT--GEQQPDT---GTVTLGESVKV---------AYVGQIR 395
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLSteGEIQIDGvswNSVTLQTWRKAfgvipqkvfIFSGTFR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 396 DTLDNNKTVWEEvsgglDILKVGDyEIASRAYIGRFNFKGQDQQKRVGE-LSGGERNRLQLAKILQQGANVILLDEPSND 474
Cdd:TIGR01271 1310 KNLDPYEQWSDE-----EIWKVAE-EVGLKSVIEQFPDKLDFVLVDGGYvLSNGHKQLMCLARSILSKAKILLLDEPSAH 1383
|
....*....
gi 491208697 475 LDIETLRAL 483
Cdd:TIGR01271 1384 LDPVTLQII 1392
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-249 |
2.14e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.48 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKrEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPgiKIGYLEQEP-PLDPTkdVRGNV----- 90
Cdd:PTZ00243 672 PK-VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER--SIAYVPQQAwIMNAT--VRGNIlffde 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 91 EDGVREAlDALeRLDQVfaeyadpDADfdaLAKEQEKLESiihawdahnlnnqlEIAADALNlpawdadvtkLSGGERRR 170
Cdd:PTZ00243 747 EDAARLA-DAV-RVSQL-------EAD---LAQLGGGLET--------------EIGEKGVN----------LSGGQKAR 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 171 VALCRLLLSKPDMLLLDEPTNHLDAEsVSwlERFLKD-FPG-----TIVAITHDRYFLDNvAEWILELDRGHgIPYQGNY 244
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPLSALDAH-VG--ERVVEEcFLGalagkTRVLATHQVHVVPR-ADYVVALGDGR-VEFSGSS 865
|
....*
gi 491208697 245 SSWLE 249
Cdd:PTZ00243 866 ADFMR 870
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
18-236 |
2.32e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 56.27 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE---------ARAQPGIKIGYLEQEPPLDPTKDVRG 88
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQifidgedvtHRSIQQRDICMVFQSYALFPHMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 89 NVEDGVR-EALDALERLDQVfaeyadpdadfdalakeQEKLESIihawdahnlnnQLEIAADALnlpawdadVTKLSGGE 167
Cdd:PRK11432 98 NVGYGLKmLGVPKEERKQRV-----------------KEALELV-----------DLAGFEDRY--------VDQISGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 168 RRRVALCRLLLSKPDMLLLDEPTNHLDAEsvswLERFLKD--------FPGTIVAITHDRYFLDNVAEWILELDRGH 236
Cdd:PRK11432 142 QQRVALARALILKPKVLLFDEPLSNLDAN----LRRSMREkirelqqqFNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-197 |
2.60e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.81 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--VDKDFSGEARAQPGI-------KIGYLEQEPPLDPTKDVRG 88
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKptkqilkRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 89 NVedgvreALDALERLDQvfaeyadpdadfdALAKeQEKL---ESIIHAWDAHNLNNQLeiaadalnlpAWDADVTKLSG 165
Cdd:PLN03211 160 TL------VFCSLLRLPK-------------SLTK-QEKIlvaESVISELGLTKCENTI----------IGNSFIRGISG 209
|
170 180 190
....*....|....*....|....*....|..
gi 491208697 166 GERRRVALCRLLLSKPDMLLLDEPTNHLDAES 197
Cdd:PLN03211 210 GERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-217 |
2.70e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 55.04 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 18 KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRI---MAgvdkDFSGEARA------------QPGI-------KIGYLE 75
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrMN----DLIPGARVegeilldgediyDPDVdvvelrrRVGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 76 QEP-PLdPtKDVRGNVEDGVR-------EALDAL-ER-LDQVfaeyadpdadfdALakeqeklesiihaWDahnlnnqlE 145
Cdd:COG1117 99 QKPnPF-P-KSIYDNVAYGLRlhgikskSELDEIvEEsLRKA------------AL-------------WD--------E 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 146 IAaDALNLPAwdadvTKLSGGERRRvaLC--RLLLSKPDMLLLDEPTNHLDAESVSWLERFL----KDFpgTIVAITH 217
Cdd:COG1117 144 VK-DRLKKSA-----LGLSGGQQQR--LCiaRALAVEPEVLLMDEPTSALDPISTAKIEELIlelkKDY--TIVIVTH 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
334-500 |
2.74e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.40 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 334 DGRVLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTV-------------TLGESVKVAYVGQIRDTLDN 400
Cdd:PRK13638 13 DEPVL-KGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldyskrgLLALRQQVATVFQDPEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 401 NKTVWEEVSGGLDILKVGDYEIASRAYIGRFNFKGQD-QQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIET 479
Cdd:PRK13638 92 YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHfRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180
....*....|....*....|....*
gi 491208697 480 lRALEDAI---LVFPGT-VMVVSHD 500
Cdd:PRK13638 172 -RTQMIAIirrIVAQGNhVIISSHD 195
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
323-508 |
3.34e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.78 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMT--GEQQPD---TGTVTL-GESVkvayVGQIRD 396
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYnGHNI----YSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 397 TLDNNK--------------TVWEEVSGGLDILKVGDYEIASRAYigRFNFKGQDQQKRVGE--------LSGGERNRLQ 454
Cdd:PRK14239 81 TVDLRKeigmvfqqpnpfpmSIYENVVYGLRLKGIKDKQVLDEAV--EKSLKGASIWDEVKDrlhdsalgLSGGQQQRVC 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 455 LAKILQQGANVILLDEPSNDLDIETLRALEDAILVFPG--TVMVVSHDRWFLDRIA 508
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQQASRIS 214
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
334-501 |
3.92e-08 |
|
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: 54.86 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 334 DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLF----RMMT--GEQQPDT---GTVTLGESVKV---------AYVGQIR 395
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLNteGDIQIDGvswNSVPLQKWRKAfgvipqkvfIFSGTFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 396 DTLDNNKTVWEEvsgglDILKVGDyEIASRAYIGRFNFKGQDQQKRVG-ELSGGERNRLQLAKILQQGANVILLDEPSND 474
Cdd:cd03289 95 KNLDPYGKWSDE-----EIWKVAE-EVGLKSVIEQFPGQLDFVLVDGGcVLSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
170 180
....*....|....*....|....*...
gi 491208697 475 LDIETLRALEDAI-LVFPGTVMVVSHDR 501
Cdd:cd03289 169 LDPITYQVIRKTLkQAFADCTVILSEHR 196
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
321-509 |
4.56e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 54.71 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 321 NKVVEVEGISKSFDGRVLYENL---SFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVKVAYVGQIRD 396
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 397 TL-------DNN---KTVWEEVSGGLDILKVGDYEIASRA-----YIGRFNFKGQDQQKrvgeLSGGERNRLQLAKILQQ 461
Cdd:PRK13642 82 KIgmvfqnpDNQfvgATVEDDVAFGMENQGIPREEMIKRVdeallAVNMLDFKTREPAR----LSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491208697 462 GANVILLDEPSNDLD----IETLRALEDAILVFPGTVMVVSHDrwfLDRIAT 509
Cdd:PRK13642 158 RPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD---LDEAAS 206
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
321-476 |
4.63e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 54.61 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 321 NKVVEVEGISKSFDGRVLY--ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVKVAYVGQIRDT 397
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENNalKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 L-------DNN---KTVWEEVSGGLDILKVGDYEIASRAYigrfnfkgqDQQKRVG----------ELSGGERNRLQLAK 457
Cdd:PRK13632 85 IgiifqnpDNQfigATVEDDIAFGLENKKVPPKKMKDIID---------DLAKKVGmedyldkepqNLSGGQKQRVAIAS 155
|
170
....*....|....*....
gi 491208697 458 ILQQGANVILLDEPSNDLD 476
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLD 174
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-272 |
5.25e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 55.74 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 11 VSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGVDK----DFSGEARAQPGIKIGYLEQEPP 79
Cdd:PRK13657 340 VSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILidgtDIRTVTRASLRRNIAVVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 80 LdPTKDVRGNVEDG--------VREALDALERLDqvFAEyADPDAdFDALAKEQEKlesiihawdahnlnnqleiaadal 151
Cdd:PRK13657 420 L-FNRSIEDNIRVGrpdatdeeMRAAAERAQAHD--FIE-RKPDG-YDTVVGERGR------------------------ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 152 nlpawdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvswlERFLKDfpgTIVAITHDR------YFLDNV 225
Cdd:PRK13657 471 ----------QLSGGERQRLAIARALLKDPPILILDEATSALDVET----EAKVKA---ALDELMKGRttfiiaHRLSTV 533
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 491208697 226 --AEWILELDRGHGIPyQGNYSSwLEQKN---ARLEQEQ--KQEESFAKALKKE 272
Cdd:PRK13657 534 rnADRILVFDNGRVVE-SGSFDE-LVARGgrfAALLRAQgmLQEDERRKQPAAE 585
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
291-528 |
5.50e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 291 MERFEELNSKEfqqrnetsEIYIPPGPRL--GNKVVEVEGISKSFDGRV---LYENLSFTVPPTAIVGIVGPNGAGKTTL 365
Cdd:PLN03232 588 LQRIEELLLSE--------ERILAQNPPLqpGAPAISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSL 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 366 FRMMTGEQQP-DTGTVTLGESvkVAYVGQIRDTLdnNKTVWEevsgglDILKVGDYEiaSRAYIGRFN----------FK 434
Cdd:PLN03232 660 ISAMLGELSHaETSSVVIRGS--VAYVPQVSWIF--NATVRE------NILFGSDFE--SERYWRAIDvtalqhdldlLP 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 435 GQDQQKrVGE----LSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAIL---VFPGTVMVVSHDRWFLDRI 507
Cdd:PLN03232 728 GRDLTE-IGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMkdeLKGKTRVLVTNQLHFLPLM 806
|
250 260
....*....|....*....|.
gi 491208697 508 ATHILSFENEQPEfyTGNYAE 528
Cdd:PLN03232 807 DRIILVSEGMIKE--EGTFAE 825
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-268 |
5.70e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.25 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 7 TMNRVSKMVPP--KREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DK-----------DFSGEARAQPGIK 70
Cdd:PRK09984 3 TIIRVEKLAKTfnQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKsagshiellgrTVQREGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 71 -----IGYLEQEPPLDPTKDVRGNVEDGvreALDALERLDQVFAEYADpdadfdalAKEQEKLESIIHAWDAHNLNNQle 145
Cdd:PRK09984 83 ksranTGYIFQQFNLVNRLSVLENVLIG---ALGSTPFWRTCFSWFTR--------EQKQRALQALTRVGMVHFAHQR-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 146 iaadalnlpawdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG----TIVAITHDRYF 221
Cdd:PRK09984 150 --------------VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDY 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 491208697 222 LDNVAEWILELDRGHgIPYQGNYSSWLEQKNARLEQEQKQEESFAKA 268
Cdd:PRK09984 216 ALRYCERIVALRQGH-VFYDGSSQQFDNERFDHLYRSINRVEENAKA 261
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
341-476 |
6.52e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.90 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 341 NLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQP--DTGTVTLGesvKVAYVGQIRDTLdnNKTVWEEVSGGLDiLKVG 418
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrsDASVVIRG---TVAYVPQVSWIF--NATVRDNILFGSP-FDPE 708
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 419 DYEIASRAYIGRFNFK---GQDQQKrVGE----LSGGERNRLQLAKILQQGANVILLDEPSNDLD 476
Cdd:PLN03130 709 RYERAIDVTALQHDLDllpGGDLTE-IGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-194 |
6.54e-08 |
|
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: 55.69 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPgiKIGYLEQEPPLDPtkdvrGNVEDGVrealda 100
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RISFSPQTSWIMP-----GTIKDNI------ 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 101 lerldqVFAeyadpdadfdaLAKEQEKLESIIHAWdahNLNNQLEIAADALNLPAWDADVTkLSGGERRRVALCRLLLSK 180
Cdd:TIGR01271 508 ------IFG-----------LSYDEYRYTSVIKAC---QLEEDIALFPEKDKTVLGEGGIT-LSGGQRARISLARAVYKD 566
|
170
....*....|....
gi 491208697 181 PDMLLLDEPTNHLD 194
Cdd:TIGR01271 567 ADLYLLDSPFTHLD 580
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
324-497 |
7.06e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.11 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSF-DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTV--------TLGESV---KVAYV 391
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrplsSLSHSVlrqGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 392 GQ----IRDTLDNNKTVWEEVS-----GGLDILKVGDYeiaSRAYIGRFNfkgqdqqKRVGE----LSGGERNRLQLAKI 458
Cdd:PRK10790 421 QQdpvvLADTFLANVTLGRDISeeqvwQALETVQLAEL---ARSLPDGLY-------TPLGEqgnnLSVGQKQLLALARV 490
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491208697 459 LQQGANVILLDEPSNDLDIETLRALEDAI-LVFPGTVMVV 497
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALaAVREHTTLVV 530
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
324-499 |
8.62e-08 |
|
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: 55.40 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFD--GRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQIRDTLD-- 399
Cdd:TIGR01257 929 VCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGmc 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 400 -------NNKTVWEEVSGGLDiLKVGDYEIASRAYIGRFNFKG--QDQQKRVGELSGGERNRLQLAKILQQGANVILLDE 470
Cdd:TIGR01257 1009 pqhnilfHHLTVAEHILFYAQ-LKGRSWEEAQLEMEAMLEDTGlhHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190
....*....|....*....|....*....|.
gi 491208697 471 PSNDLDIETLRALEDAILVFPG--TVMVVSH 499
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKYRSgrTIIMSTH 1118
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
320-488 |
8.84e-08 |
|
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: 55.40 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 320 GNK--VVEVEGISKSFDGRV--LYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV-------- 386
Cdd:TIGR01257 1932 GNKtdILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSIltnisdvh 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 387 -KVAYVGQIrDTLDNNKT------VWEEVSG--GLDILKVGDYEIAS---RAYIGRFnfkgqdqqkrVGELSGGERNRLQ 454
Cdd:TIGR01257 2012 qNMGYCPQF-DAIDDLLTgrehlyLYARLRGvpAEEIEKVANWSIQSlglSLYADRL----------AGTYSGGNKRKLS 2080
|
170 180 190
....*....|....*....|....*....|....
gi 491208697 455 LAKILQQGANVILLDEPSNDLDIETLRALEDAIL 488
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
329-500 |
8.92e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.56 E-value: 8.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 329 ISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQP-----DTGTVTLGESVKVAYvgqiRDTLDNNKT 403
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNY----RDVLEFRRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 404 VweevsgGLDILKVGDYEIA--------SRAY--IGRFNFKGQDQQK--RVG--------------ELSGGERNRLQLAK 457
Cdd:PRK14271 103 V------GMLFQRPNPFPMSimdnvlagVRAHklVPRKEFRGVAQARltEVGlwdavkdrlsdspfRLSGGQQQLLCLAR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491208697 458 ILQQGANVILLDEPSNDLDIETLRALEDAILVFPG--TVMVVSHD 500
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
324-500 |
9.84e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.94 E-value: 9.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYE-----NLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTV-------------TLGES 385
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 386 V------------KVAYVGQIRDTLDN----------NKTVWEEVSGGLDILKVGDYEIASRA--YIgrfNFKGQDQ--- 438
Cdd:PRK13651 83 VleklviqktrfkKIKKIKEIRRRVGVvfqfaeyqlfEQTIEKDIIFGPVSMGVSKEEAKKRAakYI---ELVGLDEsyl 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 439 QKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLD----IETLRALEDaiLVFPG-TVMVVSHD 500
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDN--LNKQGkTIILVTHD 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-236 |
9.96e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.59 E-value: 9.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIgyleqePPLDPTKDVRgNVEDGVR 95
Cdd:PRK13649 17 PFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVD-DTLI------TSTSKNKDIK-QIRKKVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 96 EALDALErlDQVFAEYADPDADF--DALAKEQEKLESIihawdahnlnnqleiAADALNLPAWDADVT-----KLSGGER 168
Cdd:PRK13649 89 LVFQFPE--SQLFEETVLKDVAFgpQNFGVSQEEAEAL---------------AREKLALVGISESLFeknpfELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 169 RRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG---TIVAITHdryFLDNVAE---WILELDRGH 236
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsgmTIVLVTH---LMDDVANyadFVYVLEKGK 222
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
324-499 |
1.07e-07 |
|
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: 52.41 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDG---RVLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESVK------------ 387
Cdd:cd03369 7 IEVENLSVRYAPdlpPVL-KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdGIDIStipledlrsslt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 388 ------VAYVGQIRDTLDN-NKTVWEEVSGGLDILKVGDyeiasrayigrfnfkgqdqqkrvgELSGGERNRLQLAKILQ 460
Cdd:cd03369 86 iipqdpTLFSGTIRSNLDPfDEYSDEEIYGALRVSEGGL------------------------NLSQGQRQLLCLARALL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491208697 461 QGANVILLDEPSNDLDIETLRALEDAI--LVFPGTVMVVSH 499
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIreEFTNSTILTIAH 182
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-198 |
1.08e-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: 52.26 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkdfsgearaqpgikigyleqeppLDPTKDVRGNVE-DGvr 95
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR------------------------TEGNVSVEGDIHyNG-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 96 eaLDALErldqvFAEYADPDADFDAlakeqeklESIIHAwdaHNLNNQ--LEIAADALNlpawDADVTKLSGGERRRVAL 173
Cdd:cd03233 72 --IPYKE-----FAEKYPGEIIYVS--------EEDVHF---PTLTVRetLDFALRCKG----NEFVRGISGGERKRVSI 129
|
170 180
....*....|....*....|....*
gi 491208697 174 CRLLLSKPDMLLLDEPTNHLDAESV 198
Cdd:cd03233 130 AEALVSRASVLCWDNSTRGLDSSTA 154
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
321-476 |
1.19e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 53.27 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 321 NKVVEVEGISKSF--DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTG----EQQPDTGTVTLGESVKVAYVGQI 394
Cdd:PRK13640 3 DNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpDDNPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 395 RDTL-------DNN---KTVWEEVSGGLDILKVGDYEIAS-----RAYIGRFNFKGQDQQKrvgeLSGGERNRLQLAKIL 459
Cdd:PRK13640 83 REKVgivfqnpDNQfvgATVGDDVAFGLENRAVPRPEMIKivrdvLADVGMLDYIDSEPAN----LSGGQKQRVAIAGIL 158
|
170
....*....|....*..
gi 491208697 460 QQGANVILLDEPSNDLD 476
Cdd:PRK13640 159 AVEPKIIILDESTSMLD 175
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-219 |
1.33e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.41 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKD---FSGEARAQpgiKIGYLEQEPPLdptk 84
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLisptsgtllfeGEDistLKPEIYRQ---QVSYCAQTPTL---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 85 dvrgnVEDGVRealDALERLDQVFAEYADPDADFDALAkeqeklesiihawdahnlnnQLEIAADALNLPawdadVTKLS 164
Cdd:PRK10247 93 -----FGDTVY---DNLIFPWQIRNQQPDPAIFLDDLE--------------------RFALPDTILTKN-----IAELS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 165 GGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVSWL-ERFLKDFPGTIVAITHDR 219
Cdd:PRK10247 140 GGEKQRISLIRNLQFMPKVLLLDEITSALDesnKHNVNEIiHRYVREQNIAVLWVTHDK 198
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
20-219 |
1.77e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 53.41 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIGYL--EQEP--------PLDPTKDVRGN 89
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-GQDITHVpaENRHvntvfqsyALFPHMTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 90 VEDGVRealdalerLDQVFAEYADPDAdFDALAKEQekLESIIhawdahnlnnqleiaadalnlpawDADVTKLSGGERR 169
Cdd:PRK09452 107 VAFGLR--------MQKTPAAEITPRV-MEALRMVQ--LEEFA------------------------QRKPHQLSGGQQQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491208697 170 RVALCRLLLSKPDMLLLDEPTNHLDA----ESVSWLERFLKDFPGTIVAITHDR 219
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYklrkQMQNELKALQRKLGITFVFVTHDQ 205
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-226 |
1.80e-07 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 53.13 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 24 DISLSFFPGAKIGVLGLNGAGKSTLLR-IM---------------AGVD-KDFSGEARAQpgI---KIGYLEQEP--PLD 81
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARaILgllpppgitsgeilfDGEDlLKLSEKELRK--IrgrEIQMIFQDPmtSLN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 82 PTKDVRgnveDGVREALDALERLDqvfaeyadpDADFDALAKEqeklesiihawdahnlnnqleiAADALNLPAWDADVT 161
Cdd:COG0444 101 PVMTVG----DQIAEPLRIHGGLS---------KAEARERAIE----------------------LLERVGLPDPERRLD 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 162 K----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHD----RYFLDNVA 226
Cdd:COG0444 146 RypheLSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqAQILNLLKDLQRELGLAILFITHDlgvvAEIADRVA 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-194 |
2.02e-07 |
|
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: 51.28 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARaqpgikigyleqeppLDPTKDVRGNVEDGVREALdal 101
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEIT---------------LDGKPVTRRSPRDAIRAGI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 102 erldqvfaeyadpdadfdALAKEQEKLESIIHAWD-AHNlnnqleiaadaLNLPAWdadvtkLSGGERRRVALCRLLLSK 180
Cdd:cd03215 78 ------------------AYVPEDRKREGLVLDLSvAEN-----------IALSSL------LSGGNQQKVVLARWLARD 122
|
170
....*....|....
gi 491208697 181 PDMLLLDEPTNHLD 194
Cdd:cd03215 123 PRVLILDEPTRGVD 136
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
320-516 |
2.12e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.36 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 320 GNKVVEVEGISKSF---DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLgeSVKVAYVGQIRD 396
Cdd:PRK14246 4 GKSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKV--DGKVLYFGKDIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 397 TLDNNK------TVWEEVSG--GLDILKVGDYEIASRAYIGRFNFKG--QDQQKRVG--------------ELSGGERNR 452
Cdd:PRK14246 82 QIDAIKlrkevgMVFQQPNPfpHLSIYDNIAYPLKSHGIKEKREIKKivEECLRKVGlwkevydrlnspasQLSGGQQQR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 453 LQLAKILQQGANVILLDEPSNDLDIETLRALEDAILVFPG--TVMVVSHDRWFLDRIATHILSFEN 516
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYN 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
163-253 |
2.21e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.48 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 163 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDfpGTIVAITHDRYFLDNvAEWILELDRGHgI 238
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESeraiQAALDELQKN--RTSLVIAHRLSTIEK-ADEILVVEDGE-I 556
|
90
....*....|....*
gi 491208697 239 PYQGNYSSWLEQKNA 253
Cdd:PRK11176 557 VERGTHAELLAQNGV 571
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-195 |
2.46e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.92 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 11 VSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEaraqpgIKIG-----YLE---------- 75
Cdd:PRK11650 9 VRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE------IWIGgrvvnELEpadrdiamvf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 76 QEPPLDPTKDVRGNVEDGVREAldalerldqvfaeyadpdadfdALAKEQeklesiihawdahnLNNQLEIAADALNL-P 154
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIR----------------------GMPKAE--------------IEERVAEAARILELeP 126
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491208697 155 AWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA 195
Cdd:PRK11650 127 LLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
324-529 |
2.68e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 51.94 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSF-DGRVLYeNLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV----KVAYVGQIRDTL 398
Cdd:PRK11124 3 IQLNGINCFYgAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 399 DNNKTVWEE-------------VSGGLDILKVGDYEIASRA-----------YIGRFNFkgqdqqkrvgELSGGERNRLQ 454
Cdd:PRK11124 82 RNVGMVFQQynlwphltvqqnlIEAPCRVLGLSKDQALARAekllerlrlkpYADRFPL----------HLSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 455 LAKILQQGANVILLDEPSNDLDIETLRALEDAILVFPGT---VMVVSHDRWFLDRIATHILSFEN------------EQP 519
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgitQVIVTHEVEVARKTASRVVYMENghiveqgdascfTQP 231
|
250
....*....|
gi 491208697 520 EfyTGNYAEY 529
Cdd:PRK11124 232 Q--TEAFKNY 239
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
333-476 |
3.00e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 52.33 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 333 FDGRVLYEnLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV---------------KVAYVGQIRDT 397
Cdd:PRK13634 18 FERRALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkplrkKVGIVFQFPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 LDNNKTVWEEVSGGLDILKVGDYEIASRAyigrfnfkgQDQQKRVG-----------ELSGGERNRLQLAKILQQGANVI 466
Cdd:PRK13634 97 QLFEETVEKDICFGPMNFGVSEEDAKQKA---------REMIELVGlpeellarspfELSGGQMRRVAIAGVLAMEPEVL 167
|
170
....*....|
gi 491208697 467 LLDEPSNDLD 476
Cdd:PRK13634 168 VLDEPTAGLD 177
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-235 |
3.11e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 51.97 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIgyLEQEPPLdptKDVRGNVedGVr 95
Cdd:PRK13637 17 PFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID-GVDI--TDKKVKL---SDIRKKV--GL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 96 eALDALERldQVFAEYADPDADFDA--LAKEQEKLESIIHAwdahnlnnqleiaadALNLPAWDADVTK------LSGGE 167
Cdd:PRK13637 88 -VFQYPEY--QLFEETIEKDIAFGPinLGLSEEEIENRVKR---------------AMNIVGLDYEDYKdkspfeLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 168 RRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRG 235
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKG 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-218 |
3.30e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.02 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARaqpgikigyleqeppLDPTKDVRGNVEDGVREALDAL 101
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVK---------------IDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 102 ERLDQVFAEYADPDADFDALAKEQEKLESIIHAWDahnlnnQLEIAADALNLPAWDAdvTKLSGGERRRVALCRLLLSKP 181
Cdd:PRK13642 88 QNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVD------EALLAVNMLDFKTREP--ARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491208697 182 DMLLLDEPTNHLDAESVSWLERFLKDFPG----TIVAITHD 218
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEkyqlTVLSITHD 200
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-227 |
3.30e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 52.01 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAraqpgikigYLEQeppLDpTKDVrGNVEDGVREALDAL 101
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV---------YVDG---LD-TSDE-ENLWDIRNKAGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 102 ERLD-QVFAEYADPDADF--DALAKEQEKLESIIHawDAHNLNNQLEIAADALNLpawdadvtkLSGGERRRVALCRLLL 178
Cdd:PRK13633 92 QNPDnQIVATIVEEDVAFgpENLGIPPEEIRERVD--ESLKKVGMYEYRRHAPHL---------LSGGQKQRVAIAGILA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491208697 179 SKPDMLLLDEPTNHLDA----ESVSWLERFLKDFPGTIVAITHdryFLDNVAE 227
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPsgrrEVVNTIKELNKKYGITIILITH---YMEEAVE 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
163-217 |
3.63e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 3.63e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 163 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG----TIVAITH 217
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH 1417
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
12-241 |
5.14e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.55 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 12 SKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----DKDFSGEARAQPGIKigyleqepPLDPTKDV 86
Cdd:PRK13645 17 AKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetGQTIVGDYAIPANLK--------KIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 RGNVedGVREALDALerldQVFAEYADPDADFDALAKEQEKLESIihawdahnlnNQLEIAADALNLPAWDADVT--KLS 164
Cdd:PRK13645 89 RKEI--GLVFQFPEY----QLFQETIEKDIAFGPVNLGENKQEAY----------KKVPELLKLVQLPEDYVKRSpfELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 165 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDFPGTIVAITHDRYFLDNVAEWILELDRGH---- 236
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKvisi 232
|
....*
gi 491208697 237 GIPYQ 241
Cdd:PRK13645 233 GSPFE 237
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
351-509 |
5.47e-07 |
|
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: 49.29 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 351 IVGIVGPNGAGKTTLFRMMTGEQQPDTGTVtlgesvkvayvgqIRDTLDNNKTVWEEVSGGLDILKVGdyeiasrayigr 430
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGV-------------IYIDGEDILEEVLDQLLLIIVGGKK------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 431 fnfkgqdqqkrvGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAILVF---------PGTVMVVSHDR 501
Cdd:smart00382 59 ------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRlllllksekNLTVILTTNDE 126
|
....*...
gi 491208697 502 WFLDRIAT 509
Cdd:smart00382 127 KDLGPALL 134
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
327-475 |
5.96e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 327 EGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVT-LGESVkvayvgqirdtldNNKTVW 405
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILfQGKEI-------------DFKSSK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 406 EEVSGGLDIL-----KVGDYEIASRAYIGRFNFKGQ----------------------DQQKRVGELSGGERNRLQLAKI 458
Cdd:PRK10982 69 EALENGISMVhqelnLVLQRSVMDNMWLGRYPTKGMfvdqdkmyrdtkaifdeldidiDPRAKVATLSVSQMQMIEIAKA 148
|
170
....*....|....*..
gi 491208697 459 LQQGANVILLDEPSNDL 475
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSL 165
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
323-483 |
5.98e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 51.14 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSF-DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-----GESVK-------VA 389
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtGDFSKlqgirklVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 390 YVGQIRDTLDNNKTVWEEVSGGLDILKVGDYEIASR-----AYIGRFNFKGQDQQKrvgeLSGGERNRLQLAKILQQGAN 464
Cdd:PRK13644 81 IVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRvdralAEIGLEKYRHRSPKT----LSGGQGQCVALAGILTMEPE 156
|
170
....*....|....*....
gi 491208697 465 VILLDEPSNDLDIETLRAL 483
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAV 175
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-226 |
6.17e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.27 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEaraqpgikIGYLEQEPPLDPTKDVRgnvedgvrealda 100
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQ--------IIIDGDLLTEENVWDIR------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 101 lERLDQVFAeyaDPDADFDALAKEQEKlesiihawdAHNLNNQ-------LEIAADALNLPAW----DADVTKLSGGERR 169
Cdd:PRK13650 81 -HKIGMVFQ---NPDNQFVGATVEDDV---------AFGLENKgipheemKERVNEALELVGMqdfkEREPARLSGGQKQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491208697 170 RVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDFPGTIVAITHDryfLDNVA 226
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGrlelIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
321-500 |
6.28e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.42 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 321 NKVVEVEGISKSF---DGRV-LYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVtlgesvKVAyvGQIRD 396
Cdd:PRK10535 2 TALLELKDIRRSYpsgEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTY------RVA--GQDVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 397 TLDNNK----------------------TVWEEVSGGLDILKVGDYEIASRA--YIGRFNFkGQDQQKRVGELSGGERNR 452
Cdd:PRK10535 74 TLDADAlaqlrrehfgfifqryhllshlTAAQNVEVPAVYAGLERKQRLLRAqeLLQRLGL-EDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 453 LQLAKILQQGANVILLDEPSNDLD-------IETLRALEDAilvfPGTVMVVSHD 500
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDshsgeevMAILHQLRDR----GHTVIIVTHD 203
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-518 |
6.30e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.81 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTT----LFRM--MTGEQQPDTGTVTLGESV--KVAYVGQIR 395
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTflkcLNRMneLESEVRVEGRVEFFNQNIyeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 396 DTLDN--------NKTVWEEVSGGLDIL----KVGDYEIASRAyigrfnFKGQDQ--------QKRVGELSGGERNRLQL 455
Cdd:PRK14258 88 RQVSMvhpkpnlfPMSVYDNVAYGVKIVgwrpKLEIDDIVESA------LKDADLwdeikhkiHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 456 AKILQQGANVILLDEPSNDLD------IETLraLEDAILVFPGTVMVVSHDRWFLDRIATHILSFENEQ 518
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDpiasmkVESL--IQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
24-218 |
6.60e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 50.69 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 24 DISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkdfSGEARAQPGiKIGYLEQEPPLDPTKD----------------VR 87
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNAL-------SARLAPDAG-EVHYRMRDGQLRDLYAlseaerrrllrtewgfVH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNVEDGVREALDA----LERLDQVFAE-YADpdadfdalakeqeklesiIHAWDAHNLNnQLEIAADALnlpawDADVTK 162
Cdd:PRK11701 96 QHPRDGLRMQVSAggniGERLMAVGARhYGD------------------IRATAGDWLE-RVEIDAARI-----DDLPTT 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491208697 163 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDaesVSWLERFL-------KDFPGTIVAITHD 218
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD---VSVQARLLdllrglvRELGLAVVIVTHD 211
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
163-223 |
7.90e-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: 49.91 E-value: 7.90e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 163 LSGGERR------RVALCRLLLSKPDMLLLDEPTNHLDAESVSW-----LERFLKDFPGTIVAITHDRYFLD 223
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVD 187
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
164-218 |
9.13e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.88 E-value: 9.13e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 164 SGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHD 218
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-235 |
9.92e-07 |
|
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: 51.87 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR------AQPGI-----KIGYLEQEPPLdptkdvrgn 89
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIidglniAKIGLhdlrfKITIIPQDPVL--------- 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 90 VEDGVREALDAlerldqvFAEYADPDAdfdALAKEQEKLESIIHAWDAhNLNNQLEIAADalnlpawdadvtKLSGGERR 169
Cdd:TIGR00957 1372 FSGSLRMNLDP-------FSQYSDEEV---WWALELAHLKTFVSALPD-KLDHECAEGGE------------NLSVGQRQ 1428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 170 RVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLK-DFPG-TIVAITHDryfLDNVAEW--ILELDRG 235
Cdd:TIGR00957 1429 LVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRtQFEDcTVLTIAHR---LNTIMDYtrVIVLDKG 1495
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
334-500 |
9.95e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 50.62 E-value: 9.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 334 DGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESvKVAY-----------VGQIRDTLDN-- 400
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYsrkglmklresVGMVFQDPDNql 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 401 -NKTVWEEVSGGLDILKVGDYEIASR-----AYIGRFNFKgqdqQKRVGELSGGERNRLQLAKILQQGANVILLDEPSND 474
Cdd:PRK13636 96 fSASVYQDVSFGAVNLKLPEDEVRKRvdnalKRTGIEHLK----DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190
....*....|....*....|....*....|
gi 491208697 475 LD----IETLRALEDAILVFPGTVMVVSHD 500
Cdd:PRK13636 172 LDpmgvSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
329-498 |
1.17e-06 |
|
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: 49.18 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 329 ISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPD---TGTVTL-GESVK---------VAYVGQ-- 393
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYnGIPYKefaekypgeIIYVSEed 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 394 -------IRDTLDnnktvweevsggldilkvgdyeIASRAyigrfnfKGqDQQKRVgeLSGGERNRLQLAKILQQGANVI 466
Cdd:cd03233 93 vhfptltVRETLD----------------------FALRC-------KG-NEFVRG--ISGGERKRVSIAEALVSRASVL 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 491208697 467 LLDEPSNDLD-------IETLRALEDAIlvfpGTVMVVS 498
Cdd:cd03233 141 CWDNSTRGLDsstaleiLKCIRTMADVL----KTTTFVS 175
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-197 |
1.26e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.55 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 5 IYTMNRVSKMVPPKREILKD-ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEAR-AQPGI--KIGYLEQEPPL 80
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPAVDrLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATvAGKSIltNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 81 DPTKDVRGNVEDGvREALDALERLDQVFAEyadpdadfdalakEQEKLESiihaWDAHNLNnqLEIAADALnlpawdadV 160
Cdd:TIGR01257 2017 CPQFDAIDDLLTG-REHLYLYARLRGVPAE-------------EIEKVAN----WSIQSLG--LSLYADRL--------A 2068
|
170 180 190
....*....|....*....|....*....|....*..
gi 491208697 161 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 197
Cdd:TIGR01257 2069 GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
333-476 |
1.30e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.39 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 333 FDGRVLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVAYVGQIRDTLDNNKTVweevsgGL 412
Cdd:PRK13645 22 FEFKAL-NNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRLRKEI------GL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 413 dILKVGDYE-----IASRAYIGRFNFkGQDQQ---KRVG------------------ELSGGERNRLQLAKILQQGANVI 466
Cdd:PRK13645 95 -VFQFPEYQlfqetIEKDIAFGPVNL-GENKQeayKKVPellklvqlpedyvkrspfELSGGQKRRVALAGIIAMDGNTL 172
|
170
....*....|
gi 491208697 467 LLDEPSNDLD 476
Cdd:PRK13645 173 VLDEPTGGLD 182
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-250 |
1.31e-06 |
|
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: 51.26 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIgyleQEPPLDptkDVRGNVedgvreAL 98
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLD-GHDL----ADYTLA---SLRRQV------AL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 99 ---DALERLDQVFAE--YADPDaDFDalakeQEKLESIIHAWDAHNLNNQLEiaaDALNLPAWDADVtKLSGGERRRVAL 173
Cdd:TIGR02203 411 vsqDVVLFNDTIANNiaYGRTE-QAD-----RAEIERALAAAYAQDFVDKLP---LGLDTPIGENGV-LLSGGQRQRLAI 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 174 CRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDFPGTIVAitHDRYFLDNvAEWILELDRGHgIPYQGNYSSWLE 249
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESerlvQAALERLMQGRTTLVIA--HRLSTIEK-ADRIVVMDDGR-IVERGTHNELLA 556
|
.
gi 491208697 250 Q 250
Cdd:TIGR02203 557 R 557
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-235 |
1.31e-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: 49.64 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGearaqpgiKIGYLEQEPPLDPTKDVRGNVEDGVREALDAL 101
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG--------KVHWSNKNESEPSFEATRSRNRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 102 ERLDQVFAEYADPDADFDalakeQEKLESIIHAW------DAHNLNNQLEIAADALNLpawdadvtklSGGERRRVALCR 175
Cdd:cd03290 89 WLLNATVEENITFGSPFN-----KQRYKAVTDACslqpdiDLLPFGDQTEIGERGINL----------SGGQRQRICVAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 176 LLLSKPDMLLLDEPTNHLDAESVSWLE-----RFLKDFPGTIVAITHDRYFLDNvAEWILELDRG 235
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIHLSDHLMqegilKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-223 |
1.33e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.03 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK----------------DFSGEARAQPGIKIGYleQEPpldp 82
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykilegdilfkgesilDLEPEERAHLGIFLAF--QYP---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 83 tKDVRG-NVEDGVREALDALERldqvfaEYADPDAD---FDALAKEQEKLESIIHAWDAHNLNNqleiaadalnlpawda 158
Cdd:CHL00131 94 -IEIPGvSNADFLRLAYNSKRK------FQGLPELDpleFLEIINEKLKLVGMDPSFLSRNVNE---------------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 159 dvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVSWLERFLKDFPGTIVAITHDRYFLD 223
Cdd:CHL00131 151 ---GFSGGEKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSENSIILITHYQRLLD 215
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
341-518 |
1.55e-06 |
|
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: 49.80 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 341 NLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL---------GESVK-----VAYVGQIRDTLDNNKTVWE 406
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFrgqdlyqldRKQRRafrrdVQLVFQDSPSAVNPRMTVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 407 EVSG----GLDILKVGDYEIASRAYIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLD------ 476
Cdd:TIGR02769 109 QIIGeplrHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDmvlqav 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491208697 477 -IETLRALEDAilvFPGTVMVVSHDRWFLDRIATHILSFENEQ 518
Cdd:TIGR02769 189 iLELLRKLQQA---FGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
340-533 |
1.57e-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: 51.45 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 340 ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTlgESVKVAYVGQIRDTLDNnkTVWEEVSGGL------- 412
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--HSGRISFSPQTSWIMPG--TIKDNIIFGLsydeyry 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 413 -DILKVGDYEiasrAYIGRFNFKGQDQQKRVG-ELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAI--- 487
Cdd:TIGR01271 519 tSVIKACQLE----EDIALFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESClck 594
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491208697 488 LVFPGTVMVVSHDRWFLDRiATHILSFENEQPEFYtGNYAEYEAYR 533
Cdd:TIGR01271 595 LMSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFY-GTFSELQAKR 638
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
354-500 |
1.73e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 49.78 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 354 IVGPNGAGKTTLFRMMTGEQQPDTGTVTLGE---------------SVKVAYVGQIRDTLDNNKTVWEEVSGGLDILKVG 418
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvRKRIGMVFQFPESQLFEDTVEREIIFGPKNFKMN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 419 DYEIASRAY--IGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLD----IETLRALEDAILVFPG 492
Cdd:PRK13646 118 LDEVKNYAHrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqskRQVMRLLKSLQTDENK 197
|
....*...
gi 491208697 493 TVMVVSHD 500
Cdd:PRK13646 198 TIILVSHD 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
340-512 |
2.22e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 49.66 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 340 ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL------GESVK-------VAYVGQIRDTLDNNKTVWE 406
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditDKKVKlsdirkkVGLVFQYPEYQLFEETIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 407 EVSGGLDILKVGDYEIASRAYIGrFNFKGQD----QQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLD------ 476
Cdd:PRK13637 104 DIAFGPINLGLSEEEIENRVKRA-MNIVGLDyedyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrde 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 491208697 477 -IETLRALEDAilvFPGTVMVVSHDRWFLDRIATHIL 512
Cdd:PRK13637 183 iLNKIKELHKE---YNMTIILVSHSMEDVAKLADRII 216
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-219 |
2.39e-06 |
|
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: 49.47 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRImagvdkdFSGEARAQPGIKI-GYLEQEPPLDPTKDVRGNVEDGVReald 99
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSA-------FLRLLNTEGDIQIdGVSWNSVPLQKWRKAFGVIPQKVF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 100 aleRLDQVFAEYADPdadfdalaKEQEKLESIIHAWDAHNLNNQLEIAADALNLPAWDADVTkLSGGERRRVALCRLLLS 179
Cdd:cd03289 88 ---IFSGTFRKNLDP--------YGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCV-LSHGHKQLMCLARSVLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491208697 180 KPDMLLLDEPTNHLDAESVSWLERFLKD-FPGTIVAITHDR 219
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQaFADCTVILSEHR 196
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
21-218 |
2.79e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 48.93 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD-KDFSGEARAQpgiKIGYLEQEPPLDPTKDV 86
Cdd:COG4604 16 VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISrllppdsgevlvdGLDvATTPSRELAK---RLAILRQENHINSRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 R-----G---------NVEDgvREALD-ALERLDqvfaeyadpdadfdalakeqekLESIIHAWdahnlnnqleiaadal 151
Cdd:COG4604 93 RelvafGrfpyskgrlTAED--REIIDeAIAYLD----------------------LEDLADRY---------------- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491208697 152 nlpawdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD-AESVSW---LERFLKDFPGTIVAITHD 218
Cdd:COG4604 133 --------LDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmKHSVQMmklLRRLADELGKTVVIVLHD 195
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
331-470 |
2.96e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 331 KSFDGRVLY--ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESvkvAYVGQIRDTLDNNKTVWE-- 406
Cdd:PRK13545 30 RSKDGEYHYalNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS---AALIAISSGLNGQLTGIEni 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 407 EVSG---GLDILKVGDY--EIASRAYIGRFnfkgqdQQKRVGELSGGERNRLQLAKILQQGANVILLDE 470
Cdd:PRK13545 107 ELKGlmmGLTKEKIKEIipEIIEFADIGKF------IYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-194 |
3.35e-06 |
|
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: 49.82 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkdfsgearAQPGIKIG--YLEQEPpLD---PTKDVRGNV- 90
Cdd:TIGR02633 271 PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG----------AYPGKFEGnvFINGKP-VDirnPAQAIRAGIa 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 91 ---EDGVREA------------LDALERldqvFAEYADPDAdfdalAKEQEKLESIIhawdahnlnNQLEIAADALNLPa 155
Cdd:TIGR02633 340 mvpEDRKRHGivpilgvgknitLSVLKS----FCFKMRIDA-----AAELQIIGSAI---------QRLKVKTASPFLP- 400
|
170 180 190
....*....|....*....|....*....|....*....
gi 491208697 156 wdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 194
Cdd:TIGR02633 401 ----IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
341-476 |
3.67e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 48.59 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 341 NLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVKVA--------YVGQIRDTLDNN---KTVWEEVS 409
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdnfeklrkHIGIVFQNPDNQfvgSIVKYDVA 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 410 GGLDILKVGDYEIASR-----AYIGRFNFKGQDQQkrvgELSGGERNRLQLAKILQQGANVILLDEPSNDLD 476
Cdd:PRK13648 107 FGLENHAVPYDEMHRRvsealKQVDMLERADYEPN----ALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
340-533 |
4.39e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 48.70 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 340 ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTlgESVKVAYVGQIRDTLDNnkTVWEEVSGGLDILKVGD 419
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--HSGRISFSSQFSWIMPG--TIKENIIFGVSYDEYRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 420 YEIASRAYIGRFNFKGQDQQKRV-GE----LSGGERNRLQLAKILQQGANVILLDEPSNDLDIETLRALEDAI---LVFP 491
Cdd:cd03291 130 KSVVKACQLEEDITKFPEKDNTVlGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCvckLMAN 209
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491208697 492 GTVMVVSHDRWFLdRIATHILSFENEQPEFYtGNYAEYEAYR 533
Cdd:cd03291 210 KTRILVTSKMEHL-KKADKILILHEGSSYFY-GTFSELQSLR 249
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
333-476 |
5.61e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.20 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 333 FDGRVLYeNLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESV---------------KVAYVGQIRDT 397
Cdd:PRK13649 18 FEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirkKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 398 LDNNKTVWEEVSGGLDILKVGDYEIASRAYiGRFNFKGQDQQ---KRVGELSGGERNRLQLAKILQQGANVILLDEPSND 474
Cdd:PRK13649 97 QLFEETVLKDVAFGPQNFGVSQEEAEALAR-EKLALVGISESlfeKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
..
gi 491208697 475 LD 476
Cdd:PRK13649 176 LD 177
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
22-197 |
6.04e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIGYLEQeppldPTKDVRGNvEDGVREALDAL 101
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYK-NCNINNIAK-----PYCTYIGH-NLGLKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 102 ERLdQVFAEYADpdadfdalakEQEKLESIIHAWDAHNLnnqleiaadalnlpaWDADVTKLSGGERRRVALCRLLLSKP 181
Cdd:PRK13541 89 ENL-KFWSEIYN----------SAETLYAAIHYFKLHDL---------------LDEKCYSLSSGMQKIVAIARLIACQS 142
|
170
....*....|....*.
gi 491208697 182 DMLLLDEPTNHLDAES 197
Cdd:PRK13541 143 DLWLLDEVETNLSKEN 158
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
336-515 |
6.33e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.14 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 336 RVLyENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTV--------TLGESVKVAYVGQI----RDTL---DN 400
Cdd:PRK10419 26 TVL-NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplaKLNRAQRKAFRRDIqmvfQDSIsavNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 401 NKTVWE---EVSGGLDILKVGDYEIASRAYIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLD- 476
Cdd:PRK10419 105 RKTVREiirEPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDl 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 477 ------IETLRALE------------DAILV--FPGTVMVVSHDRWFLDRIATHILSFE 515
Cdd:PRK10419 185 vlqagvIRLLKKLQqqfgtaclfithDLRLVerFCQRVMVMDNGQIVETQPVGDKLTFS 243
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-218 |
6.68e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 47.72 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 11 VSKMVPPKR-----------EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDkDFSGEARaqpgikigyleqepp 79
Cdd:PRK14258 1 MSKLIPAIKvnnlsfyydtqKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVR--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 80 ldptkdVRGNVE---DGVREALDALERLD-QVFAEYADPD----ADFDALAKEQEklesiIHAWDAH-NLNNQLEIAADA 150
Cdd:PRK14258 65 ------VEGRVEffnQNIYERRVNLNRLRrQVSMVHPKPNlfpmSVYDNVAYGVK-----IVGWRPKlEIDDIVESALKD 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 151 LNLpaWDADVTK-------LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFP----GTIVAITHD 218
Cdd:PRK14258 134 ADL--WDEIKHKihksaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN 210
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
120-223 |
9.21e-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: 45.83 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 120 ALAKEQEKLESIIHAwdaHNLNNQLEIAADALNLPAWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES-- 197
Cdd:smart00382 21 ALARELGPPGGGVIY---IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQea 97
|
90 100 110
....*....|....*....|....*....|...
gi 491208697 198 -------VSWLERFLKDFPGTIVAITHDRYFLD 223
Cdd:smart00382 98 llllleeLRLLLLLKSEKNLTVILTTNDEKDLG 130
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-227 |
1.18e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 1 MAQYIYTMNRVSKMVPPKREiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV--------DKDFSGEARAQPGIK-- 70
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKA-LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyegEIIFEGEELQASNIRdt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 71 ----IGYLEQEPPLDPTKDVRGNVEDGvrEALDALERLdqvfaeyadpdaDFDALAKEQEKLEsiihawdahnlnNQLEI 146
Cdd:PRK13549 80 eragIAIIHQELALVKELSVLENIFLG--NEITPGGIM------------DYDAMYLRAQKLL------------AQLKL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 147 AADAlNLPawdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGTIVA---ITHDryfLD 223
Cdd:PRK13549 134 DINP-ATP-----VGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIAciyISHK---LN 204
|
....
gi 491208697 224 NVAE 227
Cdd:PRK13549 205 EVKA 208
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
324-500 |
1.28e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.16 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGIsKSFDGRvlyENLSFTVPptaIVGIVGPNGAGKTTLFRMMT----GE-------------QQPDTGTVTL---- 382
Cdd:COG0419 5 LRLENF-RSYRDT---ETIDFDDG---LNLIVGPNGAGKSTILEAIRyalyGKarsrsklrsdlinVGSEEASVELefeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 383 -GESVKVAY-VGQIRDTLDNN----KTVWEEVSGgLDIL-----KVGDYEIASRAYIGRFNFKGQDQQKR---------V 442
Cdd:COG0419 78 gGKRYRIERrQGEFAEFLEAKpserKEALKRLLG-LEIYeelkeRLKELEEALESALEELAELQKLKQEIlaqlsgldpI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 443 GELSGGERNRLQLAKILQqganvILLDEPSndLDIETLRALEDAILvfpgTVMVVSHD 500
Cdd:COG0419 157 ETLSGGERLRLALADLLS-----LILDFGS--LDEERLERLLDALE----ELAIITHV 203
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-198 |
1.41e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.10 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEA----------RAQPGIKIGYLEQEPPLDPTKDVRGNV 90
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferqsikkdLCTYQKQLCFVGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 91 EDGVREALDALE--RLDQVFaeyadpdadfdalakeqeKLESIIhawdahnlnnqleiaadalnlpawDADVTKLSGGER 168
Cdd:PRK13540 96 LYDIHFSPGAVGitELCRLF------------------SLEHLI------------------------DYPCGLLSSGQK 133
|
170 180 190
....*....|....*....|....*....|
gi 491208697 169 RRVALCRLLLSKPDMLLLDEPTNHLDAESV 198
Cdd:PRK13540 134 RQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-218 |
1.43e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 47.34 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD--KDFSGEARAQPGIKIGYLEQEPPLDPTKDV 86
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNrlieptrgqvlidGVDiaKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 87 RGNVEDGVREA-LDALERLDQVFaeyadpdadfDALakEQEKLESIIHAWDahnlnnqleiaadalnlpawdadvTKLSG 165
Cdd:PRK10070 124 LDNTAFGMELAgINAEERREKAL----------DAL--RQVGLENYAHSYP------------------------DELSG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 166 GERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHD 218
Cdd:PRK10070 168 GMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
335-487 |
1.62e-05 |
|
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: 47.82 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 335 GRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMtGEQQPD-TGTVTLGESVKVAYV--------GQIRDTLDNNKTVW 405
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVyGGRLTKPAKGKLFYVpqrpymtlGTLRDQIIYPDSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 406 EEVSGGL------DILKVGDYEiasraYIGRFNFKGQDQQKRVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIEt 479
Cdd:TIGR00954 543 DMKRRGLsdkdleQILDNVQLT-----HILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD- 616
|
....*...
gi 491208697 480 lraLEDAI 487
Cdd:TIGR00954 617 ---VEGYM 621
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
342-386 |
1.76e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.49 E-value: 1.76e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 491208697 342 LSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL-GESV 386
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLdGQPV 396
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
22-225 |
1.80e-05 |
|
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: 46.92 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGakIGVL-GLNGAGKSTLLRIMAGVdkdFSGEARAQPGIKIGYLEQEPPLdPTKDVRGNVEDGVREALDA 100
Cdd:COG3593 14 IKDLSIELSDD--LTVLvGENNSGKSSILEALRLL---LGPSSSRKFDEEDFYLGDDPDL-PEIEIELTFGSLLSRLLRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 101 L---ERLDQVFAEYADPDADFDALAKE-QEKLEsiiHAWDAHNLNNQLEIAADALNLPAWDADVT------------KLS 164
Cdd:COG3593 88 LlkeEDKEELEEALEELNEELKEALKAlNELLS---EYLKELLDGLDLELELSLDELEDLLKSLSlriedgkelpldRLG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 165 GGERRRV--ALCRLLL-----SKPDMLLLDEPTNHLDAESVSWLERFLKDFPGT----IVAiTHDRYFLDNV 225
Cdd:COG3593 165 SGFQRLIllALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKpnqvIIT-THSPHLLSEV 235
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
99-223 |
1.99e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 46.61 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 99 DALERLDQVFAEYADPDADFDALAKEQEKLESIIHAWDAHNLnnQLEIAADALNLPAWDadvtkLSGGERR---RVALCR 175
Cdd:pfam13304 180 DLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGL--ILLENGGGGELPAFE-----LSDGTKRllaLLAALL 252
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491208697 176 LLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPGT---IVAITHDRYFLD 223
Cdd:pfam13304 253 SALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNgaqLILTTHSPLLLD 303
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-264 |
2.14e-05 |
|
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: 47.63 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKreiLKDISLSFFPGAKIGVLGLNGAGKSTLLR-IMAGVDKDfsgEARAQPGIKIGYLEQEPPLDptkdvrgnvEDGV 94
Cdd:TIGR00957 651 PPT---LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV---EGHVHMKGSVAYVPQQAWIQ---------NDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 95 REALDALERLDQvfaEYADPDADFDALAKEQEKLESiihawdahnlNNQLEIAADALNLpawdadvtklSGGERRRVALC 174
Cdd:TIGR00957 716 RENILFGKALNE---KYYQQVLEACALLPDLEILPS----------GDRTEIGEKGVNL----------SGGQKQRVSLA 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 175 RLLLSKPDMLLLDEPTNHLDA-------ESVSWLERFLKDfpGTIVAITHDRYFLDNVaEWILELDRGHgIPYQGNYSSW 247
Cdd:TIGR00957 773 RAVYSNADIYLFDDPLSAVDAhvgkhifEHVIGPEGVLKN--KTRILVTHGISYLPQV-DVIIVMSGGK-ISEMGSYQEL 848
|
250 260
....*....|....*....|....*.
gi 491208697 248 LEQKN---------ARLEQEQKQEES 264
Cdd:TIGR00957 849 LQRDGafaeflrtyAPDEQQGHLEDS 874
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-190 |
2.23e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 46.03 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 1 MAQYIYTMNRVSKMVPpKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkdfsgEARAQPGiKIGYLEQEPPL 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYG-KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-------DPRATSG-RIVFDGKDITD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 81 DPTKDVrgnvedgVREALDALERLDQVFAEYADPD--ADFDALAKEQEKLESIIHAWDAHNLNNQLEIAADAlnlpawda 158
Cdd:PRK11614 72 WQTAKI-------MREAVAIVPEGRRVFSRMTVEEnlAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAG-------- 136
|
170 180 190
....*....|....*....|....*....|..
gi 491208697 159 dvtKLSGGERRRVALCRLLLSKPDMLLLDEPT 190
Cdd:PRK11614 137 ---TMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-217 |
2.61e-05 |
|
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: 47.32 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 9 NRVSKMVPPKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEaraqpgIKIGyleqeppldpTKDVRG 88
Cdd:TIGR01257 933 NLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGT------VLVG----------GKDIET 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 89 NVeDGVREALDALERLDQVF-----AEYADPDADFDALAKEQEKL--ESIIHAWDAHNLNNQleiaadalnlpawdaDVT 161
Cdd:TIGR01257 997 NL-DAVRQSLGMCPQHNILFhhltvAEHILFYAQLKGRSWEEAQLemEAMLEDTGLHHKRNE---------------EAQ 1060
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES-VSWLERFLKDFPG-TIVAITH 217
Cdd:TIGR01257 1061 DLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSrRSIWDLLLKYRSGrTIIMSTH 1118
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
154-229 |
2.69e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 154 PAWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE----SVSWLERFLKDFPGTIVAITHDRYFLDNVAEWI 229
Cdd:cd03222 63 PVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRI 142
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-226 |
2.91e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 46.26 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 24 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARaqpgikigyleqeppldptkdVRG-NVEDGVREALDALE 102
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEIL---------------------FDGqDITGLSGRELRPLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 103 RLDQ-VFAeyaDPdadFDALAKEQeKLESIIH-AWDAHNL---NNQLEIAADALN---LPAWDADvtK----LSGGERRR 170
Cdd:COG4608 95 RRMQmVFQ---DP---YASLNPRM-TVGDIIAePLRIHGLaskAERRERVAELLElvgLRPEHAD--RypheFSGGQRQR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491208697 171 VALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHD----RYFLDNVA 226
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDvsiqAQVLNLLEDLQDELGLTYLFISHDlsvvRHISDRVA 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
346-511 |
3.32e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.60 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 346 VPPTAIVGIVGPNGAGKTTLFRMMT-----GEQQPDTGTVTL-GESV------------KVAYVGQIRDTLDNnKTVWEE 407
Cdd:PRK14267 27 IPQNGVFALMGPSGCGKSTLLRTFNrllelNEEARVEGEVRLfGRNIyspdvdpievrrEVGMVFQYPNPFPH-LTIYDN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 408 VSGGLDI--LKVGDYEIASRAYIGRFNFKGQDQQK-----RVGELSGGERNRLQLAKILQQGANVILLDEPSNDLDIETL 480
Cdd:PRK14267 106 VAIGVKLngLVKSKKELDERVEWALKKAALWDEVKdrlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGT 185
|
170 180 190
....*....|....*....|....*....|...
gi 491208697 481 RALEDAILVFPG--TVMVVSHDRWFLDRIATHI 511
Cdd:PRK14267 186 AKIEELLFELKKeyTIVLVTHSPAQAARVSDYV 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
340-476 |
3.55e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 45.85 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 340 ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVtlgesvkvaYVGQIrDTLDNNKT---------------- 403
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV---------YVDGL-DTSDEENLwdirnkagmvfqnpdn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 404 ------VWEEVSGGLDILKVGDYEIASRAyigrfnfkgQDQQKRVGE----------LSGGERNRLQLAKILQQGANVIL 467
Cdd:PRK13633 97 qivatiVEEDVAFGPENLGIPPEEIRERV---------DESLKKVGMyeyrrhaphlLSGGQKQRVAIAGILAMRPECII 167
|
....*....
gi 491208697 468 LDEPSNDLD 476
Cdd:PRK13633 168 FDEPTAMLD 176
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
324-476 |
4.01e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.99 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVL-YENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGESVkvayVGQI----RD-- 396
Cdd:PRK11650 4 LKLQAVRKSYDGKTQvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV----VNELepadRDia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 397 ------TLDNNKTVWEEVSGGLDILKVGDYEIASR----AYIGRFnfkGQDQQKRVGELSGGERNRLQLAK-ILQQGAnV 465
Cdd:PRK11650 80 mvfqnyALYPHMSVRENMAYGLKIRGMPKAEIEERvaeaARILEL---EPLLDRKPRELSGGQRQRVAMGRaIVREPA-V 155
|
170
....*....|.
gi 491208697 466 ILLDEPSNDLD 476
Cdd:PRK11650 156 FLFDEPLSNLD 166
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
163-483 |
4.21e-05 |
|
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: 46.22 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 163 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHD----RYFLDNVAewileldr 234
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqAQILDLLKDLQRELGMALLLITHDlgvvRRFADRVA-------- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 235 ghgIPYQGnysswleqknaRLEQEQKQEESFA-------KALkkelewvrsnakgqqkknkarmerfeeLNSkefqqRNE 307
Cdd:COG4172 229 ---VMRQG-----------EIVEQGPTAELFAapqhpytRKL---------------------------LAA-----EPR 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 308 TSEIYIPPGPRLgnkVVEVEGISKSFDGR-------VLY----ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGeQQPD 376
Cdd:COG4172 263 GDPRPVPPDAPP---LLEARDLKVWFPIKrglfrrtVGHvkavDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPS 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 377 TGTVTLGesvkvayvGQIRDTLDNNK-----------------------TVWEEVSGGLDILKVGdyeiasrayigrfnF 433
Cdd:COG4172 339 EGEIRFD--------GQDLDGLSRRAlrplrrrmqvvfqdpfgslsprmTVGQIIAEGLRVHGPG--------------L 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 434 KGQDQQKRVG------------------ELSGGERNRLQLAK--ILQqgANVILLDEPSNDLD-------IETLRAL 483
Cdd:COG4172 397 SAAERRARVAealeevgldpaarhryphEFSGGQRQRIAIARalILE--PKLLVLDEPTSALDvsvqaqiLDLLRDL 471
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
323-383 |
4.43e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 4.43e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVT-LG 383
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLG 62
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
317-477 |
5.09e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 317 PRLGNKVVEVEGIS---KSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTL----F-----RMMTGE-----QQPDTGT 379
Cdd:NF040905 251 PKIGEVVFEVKNWTvyhPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELamsvFgrsygRNISGTvfkdgKEVDVST 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 380 VTLGESVKVAYVGQIR--------DTLDNNKTV--WEEVSGGLDILKVGDYEIASRaYIGRFNFKGQDQQKRVGELSGGE 449
Cdd:NF040905 331 VSDAIDAGLAYVTEDRkgyglnliDDIKRNITLanLGKVSRRGVIDENEEIKVAEE-YRKKMNIKTPSVFQKVGNLSGGN 409
|
170 180
....*....|....*....|....*...
gi 491208697 450 RNRLQLAKILQQGANVILLDEPSNDLDI 477
Cdd:NF040905 410 QQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-194 |
5.86e-05 |
|
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: 45.83 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTL----LRIMAgvdkdFSGEARAQpGIKIGYLE---------------QEP--PL 80
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFD-GQDLDGLSrralrplrrrmqvvfQDPfgSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 81 DPtkdvRGNVEDGVREALDALErldqvfaeyadPDADfdalAKEQEklesiihawdahnlnnqlEIAADAL---NLPAWD 157
Cdd:COG4172 376 SP----RMTVGQIIAEGLRVHG-----------PGLS----AAERR------------------ARVAEALeevGLDPAA 418
|
170 180 190
....*....|....*....|....*....|....*....
gi 491208697 158 AD--VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 194
Cdd:COG4172 419 RHryPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-194 |
7.41e-05 |
|
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: 44.85 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 21 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQPgiKIGYLEQEPPLDPTKdVRGNVEDGVRealda 100
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQFSWIMPGT-IKENIIFGVS----- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 101 lerldqvFAEYadpdadfdalakeqeKLESIIHAWdahNLNNQLEIAADALNLPAWDADVTkLSGGERRRVALCRLLLSK 180
Cdd:cd03291 124 -------YDEY---------------RYKSVVKAC---QLEEDITKFPEKDNTVLGEGGIT-LSGGQRARISLARAVYKD 177
|
170
....*....|....
gi 491208697 181 PDMLLLDEPTNHLD 194
Cdd:cd03291 178 ADLYLLDSPFGYLD 191
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
163-238 |
8.01e-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: 43.47 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 163 LSGGERRRVALCRLLLS--KPDMLLLDEPTNHLDAESvswLERFLKDFPG------TIVAITHDRYFLDNvAEWILELDR 234
Cdd:cd03238 88 LSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQD---INQLLEVIKGlidlgnTVILIEHNLDVLSS-ADWIIDFGP 163
|
....
gi 491208697 235 GHGI 238
Cdd:cd03238 164 GSGK 167
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
342-479 |
9.51e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 342 LSFTVPPTAIVGIVGPNGAGKT----TLFRMMtgeqQPDTGTVTLGE-------------------SVKVAYVGQIRDTL 398
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSsmlnALFRIV----ELERGRILIDGcdiskfglmdlrkvlgiipQAPVLFSGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 399 D-----NNKTVWEEVsggldilkvgdyeiaSRAYIG---RFNFKGQDQQ-KRVGE-LSGGERNRLQLAKILQQGANVILL 468
Cdd:PLN03130 1334 DpfnehNDADLWESL---------------ERAHLKdviRRNSLGLDAEvSEAGEnFSVGQRQLLSLARALLRRSKILVL 1398
|
170
....*....|.
gi 491208697 469 DEPSNDLDIET 479
Cdd:PLN03130 1399 DEATAAVDVRT 1409
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-228 |
1.01e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 44.49 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 1 MAQYIYTMNRVSKMVPPKREILKDISLSFfPGAKIGVL-GLNGAGKSTLLRIMAGVDKDFSGEAR--AQPGIK------I 71
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTV-PGGSIAALvGVNGSGKSTLFKALMGFVRLASGKISilGQPTRQalqknlV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 72 GYLEQEPPLDPTKDVRgnVEDGVrealdalerldqVFAEYADPDADFDALAKEQEKLESIIHAWDAHNLNNQleiaadal 151
Cdd:PRK15056 81 AYVPQSEEVDWSFPVL--VEDVV------------MMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHR-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 152 nlpawdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VSWLERFLKDFPGTIVAITHDryfLDNVAEW 228
Cdd:PRK15056 139 -------QIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTearIISLLRELRDEGKTMLVSTHN---LGSVTEF 208
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
440-500 |
1.04e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 1.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491208697 440 KRVGELSGGERNRLQLAKilQQGANVI----LLDEPS-------NDLDIETLRALEDailvFPGTVMVVSHD 500
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLAT--QIGSGLTgvlyVLDEPSiglhqrdNRRLINTLKRLRD----LGNTLIVVEHD 549
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
163-218 |
1.13e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.00 E-value: 1.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 491208697 163 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDFPG--TIVAITHD 218
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN 209
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
321-380 |
1.18e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 44.01 E-value: 1.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 321 NKVVEVEGISKSFDGRV---------LYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTV 380
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL 70
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
39-218 |
1.36e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.08 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 39 GLNGAGKSTLLRIMAGVdkdFSGEARAQPGIKIGYLEqepplDPTKDVRGNVEDGVREALDALERLDQVFAE--YADPDA 116
Cdd:COG0419 30 GPNGAGKSTILEAIRYA---LYGKARSRSKLRSDLIN-----VGSEEASVELEFEHGGKRYRIERRQGEFAEflEAKPSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 117 ------------DFDALAKEQEKLESIIHAwDAHNLNNQLEIAADALNLPAWDADVTKLSGGERRRVALCRLLlskpdML 184
Cdd:COG0419 102 rkealkrllgleIYEELKERLKELEEALES-ALEELAELQKLKQEILAQLSGLDPIETLSGGERLRLALADLL-----SL 175
|
170 180 190
....*....|....*....|....*....|....
gi 491208697 185 LLDepTNHLDAESVSWLERFLKDfpgtIVAITHD 218
Cdd:COG0419 176 ILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-194 |
1.39e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 17 PKREILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkdfsgearAQPGIKIG--YLEQEP---------------- 78
Cdd:PRK13549 273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG----------AYPGRWEGeiFIDGKPvkirnpqqaiaqgiam 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 79 -PLDPTKDvrGNVED-GVRE--ALDALERldqvFAEYADPDAdfdalAKEQEKLESIIhawdahnlnNQLEIAADALNLP 154
Cdd:PRK13549 343 vPEDRKRD--GIVPVmGVGKniTLAALDR----FTGGSRIDD-----AAELKTILESI---------QRLKVKTASPELA 402
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491208697 155 awdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 194
Cdd:PRK13549 403 -----IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-194 |
2.24e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 22 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpgikigyleqeppldpTKDVRGNvedgvrealDAL 101
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLH----------------GKKINNH---------NAN 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 102 ERLDQVFAE----------YADPDADFDALAKEQEKLESIIHAWDAHNLNNQLEIAADALNL--PAWDADVTKLSGGERR 169
Cdd:PRK10982 319 EAINHGFALvteerrstgiYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVktPGHRTQIGSLSGGNQQ 398
|
170 180
....*....|....*....|....*
gi 491208697 170 RVALCRLLLSKPDMLLLDEPTNHLD 194
Cdd:PRK10982 399 KVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
323-508 |
2.38e-04 |
|
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: 43.50 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLY----ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTG---EQQPDTGTVTL-GESV-------- 386
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkavDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFdGEDLlklsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 387 ------KVAYVGQirD---TLDNNKTVWEEVSGGLDILKVGDYEIASRAYIGRFnfkgqdqqKRVG-------------E 444
Cdd:COG0444 81 rkirgrEIQMIFQ--DpmtSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELL--------ERVGlpdperrldryphE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 445 LSGGERNRLQLAKILQQGANVILLDEPSNDLD-------IETLRAL-EDAILvfpgTVMVVSHD----RWFLDRIA 508
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqaqiLNLLKDLqRELGL----AILFITHDlgvvAEIADRVA 222
|
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
351-501 |
2.75e-04 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 43.36 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 351 IVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTL---------GESVKVAYVGQIRDTLDNNKTVWEEVSGGL-DILKVGDY 420
Cdd:COG4928 31 VIGLDGEWGSGKTSFLNLIEKELESNEKVIVVyfnawlydgEEDLLAALLSEIAAELEKKKKKDKKAAKKLkKYAKRLSK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 421 EIASRAYIGRFNFKGQDQQKRVGELSGGERN------RLQLAKILQQGAN---VILLDepsnDLD-------IETLRALE 484
Cdd:COG4928 111 LALKAGLLGGPAEAVAEALKALLKKEYKSKKksieafREELEELLKELKGkrlVVFID----DLDrcepdeaIEVLELIK 186
|
170
....*....|....*..
gi 491208697 485 dAILVFPGTVMVVSHDR 501
Cdd:COG4928 187 -LFFDFPNVVFVLAFDR 202
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
164-194 |
2.82e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.03 E-value: 2.82e-04
10 20 30
....*....|....*....|....*....|.
gi 491208697 164 SGGERRRVALCRLLLSKPDMLLLDEPTNHLD 194
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
342-479 |
2.90e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 342 LSFTVPPTAIVGIVGPNGAGKTT----LFRMMTGEQqpdtGTVTLGE-------------------SVKVAYVGQIRDTL 398
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSmlnaLFRIVELEK----GRIMIDDcdvakfgltdlrrvlsiipQSPVLFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 399 D-----NNKTVWE--EVSGGLDILKVGDYEIASRAYIGRFNFkgqdqqkrvgelSGGERNRLQLAKILQQGANVILLDEP 471
Cdd:PLN03232 1331 DpfsehNDADLWEalERAHIKDVIDRNPFGLDAEVSEGGENF------------SVGQRQLLSLARALLRRSKILVLDEA 1398
|
....*...
gi 491208697 472 SNDLDIET 479
Cdd:PLN03232 1399 TASVDVRT 1406
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
160-242 |
3.45e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 160 VTKLSGGERRRVALCRLLLSK---PDMLLLDEPTNHLDAESVSWL----ERfLKDFPGTIVAITHDryfLD--NVAEWIL 230
Cdd:TIGR00630 827 ATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLlevlQR-LVDKGNTVVVIEHN---LDviKTADYII 902
|
90
....*....|....*..
gi 491208697 231 EL-----DRGHGIPYQG 242
Cdd:TIGR00630 903 DLgpeggDGGGTVVASG 919
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
445-501 |
4.33e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 4.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491208697 445 LSGGERNRLQLAKilQQGA---NVI-LLDEPS-------NDLDIETLRALEDAilvfpG-TVMVVSHDR 501
Cdd:COG0178 486 LSGGEAQRIRLAT--QIGSglvGVLyVLDEPSiglhqrdNDRLIETLKRLRDL-----GnTVIVVEHDE 547
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
19-251 |
4.67e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 42.78 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEARAQpGIKIGYLE-----------QEPPLDPTKDVR 87
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLD-GRPLSSLShsvlrqgvamvQQDPVVLADTFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 88 GNV-------EDGVREALDALErldqvfaeyadpdadfdaLAKEQEKLESIIHAWDAHNLNNqleiaadalnlpawdadv 160
Cdd:PRK10790 433 ANVtlgrdisEEQVWQALETVQ------------------LAELARSLPDGLYTPLGEQGNN------------------ 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 161 tkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVSWLERFLKDF--PGTIVAITHDryfLDNV--AEWILELDRGH 236
Cdd:PRK10790 477 --LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHR---LSTIveADTILVLHRGQ 551
|
250
....*....|....*
gi 491208697 237 GIPyQGNYSSWLEQK 251
Cdd:PRK10790 552 AVE-QGTHQQLLAAQ 565
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
444-512 |
5.33e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.83 E-value: 5.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491208697 444 ELSGGERNRLQLAKILQQGAN---VILLDEPSNDLDIETLRALEDAI--LVFPG-TVMVVSHDrwfLD--RIATHIL 512
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLqrLVDKGnTVVVIEHN---LDviKCADWII 242
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
323-500 |
5.36e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.08 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLGesvKVAYVGQirDTLDNN- 401
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEG---KVTFHGK--NLYAPDv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 402 --------------------KTVWEEVSGGLDILKV-GDY-EIASRAYIGRFNF-KGQDQQKRVG-ELSGGERNRLQLAK 457
Cdd:PRK14243 85 dpvevrrrigmvfqkpnpfpKSIYDNIAYGARINGYkGDMdELVERSLRQAALWdEVKDKLKQSGlSLSGGQQQRLCIAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491208697 458 ILQQGANVILLDEPSNDLD-IETLRaLEDAI--LVFPGTVMVVSHD 500
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDpISTLR-IEELMheLKEQYTIIIVTHN 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
340-516 |
5.92e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 42.33 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 340 ENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTGEQQPDTGTVTLgESVKVAYV--GQIRDT-------------LDNNKTV 404
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI-DGVDIAKIsdAELREVrrkkiamvfqsfaLMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 405 WEEVSGGLDILKVGDYEIASRAYigrfnfkgqDQQKRVG----------ELSGGERNRLQLAKILQQGANVILLDEPSND 474
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKAL---------DALRQVGlenyahsypdELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491208697 475 LDIETLRALEDAILVFPG----TVMVVSHDRWFLDRIATHILSFEN 516
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAkhqrTIVFISHDLDEAMRIGDRIAIMQN 240
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
159-218 |
6.16e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 6.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 159 DVTKLSGGER------RRVALCRLLLSKPDMLLLDEPTNHLDAES----VSWLERFLKDFPGTIVaITHD 218
Cdd:PRK03918 785 PLTFLSGGERialglaFRLALSLYLAGNIPLLILDEPTPFLDEERrrklVDIMERYLRKIPQVII-VSHD 853
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
323-371 |
1.08e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 1.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 491208697 323 VVEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAGKTTLFRMMTG 371
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
159-237 |
1.57e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 159 DVTKLSGGERR------RVALCRLLLSKPDMLLLDEPTNHLDAESVSWL----ERFLKDFPG--TIVAITHDRYFLdNVA 226
Cdd:PRK01156 798 GIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLkdiiEYSLKDSSDipQVIMISHHRELL-SVA 876
|
90
....*....|.
gi 491208697 227 EWILELDRGHG 237
Cdd:PRK01156 877 DVAYEVKKSSG 887
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-218 |
1.59e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 40.85 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 16 PPKR-EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEaraqpgikIGYLeqeppldpTKDVRGNVEDGV 94
Cdd:PRK15079 30 PPKTlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGE--------VAWL--------GKDLLGMKDDEW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 95 REALDALERLDQvfaeyadpdadfDALAkeqeklesiihawdahNLNNQL---EIAADALNL--PAWDADVTK------- 162
Cdd:PRK15079 94 RAVRSDIQMIFQ------------DPLA----------------SLNPRMtigEIIAEPLRTyhPKLSRQEVKdrvkamm 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 163 ----------------LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVSWLERFLKDFPGTIVAITHD 218
Cdd:PRK15079 146 lkvgllpnlinrypheFSGGQCQRIGIARALILEPKLIICDEPVSALDvsiqAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
443-500 |
1.83e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 1.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 443 GELSGGERNRLQLAKilQQGAN---VI-LLDEPS-------NDLDIETLRALEDAilvfpG-TVMVVSHD 500
Cdd:PRK00349 488 GTLSGGEAQRIRLAT--QIGSGltgVLyVLDEPSiglhqrdNDRLIETLKHLRDL-----GnTLIVVEHD 550
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
445-512 |
1.86e-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: 41.15 E-value: 1.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 445 LSGGERNRLQLAKILQQ---GANVILLDEPSNDLDIETLRALEDAI--LVFPG-TVMVVSHDrwfLDRI--ATHIL 512
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLqrLVDKGnTVVVIEHN---LDVIktADYII 902
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-289 |
1.87e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 19 REILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkdfsgearaqpgikigylEQEPPLDPTKDVRGNVE--DGVRE 96
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG--------------------ELPPRSDASVVIRGTVAyvPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 97 ALDALERLDQVFAeyadpdADFDAlakeqEKLESIIHAWD-AHNLN-----NQLEIAADALNLpawdadvtklSGGERRR 170
Cdd:PLN03130 690 IFNATVRDNILFG------SPFDP-----ERYERAIDVTAlQHDLDllpggDLTEIGERGVNI----------SGGQKQR 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 171 VALCRLLLSKPDMLLLDEPTNHLDAE-SVSWLERFLKDFPG--TIVAITHDRYFLDNVAEWILeLDRGHgIPYQGNYSSW 247
Cdd:PLN03130 749 VSMARAVYSNSDVYIFDDPLSALDAHvGRQVFDKCIKDELRgkTRVLVTNQLHFLSQVDRIIL-VHEGM-IKEEGTYEEL 826
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 491208697 248 LeqKNARLEQ---------EQKQEESFAKALKKELEWVRSNAKGQQKKNKA 289
Cdd:PLN03130 827 S--NNGPLFQklmenagkmEEYVEENGEEEDDQTSSKPVANGNANNLKKDS 875
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
154-194 |
2.24e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 2.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 491208697 154 PAWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 194
Cdd:NF040905 396 PSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
324-487 |
2.40e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 324 VEVEGISKSFDGRVLYENLSFTVPPTAIVGIVGPNGAG--KTTLFRMMTGeqqPDTGTVTLGESVKVAYVGQIRDTLDNN 401
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 402 KTVW----EEVSGGLDILKVG--------DYEIASRAYIGRFNFKgQDQQKRVGELSGGERNRLQLAKILQQGANVILLD 469
Cdd:NF000106 91 RPVR*grrESFSGRENLYMIGr*ldlsrkDARARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170
....*....|....*...
gi 491208697 470 EPSNDLDIETLRALEDAI 487
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEV 187
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
445-509 |
3.59e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 3.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491208697 445 LSGGERNRLQLAKILQQGAN---VILLDEPSNDL---DIETL----RALEDAilvfpG-TVMVVSHDrwfLDRIAT 509
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhDIRKLlevlHRLVDK-----GnTVVVIEHN---LDVIKT 894
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
5-62 |
4.25e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 4.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491208697 5 IYTMN--RVSKMVPPKRE-----ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGE 62
Cdd:PRK13546 16 IYRTNkeRMKDALIPKHKnktffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-194 |
5.72e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 39.00 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 20 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFSGEA--------------RAQpgiKIGYLEQEPPldptkd 85
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhplhfgdysyRSQ---RIRMIFQDPS------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 86 vrgnvedgvrEALDALERLDQVFAEYADPDADFDALAKEQEKLESIihawdahnlnNQLEIAADALN-LPAwdadvtKLS 164
Cdd:PRK15112 98 ----------TSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETL----------RQVGLLPDHASyYPH------MLA 151
|
170 180 190
....*....|....*....|....*....|
gi 491208697 165 GGERRRVALCRLLLSKPDMLLLDEPTNHLD 194
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
162-238 |
5.76e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 39.33 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491208697 162 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVS--WLE-RFLKDFPGTIVAITHDRYFLDNVAEWILELDRGHGI 238
Cdd:NF000106 144 KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNevWDEvRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
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