|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-555 |
0e+00 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 1211.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 1 MAQFVYTMHRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDIKIGYLPQEPQL 80
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 81 NPEHTVRESIEEAVSEVVNALKRLDEVYALYADPDADFDKLAAEQGRLEEIIQAHDGHNLNVQLERAADALRLPDWDAKI 160
Cdd:PRK11819 82 DPEKTVRENVEEGVAEVKAALDRFNEIYAAYAEPDADFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPWDAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 161 ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPW 240
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 241 EGNYSSWLEQKDQRLAQEASQEAARRKSIEKELEWVRQGTKGRQSKGKARLARFEELNSTEYQKRNETNELFIPPGPRLG 320
Cdd:PRK11819 242 EGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYEELLSEEYQKRNETNEIFIPPGPRLG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFRDSMDN 400
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 401 SKTVWEEVSGGLDIMKIGNTEMPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETL 480
Cdd:PRK11819 402 NKTVWEEISGGLDIIKVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETL 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 481 RALENALLEFPGCAMVISHDRWFLDRIATHILDYQDEGKVEFFEGNFTEYEEYKKRTLGADALEPKRIKYKRIAK 555
Cdd:PRK11819 482 RALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSQVEWFEGNFQEYEEDKKRRLGADAARPHRIKYKKLTR 556
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-553 |
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: 1150.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 2 AQFVYTMHRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDIKIGYLPQEPQLN 81
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 82 PEHTVRESIEEAVSEVVNALKRLDEVYALYADPDADFDKLAAEQGRLEEIIQAHDGHNLNVQLERAADALRLPDWDAKIA 161
Cdd:TIGR03719 81 PTKTVRENVEEGVAEIKDALDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDADVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWE 241
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 242 GNYSSWLEQKDQRLAQEASQEAARRKSIEKELEWVRQGTKGRQSKGKARLARFEELNSTEYQKRNETNELFIPPGPRLGD 321
Cdd:TIGR03719 241 GNYSSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRNETAEIYIPPGPRLGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 322 KVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFRDSMDNS 401
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 402 KTVWEEVSGGLDIMKIGNTEMPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLR 481
Cdd:TIGR03719 401 KTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLR 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 482 ALENALLEFPGCAMVISHDRWFLDRIATHILDYQDEGKVEFFEGNFTEYEEYKKRTLGADALEPKRIKYKRI 553
Cdd:TIGR03719 481 ALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEEDKKRRLGEDADQPHRIKYKKL 552
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-533 |
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: 720.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 8 MHRVGKVVPpKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDIKIGYLPQEPQLNPEHTVR 87
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 88 ESIEEAVSEVVNALKRLDEVYALYADPDADfdklAAEQGRLEEIIQAHDGHNLNVQLERAADALRLP--DWDAKIANLSG 165
Cdd:COG0488 80 DTVLDGDAELRALEAELEELEAKLAEPDED----LERLAELQEEFEALGGWEAEARAEEILSGLGFPeeDLDRPVSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 166 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYS 245
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 246 SWLEQKDQRLAQEASQEAARRKSIEKELEWVRQ-GTKGRQSK-GKARLARFEELNSTEYQKRNETNELFIPPGPRLGDKV 323
Cdd:COG0488 236 AYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARKAKqAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFRDSMDNSKT 403
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 404 VWEEVSGGLDimkiGNTEMPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRAL 483
Cdd:COG0488 396 VLDELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2788209839 484 ENALLEFPGCAMVISHDRWFLDRIATHILDYQDeGKVEFFEGNFTEYEEY 533
Cdd:COG0488 472 EEALDDFPGTVLLVSHDRYFLDRVATRILEFED-GGVREYPGGYDDYLEK 520
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-527 |
9.33e-109 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 338.46 E-value: 9.33e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGidkDI---EGEARPQPDIKIGYLPQEPQLNPEHTVRESIEEAVSEV 97
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG---EVlldDGRIIYEQDLIVARLQQDPPRNVEGTVYDFVAEGIEEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 98 VNALKRLDEVYALYA-DPDadfDKLAAEQGRLEEIIQAHDGHNLNVQLERAADALRLpDWDAKIANLSGGERRRVALCRL 176
Cdd:PRK11147 95 AEYLKRYHDISHLVEtDPS---EKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGL-DPDAALSSLSGGWLRKAALGRA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 177 LLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQKDQRLA 256
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 257 QEASQEAARRKSIEKELEWVRQGTKGRQSKGKARLARFEELNSTEYQKRNE--TNELFIPPGPRLGDKVLEVSNLRKSYG 334
Cdd:PRK11147 251 VEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVmgTAKMQVEEASRSGKIVFEMENVNYQID 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 335 DRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFRDSMDNSKTVWEEVSGGLDI 414
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNLAEGKQE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 415 MKIGNTEMPSRAYVGRFNFkgvdQGKR----VGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEF 490
Cdd:PRK11147 411 VMVNGRPRHVLGYLQDFLF----HPKRamtpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY 486
|
490 500 510
....*....|....*....|....*....|....*..
gi 2788209839 491 PGCAMVISHDRWFLDRIATHILDYQDEGKVEFFEGNF 527
Cdd:PRK11147 487 QGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGY 523
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
24-530 |
1.65e-75 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 248.65 E-value: 1.65e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 24 NISLSFFPGAKIGVLGLNGAGKSTLLRIMAGidkDIE---GEARPQPDIKIGYLPQEPQLNPEHTVRESIEEAVSEVVNA 100
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGG---DLEpsaGNVSLDPNERLGKLRQDQFAFEEFTVLDTVIMGHTELWEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 101 LKRLDEVYALYADPDADFDKlAAEqgrLEEIIQAHDGHNLNvqlERAADAL-----RLPDWDAKIANLSGGERRRVALCR 175
Cdd:PRK15064 96 KQERDRIYALPEMSEEDGMK-VAD---LEVKFAEMDGYTAE---ARAGELLlgvgiPEEQHYGLMSEVAPGWKLRVLLAQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 176 LLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQKDQRL 255
Cdd:PRK15064 169 ALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQAR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 256 AQEASQEAARRKSIEKELEWVRQ----GTKGRQSKGKARLA---RFEELNSTEYQKRnetnelFI--PPGPRLGDKVLEV 326
Cdd:PRK15064 249 ERLLADNAKKKAQIAELQSFVSRfsanASKAKQATSRAKQIdkiKLEEVKPSSRQNP------FIrfEQDKKLHRNALEV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 327 SNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLA-----SVDQFrdsmDNS 401
Cdd:PRK15064 323 ENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGyyaqdHAYDF----END 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 402 KTVWEEVSgglDIMKIGNTEMPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLR 481
Cdd:PRK15064 399 LTLFDWMS---QWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIE 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2788209839 482 ALENALLEFPGCAMVISHDRWFLDRIATHILDYQDEGkVEFFEGNFTEY 530
Cdd:PRK15064 476 SLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDG-VVDFSGTYEEY 523
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-533 |
1.85e-65 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 224.66 E-value: 1.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-IDKDIEGEARPQpDIKIGYLPQE-PQLNpehtvRESIEEAVse 96
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNeISADGGSYTFPG-NWQLAWVNQEtPALP-----QPALEYVI-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 97 vvnalkrldevyalyaDPDADFDKLAAEqgrLEEIIQAHDGH---NLNVQLE---------RAADALR-----LPDWDAK 159
Cdd:PRK10636 86 ----------------DGDREYRQLEAQ---LHDANERNDGHaiaTIHGKLDaidawtirsRAASLLHglgfsNEQLERP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 160 IANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIP 239
Cdd:PRK10636 147 VSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 240 WEGNYSSWLEQKDQRLAQEAS---QEAARRKSIEKELEWVR-QGTKGRQSKGKARLARFEELNSTEYQKrNETNELFIPP 315
Cdd:PRK10636 227 YTGNYSSFEVQRATRLAQQQAmyeSQQERVAHLQSYIDRFRaKATKAKQAQSRIKMLERMELIAPAHVD-NPFHFSFRAP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 316 gPRLGDKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFR 395
Cdd:PRK10636 306 -ESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 DSMDNSKtvwEEVSGGLDIMKIGNTEMPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDL 475
Cdd:PRK10636 385 LEFLRAD---ESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 476 DIETLRALENALLEFPGCAMVISHDRWFLdRIATHILDYQDEGKVEFFEGNFTEYEEY 533
Cdd:PRK10636 462 DLDMRQALTEALIDFEGALVVVSHDRHLL-RSTTDDLYLVHDGKVEPFDGDLEDYQQW 518
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
326-534 |
5.42e-65 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 220.32 E-value: 5.42e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 326 VSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQfRDSMDNSKTVW 405
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQ-EPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 406 EEVSGGL----------------------DIMKIGNTE----------MPSRA--YVGRFNFKGVDQGKRVGELSGGERG 451
Cdd:COG0488 80 DTVLDGDaelraleaeleeleaklaepdeDLERLAELQeefealggweAEARAeeILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 452 RLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEFPGCAMVISHDRWFLDRIATHILDYqDEGKVEFFEGNFTEYE 531
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILEL-DRGKLTLYPGNYSAYL 238
|
...
gi 2788209839 532 EYK 534
Cdd:COG0488 239 EQR 241
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
324-518 |
8.56e-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: 184.19 E-value: 8.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQfrdsmdnskt 403
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 404 vweevsggldimkigntempsrayvgrfnfkgvdqgkrvgeLSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRAL 483
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 2788209839 484 ENALLEFPGCAMVISHDRWFLDRIATHILDYQDEG 518
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
25-538 |
6.36e-53 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 191.61 E-value: 6.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 25 ISLSFfpGAKIGVLGLNGAGKSTLLRIMAGidKDIEGEARpqpDIKIGYLPQEPQ----------LNPEHTVRESIEEAV 94
Cdd:PLN03073 198 VTLAF--GRHYGLVGRNGTGKTTFLRYMAM--HAIDGIPK---NCQILHVEQEVVgddttalqcvLNTDIERTQLLEEEA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 95 SEVvnALKRLDEVYALYADP----DADFDKLAAEQgRLEEIIQAHDGHNLNVQLERAADALR----LPDWDAKIAN-LSG 165
Cdd:PLN03073 271 QLV--AQQRELEFETETGKGkganKDGVDKDAVSQ-RLEEIYKRLELIDAYTAEARAASILAglsfTPEMQVKATKtFSG 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 166 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYS 245
Cdd:PLN03073 348 GWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYD 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 246 SWLEQKDQRL-----AQEASQEAarRKSIEKELEWVRQGTKGR---QSKGKA--RLARFEE-LNSTEYQKRnetnelFIP 314
Cdd:PLN03073 428 TFERTREEQLknqqkAFESNERS--RSHMQAFIDKFRYNAKRAslvQSRIKAldRLGHVDAvVNDPDYKFE------FPT 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 315 PGPRLGDKVLEVSNLRKSY-GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQ 393
Cdd:PLN03073 500 PDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQ 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 FR-DSMDNSKTVWeevsggLDIMKI--GNTEMPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDE 470
Cdd:PLN03073 580 HHvDGLDLSSNPL------LYMMRCfpGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDE 653
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 471 PTNDLDIETLRALENALLEFPGCAMVISHDRWFLDRiATHILDYQDEGKVEFFEGNFTEYeeykKRTL 538
Cdd:PLN03073 654 PSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISG-SVDELWVVSEGKVTPFHGTFHDY----KKTL 716
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
18-236 |
5.30e-49 |
|
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: 166.08 E-value: 5.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDIKIGYLPQepqlnpehtvresieeavsev 97
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 98 vnalkrldevyalyadpdadfdklaaeqgrleeiiqahdghnlnvqleraadalrlpdwdakianLSGGERRRVALCRLL 177
Cdd:cd03221 71 -----------------------------------------------------------------LSGGEKMRLALAKLL 85
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 178 LEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-512 |
4.24e-48 |
|
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: 174.71 E-value: 4.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI--------------DKDIEGEARPQPDIKIGYLPQEP--QLNP 82
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphggrisgevlldGRDLLELSEALRGRRIGMVFQDPmtQLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 83 eHTVRESIEEAVsevvnalkRLDEVyalyadPDADFDKLAAEQgrLEEiiqahdghnlnVQLERAADAlrlpdwdaKIAN 162
Cdd:COG1123 99 -VTVGDQIAEAL--------ENLGL------SRAEARARVLEL--LEA-----------VGLERRLDR--------YPHQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEgI 238
Cdd:COG1123 143 LSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGR-I 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 239 PWEGNYSSWLEQkDQRLAQEASQEAARRKSiekelewvrqgtkgrqskgkarlarfeelnsteyqkrnetnelfiPPGPR 318
Cdd:COG1123 222 VEDGPPEEILAA-PQALAAVPRLGAARGRA---------------------------------------------APAAA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 319 LGDKVLEVSNLRKSY-----GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVD 392
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdGKDLTKLSRR 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 393 QFRD--------------SMDNSKTVWEEVSGGLDIMKIGN-TEMPSRAY-----VG---RFnfkgvdQGKRVGELSGGE 449
Cdd:COG1123 336 SLRElrrrvqmvfqdpysSLNPRMTVGDIIAEPLRLHGLLSrAERRERVAellerVGlppDL------ADRYPHELSGGQ 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 450 RGRLHLAKLLQVGGNMLLLDEPTNDLD-------IETLRALENALlefpGCAMV-ISHDRWFLDRIATHIL 512
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDvsvqaqiLNLLRDLQREL----GLTYLfISHDLAVVRYIADRVA 476
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
19-236 |
3.19e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.87 E-value: 3.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEA----RPQPDI-------KIGYLPQEPQLnPEHTVR 87
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMpppewrrQVAYVPQEPAL-WGGTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 88 ESIEEAVSevvnalkrldevyalYADPDADFDKLAAEqgrLEeiiqahdghnlnvQLERAADALrlpdwDAKIANLSGGE 167
Cdd:COG4619 92 DNLPFPFQ---------------LRERKFDRERALEL---LE-------------RLGLPPDIL-----DKPVERLSGGE 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG4619 136 RQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-191 |
2.12e-36 |
|
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: 132.39 E-value: 2.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE-----------ARPQPDIKIGYLPQEPQLNPEHTVRESI 90
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqdltddERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 91 EEAVsevvnalkrldevyalyadpdadfdklaaeqgrleeIIQAHDGHNLNVQLERAADALRLPDWDAKIA-----NLSG 165
Cdd:pfam00005 81 RLGL------------------------------------LLKGLSKREKDARAEEALEKLGLGDLADRPVgerpgTLSG 124
|
170 180
....*....|....*....|....*.
gi 2788209839 166 GERRRVALCRLLLEKPDMLLLDEPTN 191
Cdd:pfam00005 125 GQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
324-513 |
2.45e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 135.19 E-value: 2.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTIT-LGETV---------KLASVDQ 393
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVardpaevrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 fRDSMDNSKTVWE--EVSGGLdiMKIGNTEMPSRA--YVGRFNFKGVdQGKRVGELSGGERGRLHLAKLL----QVggnm 465
Cdd:COG1131 81 -EPALYPDLTVREnlRFFARL--YGLPRKEARERIdeLLELFGLTDA-ADRKVGTLSGGMKQRLGLALALlhdpEL---- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788209839 466 LLLDEPTNDLDIETLRALENALLEF--PGCAMVIShdrwfldriaTHILD 513
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELaaEGKTVLLS----------THYLE 192
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
339-473 |
5.51e-36 |
|
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: 131.23 E-value: 5.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGET-----------VKLASVDQFrDSMDNSKTVWEE 407
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrKEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 408 VSGGLDIMKIGNTEMPSRAYVGRFNFKGVDQGKRV-----GELSGGERGRLHLAKLLQVGGNMLLLDEPTN 473
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-225 |
6.99e-36 |
|
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: 132.99 E-value: 6.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE----------ARPQPDIKIGYLPQEPQLNPEHTVRE 88
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEvlwngepirdAREDYRRRLAYLGHADGLKPELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 89 SIeeavsevvnalkrldevyALYadpdADFDKLAAEQGRLEEIIQAhdghnlnVQLERAAdalrlpdwDAKIANLSGGER 168
Cdd:COG4133 95 NL------------------RFW----AALYGLRADREAIDEALEA-------VGLAGLA--------DLPVRQLSAGQK 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 169 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF---EGTVVAITHDRYFLDNV 225
Cdd:COG4133 138 RRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
321-512 |
4.31e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.14 E-value: 4.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLAS-----VDQf 394
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPRRARrrigyVPQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 395 RDSMDNSK--TVWEEVSGGLDImKIGNTEMPSRAY----------VGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVG 462
Cdd:COG1121 83 RAEVDWDFpiTVRDVVLMGRYG-RRGLFRRPSRADreavdealerVGLEDLA----DRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 463 GNMLLLDEPTNDLDIETLRALENALLEFP--GCAM-VISHDRWFLDRIATHIL 512
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRreGKTIlVVTHDLGAVREYFDRVL 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-235 |
2.40e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.13 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR------PQPDIKIGYLPQEPQLNPEHTVResie 91
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQRAEVDWDFPIT---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 92 eaVSEVVnalkrldevyALYADPdadfdklaaeQGRLEEIIQAHDghnlnvqLERAADALRLPD----WDAKIANLSGGE 167
Cdd:COG1121 94 --VRDVV----------LMGRYG----------RRGLFRRPSRAD-------REAVDEALERVGledlADRPIGELSGGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELDRG 235
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-236 |
2.49e-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: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE---------ARPQPDI--KIGYLPQepqlNPEH-- 84
Cdd:cd03225 13 ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvlvdgkdltKLSLKELrrKVGLVFQ----NPDDqf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 ---TVREsieeavsEVVNALKRLdevyalyadpdadfdKLAAEqgrleEIIQAhdghnlnvqLERAADALRLPDW-DAKI 160
Cdd:cd03225 89 fgpTVEE-------EVAFGLENL---------------GLPEE-----EIEER---------VEEALELVGLEGLrDRSP 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 161 ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03225 133 FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
323-512 |
2.70e-33 |
|
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: 127.47 E-value: 2.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETV----------KLASV 391
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 392 DQFRDSMDNSkTVWEEVSGGLdimkigntempsRAYVGRFNFKG------VDQ-----------GKRVGELSGGERGRLH 454
Cdd:COG1120 81 PQEPPAPFGL-TVRELVALGR------------YPHLGLFGRPSaedreaVEEalertglehlaDRPVDELSGGERQRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 455 LAKLLQVGGNMLLLDEPTNDLDI----ETLRALEnALLEFPGCAMVIS-HDrwfLD---RIATHIL 512
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLahqlEVLELLR-RLARERGRTVVMVlHD---LNlaaRYADRLV 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
324-513 |
4.57e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.31 E-value: 4.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRdsmdnSK 402
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPLSAMPPPEWR-----RQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 403 -------------TVWEEVSGGLDIMKIGNTEMPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLD 469
Cdd:COG4619 76 vayvpqepalwggTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788209839 470 EPTNDLDIETLRALENALLEFP----GCAMVISHDRWFLDRIATHILD 513
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLT 203
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
325-512 |
5.33e-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: 125.27 E-value: 5.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 325 EVSNLRKSYGD--RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFR------ 395
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLTKLSLKELRrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 ----DSMDNSKTVWEEVSGGLDIMKIGNTEMPSRA--YVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLD 469
Cdd:cd03225 81 fqnpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVeeALELVGLEGL-RDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2788209839 470 EPTNDLDIETLRALENALLEFPGCAM---VISHDRWFLDRIATHIL 512
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKtiiIVTHDLDLLLELADRVI 205
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
324-512 |
1.23e-32 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 122.89 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTIT-LGETVKLASVDQFR------- 395
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvLGKDIKKEPEEVKRrigylpe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 -DSMDNSKTVWEevsggldimkigntempsrayvgrfNFKgvdqgkrvgeLSGGERGRLHLAKLLQVGGNMLLLDEPTND 474
Cdd:cd03230 81 ePSLYENLTVRE-------------------------NLK----------LSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2788209839 475 LDIETLRALENALLEFP--GCAMVI-SHDRWFLDRIATHIL 512
Cdd:cd03230 126 LDPESRREFWELLRELKkeGKTILLsSHILEEAERLCDRVA 166
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-236 |
1.25e-32 |
|
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: 124.75 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE---------ARPQPDI--KIGYLPQepqlNPEH 84
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEvlvdgkditKKNLRELrrKVGLVFQ----NPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 -----TVREsieeavsEVVNALKRLdevyalyadpdadfdklaaeqGRLEEIIQAhdghnlnvQLERAADALRLPDW-DA 158
Cdd:COG1122 87 qlfapTVEE-------DVAFGPENL---------------------GLPREEIRE--------RVEEALELVGLEHLaDR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 159 KIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELDRG 235
Cdd:COG1122 131 PPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVLDDG 210
|
.
gi 2788209839 236 E 236
Cdd:COG1122 211 R 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
325-512 |
1.71e-32 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 123.80 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 325 EVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETV-----KLASVDQFRdSM 398
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLekerkRIGYVPQRR-SI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 DNSK--TVWEEVSGGLDImKIGNTEMPSRAY----------VGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNML 466
Cdd:cd03235 80 DRDFpiSVRDVVLMGLYG-HKGLFRRLSKADkakvdealerVGLSELA----DRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2788209839 467 LLDEPTNDLDIETLRALENALLEF--PGCAM-VISHDRWFLDRIATHIL 512
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELrrEGMTIlVVTHDLGLVLEYFDRVL 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
17-218 |
1.93e-32 |
|
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: 125.16 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR---------PQPDI--KIGYLPQEPQLNPEHT 85
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlaslSRRELarRIAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VREsieeavseVVnALKRLDEVYALYADPDADfdklaaeqgrlEEIIqahdghnlnvqlERAADALRLPDW-DAKIANLS 164
Cdd:COG1120 92 VRE--------LV-ALGRYPHLGLFGRPSAED-----------REAV------------EEALERTGLEHLaDRPVDELS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLD-AESVAWLE--RFLHDFEG-TVVAITHD 218
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDlAHQLEVLEllRRLARERGrTVVMVLHD 197
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
18-236 |
2.20e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 124.41 E-value: 2.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR--------PQPDIK--IGYLPQEPQLNPEHTVR 87
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvarDPAEVRrrIGYVPQEPALYPDLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 88 ESIEeavsevvnalkrldeVYA-LYADPDADFDKlaaeqgRLEEIIQAhdghnlnVQLERAADAlrlpdwdaKIANLSGG 166
Cdd:COG1131 92 ENLR---------------FFArLYGLPRKEARE------RIDELLEL-------FGLTDAADR--------KVGTLSGG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG1131 136 MKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaEGkTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-251 |
3.06e-32 |
|
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: 131.49 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR----PQPDI-------KIGYLPQEPQLNPEh 84
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgiDLRQIdpaslrrQIGVVLQDVFLFSG- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 TVRESIeeavsevvnalkrldevyaLYADPDADFDKL--AAEQGRLEEIIQAH-DGHNLNVQlERAAdalrlpdwdakia 161
Cdd:COG2274 564 TIRENI-------------------TLGDPDATDEEIieAARLAGLHDFIEALpMGYDTVVG-EGGS------------- 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAITHDRYFLDNvAGWILELDRGEgIP 239
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-ADRIIVLDKGR-IV 688
|
250
....*....|..
gi 2788209839 240 WEGNYSSWLEQK 251
Cdd:COG2274 689 EDGTHEELLARK 700
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
325-516 |
3.44e-32 |
|
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: 121.20 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 325 EVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLgetvklasvdqfrdsmdnsktv 404
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 405 weevsGGLDIMKIGNTEMPSRAYVgrfnfkgvdqgkrVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALE 484
Cdd:cd00267 59 -----DGKDIAKLPLEELRRRIGY-------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 2788209839 485 NALLEF--PGCAMV-ISHDRWFLDRIATHILDYQD 516
Cdd:cd00267 121 ELLRELaeEGRTVIiVTHDPELAELAADRVIVLKD 155
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
323-520 |
4.06e-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: 123.81 E-value: 4.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFRDSM---- 398
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIgvlp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 -----DNSKTVWEEVSGGLDIMKIGNTEMPSRA--YVGRFNFkGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEP 471
Cdd:COG4555 81 derglYDRLTVRENIRYFAELYGLFDEELKKRIeeLIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 472 TNDLDIETLRALENALLEF---PGCAMVISHDRWFLDRIATHILdYQDEGKV 520
Cdd:COG4555 160 TNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVV-ILHKGKV 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
325-512 |
4.20e-32 |
|
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: 121.77 E-value: 4.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 325 EVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLgetvklasvdqfrdsmdnsktv 404
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 405 weevsGGLDIMKIGNTEM-PSRAYV-------GRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:cd03214 59 -----DGKDLASLSPKELaRKIAYVpqalellGLAHLA----DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2788209839 477 I-------ETLRALENALlefpGCAMVIS-HDRWFLDRIATHIL 512
Cdd:cd03214 130 IahqiellELLRRLARER----GKTVVMVlHDLNLAARYADRVI 169
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
324-532 |
5.70e-32 |
|
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: 122.83 E-value: 5.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSY-GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRDSM--- 398
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDITKKNLRELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 ----DN---SKTVWEEVSGGLDIMKIGNTEMPSR-----AYVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNML 466
Cdd:COG1122 81 fqnpDDqlfAPTVEEDVAFGPENLGLPREEIRERveealELVGLEHLA----DRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 467 LLDEPTNDLDIETLRALENALLEFP--GCAMV-ISHDRWFLDRIATHILdYQDEGKVeFFEGN----FTEYEE 532
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNkeGKTVIiVTHDLDLVAELADRVI-VLDDGRI-VADGTprevFSDYEL 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
323-513 |
7.37e-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: 121.82 E-value: 7.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFR------- 395
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRrrlaylg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 --DSMDNSKTVWEEVSGGLDIMKIGNTEMPSRAYVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTN 473
Cdd:COG4133 82 haDGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2788209839 474 DLDIETLRALENALLEFP---GCAMVISHDRwfLDRIATHILD 513
Cdd:COG4133 161 ALDAAGVALLAELIAAHLargGAVLLTTHQP--LELAAARVLD 201
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-251 |
3.56e-31 |
|
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: 127.57 E-value: 3.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR----PQPDI-------KIGYLPQEPQLnPEH 84
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvDLSDLdpaswrrQIAWVPQNPYL-FAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 TVRESIeeavsevvnalkRLdevyalyADPDADFDKL--AAEQGRLEEIIQahdghnlnvqleraadalRLPD-WDAKI- 160
Cdd:COG4988 426 TIRENL------------RL-------GRPDASDEELeaALEAAGLDEFVA------------------ALPDgLDTPLg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 161 ---ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD-FEG-TVVAITHDRYFLDNvAGWILELDRG 235
Cdd:COG4988 469 eggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGrTVILITHRLALLAQ-ADRILVLDDG 547
|
250
....*....|....*.
gi 2788209839 236 EGIPwEGNYSSWLEQK 251
Cdd:COG4988 548 RIVE-QGTHEELLAKN 562
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-235 |
1.43e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 118.40 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR--PQPDIK----IGYLPQEPQLNPEHTVResiee 92
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfGKPLEKerkrIGYVPQRRSIDRDFPIS----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 93 aVSEVVnALKRLDEVYALYADPDADFDKlaaeqgrleeIIQAHDghnlNVQLEraadALRlpdwDAKIANLSGGERRRVA 172
Cdd:cd03235 87 -VRDVV-LMGLYGHKGLFRRLSKADKAK----------VDEALE----RVGLS----ELA----DRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 173 LCRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDFEGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELlreLRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-236 |
2.81e-30 |
|
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: 118.81 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-IDKD-----IEGE-ARPQPDI---KIGYLPQEPQLNPEHTVR 87
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGlLKPDsgsilIDGEdVRKEPREarrQIGVLPDERGLYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 88 ESIEeavsevvnalkrldEVYALYADPDADFDKlaaeqgRLEEIIQAhdghnlnVQLERAAdalrlpdwDAKIANLSGGE 167
Cdd:COG4555 93 ENIR--------------YFAELYGLFDEELKK------RIEELIEL-------LGLEEFL--------DRRVGELSTGM 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF---EGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG4555 138 KKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGK 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-236 |
4.71e-30 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 115.96 E-value: 4.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEA--------RPQPDIK--IGYLPQEPQLNPEHTVR 87
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdikKEPEEVKrrIGYLPEEPSLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 88 ESIEeavsevvnalkrldevyalyadpdadfdklaaeqgrleeiiqahdghnlnvqleraadalrlpdwdakianLSGGE 167
Cdd:cd03230 92 ENLK-----------------------------------------------------------------------LSGGM 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF---EGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03230 101 KQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
324-508 |
5.09e-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: 116.85 E-value: 5.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRDSM---D 399
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVTGVPPERRNIGMvfqD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 400 NS----KTVWEEVSGGLDIMKIGNTEMPSRAY-----VGRFNFkgvdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDE 470
Cdd:cd03259 81 YAlfphLTVAENIAFGLKLRGVPKAEIRARVRellelVGLEGL----LNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2788209839 471 PTNDLDIET---LRALENALLEFPGCAMV-ISHDR----WFLDRIA 508
Cdd:cd03259 157 PLSALDAKLreeLREELKELQRELGITTIyVTHDQeealALADRIA 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
19-251 |
1.15e-29 |
|
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: 122.95 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR---------PQPDI--KIGYLPQEPQL-NpeHTV 86
Cdd:COG4987 348 RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdlDEDDLrrRIAVVPQRPHLfD--TTL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 87 RESIeeavsevvnalkrldevyaLYADPDADFDKL--AAEQGRLEEIIQAhdghnlnvqleraadalrLPD-WDAKI--- 160
Cdd:COG4987 426 RENL-------------------RLARPDATDEELwaALERVGLGDWLAA------------------LPDgLDTWLgeg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 161 -ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV-AWLERFLHDFEG-TVVAITHDRYFLDNVAGwILELDRGEG 237
Cdd:COG4987 469 gRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEqALLADLLEALAGrTVLLITHRLAGLERMDR-ILVLEDGRI 547
|
250
....*....|....
gi 2788209839 238 IPwEGNYSSWLEQK 251
Cdd:COG4987 548 VE-QGTHEELLAQN 560
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-512 |
2.44e-29 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 122.22 E-value: 2.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 31 PGAKIGVLGLNGAGKSTLLRIMAGIDK----DIEGEARP--------------------QPDIKIGYLPQEPQLNPEH-- 84
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIpnlgDYEEEPSWdevlkrfrgtelqnyfkklyNGEIKVVHKPQYVDLIPKVfk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 -TVREsieeavsevvnALKRLDEvyalyadpdadfdklaaeQGRLEEIIQAHDGHNLnvqleraadalrlpdWDAKIANL 163
Cdd:PRK13409 178 gKVRE-----------LLKKVDE------------------RGKLDEVVERLGLENI---------------LDRDISEL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDfEGTVVAITHDRYFLDNVA-------------G 227
Cdd:PRK13409 214 SGGELQRVAIAAALLRDADFYFFDEPTSYLDIRqrlNVARLIRELAE-GKYVLVVEHDLAVLDYLAdnvhiaygepgayG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 228 wILELDRG--EGIpweGNY-SSWLEQKDQRLaqeasqeaaRRKSIEkelewvrqgtkgrqskgkarlarFEELNSTEYQK 304
Cdd:PRK13409 293 -VVSKPKGvrVGI---NEYlKGYLPEENMRI---------RPEPIE-----------------------FEERPPRDESE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 305 RnetnelfippgprlgDKVLEVSNLRKSYGD-RLLIDdlSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLg 383
Cdd:PRK13409 337 R---------------ETLVEYPDLTKKLGDfSLEVE--GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 384 eTVKLA------------SVDQFRDSMD---NSKTVWEEVSGGLDIMKIGNtempsrayvgrfnfkgvdqgKRVGELSGG 448
Cdd:PRK13409 399 -ELKISykpqyikpdydgTVEDLLRSITddlGSSYYKSEIIKPLQLERLLD--------------------KNVKDLSGG 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 449 ERGRLHLAKLLQVGGNMLLLDEPTNDLDIE----TLRALENALLEFPGCAMVISHDRWFLDRIATHIL 512
Cdd:PRK13409 458 ELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-472 |
3.42e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.81 E-value: 3.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-DKD-----IEGEARPQPDIK------IGYLPQEPQLNPEHTVRES 89
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVyQPDsgeilLDGEPVRFRSPRdaqaagIAIIHQELNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 90 IeeavsevvnalkrldevyalyadpdadFdkLAAEQGRLEEIiqahdghNLNVQLERAADALR---LP-DWDAKIANLSG 165
Cdd:COG1129 100 I---------------------------F--LGREPRRGGLI-------DWRAMRRRARELLArlgLDiDPDTPVGDLSV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 166 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHdryFLDNvagwILEL-DR------G 235
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLkaQGvAIIYISH---RLDE----VFEIaDRvtvlrdG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 236 EGIpwegnysswleqkDQRLAQEASQEAARRKSIEKELEwvrqgtkgrqskgkarlarfeelnsteyqkrnetnELFIPP 315
Cdd:COG1129 217 RLV-------------GTGPVAELTEDELVRLMVGRELE-----------------------------------DLFPKR 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 316 GPRLGDKVLEVSNLRksygDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVdqf 394
Cdd:COG1129 249 AAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdGKPVRIRSP--- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 395 RDSMDN----------------SKTVWEEVS----------GGLDIMKIGNTempSRAYVGRFNFKGVDQGKRVGELSGG 448
Cdd:COG1129 322 RDAIRAgiayvpedrkgeglvlDLSIRENITlasldrlsrgGLLDRRRERAL---AEEYIKRLRIKTPSPEQPVGNLSGG 398
|
490 500
....*....|....*....|....
gi 2788209839 449 ERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
324-511 |
3.90e-28 |
|
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: 111.83 E-value: 3.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGD--RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFRDSM--- 398
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 --DNskTVWEEVSgGLDIMKI-------GNTEMPSRA--YVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLqVGGN-ML 466
Cdd:cd03263 81 pqFD--ALFDELT-VREHLRFyarlkglPKSEIKEEVelLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIAL-IGGPsVL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2788209839 467 LLDEPTNDLDIETLRALENALLEF-PGCAMVI-SHDRWFLDRIATHI 511
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVrKGRSIILtTHSMDEAEALCDRI 202
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
323-508 |
4.64e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 112.94 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG-------ETVKLAsvdQFR 395
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNgrpladwSPAELA---RRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 ------DSMDNSKTVWEEVSGGLDIMKIGNTEMPS-----------RAYVGRFnfkgvdqgkrVGELSGGERGRLHLAKL 458
Cdd:PRK13548 79 avlpqhSSLSFPFTVEEVVAMGRAPHGLSRAEDDAlvaaalaqvdlAHLAGRD----------YPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 459 L-QV-----GGNMLLLDEPTNDLDI----ETLRALENALLEFPGCAMVISHD-----RWfLDRIA 508
Cdd:PRK13548 149 LaQLwepdgPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHDlnlaaRY-ADRIV 212
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
320-529 |
4.85e-28 |
|
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: 112.38 E-value: 4.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 320 GDKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTIT-LGETVKLASVDQFR--- 395
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvDGQDITGLSEKELYelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 -------------DSMdnskTVWEEVSGGLDImkigNTEMPS-------RAYVGRFNFKGVdQGKRVGELSGGERGRLHL 455
Cdd:COG1127 82 rrigmlfqggalfDSL----TVFENVAFPLRE----HTDLSEaeirelvLEKLELVGLPGA-ADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 456 AKLLQVGGNMLLLDEPTNDLDIETLRALENALLE----FPGCAMVISHDRWFLDRIATHILdYQDEGKVEfFEGNFTE 529
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIADRVA-VLADGKII-AEGTPEE 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-235 |
7.46e-28 |
|
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: 117.54 E-value: 7.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 14 VVPP--KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR---------PQPDIK--IGYLPQEPQL 80
Cdd:COG4618 338 VVPPgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgadlsqwDREELGrhIGYLPQDVEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 81 NPEhTVRESIeeavsevvnalkrldevyALYADPDAdfdklaaeqgrlEEIIQAhdghnlnvqlERAADA----LRLPD- 155
Cdd:COG4618 418 FDG-TIAENI------------------ARFGDADP------------EKVVAA----------AKLAGVhemiLRLPDg 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 156 WDAKI----ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFE---GTVVAITHDRYFLdNVAGW 228
Cdd:COG4618 457 YDTRIgeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKargATVVVITHRPSLL-AAVDK 535
|
....*..
gi 2788209839 229 ILELDRG 235
Cdd:COG4618 536 LLVLRDG 542
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-235 |
7.46e-28 |
|
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: 111.14 E-value: 7.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR----------PQpDIK--IGYLPQEPQLNpEHT 85
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLldgtdirqldPA-DLRrnIGYVPQDVTLF-YGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIEeavsevvnalkrldevyalYADPDADFDKL--AAEQGRLEEIIQAH-DGHNLNVQlERAAdalrlpdwdakiaN 162
Cdd:cd03245 94 LRDNIT-------------------LGAPLADDERIlrAAELAGVTDFVNKHpNGLDLQIG-ERGR-------------G 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVawlERFLHDFEG-----TVVAITHdRYFLDNVAGWILELDRG 235
Cdd:cd03245 141 LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE---ERLKERLRQllgdkTLIIITH-RPSLLDLVDRIIVMDSG 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
324-520 |
9.08e-28 |
|
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: 111.04 E-value: 9.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGD----RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASvDQFRDSM 398
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDISKLS-EKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 DNSK--------------TVWEEVSGGLDIMKIGNTEMPSRA-----YVG---RFNfkgvdqgKRVGELSGGERGRLHLA 456
Cdd:cd03255 80 RRRHigfvfqsfnllpdlTALENVELPLLLAGVPKKERRERAeelleRVGlgdRLN-------HYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 457 KLLQVGGNMLLLDEPTNDLDIETLRALENALLEF---PGCAMVI-SHDRwFLDRIATHILDYQDeGKV 520
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELnkeAGTTIVVvTHDP-ELAEYADRIIELRD-GKI 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-512 |
1.19e-27 |
|
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: 117.19 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 31 PGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPD------------------------IKIGYLPQEPQLNPEH-- 84
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSwdevlkrfrgtelqdyfkklangeIKVAHKPQYVDLIPKVfk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 -TVREsieeavsevvnALKRLDEvyalyadpdadfdklaaeQGRLEEIIqahdghnlnvqleraaDALRL-PDWDAKIAN 162
Cdd:COG1245 178 gTVRE-----------LLEKVDE------------------RGKLDELA----------------EKLGLeNILDRDISE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDFEGTVVAITHDRYFLDNVAGWIlELDRGE--- 236
Cdd:COG1245 213 LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYqrlNVARLIRELAEEGKYVLVVEHDLAILDYLADYV-HILYGEpgv 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 237 ------------GIpweGNY-SSWLEQKDQRLaqeasqeaaRRKSIEkelewvrqgtkgrqskgkarlarFEELNSTEYQ 303
Cdd:COG1245 292 ygvvskpksvrvGI---NQYlDGYLPEENVRI---------RDEPIE-----------------------FEVHAPRREK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 304 KRnetnelfippgprlgDKVLEVSNLRKSYGD-RLLIDdlSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITl 382
Cdd:COG1245 337 EE---------------ETLVEYPDLTKSYGGfSLEVE--GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 383 gETVKLA------------SVDQF-----RDSMDNSKtVWEEVSGGLDIMKIGNtempsrayvgrfnfkgvdqgKRVGEL 445
Cdd:COG1245 399 -EDLKISykpqyispdydgTVEEFlrsanTDDFGSSY-YKTEIIKPLGLEKLLD--------------------KNVKDL 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 446 SGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIE----TLRALENALLEFPGCAMVISHDRWFLDRIATHIL 512
Cdd:COG1245 457 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-236 |
2.11e-27 |
|
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: 110.66 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKD------IEGEARPQPDIK-----IGYLPQEPQ--LNPEH 84
Cdd:COG1124 17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPwsgevtFDGRPVTRRRRKafrrrVQMVFQDPYasLHPRH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 TVRESIEEAVsevvnALKRLDEVyalyadpdadfdklaaeQGRLEEIIQAhdghnlnVQLERAAdALRLPdwdakiANLS 164
Cdd:COG1124 97 TVDRILAEPL-----RIHGLPDR-----------------EERIAELLEQ-------VGLPPSF-LDRYP------HQLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG1124 141 GGQRQRVAIARALILEPELLLLDEPTSALDvsvqAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGR 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
324-512 |
2.61e-27 |
|
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: 108.43 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLgetvklasvdqfrdsmdnskt 403
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 404 vweevsGGLDIMKIGNTEMPSRAYVG----RFN-FKGVDQGKRVGE-LSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDI 477
Cdd:cd03229 60 ------DGEDLTDLEDELPPLRRRIGmvfqDFAlFPHLTVLENIALgLSGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 2788209839 478 ET---LRALENALLEFPGCAMV-ISHDRWFLDRIATHIL 512
Cdd:cd03229 134 ITrreVRALLKSLQAQLGITVVlVTHDLDEAARLADRVV 172
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-237 |
5.34e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 114.90 E-value: 5.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE-ARPQPDiKIGYLPQEPQLnPEHTVRESIeeav 94
Cdd:COG4178 373 PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRiARPAGA-RVLFLPQRPYL-PLGTLREAL---- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 95 sevvnalkrldevyaLYADPDADFDklaaeQGRLEEIIQAhdghnlnVQLERAADALRLP-DWDAKianLSGGERRRVAL 173
Cdd:COG4178 447 ---------------LYPATAEAFS-----DAELREALEA-------VGLGHLAERLDEEaDWDQV---LSLGEQQRLAF 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 174 CRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD--FEGTVVAITHdRYFLDNVAGWILELDRGEG 237
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGDGS 561
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-218 |
5.91e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 109.79 E-value: 5.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 7 TMHRVGKVVPPK---RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKD------IEGEARPQPDIKIGYLPQE 77
Cdd:COG1116 9 ELRGVSKRFPTGgggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPtsgevlVDGKPVTGPGPDRGVVFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 78 PQLNPEHTVRESIEeavsevvnalkrldevYALyadPDADFDKLAAEQgRLEEIIQAhdghnlnVQLERAADALrlPdwd 157
Cdd:COG1116 89 PALLPWLTVLDNVA----------------LGL---ELRGVPKAERRE-RARELLEL-------VGLAGFEDAY--P--- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 158 akiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA----WLERFLHDFEGTVVAITHD 218
Cdd:COG1116 137 ---HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRErlqdELLRLWQETGKTVLFVTHD 198
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
291-483 |
6.08e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 111.85 E-value: 6.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 291 LARFEELNSTEYQKRNETNELFIPPGpRLGDKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMIS 370
Cdd:PRK13536 10 APRRLELSPIERKHQGISEAKASIPG-SMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 371 GQEQPDSGTIT-LGETV---------KLASVDQFrDSMDNSKTVWEE--VSGGLDIMKIGNTE--MPSRAYVGRFNFKGv 436
Cdd:PRK13536 89 GMTSPDAGKITvLGVPVpararlaraRIGVVPQF-DNLDLEFTVRENllVFGRYFGMSTREIEavIPSLLEFARLESKA- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 437 dqGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD-------IETLRAL 483
Cdd:PRK13536 167 --DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDpharhliWERLRSL 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
17-236 |
7.54e-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: 106.18 E-value: 7.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARpqpdikigYLPQEPQLNPEHTVRESIeeavse 96
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL--------IDGKDIAKLPLEELRRRI------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 97 vvnalkrldeVYalyadpdadfdklaaeqgrleeIIQahdghnlnvqleraadalrlpdwdakianLSGGERRRVALCRL 176
Cdd:cd00267 76 ----------GY----------------------VPQ-----------------------------LSGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 177 LLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELaeEGrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
324-529 |
1.48e-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: 107.91 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQ--------- 393
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFdGEDITGLPPHEiarlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 ------FRDSmdnskTVWEEV--------SGGLDIMKIGNTEMPSRAYVGRF-NFKGVD--QGKRVGELSGGERGRLHLA 456
Cdd:cd03219 81 fqiprlFPEL-----TVLENVmvaaqartGSGLLLARARREEREARERAEELlERVGLAdlADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 457 KLLQVGGNMLLLDEPT---NDLDIETLRALENALLEFpGCA-MVISHDRWFLDRIATHI--LDYqdeGKVeFFEGNFTE 529
Cdd:cd03219 156 RALATDPKLLLLDEPAaglNPEETEELAELIRELRER-GITvLLVEHDMDVVMSLADRVtvLDQ---GRV-IAEGTPDE 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
324-511 |
1.82e-26 |
|
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: 106.92 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL--GETVKLASVDQFRDSMDNS 401
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdgKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 402 KTVWEEVSgGLDIMKIGNTEMpsrayvgRFNFKGVDQ-----------GKRVGELSGGERGRLHLAKLLQVGGNMLLLDE 470
Cdd:cd03268 81 PGFYPNLT-ARENLRLLARLL-------GIRKKRIDEvldvvglkdsaKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2788209839 471 PTNDLD---IETLRALENALLEFPGCAMVISHDRWFLDRIATHI 511
Cdd:cd03268 153 PTNGLDpdgIKELRELILSLRDQGITVLISSHLLSEIQKVADRI 196
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
324-489 |
1.94e-26 |
|
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: 107.17 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDR----LLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQ---FR 395
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdGEPVTGPGPDRgyvFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 DsmDNS---KTVWEEVSGGLDIMKIGNTEMPSRA--YVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDE 470
Cdd:cd03293 81 Q--DALlpwLTVLDNVALGLELQGVPKAEARERAeeLLELVGLSGF-ENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170
....*....|....*....
gi 2788209839 471 PTNDLDIETLRALENALLE 489
Cdd:cd03293 158 PFSALDALTREQLQEELLD 176
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
320-520 |
1.97e-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: 108.20 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 320 GDKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQ----- 393
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFdGRDITGLPPHRiarlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 ----------FRDsMdnskTVWEEV-------------SGGLDIMKIGNTEMPSRAYV----GRFNFKGVdQGKRVGELS 446
Cdd:COG0411 81 iartfqnprlFPE-L----TVLENVlvaaharlgrgllAALLRLPRARREEREARERAeellERVGLADR-ADEPAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 447 GGERGRLHLAKLLQVGGNMLLLDEPT---NDLDIETLRALENALLEFPGCAMV-ISHDRWFLDRIATHI--LDYqdeGKV 520
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGITILlIEHDMDLVMGLADRIvvLDF---GRV 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
18-226 |
2.80e-26 |
|
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: 106.82 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDI--------------KIGYLPQEPQ--LN 81
Cdd:cd03257 17 SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkirrkEIQMVFQDPMssLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 82 PEHTVRESIEEAVsevvnalkrldevYALYADPDADFDKLAAEQgrleeiiqahdghnLNVQLERAADAL-RLPDWdaki 160
Cdd:cd03257 97 PRMTIGEQIAEPL-------------RIHGKLSKKEARKEAVLL--------------LLVGVGLPEEVLnRYPHE---- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 161 anLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD----FEGTVVAITHD----RYFLDNVA 226
Cdd:cd03257 146 --LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHDlgvvAKIADRVA 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
17-218 |
3.33e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 105.21 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE----------------ARpqpdiKIGYLPQepql 80
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEilldgkdlaslspkelAR-----KIAYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 81 npehtvresieeavsevvnALKRLDevyalyadpdadfdklaaeqgrleeiiqahdghnlnvqleraADALRlpdwDAKI 160
Cdd:cd03214 81 -------------------ALELLG------------------------------------------LAHLA----DRPF 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 161 ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD 218
Cdd:cd03214 96 NELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIELLELLRRLARERGKTVVMVLHD 157
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
324-544 |
3.59e-26 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 112.74 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQfrDSMDNSK- 402
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQ--DPPRNVEg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 403 TVWEEVSGGL-----------DIMKIGNTEmPSRAYVGRF---------------------NFK--GVDQGKRVGELSGG 448
Cdd:PRK11147 82 TVYDFVAEGIeeqaeylkryhDISHLVETD-PSEKNLNELaklqeqldhhnlwqlenrineVLAqlGLDPDAALSSLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 449 ERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEFPGCAMVISHDRWFLDRIATHILDYqDEGKVEFFEGNFT 528
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDL-DRGKLVSYPGNYD 239
|
250
....*....|....*.
gi 2788209839 529 EYEEYKKRTLGADALE 544
Cdd:PRK11147 240 QYLLEKEEALRVEELQ 255
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-226 |
3.67e-26 |
|
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: 111.92 E-value: 3.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE---------ARPQPDIK-----IGYLPQEP--Q 79
Cdd:COG1123 275 KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSilfdgkdltKLSRRSLRelrrrVQMVFQDPysS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 80 LNPEHTVRESIEEAvsevVNALKRLDEvyalyadpdadfdklAAEQGRLEEIIQAhdghnlnVQLERAAdALRLPdwdak 159
Cdd:COG1123 355 LNPRMTVGDIIAEP----LRLHGLLSR---------------AERRERVAELLER-------VGLPPDL-ADRYP----- 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 160 iANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAeSVAW-----LERFLHDFEGTVVAITHD----RYFLDNVA 226
Cdd:COG1123 403 -HELSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAqilnlLRDLQRELGLTYLFISHDlavvRYIADRVA 476
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
17-219 |
6.04e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 109.08 E-value: 6.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK-D-----IEGE----ARPQPDIKIGYLPQEPQLNPEHTV 86
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETpDsgrivLNGRdlftNLPPRERRVGFVFQHYALFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 87 RESIEEAVSevvnALKRldevyalyadPDADFDKLAAEQgrLEEiiqahdghnlnVQLERAADalRLPdwdakiANLSGG 166
Cdd:COG1118 93 AENIAFGLR----VRPP----------SKAEIRARVEEL--LEL-----------VQLEGLAD--RYP------SQLSGG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAeSVA-----WLERFLHDFEGTVVAITHDR 219
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDA-KVRkelrrWLRRLHDELGGTTVFVTHDQ 194
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
325-477 |
7.52e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 106.32 E-value: 7.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 325 EVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLgetvklasvdqfrDSMDNSKTV 404
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLV-------------DGLDVATTP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 405 WEEVSGGLDIMKIGNTeMPSRAYV------GRFNF-KG---------VDQ-----------GKRVGELSGGERGRLHLAK 457
Cdd:COG4604 70 SRELAKRLAILRQENH-INSRLTVrelvafGRFPYsKGrltaedreiIDEaiayldledlaDRYLDELSGGQRQRAFIAM 148
|
170 180
....*....|....*....|
gi 2788209839 458 LLQVGGNMLLLDEPTNDLDI 477
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDM 168
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
324-499 |
1.42e-25 |
|
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: 103.23 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRL--LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLgetvklasvdqfrdsmdns 401
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 402 ktvweevsGGLDIMKIGNTEMPSR-AYVG----------RFNFkgvdqgkrvgeLSGGERGRLHLAKLLQVGGNMLLLDE 470
Cdd:cd03228 62 --------DGVDLRDLDLESLRKNiAYVPqdpflfsgtiRENI-----------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190
....*....|....*....|....*....|.
gi 2788209839 471 PTNDLDIETLRALENALLEFPGCAMV--ISH 499
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVivIAH 153
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-281 |
2.93e-25 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 110.04 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 10 RVGKVV---------PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDIKIGYLPQ-EPQ 79
Cdd:PRK11147 314 RSGKIVfemenvnyqIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQhRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 80 LNPEHTVRESIEEAVSEV-VNALKRldevYALyadpdadfdklaaeqGRLEEIIqahdghnlnVQLERAadalRLPdwda 158
Cdd:PRK11147 394 LDPEKTVMDNLAEGKQEVmVNGRPR----HVL---------------GYLQDFL---------FHPKRA----MTP---- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 159 kIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVA--GWILEldrGE 236
Cdd:PRK11147 438 -VKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVteCWIFE---GN 513
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2788209839 237 GIpWE---GNYSSWLEQKDQRLAQEASQEAARRKSIEKELEWVRQGTK 281
Cdd:PRK11147 514 GK-IGryvGGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSK 560
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
324-483 |
3.17e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.81 E-value: 3.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETvklaSVDQFRD------- 396
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR----PLAAWSPwelarrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 -------SMDNSKTVWEEVSGGLD---IMKIGNTEMPSRA--------YVGRFnfkgvdqgkrVGELSGGERGRLHLAK- 457
Cdd:COG4559 78 avlpqhsSLAFPFTVEEVVALGRAphgSSAAQDRQIVREAlalvglahLAGRS----------YQTLSGGEQQRVQLARv 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 2788209839 458 LLQV------GGNMLLLDEPTNDLDI----ETLRAL 483
Cdd:COG4559 148 LAQLwepvdgGPRWLFLDEPTSALDLahqhAVLRLA 183
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-396 |
6.12e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.19 E-value: 6.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK-D-----IEGEARPQPD----IK--IGYLPQEPQLNPEHTVRES 89
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQpDsgeilIDGKPVRIRSprdaIAlgIGMVHQHFMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 90 IeeavsevvnalkrldevyALYADPDADFD-KLAAEQGRLEEIIQAHdghNLNVqleraadalrlpDWDAKIANLSGGER 168
Cdd:COG3845 101 I------------------VLGLEPTKGGRlDRKAARARIRELSERY---GLDV------------DPDAKVEDLSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 169 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDryfLDNVagwileldrgegipwegnys 245
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITHK---LREV-------------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 246 swleqkdqrlaQEASQEAA--RR-KSIekelewvrqGTKGRQSKGKARLARF---EELNSTEYqkrnetnelfiPPGPRL 319
Cdd:COG3845 205 -----------MAIADRVTvlRRgKVV---------GTVDTAETSEEELAELmvgREVLLRVE-----------KAPAEP 253
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 320 GDKVLEVSNLR-KSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRD 396
Cdd:COG3845 254 GEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLdGEDITGLSPRERRR 332
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
324-490 |
6.65e-25 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 103.03 E-value: 6.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISG-----QEQPDSGTITL-GETVKLASVDQ---- 393
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLdGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 ------FRDSMDNSKTVWEEVSGGLDIMKI-GNTEMPSRAYVGrfnFKGVDQGKRV------GELSGGERGRLHLAKLLQ 460
Cdd:cd03260 81 rrvgmvFQKPNPFPGSIYDNVAYGLRLHGIkLKEELDERVEEA---LRKAALWDEVkdrlhaLGLSGGQQQRLCLARALA 157
|
170 180 190
....*....|....*....|....*....|
gi 2788209839 461 VGGNMLLLDEPTNDLDIETLRALENALLEF 490
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAEL 187
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
18-236 |
7.24e-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: 102.57 E-value: 7.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARpqpdI-------------------KIGYLPQEP 78
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVR----VdgtdisklsekelaafrrrHIGFVFQSF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 79 QLNPEHTVRESIEEAVsEVVNALKRLDEVYALYAdpdadfdklaaeqgrLEEiiqahdghnlnVQLERAADAlrlpdwda 158
Cdd:cd03255 92 NLLPDLTALENVELPL-LLAGVPKKERRERAEEL---------------LER-----------VGLGDRLNH-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 159 KIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHDRyFLDNVAGWILELDR 234
Cdd:cd03255 137 YPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRD 215
|
..
gi 2788209839 235 GE 236
Cdd:cd03255 216 GK 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-251 |
9.78e-25 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 108.06 E-value: 9.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDIKIGYLPQEpqlnpeHTvrESIEEAVSevvna 100
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQD------HA--YDFENDLT----- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 101 lkrLDEVYALYADPDADFDKLAAEQGRLeeiiqahdghnlnvqLERAADALRlpdwdaKIANLSGGERRRVALCRLLLEK 180
Cdd:PRK15064 401 ---LFDWMSQWRQEGDDEQAVRGTLGRL---------------LFSQDDIKK------SVKVLSGGEKGRMLFGKLMMQK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 181 PDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQK 251
Cdd:PRK15064 457 PNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-236 |
1.12e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 102.05 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 8 MHRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR---------PQPDI-----KIGY 73
Cdd:COG2884 4 FENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrlKRREIpylrrRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 74 LPQEPQLNPEHTVRESIEeavsevvnalkrldevYALYAdpdadfdklaaeQGRLEEIIQahdghnlnvqlERAADALrl 153
Cdd:COG2884 84 VFQDFRLLPDRTVYENVA----------------LPLRV------------TGKSRKEIR-----------RRVREVL-- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 154 pDW-------DAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLD 223
Cdd:COG2884 123 -DLvglsdkaKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVD 201
|
250
....*....|...
gi 2788209839 224 NVAGWILELDRGE 236
Cdd:COG2884 202 RMPKRVLELEDGR 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-218 |
1.34e-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: 101.78 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 7 TMHRVGKVVPPKR---HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKD------IEGEARPQPDIKIGYLPQE 77
Cdd:cd03293 2 EVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPtsgevlVDGEPVTGPGPDRGYVFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 78 PQLNPEHTVRESIEeavsevvnalkrldevyalyadpdadfdkLAAE-QGRLEEIIQAHDGHNLN-VQLERAADalRLPd 155
Cdd:cd03293 82 DALLPWLTVLDNVA-----------------------------LGLElQGVPKAEARERAEELLElVGLSGFEN--AYP- 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788209839 156 wdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESV-AWLERFLHDFEGTVVAITHD 218
Cdd:cd03293 130 -----HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltrEQLqEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
17-196 |
1.71e-24 |
|
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: 101.50 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAkIGVLGLNGAGKSTLLRIMAGIDKDIEG-------EARPQPDI---KIGYLPQEPQLNPEHTV 86
Cdd:cd03264 11 GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGtiridgqDVLKQPQKlrrRIGYLPQEFGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 87 RESieeavsevvnalkrLDEVYALYADPDADFDKlaaeqgRLEEIIQAhdghnlnVQLERAADAlrlpdwdaKIANLSGG 166
Cdd:cd03264 90 REF--------------LDYIAWLKGIPSKEVKA------RVDEVLEL-------VNLGDRAKK--------KIGSLSGG 134
|
170 180 190
....*....|....*....|....*....|
gi 2788209839 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAE 196
Cdd:cd03264 135 MRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
323-476 |
1.80e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.73 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETV---------KLASVD 392
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVpsrarharqRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 393 QFrDSMDNSKTVWEE--VSG---GLDIMKIgNTEMPSRAYVGRFNFKGvdqGKRVGELSGGERGRLHLAKLLQVGGNMLL 467
Cdd:PRK13537 87 QF-DNLDPDFTVRENllVFGryfGLSAAAA-RALVPPLLEFAKLENKA---DAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
....*....
gi 2788209839 468 LDEPTNDLD 476
Cdd:PRK13537 162 LDEPTTGLD 170
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-219 |
3.05e-24 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 100.67 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE---------ARPQPDIKIGYLPQEPQLNPEHTVRESI 90
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEilidgrdvtGVPPERRNIGMVFQDYALFPHLTVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 91 eeavsevvnalkrldeVYALYAdpdadfdklaaeQGRLEEIIQAhdghnlnvQLERAADALRLPDW-DAKIANLSGGERR 169
Cdd:cd03259 94 ----------------AFGLKL------------RGVPKAEIRA--------RVRELLELVGLEGLlNRYPHELSGGQQQ 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 170 RVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHDR 219
Cdd:cd03259 138 RVALARALAREPSLLLLDEPLSALDAKLreelREELKELQRELGITTIYVTHDQ 191
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
324-501 |
5.44e-24 |
|
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: 100.88 E-value: 5.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQ--------- 393
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFgGEDATDVPVQErnvgfvfqh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 ---FRdsmdnSKTVWEEVSGGLDIMKIgnTEMPSRAYVGR-----FNFKGVDQ-GKRV-GELSGGERGRLHLAKLLQVGG 463
Cdd:cd03296 83 yalFR-----HMTVFDNVAFGLRVKPR--SERPPEAEIRAkvhelLKLVQLDWlADRYpAQLSGGQRQRVALARALAVEP 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 2788209839 464 NMLLLDEPTNDLDIETLRALENALLEFpgcamvisHDR 501
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRL--------HDE 185
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
323-521 |
6.14e-24 |
|
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: 100.35 E-value: 6.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDR----LLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKL---ASVDQF 394
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLTLlsgKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 395 RDSMD---------NSKTVWEEVSGGLDIMKIGNTEMPSRAY-----VGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQ 460
Cdd:cd03258 81 RRRIGmifqhfnllSSRTVFENVALPLEIAGVPKAEIEERVLellelVGLEDKA----DAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 461 VGGNMLLLDEPTNDLDIETLRALENALL----EFPGCAMVISHDRWFLDRIATHILdYQDEGKVE 521
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRdinrELGLTIVLITHEMEVVKRICDRVA-VMEKGEVV 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-236 |
6.54e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 105.63 E-value: 6.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GID-KDIegearPQPDI--KIGYLPQEPQ 79
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLrfydptsgrilidGVDiRDL-----TLESLrrQIGVVPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 80 LNPEhTVRESIeeavsevvnalkrldevyaLYADPDADFDKL--AAEQGRLEEIIQahdghnlnvqleraadalRLPD-W 156
Cdd:COG1132 425 LFSG-TIRENI-------------------RYGRPDATDEEVeeAAKAAQAHEFIE------------------ALPDgY 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 157 DAKI----ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAW----LERFLHDfeGTVVAITH--------DRy 220
Cdd:COG1132 467 DTVVgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALiqeaLERLMKG--RTTIVIAHrlstirnaDR- 543
|
250
....*....|....*.
gi 2788209839 221 fldnvagwILELDRGE 236
Cdd:COG1132 544 --------ILVLDDGR 551
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-508 |
6.87e-24 |
|
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: 105.27 E-value: 6.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGID--KDIEGE--------------------ARPQPDIKIGYLPQEP 78
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRiiyhvalcekcgyverpskvGEPCPVCGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 79 QL-NPEHTVRESIEEAVSEVvnalkrLDEVYALYADpdadfdklaaeQGRLEEIIQA-HD-GHNLNVQLERAADALRLPD 155
Cdd:TIGR03269 95 DFwNLSDKLRRRIRKRIAIM------LQRTFALYGD-----------DTVLDNVLEAlEEiGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 156 WDAKIA----NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV----AWLERFLHDFEGTVVAITHDRYFLDNVAg 227
Cdd:TIGR03269 158 LSHRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLS- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 228 wileldrgegipwegNYSSWLEQKdqrlaqEASQEAARRKSIEKELEWVRQgtkgrqskgkarLARFEELnsteyqkrne 307
Cdd:TIGR03269 237 ---------------DKAIWLENG------EIKEEGTPDEVVAVFMEGVSE------------VEKECEV---------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 308 tnelfippgpRLGDKVLEVSNLRKSYG--DRLLI---DDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTItl 382
Cdd:TIGR03269 274 ----------EVGEPIIKVRNVSKRYIsvDRGVVkavDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV-- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 383 geTVKLAS--VDQFRDSMDNS-------------------KTVWEEVSG--GLDIMKigntEMPSRAYVGRFNFKGVDQG 439
Cdd:TIGR03269 342 --NVRVGDewVDMTKPGPDGRgrakryigilhqeydlyphRTVLDNLTEaiGLELPD----ELARMKAVITLKMVGFDEE 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 440 KRVG-------ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALL----EFPGCAMVISHDRWFL---- 504
Cdd:TIGR03269 416 KAEEildkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkareEMEQTFIIVSHDMDFVldvc 495
|
....
gi 2788209839 505 DRIA 508
Cdd:TIGR03269 496 DRAA 499
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
323-471 |
7.42e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.49 E-value: 7.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETV--KL------------ 388
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDitHLpmhkrarlgigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 389 ----ASVdqFRDSmdnskTVWEEVSGGLDIMKIGNTEMPSR--AYVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVG 462
Cdd:COG1137 83 lpqeASI--FRKL-----TVEDNILAVLELRKLSKKEREERleELLEEFGITHL-RKSKAYSLSGGERRRVEIARALATN 154
|
....*....
gi 2788209839 463 GNMLLLDEP 471
Cdd:COG1137 155 PKFILLDEP 163
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
324-523 |
9.24e-24 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 99.88 E-value: 9.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG--ETVKLASVDQFR------ 395
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgeDISGLSEAELYRlrrrmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 ---------DSMdnskTVWEEVSGGLDImkigNTEMPS-------RAYVGRFNFKGVDQgKRVGELSGGERGRLHLAKLL 459
Cdd:cd03261 81 mlfqsgalfDSL----TVFENVAFPLRE----HTRLSEeeireivLEKLEAVGLRGAED-LYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 460 QVGGNMLLLDEPTNDLDIETLRALENALL----EFPGCAMVISHDRWFLDRIATHILdYQDEGKVEFF 523
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRslkkELGLTSIMVTHDLDTAFAIADRIA-VLYDGKIVAE 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-236 |
9.60e-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: 9.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR----PQPDI-------KIGYLPQEPQLNPEhTVR 87
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvDLRDLdleslrkNIAYVPQDPFLFSG-TIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 88 ESIeeavsevvnalkrldevyalyadpdadfdklaaeqgrleeiiqahdghnlnvqleraadalrlpdwdakianLSGGE 167
Cdd:cd03228 94 ENI------------------------------------------------------------------------LSGGQ 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAITHdRYFLDNVAGWILELDRGE 236
Cdd:cd03228 102 RQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
323-512 |
9.94e-24 |
|
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: 99.50 E-value: 9.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLL----IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFRD-- 396
Cdd:cd03257 1 LLEVKNLSVSFPTGGGsvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 -------------SMDNSKTVWEEVSGGLDIMKIGNTEMPSRAYVGRfNFKGVDQGKRV-----GELSGGERGRLHLAKL 458
Cdd:cd03257 81 rkeiqmvfqdpmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLL-LLVGVGLPEEVlnrypHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 459 LQVGGNMLLLDEPTNDLD-------IETLRALENALlefpGCAMV-ISHDRWFLDRIATHIL 512
Cdd:cd03257 160 LALNPKLLIADEPTSALDvsvqaqiLDLLKKLQEEL----GLTLLfITHDLGVVAKIADRVA 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
324-484 |
1.00e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.38 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVdqfRDSMDNSK 402
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVaGDDVEALSA---RAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 403 TVWEEVSGGLDIMKIGNTEMPSRAYVGRF---------------NFKGVDQ--GKRVGELSGGERGRLHLAKLLQVGGNM 465
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHRSRFdtwtetdraaveramERTGVAQfaDRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180
....*....|....*....|
gi 2788209839 466 LLLDEPTNDLDI-ETLRALE 484
Cdd:PRK09536 161 LLLDEPTASLDInHQVRTLE 180
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-218 |
1.89e-23 |
|
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: 98.52 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSF-FPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR---------------PQPDIKIGYLPQEPQLN 81
Cdd:cd03297 8 KRLPDFTLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkinlPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 82 PEHTVRESIEEAVSEVVNALKRLdevyalyadpdadfdklaaeqgRLEEIIQAhdghnlnVQLERAADAlrlpdwdaKIA 161
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNREDRI----------------------SVDELLDL-------LGLDHLLNR--------YPA 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHD 218
Cdd:cd03297 131 QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHD 191
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
18-218 |
1.95e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 98.96 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR---------PQPDI------KIGYLPQEPQLNP 82
Cdd:COG1136 20 EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdisslSERELarlrrrHIGFVFQFFNLLP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 83 EHTVRESIEEAvsevvnalkrldevyALYAdpdadfdklaaeqgrleeiiqahdGHNLNVQLERAADALR---LPDW-DA 158
Cdd:COG1136 100 ELTALENVALP---------------LLLA------------------------GVSRKERRERARELLErvgLGDRlDH 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 159 KIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHD 218
Cdd:COG1136 141 RPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHD 204
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-234 |
2.05e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 103.91 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE----ARPQPDIK-------IGYLPQEPQLnPEH 84
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavnGVPLADADadswrdqIAWVPQHPFL-FAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 TVRESIeeavsevvnalkrldevyaLYADPDADFDKL--AAEQGRLEEIIQAhdghnlnvqleraadalrLPD-WDAKI- 160
Cdd:TIGR02857 411 TIAENI-------------------RLARPDASDAEIreALERAGLDEFVAA------------------LPQgLDTPIg 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 161 ---ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAITHDRyfldnvaGWILELDR 234
Cdd:TIGR02857 454 eggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL-------ALAALADR 525
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
323-394 |
2.43e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 100.18 E-value: 2.43e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQF 394
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEPLDPEDRRRI 73
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
324-499 |
3.19e-23 |
|
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: 96.34 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVdqfRDSMDNsk 402
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEVSFASP---RDARRA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 403 tvweevsggldimKIGntempsrayvgrfnfkgvdqgkRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD------ 476
Cdd:cd03216 76 -------------GIA----------------------MVYQLSVGERQMVEIARALARNARLLILDEPTAALTpaever 120
|
170 180
....*....|....*....|....*
gi 2788209839 477 -IETLRALENAllefpGCAMV-ISH 499
Cdd:cd03216 121 lFKVIRRLRAQ-----GVAVIfISH 140
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
315-529 |
3.51e-23 |
|
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: 103.30 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 315 PGPRLGDKVLEVSNLRKSYGD-RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGEtVKLASVDQ 393
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING-VDLSDLDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 frdsmdnsKTVWEEVS----------GGL-DIMKIGNTEMPS--------RAYVGRFnFKGVDQG--KRVGE----LSGG 448
Cdd:COG4988 407 --------ASWRRQIAwvpqnpylfaGTIrENLRLGRPDASDeeleaaleAAGLDEF-VAALPDGldTPLGEggrgLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 449 ERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEFPG--CAMVISHdRWFLDRIATHILDYQDEGKVEffEGN 526
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITH-RLALLAQADRILVLDDGRIVE--QGT 554
|
...
gi 2788209839 527 FTE 529
Cdd:COG4988 555 HEE 557
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-235 |
4.21e-23 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 102.81 E-value: 4.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 14 VVPP--KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR-PQPDIK----------IGYLPQEPQL 80
Cdd:TIGR01842 324 IVPPggKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRlDGADLKqwdretfgkhIGYLPQDVEL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 81 NPeHTVRESIeeavsevvnalKRLDEvyalyaDPDAdfdklaaeqgrlEEIIQAhdghnlnvqlERAADA----LRLPD- 155
Cdd:TIGR01842 404 FP-GTVAENI-----------ARFGE------NADP------------EKIIEA----------AKLAGVheliLRLPDg 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 156 WDAKI----ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFE---GTVVAITHdRYFLDNVAGW 228
Cdd:TIGR01842 444 YDTVIgpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITH-RPSLLGCVDK 522
|
....*..
gi 2788209839 229 ILELDRG 235
Cdd:TIGR01842 523 ILVLQDG 529
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
306-500 |
5.01e-23 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 103.38 E-value: 5.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 306 NETNELFIPPGPRLGDkvLEVSNLRKSYGDR--LLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG 383
Cdd:COG2274 458 REEGRSKLSLPRLKGD--IELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 384 ----ETVKLAS-------VDQ----FRDS-MDN---------SKTVWE--EVSGGLD-IMKignteMPsrayvgrfnfKG 435
Cdd:COG2274 536 gidlRQIDPASlrrqigvVLQdvflFSGTiRENitlgdpdatDEEIIEaaRLAGLHDfIEA-----LP----------MG 600
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 436 VDQgkRVGE----LSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLE-FPGCAM-VISHD 500
Cdd:COG2274 601 YDT--VVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRlLKGRTViIIAHR 669
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
320-499 |
5.47e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.41 E-value: 5.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 320 GDKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLAS-------- 390
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdGKPVRIRSprdaialg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 391 ---VDQ-FR--DSMdnskTVWEEVSGGLDIMKIGNTEMPS-----RAYVGRFNFKgVDQGKRVGELSGGERGRLHLAKLL 459
Cdd:COG3845 82 igmVHQhFMlvPNL----TVAENIVLGLEPTKGGRLDRKAarariRELSERYGLD-VDPDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2788209839 460 QVGGNMLLLDEPT--------NDLdIETLRALENAllefpGCAMV-ISH 499
Cdd:COG3845 157 YRGARILILDEPTavltpqeaDEL-FEILRRLAAE-----GKSIIfITH 199
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
324-471 |
5.48e-23 |
|
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: 97.61 E-value: 5.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGET--VKL------------- 388
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQdiTKLpmhkrarlgigyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 389 ---ASVdqFRDsmdnsKTVWEEVSGGLDIMKIGNTEMPSR--AYVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGG 463
Cdd:cd03218 81 pqeASI--FRK-----LTVEENILAVLEIRGLSKKEREEKleELLEEFHITHL-RKSKASSLSGGERRRVEIARALATNP 152
|
....*...
gi 2788209839 464 NMLLLDEP 471
Cdd:cd03218 153 KFLLLDEP 160
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
325-520 |
5.86e-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: 5.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 325 EVSNLRKSYGD-RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGEtVKLASVDQFRDS---MDN 400
Cdd:cd03226 1 RIENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-KPIKAKERRKSIgyvMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 401 ------SKTVWEEVSGGLDIMKIGNTEmpSRAYVGRFN-FKGVDQGKRvgELSGGERGRLHLAKLLQVGGNMLLLDEPTN 473
Cdd:cd03226 80 vdyqlfTDSVREELLLGLKELDAGNEQ--AETVLKDLDlYALKERHPL--SLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788209839 474 DLDIETLRALENALLEFP--GCAM-VISHDRWFLDRIATHILdYQDEGKV 520
Cdd:cd03226 156 GLDYKNMERVGELIRELAaqGKAViVITHDYEFLAKVCDRVL-LLANGAI 204
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
19-218 |
1.02e-22 |
|
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: 97.58 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK-----------DIEGEARPQPDIKIGYLPQEPQLNPEHTVR 87
Cdd:TIGR03873 14 RLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRpdagtvdlagvDLHGLSRRARARRVALVEQDSDTAVPLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 88 ESIeeavsevvnALKRLDEVYALYADPDADFDKLAAEQGRLEeiiqahdghnlnvqLERAADAlrlpDWDAkianLSGGE 167
Cdd:TIGR03873 94 DVV---------ALGRIPHRSLWAGDSPHDAAVVDRALARTE--------------LSHLADR----DMST----LSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG---TVVAITHD 218
Cdd:TIGR03873 143 RQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHD 196
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
324-513 |
1.47e-22 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 95.72 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGaIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFRD------- 396
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrigylpq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 --SMDNSKTVWEEvsggLDIM----KIGNTEMPSRA-----YVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNM 465
Cdd:cd03264 80 efGVYPNFTVREF----LDYIawlkGIPSKEVKARVdevleLVNLGDRA----KKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788209839 466 LLLDEPTNDLDIETLRALENALLEfpgcamvISHDRWFLdrIATHILD 513
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSE-------LGEDRIVI--LSTHIVE 190
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-274 |
2.04e-22 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 101.40 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDIKIGYLPQEpQLNpehtvresieeavsevv 98
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQH-QLE----------------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 99 naLKRLDEvyalyaDPDADFDKLAAEQgrLEEIIQAHDGhNLNVQLERAADAlrlpdwdakIANLSGGERRRVALCRLLL 178
Cdd:PRK10636 387 --FLRADE------SPLQHLARLAPQE--LEQKLRDYLG-GFGFQGDKVTEE---------TRRFSGGEKARLVLALIVW 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 179 EKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYF----------------------LDNVAGWILELDRGE 236
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLlrsttddlylvhdgkvepfdgdLEDYQQWLSDVQKQE 526
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2788209839 237 G----IPWEGNYSSWLEQKDQ--RLAQEASQEAARRKSI---EKELE 274
Cdd:PRK10636 527 NqtdeAPKENNANSAQARKDQkrREAELRTQTQPLRKEIarlEKEME 573
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
324-520 |
2.37e-22 |
|
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: 95.29 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETV---KLASVDQFRDSMD- 399
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltdDKKNINELRQKVGm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 400 --------NSKTVWEEVSGGL-DIMKIGNTEMPSRAY-----VGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNM 465
Cdd:cd03262 81 vfqqfnlfPHLTVLENITLAPiKVKGMSKAEAEERALellekVGLADKA----DAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 466 LLLDEPTNDLDIETLRALENALLEFP--GCAMVI-SHDRWFLDRIATHILdYQDEGKV 520
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAeeGMTMVVvTHEMGFAREVADRVI-FMDDGRI 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
324-476 |
2.82e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 98.25 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQ------FRD 396
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdGRDVTGLPPEKrnvgmvFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 -----SMdnskTVWEEVSGGLDIMKIGNTEMPSRA--YVGRFNFKGVdQGKRVGELSGGERGRLHLAKLL----QVggnm 465
Cdd:COG3842 86 yalfpHL----TVAENVAFGLRMRGVPKAEIRARVaeLLELVGLEGL-ADRYPHQLSGGQQQRVALARALapepRV---- 156
|
170
....*....|.
gi 2788209839 466 LLLDEPTNDLD 476
Cdd:COG3842 157 LLLDEPLSALD 167
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
327-531 |
2.83e-22 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 101.01 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 327 SNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFRDSMD------- 399
Cdd:PRK10636 5 SSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPqpaleyv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 400 --------------------NSKTVWEEVSGGLDIMKIGNTEMPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLL 459
Cdd:PRK10636 85 idgdreyrqleaqlhdanerNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 460 QVGGNMLLLDEPTNDLDIETLRALENALLEFPGCAMVISHDRWFLDRIATHILDYQDEGKVEfFEGNFTEYE 531
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE-YTGNYSSFE 235
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-238 |
3.48e-22 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 94.63 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKD------IEGEARPQPDI--KIGYLPQEP--QLNPEhT 85
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKEssgsilLNGKPIKAKERrkSIGYVMQDVdyQLFTD-S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIeeavsevvnalkrldevyaLYADPDADfdklaAEQGRLEEIIQahdghnlnvQLERAADALRLPdwdakiANLSG 165
Cdd:cd03226 89 VREEL-------------------LLGLKELD-----AGNEQAETVLK---------DLDLYALKERHP------LSLSG 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 166 GERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGI 238
Cdd:cd03226 130 GQKQRLAIAAALLSGKDLLIFDEPTSGLDYknmERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
332-500 |
5.38e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.84 E-value: 5.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 332 SYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQfRDSMDNS--KTVWEEVS 409
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-RSEVPDSlpLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 410 GGLdimkignteMPSRAYVGRFNF---KGVDQ-----------GKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDL 475
Cdd:NF040873 80 MGR---------WARRGLWRRLTRddrAAVDDalervgladlaGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180
....*....|....*....|....*...
gi 2788209839 476 DIETLRALENALLEFPG---CAMVISHD 500
Cdd:NF040873 151 DAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-218 |
6.74e-22 |
|
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: 99.36 E-value: 6.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE---------ARPQPDIK--IGYLPQEPQLNpEH 84
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEvtldgvpvsSLDQDEVRrrVSVCAQDAHLF-DT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 TVRESIeeavsevvnalkrldevyaLYADPDADFDKL--AAEQGRLEEIIQA-HDGHNLNVQlERAAdalrlpdwdakia 161
Cdd:TIGR02868 424 TVRENL-------------------RLARPDATDEELwaALERVGLADWLRAlPDGLDTVLG-EGGA------------- 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVawlERFLHDF-----EGTVVAITHD 218
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETA---DELLEDLlaalsGRTVVLITHH 529
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
18-236 |
1.41e-21 |
|
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: 92.25 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE-------------ARPQPDIKIGYLPQEPQLNPEH 84
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSilidgedltdledELPPLRRRIGMVFQDFALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 TVRESIEEAvsevvnalkrldevyalyadpdadfdklaaeqgrleeiiqahdghnlnvqleraadalrlpdwdakianLS 164
Cdd:cd03229 92 TVLENIALG---------------------------------------------------------------------LS 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDFEG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03229 103 GGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALlksLQAQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-217 |
1.62e-21 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 92.67 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR---------PQPDIKIGYLPQEPQLNPEHTVRE 88
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksyqknIEALRRIGALIEAPGFYPNLTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 89 sieeavsevvnALKRLDEVYALyadPDADFDKLaaeqgrLEEIIQAHDGHNlnvqleraadalrlpdwdaKIANLSGGER 168
Cdd:cd03268 92 -----------NLRLLARLLGI---RKKRIDEV------LDVVGLKDSAKK-------------------KVKGFSLGMK 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 169 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLH---DFEGTVVAITH 217
Cdd:cd03268 133 QRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILslrDQGITVLISSH 184
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-217 |
1.92e-21 |
|
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: 92.23 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 5 VYTMHRVGKVvppKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--IDKDIEGE----ARPQPDIK----IGYL 74
Cdd:cd03213 11 VTVKSSPSKS---GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEvlinGRPLDKRSfrkiIGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 75 PQEPQLNPEHTVRESIEeavsevvnalkrldevYAlyadpdadfdklaaeqgrleeiiqahdghnlnvqleraadalrlp 154
Cdd:cd03213 88 PQDDILHPTLTVRETLM----------------FA--------------------------------------------- 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 155 dwdAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDFEGTVVAITH 217
Cdd:cd03213 107 ---AKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDsssALQVMSLLRRLADTGRTIICSIH 169
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
324-507 |
2.29e-21 |
|
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: 93.40 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGD-RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGET----VKLASVDQFRDSM 398
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinkLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 D---------NSKTVWEEV-SGGLDIMKIGntempsRAYVGRFN-------FKGVDQ-------GKRVGELSGGERGRLH 454
Cdd:cd03256 81 GmifqqfnliERLSVLENVlSGRLGRRSTW------RSLFGLFPkeekqraLAALERvglldkaYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 455 LAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEFP---GCAMVIS-HD----RWFLDRI 507
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreeGITVIVSlHQvdlaREYADRI 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-235 |
3.16e-21 |
|
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: 92.79 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKD------IEGE---ARPQPDIKIGYLPQEPQLNPEHTVRESIee 92
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdsgtilFGGEdatDVPVQERNVGFVFQHYALFRHMTVFDNV-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 93 avsevvnalkrldeVYALYADPDADFDKLAAEQGRLEEIIQAhdghnlnVQLERAADalRLPdwdakiANLSGGERRRVA 172
Cdd:cd03296 96 --------------AFGLRVKPRSERPPEAEIRAKVHELLKL-------VQLDWLAD--RYP------AQLSGGQRQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788209839 173 LCRLLLEKPDMLLLDEPTNHLDA----ESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
324-479 |
3.81e-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: 92.05 E-value: 3.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETV---------KLASVDQ 393
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVvreprevrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 FRdSMDNSKTVWEEVSGGLDIMKIGNTEMPSRA-----YVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNMLLL 468
Cdd:cd03265 81 DL-SVDDELTGWENLYIHARLYGVPGAERRERIdelldFVGLLEAA----DRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170
....*....|.
gi 2788209839 469 DEPTNDLDIET 479
Cdd:cd03265 156 DEPTIGLDPQT 166
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
323-511 |
5.57e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.09 E-value: 5.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL----GETVKLASVDQF---R 395
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdggdIDDPDVAEACHYlghR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 DSMDNSKTVWEEVSGGLDIMkiGNTEMPSRAYVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDL 475
Cdd:PRK13539 82 NAMKPALTVAENLEFWAAFL--GGEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 2788209839 476 DIETLRALENAL---LEFPGcaMVIshdrwfldrIATHI 511
Cdd:PRK13539 159 DAAAVALFAELIrahLAQGG--IVI---------AATHI 186
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-218 |
5.76e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.76 E-value: 5.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDIKIGYLPQEPQLNPEH--TVRESIEEAV 94
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLplTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 95 SEVVNALKRLDevyalyadpdadfdklaaeqgrleeiiqAHDghnlNVQLERAADALRLPDW-DAKIANLSGGERRRVAL 173
Cdd:NF040873 83 WARRGLWRRLT----------------------------RDD----RAAVDDALERVGLADLaGRQLGELSGGQRQRALL 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788209839 174 CRLLLEKPDMLLLDEPTNHLDAESVAWLE---RFLHDFEGTVVAITHD 218
Cdd:NF040873 131 AQGLAQEADLLLLDEPTTGLDAESRERIIallAEEHARGATVVVVTHD 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
323-512 |
7.86e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 91.27 E-value: 7.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSY-GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGE----TVKLASVDQFRDS 397
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 398 M-----D----NSKTVWEEVSGGLDIMKIGNTEMPSRA-----YVGRFNFKgvdqGKRVGELSGGERGRLHLA------- 456
Cdd:COG2884 81 IgvvfqDfrllPDRTVYENVALPLRVTGKSRKEIRRRVrevldLVGLSDKA----KALPHELSGGEQQRVAIAralvnrp 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 457 KLlqvggnmLLLDEPTNDLDIETLRALENALLEF--PGCAMVI-SHDRWFLDRIATHIL 512
Cdd:COG2884 157 EL-------LLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRMPKRVL 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
324-477 |
8.84e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.00 E-value: 8.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETV-----------KLASVD 392
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 393 QFRDSMDNSkTVWEEVSGGldimkigntEMPSRAYVGRFNFKG---VDQG-----------KRVGELSGGERGRLHLAKL 458
Cdd:PRK11231 83 QHHLTPEGI-TVRELVAYG---------RSPWLSLWGRLSAEDnarVNQAmeqtrinhladRRLTDLSGGQRQRAFLAMV 152
|
170
....*....|....*....
gi 2788209839 459 LQVGGNMLLLDEPTNDLDI 477
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDI 171
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
315-501 |
1.07e-20 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 95.43 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 315 PGPRLGDKVLEVSNLRKSYGDR-LLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVD 392
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLADADAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 393 QFRDSMD--------NSKTVWEEV----SGGLDIMKIgntEMPSRAYVGRFnFKGVDQG--KRVGE----LSGGERGRLH 454
Cdd:TIGR02857 393 SWRDQIAwvpqhpflFAGTIAENIrlarPDASDAEIR---EALERAGLDEF-VAALPQGldTPIGEggagLSGGQAQRLA 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2788209839 455 LAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEFPGCAMV--ISHDR 501
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVllVTHRL 517
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-190 |
1.09e-20 |
|
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: 90.96 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DKDIEGeaRPQPDI---KIGYLPQEPQLNPEHT 85
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLlpprsgsirfdGRDITG--LPPHERaraGIGYVPEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIEEAVSEVVNALK--RLDEVYALyadpdadFDKLAaeqgrleeiiqahdghnlnvqlERaadalrlpdWDAKIANL 163
Cdd:cd03224 92 VEENLLLGAYARRRAKRkaRLERVYEL-------FPRLK----------------------ER---------RKQLAGTL 133
|
170 180
....*....|....*....|....*..
gi 2788209839 164 SGGERRRVALCRLLLEKPDMLLLDEPT 190
Cdd:cd03224 134 SGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
323-501 |
1.15e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.13 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLgETVKLASVDQFR---DSMD 399
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLSHVPPYQrpiNMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 400 NS------KTVWEEVSGGLDIMKIGNTEMPSR-----AYVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNMLLL 468
Cdd:PRK11607 98 QSyalfphMTVEQNIAFGLKQDKLPKAEIASRvnemlGLVHMQEFA----KRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 2788209839 469 DEPTNDLDiETLR---ALENA-LLEFPG--CAMViSHDR 501
Cdd:PRK11607 174 DEPMGALD-KKLRdrmQLEVVdILERVGvtCVMV-THDQ 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
324-476 |
1.20e-20 |
|
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: 90.76 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGEtVKLASVDQFRDSMD---- 399
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG-KDITNLPPHKRPVNtvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 400 -----NSKTVWEEVSGGLDIMKIGNTEMPSRA--YVGRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:cd03300 80 nyalfPHLTVFENIAFGLRLKKLPKAEIKERVaeALDLVQLEGYAN-RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
....
gi 2788209839 473 NDLD 476
Cdd:cd03300 159 GALD 162
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
323-521 |
1.39e-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: 94.97 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSY--GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPD---SGTITLGETVKLASVDQFR-- 395
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 -------DSMD--NSKTVWEEVSGGLDIMKIGNTEMPSRAyVGRFNFKGVDQ--GKRVGELSGGERGRLHLAKLLQVGGN 464
Cdd:COG1123 84 rigmvfqDPMTqlNPVTVGDQIAEALENLGLSRAEARARV-LELLEAVGLERrlDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 465 MLLLDEPTNDLDIETLR---ALENALLEFPGCAMV-ISHDRWFLDRIATHILDYQDEGKVE 521
Cdd:COG1123 163 LLIADEPTTALDVTTQAeilDLLRELQRERGTTVLlITHDLGVVAEIADRVVVMDDGRIVE 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
323-516 |
2.73e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 89.80 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSY-----GDRLL--IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL---GETVKLASVD 392
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 393 QfRDSMDNSKTVWEEVS---------GGLDIMkigntEMPSRAyvgrfnfKGVDQG---KRVGEL--------------- 445
Cdd:COG4778 84 P-REILALRRRTIGYVSqflrviprvSALDVV-----AEPLLE-------RGVDREearARARELlarlnlperlwdlpp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 446 ---SGGERGRLHLAKLLQVGGNMLLLDEPTNDLD-------IETLRALENAllefpGCAMV-ISHDRWFLDRIATHILDY 514
Cdd:COG4778 151 atfSGGEQQRVNIARGFIADPPLLLLDEPTASLDaanravvVELIEEAKAR-----GTAIIgIFHDEEVREAVADRVVDV 225
|
..
gi 2788209839 515 QD 516
Cdd:COG4778 226 TP 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
324-501 |
2.93e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.48 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQfRD------ 396
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDVTHRSIQQ-RDicmvfq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 --SMDNSKTVWEEVSGGLDIMKIGNTEMPSR-----AYV--GRFNFKGVDQgkrvgeLSGGERGRLHLAKLLQVGGNMLL 467
Cdd:PRK11432 86 syALFPHMSLGENVGYGLKMLGVPKEERKQRvkealELVdlAGFEDRYVDQ------ISGGQQQRVALARALILKPKVLL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 2788209839 468 LDEPTNDLDIETLRALENALLE----FPGCAMVISHDR 501
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRElqqqFNITSLYVTHDQ 197
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
315-512 |
3.30e-20 |
|
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: 94.06 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 315 PGPRLGDKVLEVSNLRKSY--GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGEtVKLASVD 392
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG-VDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 393 QfrdsmdnsKTVWEEVSGgldimkignteMPSRAYVgrFN-------------------------------FKGVDQG-- 439
Cdd:COG4987 404 E--------DDLRRRIAV-----------VPQRPHL--FDttlrenlrlarpdatdeelwaalervglgdwLAALPDGld 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 440 KRVGE----LSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLE-FPGCAMV-ISHDRWFLDRiATHIL 512
Cdd:COG4987 463 TWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEaLAGRTVLlITHRLAGLER-MDRIL 540
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-242 |
3.90e-20 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 89.48 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK-----------DIEG--EARPQP-DIKIGYLPQEPQLNPEH 84
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpdsgevlidgeDISGlsEAELYRlRRRMGMLFQSGALFDSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 TVRESIeeavsevvnALkRLDEVYALyadPDADFDKLAAEQgrLEEiiqahdghnlnVQLERAADalRLPdwdakiANLS 164
Cdd:cd03261 93 TVFENV---------AF-PLREHTRL---SEEEIREIVLEK--LEA-----------VGLRGAED--LYP------AELS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDFEG-TVVAITHDRYFLDNVAGWILELDRGEgIPW 240
Cdd:cd03261 139 GGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIADRIAVLYDGK-IVA 217
|
..
gi 2788209839 241 EG 242
Cdd:cd03261 218 EG 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
324-499 |
5.43e-20 |
|
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: 87.27 E-value: 5.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGD--RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRdsmDN 400
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDPNELG---DH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 401 SKTVWEEVSggLdimkigntempsrayvgrfnFKGVdqgkrVGE--LSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIE 478
Cdd:cd03246 78 VGYLPQDDE--L--------------------FSGS-----IAEniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180
....*....|....*....|....
gi 2788209839 479 TLRALENALLEFPGC---AMVISH 499
Cdd:cd03246 131 GERALNQAIAALKAAgatRIVIAH 154
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
20-219 |
5.66e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 91.31 E-value: 5.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DKDIEG---EARPqpdikIGYLPQEPQLNPEHT 85
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFetpdsgrilldGRDVTGlppEKRN-----VGMVFQDYALFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIEeavsevvnalkrldevYALYADpdaDFDKLAAEQgRLEEIIQAhdghnlnVQLERAADalRLPDwdakiaNLSG 165
Cdd:COG3842 94 VAENVA----------------FGLRMR---GVPKAEIRA-RVAELLEL-------VGLEGLAD--RYPH------QLSG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 166 GERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESV-AWLERFLHDFEGTVVAITHDR 219
Cdd:COG3842 139 GQQQRVALARALAPEPRVLLLDEPLSALDAklrEEMrEELRRLQRELGITFIYVTHDQ 196
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-217 |
6.92e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 88.99 E-value: 6.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------GIDKDIEGEARPQPDI-----KIGYLpqEPQLNPEHTV 86
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgdlpptyGNDVRLFGERRGGEDVwelrkRIGLV--SPALQLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 87 RESIEEAVsevVNALkrldevYA---LYADPDAdfdklaAEQGRLEEIIQAhdghnlnVQLERAADALrlpdwdakIANL 163
Cdd:COG1119 94 DETVLDVV---LSGF------FDsigLYREPTD------EQRERARELLEL-------LGLAHLADRP--------FGTL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITH 217
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
324-513 |
6.97e-20 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 88.19 E-value: 6.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDR----LLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG--ETVK-----LASVD 392
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfDVVKepaeaRRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 393 QFRDSMDNSK--TVWEEVS--GGLDIMKIGNTEMPSRAYVGRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLL 468
Cdd:cd03266 82 FVSDSTGLYDrlTARENLEyfAGLYGLKGDELTARLEELADRLGMEELLD-RRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2788209839 469 DEPTNDLDIETLRALENALLEF--PGCAMVIShdrwfldriaTHILD 513
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLraLGKCILFS----------THIMQ 197
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
37-386 |
7.95e-20 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 92.39 E-value: 7.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 37 VLGLNGAGKSTLLRIMAGidkdiegearpqpdiKIGYLPQEPQLNPEHTVRESIEEAVSEVVNALKRLDeVYALYADPDa 116
Cdd:PRK10938 34 FVGANGSGKSALARALAG---------------ELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNN-TDMLSPGED- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 117 DFDKLAAEqgrleeIIQahDGHNLNVQLERAADALRLPDW-DAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 195
Cdd:PRK10938 97 DTGRTTAE------IIQ--DEVKDPARCEQLAQQFGITALlDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 196 ESVAWLERFLHDFEGTVVAIthdryfldnvagwILELDRGEGIPwegnysswleqkdqrlaqeasqEAARRKSIEKELEW 275
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITL-------------VLVLNRFDEIP----------------------DFVQFAGVLADCTL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 276 VRQGTKGR--QSKGKARLARFEELN------STEYQKRNEtnelfIPPG-PRlgdkvLEVSNLRKSYGDRLLIDDLSFSI 346
Cdd:PRK10938 214 AETGEREEilQQALVAQLAHSEQLEgvqlpePDEPSARHA-----LPANePR-----IVLNNGVVSYNDRPILHNLSWQV 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2788209839 347 PKGAIVGIIGPNGAGKSTLFRMISGQE-QPDSGTITL-------GETV 386
Cdd:PRK10938 284 NPGEHWQIVGPNGAGKSTLLSLITGDHpQGYSNDLTLfgrrrgsGETI 331
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
323-530 |
9.21e-20 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 92.65 E-value: 9.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLA--SVDQFrdsmdn 400
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGklRQDQF------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 401 sktVWEEVSgGLDIMKIGNTEM------PSRAYV----------------GRF-NFKGVDQGKRVGEL------------ 445
Cdd:PRK15064 75 ---AFEEFT-VLDTVIMGHTELwevkqeRDRIYAlpemseedgmkvadleVKFaEMDGYTAEARAGELllgvgipeeqhy 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 446 ------SGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEFpGCAMV-ISHDRWFLDRIATHI--LDYqd 516
Cdd:PRK15064 151 glmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNER-NSTMIiISHDRHFLNSVCTHMadLDY-- 227
|
250
....*....|....
gi 2788209839 517 eGKVEFFEGNFTEY 530
Cdd:PRK15064 228 -GELRVYPGNYDEY 240
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-218 |
1.65e-19 |
|
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: 88.01 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 9 HRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DKDI---EGEARPQPDIKIGYL 74
Cdd:cd03256 4 ENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLveptsgsvlidGTDInklKGKALRQLRRQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 75 PQEPQLNPEHTVRESIeeavseVVNALKRLDEVYALYadpdadfdklaaeqGRLEEIiqahdghnlnvQLERAADALR-- 152
Cdd:cd03256 84 FQQFNLIERLSVLENV------LSGRLGRRSTWRSLF--------------GLFPKE-----------EKQRALAALErv 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 153 --LPDWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESV-AWLERFLHDFEGTVVAITHD 218
Cdd:cd03256 133 glLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDpasSRQVmDLLKRINREEGITVIVSLHQ 204
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
323-507 |
1.81e-19 |
|
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: 87.41 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLL----IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTIT-LGETV----------- 386
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLdtrvLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLfNGQSLsklssnerakl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 387 ---KLASVDQFRDSMDNSkTVWEEVSGGLDIMKIGNTEMPSRAYVgrfNFKGVDQGKRV----GELSGGERGRLHLAKLL 459
Cdd:TIGR02211 81 rnkKLGFIYQFHHLLPDF-TALENVAMPLLIGKKSVKEAKERAYE---MLEKVGLEHRInhrpSELSGGERQRVAIARAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 460 QVGGNMLLLDEPTNDLDIETLRALENALLEF---PGCAMVI-SHDRWFLDRI 507
Cdd:TIGR02211 157 VNQPSLVLADEPTGNLDNNNAKIIFDLMLELnreLNTSFLVvTHDLELAKKL 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-257 |
4.29e-19 |
|
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: 86.57 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DKDI---EGEARPQPDIKIGYLPQEPQLNPEH 84
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLlrpdsgeilvdGQDItglSEKELYELRRRIGMLFQGGALFDSL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 TVRESIeeavsevvnALkRLDEVYALyadPDADFDKLAAEqgRLEEiiqahdghnlnVQLERAADalRLPdwdakiANLS 164
Cdd:COG1127 98 TVFENV---------AF-PLREHTDL---SEAEIRELVLE--KLEL-----------VGLPGAAD--KMP------SELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD----FEGTVVAITHDRYFLDNVAGWILELDRGEgIPW 240
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIADRVAVLADGK-IIA 222
|
250
....*....|....*..
gi 2788209839 241 EGNYSSWLEQKDQRLAQ 257
Cdd:COG1127 223 EGTPEELLASDDPWVRQ 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
323-511 |
4.63e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.08 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVdqfRDSMDN- 400
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVRFRSP---RDAQAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 401 -SkTVWEEVS--GGLDI---MKIGNteMPSRAyvGRFNFK---------------GVDQGKRVGELSGGERGRLHLAKLL 459
Cdd:COG1129 81 iA-IIHQELNlvPNLSVaenIFLGR--EPRRG--GLIDWRamrrrarellarlglDIDPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 460 QVGGNMLLLDEPTNDLD----------IETLRALenallefpGCAMV-ISHdrwFLD---RIATHI 511
Cdd:COG1129 156 SRDARVLILDEPTASLTereverlfriIRRLKAQ--------GVAIIyISH---RLDevfEIADRV 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
324-476 |
4.70e-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: 85.77 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETV--KLASVDqfRD-SM-- 398
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtDLPPKD--RDiAMvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 DN-----SKTVWEEVSGGLDIMKIGNTEMPSRAY-VGRfnFKGVDQ--GKRVGELSGGERGRLHLAKLLQVGGNMLLLDE 470
Cdd:cd03301 79 QNyalypHMTVYDNIAFGLKLRKVPKDEIDERVReVAE--LLQIEHllDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
....*.
gi 2788209839 471 PTNDLD 476
Cdd:cd03301 157 PLSNLD 162
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-236 |
4.89e-19 |
|
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: 85.92 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 8 MHRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK--------------DIEGEARPQPDIKIGY 73
Cdd:cd03292 3 FINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELptsgtirvngqdvsDLRGRAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 74 LPQEPQLNPEHTVRESIEEAVsEVVNALKRLdevyalyadpdadfdklaaeqgrleeiIQahdghnlnvqlERAADALRL 153
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFAL-EVTGVPPRE---------------------------IR-----------KRVPAALEL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 154 PDWDAKI----ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFE---GTVVAITHDRYFLDNVA 226
Cdd:cd03292 124 VGLSHKHralpAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTTR 203
|
250
....*....|
gi 2788209839 227 GWILELDRGE 236
Cdd:cd03292 204 HRVIALERGK 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-218 |
5.00e-19 |
|
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: 86.37 E-value: 5.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKD------IEGE--ARPQPDIKIGYlpQEPQLNPEHTVRESIEEA 93
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPtsggviLEGKqiTEPGPDRMVVF--QNYSLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 94 VSEVVNALKRldevyalyadpdadfdklaAEQgrlEEIIqahDGHNLNVQLERAADAlrlpdwdaKIANLSGGERRRVAL 173
Cdd:TIGR01184 79 VDRVLPDLSK-------------------SER---RAIV---EEHIALVGLTEAADK--------RPGQLSGGMKQRVAI 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2788209839 174 CRLLLEKPDMLLLDEPTNHLDAESVAWLE----RFLHDFEGTVVAITHD 218
Cdd:TIGR01184 126 ARALSIRPKVLLLDEPFGALDALTRGNLQeelmQIWEEHRVTVLMVTHD 174
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
324-520 |
5.33e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 85.96 E-value: 5.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLidDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRDSM---D 399
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWnGQDLTALPPAERPVSMlfqE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 400 N----SKTVWEEVSGGLDI-MKIGNTEmpsRAYV----GRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLLDE 470
Cdd:COG3840 80 NnlfpHLTVAQNIGLGLRPgLKLTAEQ---RAQVeqalERVGLAGLLD-RLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 471 PTNDLD----------IETLRALENALLefpgcaMVISHDrwfLD---RIATHILdYQDEGKV 520
Cdd:COG3840 156 PFSALDpalrqemldlVDELCRERGLTV------LMVTHD---PEdaaRIADRVL-LVADGRI 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-219 |
9.06e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.83 E-value: 9.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE------------ARpqpDIKIGYLPQEPQLNPEHT 85
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHirfhgtdvsrlhAR---DRKVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIEEAVSeVVNALKRldevyalyadPDADFDKLAAEQgrLEEIiqahdghnlnVQLERAADalRLPdwdakiANLSG 165
Cdd:PRK10851 91 VFDNIAFGLT-VLPRRER----------PNAAAIKAKVTQ--LLEM----------VQLAHLAD--RYP------AQLSG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 166 GERRRVALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLERFLHDFEGTVVAITHDR 219
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQ 197
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
324-489 |
9.23e-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: 9.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTI-TLGETVKLASVDQF------RD 396
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlFDGKPLDIAARNRIgylpeeRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 SMDNSKtVWEEVS--GGLDIMKIGNTEMPSRAYVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTND 474
Cdd:cd03269 81 LYPKMK-VIDQLVylAQLKGLKKEEARRRIDEWLERLELSEY-ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170
....*....|....*
gi 2788209839 475 LDIETLRALENALLE 489
Cdd:cd03269 159 LDPVNVELLKDVIRE 173
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
324-479 |
9.80e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 87.44 E-value: 9.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSY----GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRD-- 396
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 ---SM----DN---SKTVWEEVSGGLDIMKIgntempSRAyvgrfnfkgvDQGKRVGE-----------------LSGGE 449
Cdd:COG1135 82 rkiGMifqhFNllsSRTVAENVALPLEIAGV------PKA----------EIRKRVAEllelvglsdkadaypsqLSGGQ 145
|
170 180 190
....*....|....*....|....*....|
gi 2788209839 450 RGRLHLAKLLQVGGNMLLLDEPTNDLDIET 479
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPET 175
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-231 |
1.30e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.89 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEA--RPQP--------------DIKIGYLPQEPQL 80
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswRGEPlaklnraqrkafrrDIQMVFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 81 NPEHTVRESIEEAVSEvvnaLKRLDEvyalyadpdadfdklAAEQGRLEEIIQAhdghnlnVQLeRAADALRLPdwdaki 160
Cdd:PRK10419 103 NPRKTVREIIREPLRH----LLSLDK---------------AERLARASEMLRA-------VDL-DDSVLDKRP------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 161 ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD----RYFLDNVA----GW 228
Cdd:PRK10419 150 PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDlrlvERFCQRVMvmdnGQ 229
|
...
gi 2788209839 229 ILE 231
Cdd:PRK10419 230 IVE 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-238 |
1.33e-18 |
|
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: 83.36 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 14 VVPPKRHIL-KNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI----DKDIEgeaRPqPDIKIGYLPQEPQLNPehtvre 88
Cdd:cd03223 8 LATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwpwgSGRIG---MP-EGEDLLFLPQRPYLPL------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 89 sieeavsevvnalkrldevyalyadpdadfdklaaeqGRLeeiiqahdghnlnvqleraADALRLPdWDAKianLSGGER 168
Cdd:cd03223 78 -------------------------------------GTL-------------------REQLIYP-WDDV---LSGGEQ 97
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 169 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHdRYFLDNVAGWILELDRGEGI 238
Cdd:cd03223 98 QRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGEGGW 166
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-218 |
1.67e-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: 84.54 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-IDK----------DIEGEARPQPDI-------KIGYLPQEPq 79
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlNDLipgapdegevLLDGKDIYDLDVdvlelrrRVGMVFQKP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 80 lNPEH-TVRESIeeavsevvnalkrldeVYALyadpdadfdKLAAEQGRLEEiiqahdghnlnvqLERAADALRLPD-WD 157
Cdd:cd03260 91 -NPFPgSIYDNV----------------AYGL---------RLHGIKLKEEL-------------DERVEEALRKAAlWD 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 158 -----AKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITHD 218
Cdd:cd03260 132 evkdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-239 |
1.95e-18 |
|
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: 88.69 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 32 GAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEArpQPDIKIGYLPQEPQLNPEHTVRESIEEAVSEvvnalkRLDEVYALy 111
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGTVEEFLRSANTD------DFGSSYYK- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 112 adpdadfdklaaeqgrlEEIIQAhdghnlnVQLERAadalrlpdWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTN 191
Cdd:COG1245 437 -----------------TEIIKP-------LGLEKL--------LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 192 HLDAE---SVA-WLERFLHDFEGTVVAITHDRYFLDNVAgwilelDRG---EGIP 239
Cdd:COG1245 485 HLDVEqrlAVAkAIRRFAENRGKTAMVVDHDIYLIDYIS------DRLmvfEGEP 533
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
321-499 |
2.16e-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: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSG-TIT-LGETVKLASV------- 391
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlFGERRGGEDVwelrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 392 --------DQFRDSMdnskTVWEEV-SGGLDImkIGNTEMPSRAYVGR----FNFKGVDQ--GKRVGELSGGERGRLHLA 456
Cdd:COG1119 81 glvspalqLRFPRDE----TVLDVVlSGFFDS--IGLYREPTDEQRERarelLELLGLAHlaDRPFGTLSQGEQRRVLIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2788209839 457 KLLQVGGNMLLLDEPTNDLDI---ETLRALENALLEFPGCAMV-ISH 499
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLgarELLLALLDKLAAEGAPTLVlVTH 201
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
324-476 |
2.54e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 86.67 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETV--KLASVDqfRD----- 396
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtDLPPKD--RNiamvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 -------SMdnskTVWEEVSGGLDIMKIGNTEMPSRayvgrfnfkgVDQ-----------GKRVGELSGGERGRLHLAKL 458
Cdd:COG3839 82 qsyalypHM----TVYENIAFPLKLRKVPKAEIDRR----------VREaaellgledllDRKPKQLSGGQRQRVALGRA 147
|
170 180
....*....|....*....|..
gi 2788209839 459 L----QVggnmLLLDEPTNDLD 476
Cdd:COG3839 148 LvrepKV----FLLDEPLSNLD 165
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
323-524 |
3.68e-18 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 83.89 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVklasvdqfrdsmDNS 401
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVdGEDL------------TDS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 402 KTvweevsgglDIMKIgntempsRAYVG----RFN-F----------------KGVDQG----------KRVG------- 443
Cdd:COG1126 69 KK---------DINKL-------RRKVGmvfqQFNlFphltvlenvtlapikvKKMSKAeaeeramellERVGladkada 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 444 ---ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIE-------TLRALENAllefpGCAMVI-SHDRWFLDRIATHIL 512
Cdd:COG1126 133 ypaQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPElvgevldVMRDLAKE-----GMTMVVvTHEMGFAREVADRVV 207
|
250
....*....|....*....
gi 2788209839 513 dYQDEGKV-------EFFE 524
Cdd:COG1126 208 -FMDGGRIveegppeEFFE 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-218 |
4.11e-18 |
|
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: 83.54 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR-------PQPDIK--IGYLPQEPQLNPEHTVRESIEE 92
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditNLPPEKrdISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 93 AVSEVVNALKRLDEvyalyadpdadfdklaaeqgRLEEIIQA-HDGHNLNvqleraadalRLPdwdakiANLSGGERRRV 171
Cdd:cd03299 95 GLKKRKVDKKEIER--------------------KVLEIAEMlGIDHLLN----------RKP------ETLSGGEQQRV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 172 ALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHD-FEGTVVAITHD 218
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVrtkEKLREELKKIRKeFGVTVLHVTHD 189
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-241 |
4.24e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.05 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-----------IDKDIEGEARPQPDIKIGYLPQEPQLNPEHTV 86
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGelspdsgevrlNGRPLADWSPAELARRRAVLPQHSSLSFPFTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 87 ResieeavsEVVnALKRLDevyalyadpdadfdkLAAEQGRLEEIIQAhdghnlnvQLERA-ADALRlpdwDAKIANLSG 165
Cdd:PRK13548 94 E--------EVV-AMGRAP---------------HGLSRAEDDALVAA--------ALAQVdLAHLA----GRDYPQLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 166 GERRRVALCRLLL------EKPDMLLLDEPTNHLD---AESVAWLER-FLHDFEGTVVAITHD-----RYfldnvAGWIL 230
Cdd:PRK13548 138 GEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDlahQHHVLRLARqLAHERGLAVIVVLHDlnlaaRY-----ADRIV 212
|
250
....*....|....*
gi 2788209839 231 ELDRG----EGIPWE 241
Cdd:PRK13548 213 LLHQGrlvaDGTPAE 227
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-226 |
4.71e-18 |
|
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: 83.61 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 28 SFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEArPQPDIKIGYLPQEPQLNPEHTVRESIEEAVSEVVNALKRLDEV 107
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-EIELDTVSYKPQYIKADYEGTVRDLLSSITKDFYTHPYFKTEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 108 yalyADPdadfdklaaeqgrleeiiqahdghnlnVQLERAADAlRLPDwdakianLSGGERRRVALCRLLLEKPDMLLLD 187
Cdd:cd03237 100 ----AKP---------------------------LQIEQILDR-EVPE-------LSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2788209839 188 EPTNHLDAE----SVAWLERFLHDFEGTVVAITHDRYFLDNVA 226
Cdd:cd03237 141 EPSAYLDVEqrlmASKVIRRFAENNEKTAFVVEHDIIMIDYLA 183
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
286-509 |
6.36e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 87.14 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 286 KGKARLARFEELNSTEYQKRNETNElfIPPGPRLGDkvLEVSNLRKSY-GDRLLIDDLSFSIPKGAIVGIIGPNGAGKST 364
Cdd:COG1132 306 RALASAERIFELLDEPPEIPDPPGA--VPLPPVRGE--IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKST 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 365 LFRMISGQEQPDSGTITLGET-VKLASVDQFRDSM-----DN---SKTVWEEVsggldimKIGNTEMP--------SRAY 427
Cdd:COG1132 382 LVNLLLRFYDPTSGRILIDGVdIRDLTLESLRRQIgvvpqDTflfSGTIRENI-------RYGRPDATdeeveeaaKAAQ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 428 VGRF--NF-KGVDQgkRVGE----LSGGERGRLHLAKLL----QVggnmLLLDEPTNDLDIETLRALENALLEF-PGCAM 495
Cdd:COG1132 455 AHEFieALpDGYDT--VVGErgvnLSGGQRQRIAIARALlkdpPI----LILDEATSALDTETEALIQEALERLmKGRTT 528
|
250
....*....|....*
gi 2788209839 496 -VISHdrwfldRIAT 509
Cdd:COG1132 529 iVIAH------RLST 537
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
18-236 |
6.41e-18 |
|
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: 82.58 E-value: 6.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR--------PQPDI-----KIGYLPQEPQLNPEH 84
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglkltdDKKNInelrqKVGMVFQQFNLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 TVRESIEEAVSEVvnaLKRldevyalyadpdadfDKLAAEqgrleeiiqahdghnlnvqlERAADALR---LPDW-DAKI 160
Cdd:cd03262 92 TVLENITLAPIKV---KGM---------------SKAEAE--------------------ERALELLEkvgLADKaDAYP 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 161 ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03262 134 AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeEGmTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-477 |
6.78e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.64 E-value: 6.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK------DIEGEAR----PQPDIKIG-YL-PQEPQLNPEHTVRE 88
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPpdsgtlEIGGNPCarltPAKAHQLGiYLvPQEPLLFPNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 89 SIeeavsevvnaLKRLDevyalyadpdadfdKLAAEQGRLEEIIQAhdghnLNVQLeraadalrlpDWDAKIANLSGGER 168
Cdd:PRK15439 106 NI----------LFGLP--------------KRQASMQKMKQLLAA-----LGCQL----------DLDSSAGSLEVADR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 169 RRVALCRLLLEKPDMLLLDEPTNHLD-AESVAWLERF--LHDFEGTVVAITHDRYFLDNVAGWILELdRGEGIPWEGNYS 245
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTpAETERLFSRIreLLAQGVGIVFISHKLPEIRQLADRISVM-RDGTIALSGKTA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 246 SWleqKDQRLAQEASQEAARRKSIEKELEWVR-QGTKGRQSKGKARLaRFEELnsteyqkrneTNELFIppgprlgdkvl 324
Cdd:PRK15439 226 DL---STDDIIQAITPAAREKSLSASQKLWLElPGNRRQQAAGAPVL-TVEDL----------TGEGFR----------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 325 evsnlrksygdrllidDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRDS------ 397
Cdd:PRK15439 281 ----------------NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLnGKEINALSTAQRLARglvylp 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 398 ---------MDNSKTvWEEVSGGLDIMKIGNTEMPSRAYVGRF------NFKGVDQGkrVGELSGGERGRLHLAKLLQVG 462
Cdd:PRK15439 345 edrqssglyLDAPLA-WNVCALTHNRRGFWIKPARENAVLERYrralniKFNHAEQA--ARTLSGGNQQKVLIAKCLEAS 421
|
490
....*....|....*
gi 2788209839 463 GNMLLLDEPTNDLDI 477
Cdd:PRK15439 422 PQLLIVDEPTRGVDV 436
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
324-472 |
9.78e-18 |
|
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: 82.10 E-value: 9.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG----------ETVK--LASV 391
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglpphERARagIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 392 DQFRD---SMdnskTVWEevsggldimkigNTEMPSRAYVGRFNFKGVDQ------------GKRVGELSGGERGRLHLA 456
Cdd:cd03224 81 PEGRRifpEL----TVEE------------NLLLGAYARRRAKRKARLERvyelfprlkerrKQLAGTLSGGEQQMLAIA 144
|
170
....*....|....*.
gi 2788209839 457 KLLQVGGNMLLLDEPT 472
Cdd:cd03224 145 RALMSRPKLLLLDEPS 160
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-226 |
1.20e-17 |
|
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: 84.38 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 30 FPGAKIGVL-GLNGAGKSTLLRIMAGIDKDIEG--------------------EARPqpdikIGYLPQEPQLNPEHTVRE 88
Cdd:COG4148 22 LPGRGVTALfGPSGSGKTTLLRAIAGLERPDSGrirlggevlqdsargiflppHRRR-----IGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 89 SIEeavsevvnalkrldevYALyadpdaDFDKLAAEQGRLEEIIQ----AHdghnLnvqLERaadalrlpdwdaKIANLS 164
Cdd:COG4148 97 NLL----------------YGR------KRAPRAERRISFDEVVEllgiGH----L---LDR------------RPATLS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788209839 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERfLHD-FEGTVVAITHDryfLDNVA 226
Cdd:COG4148 136 GGERQRVAIGRALLSSPRLLLMDEPLAALDlarkAEILPYLER-LRDeLDIPILYVSHS---LDEVA 198
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
324-490 |
1.47e-17 |
|
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: 80.43 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYG--DRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFRDSMdns 401
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 402 ktvweevsggldimkignTEMPSRAYVgrFNFKGVDQ-GKRvgeLSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETL 480
Cdd:cd03247 78 ------------------SVLNQRPYL--FDTTLRNNlGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170
....*....|
gi 2788209839 481 RALENALLEF 490
Cdd:cd03247 135 RQLLSLIFEV 144
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
319-521 |
1.60e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 319 LGDKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGE-----------TVK 387
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 388 LASVDQFRD------------SMDNSKTVWEEV-SGGLDIMKIGNTEMPSRA--YVGRFNFKGVDQGKRVGELSGGERGR 452
Cdd:PRK10619 81 VADKNQLRLlrtrltmvfqhfNLWSHMTVLENVmEAPIQVLGLSKQEARERAvkYLAKVGIDERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 453 LHLAKLLQVGGNMLLLDEPTNDLDI----ETLRALENaLLEFPGCAMVISHDRWFLDRIATHILdYQDEGKVE 521
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPelvgEVLRIMQQ-LAEEGKTMVVVTHEMGFARHVSSHVI-FLHQGKIE 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
22-241 |
1.90e-17 |
|
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: 81.26 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEA--------RPQPDIK--IGYLPQEPQLNPEHTVRESIE 91
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAtvaghdvvREPREVRrrIGIVFQDLSVDDELTGWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 92 eavsevVNAlkrldevyALYADPDADFDKlaaeqgRLEEIIQAhdghnlnVQLERAADALrlpdwdakIANLSGGERRRV 171
Cdd:cd03265 96 ------IHA--------RLYGVPGAERRE------RIDELLDF-------VGLLEAADRL--------VKTYSGGMRRRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 172 ALCRLLLEKPDMLLLDEPTNHLDAESVA--W--LERFLHDFEGTVVAITHDRYFLDNVAGWILELDRG----EGIPWE 241
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGriiaEGTPEE 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-218 |
1.91e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 83.97 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 9 HRVGKVvppkrHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DKDIEGEARPQPDIkiGYLPQE 77
Cdd:COG3839 11 KSYGGV-----EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLedptsgeiligGRDVTDLPPKDRNI--AMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 78 PQLNPEHTVRESIEeavsevvnalkrldevYALyadpdadfdKLAaeqGRLEEIIQAhdghnlnvQLERAADALRLPDW- 156
Cdd:COG3839 84 YALYPHMTVYENIA----------------FPL---------KLR---KVPKAEIDR--------RVREAAELLGLEDLl 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 157 DAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------EsvawLERFLHDFEGTVVAITHD 218
Cdd:COG3839 128 DRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAklrvemraE----IKRLHRRLGTTTIYVTHD 193
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-236 |
1.97e-17 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 81.71 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DKDIEGeaRPQPDIK---IGYLPQEPQLNPEHT 85
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFlrptsgsvlfdGEDITG--LPPHEIArlgIGRTFQIPRLFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIEeavsevvnalkrldevyalyadpdadfdkLAAEQGRLEEIIQAHDGHNLNVQLERAADALRL----PDWDAKIA 161
Cdd:cd03219 92 VLENVM-----------------------------VAAQARTGSGLLLARARREEREARERAEELLERvglaDLADRPAG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPT---NHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
322-386 |
1.98e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.05 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 322 KVLEVSNLRKSY------GDRLL----------------IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT 379
Cdd:COG1134 3 SMIEVENVSKSYrlyhepSRSLKelllrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
....*..
gi 2788209839 380 ITLGETV 386
Cdd:COG1134 83 VEVNGRV 89
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
324-506 |
2.02e-17 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 81.30 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSY-GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGET----VKLASVDQFRDSM 398
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 -----DN----SKTVWEEVSGGLDIMKIGNTEMPSRAyVGRFNFKGVDQGKRV--GELSGGERGRLHLAKLLQVGGNMLL 467
Cdd:cd03292 81 gvvfqDFrllpDRNVYENVAFALEVTGVPPREIRKRV-PAALELVGLSHKHRAlpAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2788209839 468 LDEPTNDLDIETLRALENALLEF--PGCAMVIS-HDRWFLDR 506
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKInkAGTTVVVAtHAKELVDT 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-477 |
2.25e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-DKD---IE--GEA------RPQPDIKIGYLPQEPQLNPEHTVRES 89
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIyTRDagsILylGKEvtfngpKSSQEAGIGIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 90 IEEAvSEVVNALKRLD--EVYalyadpdADFDKLAAeqgRLEeiiQAHDGHNLnvqleraadalrlpdwdakIANLSGGE 167
Cdd:PRK10762 100 IFLG-REFVNRFGRIDwkKMY-------AEADKLLA---RLN---LRFSSDKL-------------------VGELSIGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 168 RRRVALCRLLLEKPDMLLLDEPTNHL-DAESVAwlerflhdfegtvvaithdryfLDNVagwILEL-DRGEGIPwegnYS 245
Cdd:PRK10762 147 QQMVEIAKVLSFESKVIIMDEPTDALtDTETES----------------------LFRV---IRELkSQGRGIV----YI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 246 SwleqkdQRLaQEASQeaarrksIEKELEWVRQGtkgrQSKGKARLARFEELNSTEYQKRNETNELFippgPRL----GD 321
Cdd:PRK10762 198 S------HRL-KEIFE-------ICDDVTVFRDG----QFIAEREVADLTEDSLIEMMVGRKLEDQY----PRLdkapGE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 322 KVLEVSNLRKSyGdrllIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVK-------LA---- 389
Cdd:PRK10762 256 VRLKVDNLSGP-G----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdGHEVVtrspqdgLAngiv 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 390 --SVDQFRDSM-------DN-SKTVWEEVSGGLDIMKIGNTEMPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLL 459
Cdd:PRK10762 331 yiSEDRKRDGLvlgmsvkENmSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGL 410
|
490
....*....|....*...
gi 2788209839 460 QVGGNMLLLDEPTNDLDI 477
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDV 428
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
20-218 |
2.36e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 81.34 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE--------------ARPqpdIKIgyLPQEPQLNPEHT 85
Cdd:COG3840 13 DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRilwngqdltalppaERP---VSM--LFQENNLFPHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIeeavsevvnalkrldevyALYADPDAdfdKL-AAEQGRLEEIIQahdghnlNVQLERAADalRLPdwdakiANLS 164
Cdd:COG3840 88 VAQNI------------------GLGLRPGL---KLtAEQRAQVEQALE-------RVGLAGLLD--RLP------GQLS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD 218
Cdd:COG3840 132 GGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-217 |
2.70e-17 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 81.09 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 7 TMHRVGKVVPPKR---HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE--------------ARPQPDI 69
Cdd:cd03258 3 ELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSvlvdgtdltllsgkELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 70 KIGYLPQEPQLNPEHTVRESI----EEAVSEVVNALKRLDEVYALyadpdadfdklaaeqgrleeiiqahdghnlnVQLE 145
Cdd:cd03258 83 RIGMIFQHFNLLSSRTVFENValplEIAGVPKAEIEERVLELLEL-------------------------------VGLE 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 146 RAADAlrlpdwdaKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD----FEGTVVAITH 217
Cdd:cd03258 132 DKADA--------YPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinreLGLTIVLITH 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-217 |
3.13e-17 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 81.12 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---ID-KDIEGEARPQPDIKIGYLPQEPQLNPEh 84
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvsSGsilIDgQDIREVTLDSLRRAIGVVPQDTVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 TVRESIEeavsevvnalkrldevyalYADPDADFDKL--AAEQGRLEEIIqahdghnlnvqleraadaLRLPD-WDAKIA 161
Cdd:cd03253 90 TIGYNIR-------------------YGRPDATDEEVieAAKAAQIHDKI------------------MRFPDgYDTIVG 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 162 N----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD-FEG-TVVAITH 217
Cdd:cd03253 133 ErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDvSKGrTTIVIAH 194
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
323-520 |
3.52e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.91 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-ITLGETVKLASVD--------- 392
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlIVDGLKVNDPKVDerlirqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 393 ----QFrdSMDNSKTVWEEVS-GGLDIMKIGNTEMPSRAyvgRFNFKGVDQGKRVG----ELSGGERGRLHLAKLLQVGG 463
Cdd:PRK09493 81 mvfqQF--YLFPHLTALENVMfGPLRVRGASKEEAEKQA---RELLAKVGLAERAHhypsELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 464 NMLLLDEPTNDLDI----ETLRALENALLEfpGCAMVI-SHDRWFLDRIATHILdYQDEGKV 520
Cdd:PRK09493 156 KLMLFDEPTSALDPelrhEVLKVMQDLAEE--GMTMVIvTHEIGFAEKVASRLI-FIDKGRI 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
324-507 |
3.95e-17 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 80.33 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGD--RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLgETVKLASVDQfRDSMDNS 401
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL-DGTDIRQLDP-ADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 402 KTVWEEV---SGGL-DIMKIGNTEMPSRAYVGRFNFKGVDQ---------GKRVGE----LSGGERGRLHLAKLLQVGGN 464
Cdd:cd03245 81 GYVPQDVtlfYGTLrDNITLGAPLADDERILRAAELAGVTDfvnkhpnglDLQIGErgrgLSGGQRQAVALARALLNDPP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788209839 465 MLLLDEPTNDLDIETLRALENALLEFPG--CAMVISHDRWFL---DRI 507
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLdlvDRI 208
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-217 |
4.44e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.92 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR--------PQPDIKIGYLPQEPQLNPEHTVRESI 90
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKldggdiddPDVAEACHYLGHRNAMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 91 EEAvsevvnalkrldevyalyadpdADFdkLAAEQGRLEEIIQAhdghnlnVQLERAADalrLPdwdakIANLSGGERRR 170
Cdd:PRK13539 95 EFW----------------------AAF--LGGEELDIAAALEA-------VGLAPLAH---LP-----FGYLSAGQKRR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 171 VALCRLLLEKPDMLLLDEPTNHLDAESVAwleRFLHDFE------GTVVAITH 217
Cdd:PRK13539 136 VALARLLVSNRPIWILDEPTAALDAAAVA---LFAELIRahlaqgGIVIAATH 185
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
316-524 |
4.45e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 80.27 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 316 GPRLGDKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLgeTVKLASVDQFR 395
Cdd:cd03220 15 GGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV--RGRVSSLLGLG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 DSMDNSKTVWEEVSGGLDIMKIGNTEMPSR-AYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTND 474
Cdd:cd03220 93 GGFNPELTGRENIYLNGRLLGLSRKEIDEKiDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 475 LDIETLRALENALLEF-PGCAMVI--SHDRWFLDRIATHILdYQDEGKVEFFE 524
Cdd:cd03220 173 GDAAFQEKCQRRLRELlKQGKTVIlvSHDPSSIKRLCDRAL-VLEKGKIRFDG 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
324-508 |
4.55e-17 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 80.46 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLiDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQfRD------ 396
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDITNLPPEK-RDisyvpq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 --SMDNSKTVWEEVSGGLDIMKIGNTEMPSRAY-VGRfnFKGVDQ--GKRVGELSGGERGRLHLAKLLQVGGNMLLLDEP 471
Cdd:cd03299 79 nyALFPHMTVYKNIAYGLKKRKVDKKEIERKVLeIAE--MLGIDHllNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2788209839 472 TNDLDIET----LRALENALLEFPGCAMVISHD----RWFLDRIA 508
Cdd:cd03299 157 FSALDVRTkeklREELKKIRKEFGVTVLHVTHDfeeaWALADKVA 201
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-197 |
4.66e-17 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 80.24 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEA----------RPQPDIKIGYLPQEPQLNPEHTVRE 88
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdRKAARQSLGYCPQFDALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 89 SIEeavsevvnalkrldevyaLYAdpdadfdklaaeqgrleeIIQAHDGHNLNVQLERAADALRLPD-WDAKIANLSGGE 167
Cdd:cd03263 95 HLR------------------FYA------------------RLKGLPKSEIKEEVELLLRVLGLTDkANKRARTLSGGM 138
|
170 180 190
....*....|....*....|....*....|
gi 2788209839 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAES 197
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-195 |
4.95e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 80.39 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 3 QFVYTMHRVGKVVP---PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKD---------IEGEARPQPDIK 70
Cdd:cd03234 1 QRVLPWWDVGLKAKnwnKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggttsgqilFNGQPRKPDQFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 71 --IGYLPQEPQLNPEHTVRESIEEAVsevVNALKRLDevyalyadPDADFDKLAaEQGRLEEIIQAHDGHNLnvqleraa 148
Cdd:cd03234 81 kcVAYVRQDDILLPGLTVRETLTYTA---ILRLPRKS--------SDAIRKKRV-EDVLLRDLALTRIGGNL-------- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2788209839 149 dalrlpdwdakIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 195
Cdd:cd03234 141 -----------VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-189 |
5.01e-17 |
|
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: 80.28 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE----------------ARpqpdIKIGYLPQEPQLN 81
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKilldgqditklpmhkrAR----LGIGYLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 82 PEHTVRESIeEAVSEVVNALKrldevyalyadpdadfdklAAEQGRLEEIIQAhdghnlnVQLERAAdalrlpdwDAKIA 161
Cdd:cd03218 88 RKLTVEENI-LAVLEIRGLSK-------------------KEREEKLEELLEE-------FHITHLR--------KSKAS 132
|
170 180
....*....|....*....|....*...
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEP 189
Cdd:cd03218 133 SLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
18-218 |
5.50e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.93 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDIKIGYLPQEPQLNPE--------HTVRES 89
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTlpltvnrfLRLRPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 90 IEEAvsEVVNALKRldevyalyadpdadfdklaaeqgrleeiIQAhdGHNLNVQLERaadalrlpdwdakianLSGGERR 169
Cdd:PRK09544 96 TKKE--DILPALKR----------------------------VQA--GHLIDAPMQK----------------LSGGETQ 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 170 RVALCRLLLEKPDMLLLDEPTNHLDAESVAWL----ERFLHDFEGTVVAITHD 218
Cdd:PRK09544 128 RVLLARALLNRPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHD 180
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
317-476 |
5.62e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 82.69 E-value: 5.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 317 PRLGDKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQfR 395
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLdGQDITHVPAEN-R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 D------------SMdnskTVWEEVSGGLDIMKIGNTEMPSR-----AYVGRFNFKgvdqGKRVGELSGGERGRLHLAKL 458
Cdd:PRK09452 87 HvntvfqsyalfpHM----TVFENVAFGLRMQKTPAAEITPRvmealRMVQLEEFA----QRKPHQLSGGQQQRVAIARA 158
|
170
....*....|....*...
gi 2788209839 459 LQVGGNMLLLDEPTNDLD 476
Cdd:PRK09452 159 VVNKPKVLLLDESLSALD 176
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
324-501 |
7.07e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.05 E-value: 7.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETV--------KLASVDQ- 393
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhGTDVsrlhardrKVGFVFQh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 ---FRdSMdnskTVWEEVSGGLDIMKigNTEMPSRAYVGRFNFKGVD--QGKRVGE-----LSGGERGRLHLAKLLQVGG 463
Cdd:PRK10851 83 yalFR-HM----TVFDNIAFGLTVLP--RRERPNAAAIKAKVTQLLEmvQLAHLADrypaqLSGGQKQRVALARALAVEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2788209839 464 NMLLLDEPTNDLDIET-------LRALENallEFPGCAMVISHDR 501
Cdd:PRK10851 156 QILLLDEPFGALDAQVrkelrrwLRQLHE---ELKFTSVFVTHDQ 197
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-217 |
7.39e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 78.94 E-value: 7.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEG----------EARPQPDIKIGYLPQEPQLNPEHTVRE 88
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGevrwngtplaEQRDEPHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 89 SIEeavsevvnalkrldevyaLYADpdadfdklaaeqgrleeiiqAHDGHNLNVqlERAADALRLPDW-DAKIANLSGGE 167
Cdd:TIGR01189 93 NLH------------------FWAA--------------------IHGGAQRTI--EDALAAVGLTGFeDLPAAQLSAGQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF---EGTVVAITH 217
Cdd:TIGR01189 133 QRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
20-218 |
7.67e-17 |
|
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: 79.79 E-value: 7.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE------------------ARPQpdiKIGYLPQEPQLN 81
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTvrlagqdlfaldedararLRAR---HVGFVFQSFQLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 82 PEHTVRESI----EEAvsevvnalkrldevyalyADPDAdFDKLAAEqgrleeiiqahdghnlnvqLERAADALRLpdwD 157
Cdd:COG4181 103 PTLTALENVmlplELA------------------GRRDA-RARARAL-------------------LERVGLGHRL---D 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 158 AKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHDFEG-TVVAITHD 218
Cdd:COG4181 142 HYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAatgEQIIDLLFELNRERGtTLVLVTHD 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-217 |
7.77e-17 |
|
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: 78.41 E-value: 7.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 14 VVPP--KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR-PQPDIK----------IGYLPQEPQL 80
Cdd:cd03246 8 FRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRlDGADISqwdpnelgdhVGYLPQDDEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 81 npehtvresieeavsevvnalkrldevyalyadpdadFDklaaeqGRLEEIIqahdghnlnvqleraadalrlpdwdaki 160
Cdd:cd03246 88 -------------------------------------FS------GSIAENI---------------------------- 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 161 anLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFE---GTVVAITH 217
Cdd:cd03246 97 --LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAH 154
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
326-512 |
8.40e-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: 80.14 E-value: 8.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 326 VSNLRKSYGD---RLLIDDLSFSipKGAIVGIIGPNGAGKSTLFRMISGQEQPDSG-TITLGETVKL----------ASV 391
Cdd:cd03237 1 YTYPTMKKTLgefTLEVEGGSIS--ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdIEIELDTVSYkpqyikadyeGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 392 DQFRDSMDNSKTV---WE-EVSGGLDIMKIgntempsrayvgrfnfkgVDQgkRVGELSGGERGRLHLAKLLQVGGNMLL 467
Cdd:cd03237 79 RDLLSSITKDFYThpyFKtEIAKPLQIEQI------------------LDR--EVPELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2788209839 468 LDEPTNDLDIE----TLRALENALLEFPGCAMVISHDRWFLDRIATHIL 512
Cdd:cd03237 139 LDEPSAYLDVEqrlmASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
319-500 |
9.08e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 80.83 E-value: 9.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 319 LGDKVLEVSNLRKSYGD--RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG------ETV---- 386
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlseETVwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 387 -KLASVDQFRDSMDNSKTVWEEVSGGLDIMKIGNTEMPSRayvgrfnfkgVDQG-KRVG----------ELSGGERGRLH 454
Cdd:PRK13635 81 rQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVER----------VDQAlRQVGmedflnrephRLSGGQKQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 455 LAKLLQVGGNMLLLDEPTNDLD-------IETLRALENAllefpGCAMVIS--HD 500
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDprgrrevLETVRQLKEQ-----KGITVLSitHD 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-190 |
9.13e-17 |
|
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: 79.64 E-value: 9.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DKDIEGeaRPQPDI---KIGYLPQEPQLNPEHT 85
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLlpprsgsirfdGEDITG--LPPHRIarlGIGYVPEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIE---EAVSEVVNALKRLDEVYALYadPdadfdklaaeqgRLEEiiqahdghnlnvQLERAAdalrlpdwdakiAN 162
Cdd:COG0410 95 VEENLLlgaYARRDRAEVRADLERVYELF--P------------RLKE------------RRRQRA------------GT 136
|
170 180
....*....|....*....|....*...
gi 2788209839 163 LSGGERRRVALCRLLLEKPDMLLLDEPT 190
Cdd:COG0410 137 LSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
324-520 |
1.10e-16 |
|
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: 78.72 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQE--QPDSGTITL-GETVKLASVDqfrdsmdn 400
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFkGEDITDLPPE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 401 sktvwEEVSGGLDIMKIGNTEMPSrayVGRFNF-KGVDQGkrvgeLSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIET 479
Cdd:cd03217 73 -----ERARLGIFLAFQYPPEIPG---VKNADFlRYVNEG-----FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2788209839 480 LRALENALLEF--PGCAM-VISHDRWFLDRIAT---HILdyqDEGKV 520
Cdd:cd03217 140 LRLVAEVINKLreEGKSVlIITHYQRLLDYIKPdrvHVL---YDGRI 183
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
324-490 |
1.36e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 79.30 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSY------------------GDRLLI---DDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL 382
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfkRKYREVealKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 383 GETVKLASVDQFRDS----MDNSKTVWeevsggLDIMKIGNTEMPSRAY-VGRFNFKG--------------VDQGKRvg 443
Cdd:cd03267 81 AGLVPWKRRKKFLRRigvvFGQKTQLW------WDLPVIDSFYLLAAIYdLPPARFKKrldelselldleelLDTPVR-- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2788209839 444 ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEF 490
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEY 199
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-234 |
1.46e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 78.68 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI---DKDIEGE---------ARPQPDIKIGYLPQEPQLNPEHTV 86
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlspAFSASGEvllngrrltALPAEQRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 87 RESIEEAVSEVVNALKRldevyalyadpdadfdKLAAEQGrLEEIiqahdghNLnvqlerAADALRLPdwdakiANLSGG 166
Cdd:COG4136 94 GENLAFALPPTIGRAQR----------------RARVEQA-LEEA-------GL------AGFADRDP------ATLSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERF----LHDFEGTVVAITHDRyflDNV--AGWILELDR 234
Cdd:COG4136 138 QRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDE---EDApaAGRVLDLGN 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-218 |
1.57e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.81 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DKDIEGEARPQPDIKIGYLPQEPQLNPEHTVRES 89
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTltptagtvlvaGDDVEALSARAASRRVASVPQDTSLSFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 90 IEEAVSEvvnALKRLDEvyalyADPDadfDKLAAEQGrleeiiqahdghnlnvqLERAaDALRLPDWDakIANLSGGERR 169
Cdd:PRK09536 98 VEMGRTP---HRSRFDT-----WTET---DRAAVERA-----------------MERT-GVAQFADRP--VTSLSGGERQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 170 RVALCRLLLEKPDMLLLDEPTNHLDA-ESVAWLE--RFLHDFEGTVVAITHD 218
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDInHQVRTLElvRRLVDDGKTAVAAIHD 198
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-189 |
2.07e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.92 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DKDIEGE-----ARpqpdIKIGYLPQEP--- 78
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLvkpdsgrifldGEDITHLpmhkrAR----LGIGYLPQEAsif 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 79 -QLnpehTVRESIeEAVSEVVNalkrldevyalyadpdadFDKLAAEQgRLEEIIQA-HDGHnlnvqleraadaLRlpdw 156
Cdd:COG1137 91 rKL----TVEDNI-LAVLELRK------------------LSKKEREE-RLEELLEEfGITH------------LR---- 130
|
170 180 190
....*....|....*....|....*....|...
gi 2788209839 157 DAKIANLSGGERRRVALCRLLLEKPDMLLLDEP 189
Cdd:COG1137 131 KSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-236 |
2.75e-16 |
|
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: 79.08 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEA--RPQP--------------DIKIGYLPQEPQLNPEH 84
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsfRGQDlyqldrkqrrafrrDVQLVFQDSPSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 TVRESIEEAVSEvvnaLKRLDEvyalyadpdadfdklAAEQGRLEEIIQAhdghnlnVQLeRAADALRLPdwdakiANLS 164
Cdd:TIGR02769 106 TVRQIIGEPLRH----LTSLDE---------------SEQKARIAELLDM-------VGL-RSEDADKLP------RQLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDmvlqAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
324-489 |
2.99e-16 |
|
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: 78.43 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGD-RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFR------ 395
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDIREVTLDSLRraigvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 --DSMDNSKTVW------------EEVSGGLDIMKIGNTEMpsrayvgRFNFkGVDqgKRVGE----LSGGERGRLHLAK 457
Cdd:cd03253 81 pqDTVLFNDTIGynirygrpdatdEEVIEAAKAAQIHDKIM-------RFPD-GYD--TIVGErglkLSGGEKQRVAIAR 150
|
170 180 190
....*....|....*....|....*....|..
gi 2788209839 458 LLQVGGNMLLLDEPTNDLDIETLRALENALLE 489
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRD 182
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-218 |
4.20e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.18 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE--------ARPQPDIKIGYlpQEPQLNPEHTVresi 90
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEllagtaplAEAREDTRLMF--QDARLLPWKKV---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 91 eeavsevvnalkrLDEVyalyadpdadfdKLAAEQGRLEEIIQAhdghnlnvqLERAADALRLPDWDAKianLSGGERRR 170
Cdd:PRK11247 99 -------------IDNV------------GLGLKGQWRDAALQA---------LAAVGLADRANEWPAA---LSGGQKQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 171 VALCRLLLEKPDMLLLDEPTNHLDA----------ESVaWLErflHDFegTVVAITHD 218
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDAltriemqdliESL-WQQ---HGF--TVLLVTHD 193
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
323-472 |
4.24e-16 |
|
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: 77.71 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVK-----------LAS 390
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdGEDITglpphriarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 391 VDQFRD---SMdnskTVWEevsggldimkigNTEMPsrAYVGRfNFKGVDQ----------------GKRVGELSGGERG 451
Cdd:COG0410 83 VPEGRRifpSL----TVEE------------NLLLG--AYARR-DRAEVRAdlervyelfprlkerrRQRAGTLSGGEQQ 143
|
170 180
....*....|....*....|.
gi 2788209839 452 RLHLAKLLQVGGNMLLLDEPT 472
Cdd:COG0410 144 MLAIGRALMSRPKLLLLDEPS 164
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-236 |
4.42e-16 |
|
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: 77.51 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE----ARPQPDIKIGYL-------PQEPQLNpEHT 85
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQvlldGKPISQYEHKYLhskvslvGQEPVLF-ARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIEeavsevvnalkrldevyalYADPDADFDKLAAEQgrleeiiQAHDGHNLNVQLERAADAlrlpDWDAKIANLSG 165
Cdd:cd03248 104 LQDNIA-------------------YGLQSCSFECVKEAA-------QKAHAHSFISELASGYDT----EVGEKGSQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 166 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITHdRYFLDNVAGWILELDRGE 236
Cdd:cd03248 154 GQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH-RLSTVERADQILVLDGGR 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-236 |
5.25e-16 |
|
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: 76.74 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-IDKdIEGEARPQPdiKIGYLPQEPQLNPEhTVRESI-------EE 92
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEK-LSGSVSVPG--SIAYVSQEPWIQNG-TIRENIlfgkpfdEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 93 AVSEVVNALkrldevyALyadpDADFDKLAAeqGRLEEIiqahdGhnlnvqlERAadalrlpdwdakiANLSGGERRRVA 172
Cdd:cd03250 96 RYEKVIKAC-------AL----EPDLEILPD--GDLTEI-----G-------EKG-------------INLSGGQKQRIS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 173 LCRLLLEKPDMLLLDEPTNHLDAESVAWLerFLHDFEG------TVVAITHDRYFLDNVAgWILELDRGE 236
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHI--FENCILGlllnnkTRILVTHQLQLLPHAD-QIVVLDNGR 204
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-220 |
5.32e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.13 E-value: 5.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DKDIEGEARPQPDIKIGYLPQEPqLNPEH-T 85
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLltpqsgtvflgDKPISMLSSRQLARRLALLPQHH-LTPEGiT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIEEAVSEVVNALKRLdevyalyADPDADFDKLAAEQGRLEEIIqahdghnlnvqleraadalrlpdwDAKIANLSG 165
Cdd:PRK11231 93 VRELVAYGRSPWLSLWGRL-------SAEDNARVNQAMEQTRINHLA------------------------DRRLTDLSG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 166 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHD-----RY 220
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELntQGkTVVTVLHDlnqasRY 204
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
324-500 |
5.77e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.04 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL----GETVKLASVDQFRDSMd 399
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdGQLRDLYALSEAERRR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 400 NSKTVW------------EEVSGGLDI----MKIGNtempsRAYvGRFNFKGVDQGKRV-----------GELSGGERGR 452
Cdd:PRK11701 86 LLRTEWgfvhqhprdglrMQVSAGGNIgerlMAVGA-----RHY-GDIRATAGDWLERVeidaariddlpTTFSGGMQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 453 LHLAKLLQVGGNMLLLDEPTNDLDI-------ETLRALENALlefpGCAMVI-SHD 500
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVsvqarllDLLRGLVREL----GLAVVIvTHD 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-225 |
6.17e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 78.61 E-value: 6.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-DKD-----IEGEARPQPDI-KIGYLPQEPQLNPEHTVRESI 90
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIlAPDsgevlWDGEPLDPEDRrRIGYLPEERGLYPKMKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 91 EeavsevvnALKRLdevyalyadpdADFDKLAAEQgRLEEIiqahdghnlnvqLERaadaLRLPDW-DAKIANLSGGERR 169
Cdd:COG4152 93 V--------YLARL-----------KGLSKAEAKR-RADEW------------LER----LGLGDRaNKKVEELSKGNQQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 170 RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDryfLDNV 225
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGtTVIFSSHQ---MELV 192
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
18-189 |
7.39e-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: 77.31 E-value: 7.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKST-------LLRIMAGI----DKDI-----EGEARpqpdIKIGYLPQEPQLN 81
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTsfymivgLVRPDAGKilidGQDIthlpmHERAR----LGIGYLPQEASIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 82 PEHTVRESIeEAVSEVVNALKRldevyalyadpdadfdklAAEQGRLEEIIQA-HDGHnlnvqleraadaLRlpdwDAKI 160
Cdd:TIGR04406 89 RKLTVEENI-MAVLEIRKDLDR------------------AEREERLEALLEEfQISH------------LR----DNKA 133
|
170 180
....*....|....*....|....*....
gi 2788209839 161 ANLSGGERRRVALCRLLLEKPDMLLLDEP 189
Cdd:TIGR04406 134 MSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
7-235 |
8.81e-16 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 76.70 E-value: 8.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 7 TMHRVGKVVPPkrhILKNISLSFFPGAKIGVLGLNGAGKSTLLRImagidkdIEGEARPQpDIKIGYLPQEPQLN----P 82
Cdd:COG4778 15 TLHLQGGKRLP---VLDGVSFSVAAGECVALTGPSGAGKSTLLKC-------IYGNYLPD-SGSILVRHDGGWVDlaqaS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 83 EHTV----RESIEeAVSEVVNALKR---LDEVyalyADPdadfdklAAEQGRLEEiiqahdghnlnVQLERAADALR--- 152
Cdd:COG4778 84 PREIlalrRRTIG-YVSQFLRVIPRvsaLDVV----AEP-------LLERGVDRE-----------EARARARELLArln 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 153 LPD--WDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGT-VVAITHDRYFLDNVAG 227
Cdd:COG4778 141 LPErlWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkaRGTaIIGIFHDEEVREAVAD 220
|
....*...
gi 2788209839 228 WILELDRG 235
Cdd:COG4778 221 RVVDVTPF 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
323-499 |
8.88e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.00 E-value: 8.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKlASVDQFRDSM--- 398
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIR-RQRDEYHQDLlyl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 ------DNSKTVWEEVSGGLDIMKIGNTEMpSRAYVGRFNFKGVDQGKrVGELSGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:PRK13538 80 ghqpgiKTELTALENLRFYQRLHGPGDDEA-LWEALAQVGLAGFEDVP-VRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|
gi 2788209839 473 NDLD---IETLRALENALLEFPGCAMVISH 499
Cdd:PRK13538 158 TAIDkqgVARLEALLAQHAEQGGMVILTTH 187
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-236 |
9.27e-16 |
|
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: 77.39 E-value: 9.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DKDIEGeaRPQPDI---KIGYLPQEPQLNPEHT 85
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFyrptsgrilfdGRDITG--LPPHRIarlGIARTFQNPRLFPELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIeeavseVVNALKRLDEVYAlyaDPDADFDKLAAEQGRLEEiiqahdghnlnvqleRAADALRL----PDWDAKIA 161
Cdd:COG0411 96 VLENV------LVAAHARLGRGLL---AALLRLPRARREEREARE---------------RAEELLERvglaDRADEPAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPT---NHLDAESVAWLERFLHDFEG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-218 |
9.71e-16 |
|
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: 76.14 E-value: 9.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR---------PQPDIKIGYLPQEPQLNPEHTVR 87
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdlPPKDRDIAMVFQNYALYPHMTVY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 88 ESIEeavsevvNALKRldevyalyadpdADFDKlaaeqgrlEEIiqahdghnlNVQLERAADALRLPDW-DAKIANLSGG 166
Cdd:cd03301 91 DNIA-------FGLKL------------RKVPK--------DEI---------DERVREVAELLQIEHLlDRKPKQLSGG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLERFLHDFEGTVVAITHD 218
Cdd:cd03301 135 QRQRVALGRAIVREPKVFLMDEPLSNLDAklrvQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-217 |
9.86e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.00 E-value: 9.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 24 NISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE----------ARPQPDIKIGYLPQEPQLNPEHTVRESieea 93
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEvlwqgepirrQRDEYHQDLLYLGHQPGIKTELTALEN---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 94 vsevVNALKRLdevyALYADPDADFDKLAAeqgrleeiiqahdghnlnVQLERAADALrlpdwdakIANLSGGERRRVAL 173
Cdd:PRK13538 95 ----LRFYQRL----HGPGDDEALWEALAQ------------------VGLAGFEDVP--------VRQLSAGQQRRVAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2788209839 174 CRLLLEKPDMLLLDEPTNHLDAESVAWLER-FLHDFE--GTVVAITH 217
Cdd:PRK13538 141 ARLWLTRAPLWILDEPFTAIDKQGVARLEAlLAQHAEqgGMVILTTH 187
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-203 |
1.00e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.92 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DKDIEGEARpQPDIKIGYLPQEPQLNPEHTVRES 89
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLthpdagsislcGEPVPSRAR-HARQRVGVVPQFDNLDPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 90 IEeavsevvnalkrldeVYALYADPDAdfdklAAEQGRLEEIIQAhdghnlnVQLERAADAlrlpdwdaKIANLSGGERR 169
Cdd:PRK13537 101 LL---------------VFGRYFGLSA-----AAARALVPPLLEF-------AKLENKADA--------KVGELSGGMKR 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 2788209839 170 RVALCRLLLEKPDMLLLDEPTNHLD--AESVAWlER 203
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDpqARHLMW-ER 180
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-500 |
1.14e-15 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 79.73 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKS----TLLRIMAGIDKDIEGEAR---------PQPDI------KIGYLPQEPQ 79
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILfdgqdllglSERELrrirgnRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 80 --LNPEHTvresIEEAVSEVVnALKRldevyalyadpdadfdKLAAEQGRleeiiqahdghnlnvqlERAADALR---LP 154
Cdd:COG4172 103 tsLNPLHT----IGKQIAEVL-RLHR----------------GLSGAAAR-----------------ARALELLErvgIP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 155 DwDAKIAN-----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD----RYF 221
Cdd:COG4172 145 D-PERRLDayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqAQILDLLKDLQRELGMALLLITHDlgvvRRF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 222 LDNVA----GWILEldRGEgipwegnysswleqkdqrLAQ--EASQEAARRKSIEKElewvrqgTKGRQskgkarlarfe 295
Cdd:COG4172 224 ADRVAvmrqGEIVE--QGP------------------TAElfAAPQHPYTRKLLAAE-------PRGDP----------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 296 elnsteyqkrnetnelfiPPGPRLGDKVLEVSNLRKSYGDR--LL---------IDDLSFSIPKGAIVGIIGPNGAGKST 364
Cdd:COG4172 266 ------------------RPVPPDAPPLLEARDLKVWFPIKrgLFrrtvghvkaVDGVSLTLRRGETLGLVGESGSGKST 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 365 LFRMISGQeQPDSGTITL-GETVKLASVDQFRD--------------SMDNSKTVWEEVSGGLDIMKIGNTEMPSRAYVg 429
Cdd:COG4172 328 LGLALLRL-IPSEGEIRFdGQDLDGLSRRALRPlrrrmqvvfqdpfgSLSPRMTVGQIIAEGLRVHGPGLSAAERRARV- 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 430 rfnfkgVDQGKRVG-----------ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD-------IETLRALENALlefp 491
Cdd:COG4172 406 ------AEALEEVGldpaarhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALDvsvqaqiLDLLRDLQREH---- 475
|
570
....*....|
gi 2788209839 492 GCAMV-ISHD 500
Cdd:COG4172 476 GLAYLfISHD 485
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
335-519 |
1.24e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 74.50 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 335 DRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGqeqpdsgtitlgetvklasvdqfrdsmdnsktVWEEVSGGLDI 414
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG--------------------------------LWPWGSGRIGM 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 415 MKIGNTE-MPSRAYVGRFNFKGV-----DQgkrvgELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALL 488
Cdd:cd03223 61 PEGEDLLfLPQRPYLPLGTLREQliypwDD-----VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK 135
|
170 180 190
....*....|....*....|....*....|..
gi 2788209839 489 EFpGCAMV-ISHdRWFLDRIATHILDYQDEGK 519
Cdd:cd03223 136 EL-GITVIsVGH-RPSLWKFHDRVLDLDGEGG 165
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
324-487 |
1.35e-15 |
|
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: 75.61 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETvklaSVDQFRDSMDNS-- 401
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG----PLDFQRDSIARGll 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 402 --------KTVWEEVSGGLDIMKIGNTEMPSRAyVGRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTN 473
Cdd:cd03231 77 ylghapgiKTTLSVLENLRFWHADHSDEQVEEA-LARVGLNGFED-RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170
....*....|....
gi 2788209839 474 DLDIETLRALENAL 487
Cdd:cd03231 155 ALDKAGVARFAEAM 168
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
341-500 |
1.42e-15 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 75.79 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 341 DLSFSIPkGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASvdqfRDSMDNSK------------------ 402
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDS----RKKINLPPqqrkiglvfqqyalfphl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 403 TVWEEVSGGLDIMKIGNTEMPSRAYVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRA 482
Cdd:cd03297 91 NVRENLAFGLKRKRNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180
....*....|....*....|..
gi 2788209839 483 LENALLE----FPGCAMVISHD 500
Cdd:cd03297 170 LLPELKQikknLNIPVIFVTHD 191
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-205 |
1.49e-15 |
|
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: 74.97 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--IDKDIEGE----ARPQPD---IKIGYLPQEPQLNPEHTVRE 88
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEilinGRPLDKnfqRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 89 SIEeavsevvnalkrldevyalyadpdadfdklaaeqgrleeiiqahdghnlnvqleraadalrlpdWDAKIANLSGGER 168
Cdd:cd03232 99 ALR----------------------------------------------------------------FSALLRGLSVEQR 114
|
170 180 190
....*....|....*....|....*....|....*..
gi 2788209839 169 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL 205
Cdd:cd03232 115 KRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
21-235 |
1.76e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.20 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE-----------ARPQPDI------KIGYLPQEPQLNPE 83
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQlniaghqfdfsQKPSEKAirllrqKVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 84 HTVRESIEEAVSEVVNALKrldevyalyadpdadfdklAAEQGRLEEIiqahdghnlnvqLERaadaLRLPDW-DAKIAN 162
Cdd:COG4161 97 LTVMENLIEAPCKVLGLSK-------------------EQAREKAMKL------------LAR----LRLTDKaDRFPLH 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEitaQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKG 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
324-476 |
1.86e-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: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYG----DRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQ---FR 395
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdGVPVTGPGADRgvvFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 -DSMDNSKTVWEEVSGGLDIMKIGNTEMPSRA--YVGRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:COG4525 84 kDALLPWLNVLDNVAFGLRLRGVPKAERRARAeeLLALVGLADFAR-RRIWQLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
....
gi 2788209839 473 NDLD 476
Cdd:COG4525 163 GALD 166
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-218 |
1.88e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 76.31 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE----ARPQPDIKI-------GYLPQEPQLNPEHTV 86
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEvrlnGRPLAAWSPwelarrrAVLPQHSSLAFPFTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 87 ResieeavsEVVnALKRLdevyalyadPdadfdkLAAEQGRLEEIIQAhdghnlnvQLERaADALRLpdWDAKIANLSGG 166
Cdd:COG4559 93 E--------EVV-ALGRA---------P------HGSSAAQDRQIVRE--------ALAL-VGLAHL--AGRSYQTLSGG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 167 ERRRVALCRLLL-------EKPDMLLLDEPTNHLDaesVAW---LERFLHDF---EGTVVAITHD 218
Cdd:COG4559 138 EQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD---LAHqhaVLRLARQLarrGGGVVAVLHD 199
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-218 |
1.94e-15 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 77.84 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 31 PGAKI-GVLGLNGAGKSTLLRIMAGIDKDIEGE----------ARPQPDI-----KIGYLPQEPQLNPEHTVRESIEEAV 94
Cdd:TIGR02142 21 PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEivlngrtlfdSRKGIFLppekrRIGYVFQEARLFPHLSVRGNLRYGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 95 SEVVNALKRldevyalyadpdADFDKLAAEQGrLEEIIQahdghnlnvqleraadalRLPdwdakiANLSGGERRRVALC 174
Cdd:TIGR02142 101 KRARPSERR------------ISFERVIELLG-IGHLLG------------------RLP------GRLSGGEKQRVAIG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788209839 175 RLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD 218
Cdd:TIGR02142 144 RALLSSPRLLLMDEPLAALDdprkYEILPYLERLHAEFGIPILYVSHS 191
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
18-207 |
2.00e-15 |
|
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: 75.79 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE----------ARPQPDIKIGYLPQEPQLNPEHTVR 87
Cdd:TIGR03864 13 ARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQisvaghdlrrAPRAALARLGVVFQQPTLDLDLSVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 88 ESIEeavsevvnalkrldevY--ALYADPDAdfdkLAAEqgRLEEIiqahdghnlnvqLERAADALRLpdwDAKIANLSG 165
Cdd:TIGR03864 93 QNLR----------------YhaALHGLSRA----EARA--RIAEL------------LARLGLAERA---DDKVRELNG 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2788209839 166 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD 207
Cdd:TIGR03864 136 GHRRRVEIARALLHRPALLLLDEPTVGLDPASRAAITAHVRA 177
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-217 |
2.24e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 73.62 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEarpqpdIKIgylpqepqlnpehtvresieeavsevvn 99
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE------ILV---------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 100 alkrldevyalyadpdadfdklaaeqgrleeiiqahDGHNlnVQLERAADALRlpdwdAKIA---NLSGGERRRVALCRL 176
Cdd:cd03216 60 ------------------------------------DGKE--VSFASPRDARR-----AGIAmvyQLSVGERQMVEIARA 96
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2788209839 177 LLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITH 217
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIFISH 140
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-217 |
2.33e-15 |
|
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: 74.84 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPdikigylpqepqlNPEHTVRESIEEAVSEV- 97
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG-------------GPLDFQRDSIARGLLYLg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 98 -VNALKRldevyALYADPDADFdkLAAEQGRlEEIIQAHDGHNLNvQLEraadalrlpdwDAKIANLSGGERRRVALCRL 176
Cdd:cd03231 80 hAPGIKT-----TLSVLENLRF--WHADHSD-EQVEEALARVGLN-GFE-----------DRPVAQLSAGQQRRVALARL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2788209839 177 LLEKPDMLLLDEPTNHLDAESVAWLERFLHDF---EGTVVAITH 217
Cdd:cd03231 140 LLSGRPLWILDEPTTALDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-236 |
2.61e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.57 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE--------------ARPqpdikIGYLPQEPQLNPEH 84
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQimldgvdlshvppyQRP-----INMMFQSYALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 TVRESIeeavsevVNALKRldevyalyadpdadfDKLAAEQ--GRLEEIIQAhdghnlnVQLERAADalRLPDwdakiaN 162
Cdd:PRK11607 107 TVEQNI-------AFGLKQ---------------DKLPKAEiaSRVNEMLGL-------VHMQEFAK--RKPH------Q 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------ESVAWLERflhdFEGTVVAITHDRYFLDNVAGWILELDR 234
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdrmqlEVVDILER----VGVTCVMVTHDQEEAMTMAGRIAIMNR 225
|
..
gi 2788209839 235 GE 236
Cdd:PRK11607 226 GK 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
321-476 |
2.94e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 76.18 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSYGD--RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRDS 397
Cdd:PRK13632 5 SVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 398 M-------DNS---KTVWEEVSGGLDIMKIGNTEMPSRAYvgrfnfkgvDQGKRVG----------ELSGGERGRLHLAK 457
Cdd:PRK13632 85 IgiifqnpDNQfigATVEDDIAFGLENKKVPPKKMKDIID---------DLAKKVGmedyldkepqNLSGGQKQRVAIAS 155
|
170
....*....|....*....
gi 2788209839 458 LLQVGGNMLLLDEPTNDLD 476
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLD 174
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
324-500 |
3.12e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.65 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLrkSYGDRLLidDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGqEQPDSGTITLGET----VKLASVDQFRD--- 396
Cdd:COG4138 1 LQLNDV--AVAGRLG--PISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRplsdWSAAELARHRAyls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 -------SMDnsktVWEEVSggLDIMKIGNTEMPSRAY---VGRFNFKgvDQ-GKRVGELSGGERGRLHLAK-LLQV--- 461
Cdd:COG4138 76 qqqsppfAMP----VFQYLA--LHQPAGASSEAVEQLLaqlAEALGLE--DKlSRPLTQLSGGEWQRVRLAAvLLQVwpt 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2788209839 462 ---GGNMLLLDEPTNDLDIETLRALENALLEF--PGCAMVIS-HD 500
Cdd:COG4138 148 inpEGQLLLLDEPMNSLDVAQQAALDRLLRELcqQGITVVMSsHD 192
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
324-476 |
3.18e-15 |
|
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: 74.84 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLidDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGET-VKLASVDQFRDSM---D 399
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdVTAAPPADRPVSMlfqE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 400 NSK----TVWEEV----SGGLDIMKIGNTEMPSRAyvGRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLLDEP 471
Cdd:cd03298 79 NNLfahlTVEQNVglglSPGLKLTAEDRQAIEVAL--ARVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDEP 155
|
....*
gi 2788209839 472 TNDLD 476
Cdd:cd03298 156 FAALD 160
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-252 |
3.36e-15 |
|
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: 74.95 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID-KDIEGEARPQPDIKIGYLPQEPQLNPEhT 85
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfydpqkgqilIDgIDIRDISRKSLRSMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIeeavsevvnalkrldevyaLYADPDADFD---KLAAEQGRLEEIIQAHDGHNLNVQlERAAdalrlpdwdakiaN 162
Cdd:cd03254 93 IMENI-------------------RLGRPNATDEeviEAAKEAGAHDFIMKLPNGYDTVLG-ENGG-------------N 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD-FEG-TVVAITHDRYFLDNvAGWILELDRGEgIPW 240
Cdd:cd03254 140 LSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKlMKGrTSIIIAHRLSTIKN-ADKILVLDDGK-IIE 217
|
250
....*....|..
gi 2788209839 241 EGNYSSWLEQKD 252
Cdd:cd03254 218 EGTHDELLAKKG 229
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
21-219 |
3.50e-15 |
|
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: 74.70 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE------------ARPQPD---IKIGYLPQEPQLNPEHT 85
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEvlfngqslsklsSNERAKlrnKKLGFIYQFHHLLPDFT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIeeavsevvnALKRLDevyalyadpdADFDKLAAEQGRLEEIIQAHDGHNLNvqleraadalrlpdwdAKIANLSG 165
Cdd:TIGR02211 100 ALENV---------AMPLLI----------GKKSVKEAKERAYEMLEKVGLEHRIN----------------HRPSELSG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 166 GERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDFEGT-VVAITHDR 219
Cdd:TIGR02211 145 GERQRVAIARALVNQPSLVLADEPTGNLDnnnAKIIFDLMLELNRELNTsFLVVTHDL 202
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-218 |
3.53e-15 |
|
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: 75.06 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARpqpdiKIGYLPQEPQlnPEHTVRESIEEAVSE----- 96
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR-----VAGLVPWKRR--KKFLRRIGVVFGQKTqlwwd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 97 --VVNALKRLDEVYALyadPDADFDKlaaeqgRLEEIiqahdghnlnvqleraADALRL-PDWDAKIANLSGGERRRVAL 173
Cdd:cd03267 110 lpVIDSFYLLAAIYDL---PPARFKK------RLDEL----------------SELLDLeELLDTPVRQLSLGQRMRAEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2788209839 174 CRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF----EGTVVAITHD 218
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHY 213
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
321-477 |
4.08e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.59 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVkLASVdqfrdsmdN 400
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQP-LESW--------S 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 401 SKTVWEEV---------SGGL---DIMKIGntEMPSRAYVGRFnfkGVDQGKRVGE-----------------LSGGERG 451
Cdd:PRK10575 80 SKAFARKVaylpqqlpaAEGMtvrELVAIG--RYPWHGALGRF---GAADREKVEEaislvglkplahrlvdsLSGGERQ 154
|
170 180
....*....|....*....|....*.
gi 2788209839 452 RLHLAKLLQVGGNMLLLDEPTNDLDI 477
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
289-523 |
4.45e-15 |
|
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: 77.87 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 289 ARLA--RFEELnSTEYQKRNETNELfipPGPRlGDkvLEVSNL--RKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKST 364
Cdd:COG4618 301 ARQAyrRLNEL-LAAVPAEPERMPL---PRPK-GR--LSVENLtvVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKST 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 365 LFRMISGQEQPDSGTITLGetvkLASVDQFrDSMDNSK--------------TVWEEVS--GGLDIMKI-------GNTE 421
Cdd:COG4618 374 LARLLVGVWPPTAGSVRLD----GADLSQW-DREELGRhigylpqdvelfdgTIAENIArfGDADPEKVvaaaklaGVHE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 422 MpsrayVGRFNfKGVDqgKRVGE----LSGGERGRLHLAKLLQvgGN--MLLLDEPTNDLDIETLRALENALLEF---PG 492
Cdd:COG4618 449 M-----ILRLP-DGYD--TRIGEggarLSGGQRQRIGLARALY--GDprLVVLDEPNSNLDDEGEAALAAAIRALkarGA 518
|
250 260 270
....*....|....*....|....*....|....
gi 2788209839 493 CAMVISHDRWFL---DRIAthILdyqDEGKVEFF 523
Cdd:COG4618 519 TVVVITHRPSLLaavDKLL--VL---RDGRVQAF 547
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
324-500 |
4.49e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.12 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQ--------- 393
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdGKPVEGPGAERgvvfqnegl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 --FRDSMDNsktvweeVSGGLDIMKIGNTEMPSRA--YVGRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLLD 469
Cdd:PRK11248 82 lpWRNVQDN-------VAFGLQLAGVEKMQRLEIAhqMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....*
gi 2788209839 470 EPTNDLDIETLRALENALL----EFPGCAMVISHD 500
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLklwqETGKQVLLITHD 188
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-477 |
5.45e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.52 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 1 MAQFVYTMHRVGKVVPPKrHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK------DIEGEARPQPDIK---- 70
Cdd:PRK09700 1 MATPYISMAGIGKSFGPV-HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEptkgtiTINNINYNKLDHKlaaq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 71 --IGYLPQEPQLNPEHTVRESIeeavsevvnALKRLdEVYALYADPDADFDKLaaeQGRLEEIIqahdghnLNVQLERaa 148
Cdd:PRK09700 80 lgIGIIYQELSVIDELTVLENL---------YIGRH-LTKKVCGVNIIDWREM---RVRAAMML-------LRVGLKV-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 149 dalrlpDWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGT-VVAITH-------- 217
Cdd:PRK09700 138 ------DLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLrkEGTaIVYISHklaeirri 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 218 -DRYfldnvagwileldrgeGIPWEGNYSSwleqkdQRLAQEASQEAARRKSIEKELEwvrqgtkgrqskgkarlARFEE 296
Cdd:PRK09700 212 cDRY----------------TVMKDGSSVC------SGMVSDVSNDDIVRLMVGRELQ-----------------NRFNA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 297 LNSTEYQKRNETnelfippgprlgdkVLEVSNLRKSygDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPD 376
Cdd:PRK09700 253 MKENVSNLAHET--------------VFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 377 SGTITL-GETVKLAS-VDQFRDSM--------DN--------------SKTVWEEVSGGLdiMKIGNTEMPSR---AYVG 429
Cdd:PRK09700 317 GGEIRLnGKDISPRSpLDAVKKGMayitesrrDNgffpnfsiaqnmaiSRSLKDGGYKGA--MGLFHEVDEQRtaeNQRE 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2788209839 430 RFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDI 477
Cdd:PRK09700 395 LLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-224 |
5.53e-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: 73.12 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEArpqpdikigylpqepQLN--PEHTVRESIEEAVSeV 97
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------------TLDgvPVSDLEKALSSLIS-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 98 VNalkrlDEVYaLYADPDADfdklaaeqgrleeiiqahdghNLNVQLeraadalrlpdwdakianlSGGERRRVALCRLL 177
Cdd:cd03247 80 LN-----QRPY-LFDTTLRN---------------------NLGRRF-------------------SGGERQRLALARIL 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 178 LEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITH--------DR-YFLDN 224
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVlkDKTLIWITHhltgiehmDKiLFLEN 171
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
321-476 |
5.81e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.22 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSYGD--RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISG----QEQPDSGTITLGETVKLASVDQF 394
Cdd:PRK13640 3 DNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpDDNPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 395 RDSM-------DNS---KTVWEEVSGGLDIMKIGNTEMPS-----RAYVGRFNFkgvdQGKRVGELSGGERGRLHLAKLL 459
Cdd:PRK13640 83 REKVgivfqnpDNQfvgATVGDDVAFGLENRAVPRPEMIKivrdvLADVGMLDY----IDSEPANLSGGQKQRVAIAGIL 158
|
170
....*....|....*..
gi 2788209839 460 QVGGNMLLLDEPTNDLD 476
Cdd:PRK13640 159 AVEPKIIILDESTSMLD 175
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
323-500 |
6.48e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.11 E-value: 6.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGD-RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVK-----LASVDQ-- 393
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIKydkksLLEVRKtv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 ---FRDSMDN--SKTVWEEVSGGLDIMKIGNTEMPSRAyvgrfnfkgVDQGKRVG----------ELSGGERGRLHLAKL 458
Cdd:PRK13639 81 givFQNPDDQlfAPTVEEDVAFGPLNLGLSKEEVEKRV---------KEALKAVGmegfenkpphHLSGGQKKRVAIAGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2788209839 459 LQVGGNMLLLDEPTNDLDIETLRALENALLEF--PGCAMVIS-HD 500
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGITIIIStHD 196
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-226 |
8.83e-15 |
|
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: 75.47 E-value: 8.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKD---IEGEAR---------PQPDI------KIGYLPQEPQ-- 79
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILfdgedllklSEKELrkirgrEIQMIFQDPMts 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 80 LNPEHTVRESIEEAvsevvnalkrldevyalyadpdadfdklaaeqgrleeiIQAHDGHNLNVQLERAADALR---LPDw 156
Cdd:COG0444 99 LNPVMTVGDQIAEP--------------------------------------LRIHGGLSKAEARERAIELLErvgLPD- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 157 DAKIAN-----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD----RYFLD 223
Cdd:COG0444 140 PERRLDrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqAQILNLLKDLQRELGLAILFITHDlgvvAEIAD 219
|
...
gi 2788209839 224 NVA 226
Cdd:COG0444 220 RVA 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-217 |
1.00e-14 |
|
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: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKST----LLR---------IMAGID-KDIEGEARPQpdiKIGYLPQEPQLNp 82
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTvvslLERfydptsgeiLLDGVDiRDLNLRWLRS---QIGLVSQEPVLF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 83 EHTVRESIeeavsevvnalkrldevyaLYADPDADfdklaaeqgrLEEIIQAhdghnlnvqlERAADALR----LPD-WD 157
Cdd:cd03249 90 DGTIAENI-------------------RYGKPDAT----------DEEVEEA----------AKKANIHDfimsLPDgYD 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 158 ----AKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF-EG-TVVAITH 217
Cdd:cd03249 131 tlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAmKGrTTIVIAH 196
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
313-490 |
1.10e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.45 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 313 IPPGPRLGDkVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQE--QPDSGTItlgetvklas 390
Cdd:COG2401 21 LDLSERVAI-VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 391 vdqfrDSMDNskTVWEEVSGGLDIMKIGNT----EMPSRA-YVGRFNFKgvdqgKRVGELSGGERGRLHLAKLLQVGGNM 465
Cdd:COG2401 90 -----DVPDN--QFGREASLIDAIGRKGDFkdavELLNAVgLSDAVLWL-----RRFKELSTGQKFRFRLALLLAERPKL 157
|
170 180
....*....|....*....|....*
gi 2788209839 466 LLLDEPTNDLDIETLRALENALLEF 490
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKL 182
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-203 |
1.14e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.25 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE----ARPQPD------IKIGYLPQEPQLNPEHTVREsi 90
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlGVPVPArarlarARIGVVPQFDNLDLEFTVRE-- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 91 eeavsevvNALkrldeVYALYadpdadFDKLAAEqgrLEEIIQAHdghnLN-VQLERAAdalrlpdwDAKIANLSGGERR 169
Cdd:PRK13536 134 --------NLL-----VFGRY------FGMSTRE---IEAVIPSL----LEfARLESKA--------DARVSDLSGGMKR 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 2788209839 170 RVALCRLLLEKPDMLLLDEPTNHLD--AESVAWlER 203
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDphARHLIW-ER 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
20-236 |
1.36e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 73.49 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---IDK---DIEGE--ARPQPDI-----KIGYLPQEPQLNPEHTV 86
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLleePDSgtiTVDGEdlTDSKKDInklrrKVGMVFQQFNLFPHLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 87 RESIEEAVsevVNALKRldevyalyadpdadfDKLAAEqgrleeiiqahdghnlnvqlERAADALR---LPD-WDAKIAN 162
Cdd:COG1126 95 LENVTLAP---IKVKKM---------------SKAEAE--------------------ERAMELLErvgLADkADAYPAQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788209839 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLakEGmTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-235 |
1.63e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 73.12 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGIDKDIEGEARPQpDI-----KIGYLPQEPQLNP 82
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprsgtlniAGNHFDFSKTPSDK-AIrelrrNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 83 EHTVRESIEEAVSEVvnalkrldevyalyadpdADFDKLAAEQgRLEEIIQahdghnlNVQLERAADALRLpdwdakiaN 162
Cdd:PRK11124 96 HLTVQQNLIEAPCRV------------------LGLSKDQALA-RAEKLLE-------RLRLKPYADRFPL--------H 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGT---VVAITHDRYFLDNVAGWILELDRG 235
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgitQVIVTHEVEVARKTASRVVYMENG 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
328-500 |
1.76e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.22 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 328 NLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQfRDSMDnsktvwee 407
Cdd:PRK09544 9 NVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ-KLYLD-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 408 vsggldimkignTEMPsrAYVGRF-----NFKGVDQG---KRVG----------ELSGGERGRLHLAKLLQVGGNMLLLD 469
Cdd:PRK09544 80 ------------TTLP--LTVNRFlrlrpGTKKEDILpalKRVQaghlidapmqKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190
....*....|....*....|....*....|....*
gi 2788209839 470 EPTNDLDIE---TLRALENALLEFPGCA-MVISHD 500
Cdd:PRK09544 146 EPTQGVDVNgqvALYDLIDQLRRELDCAvLMVSHD 180
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
16-205 |
1.78e-14 |
|
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: 72.79 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHI--LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK------DIEG-EARPQP---DIKIGYLPQEPQLNPE 83
Cdd:cd03266 13 DVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEpdagfaTVDGfDVVKEPaeaRRRLGFVSDSTGLYDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 84 HTVRESIEeavsevvnalkrldevyaLYADpdadfdklaaeqgrleeiIQAHDGHNLNVQLERAADALRLPDW-DAKIAN 162
Cdd:cd03266 93 LTARENLE------------------YFAG------------------LYGLKGDELTARLEELADRLGMEELlDRRVGG 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2788209839 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL 205
Cdd:cd03266 137 FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI 179
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-195 |
1.95e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.24 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLL-----RIMAGIDKD----IEGEARPQPDIKI--GYLPQEPQLNPEHT 85
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKGSgsvlLNGMPIDAKEMRAisAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIeeavseVVNALKRLDEVYALyadpdadfdklAAEQGRLEEIIQAhdghnlnVQLERAADAL-RLPDwdaKIANLS 164
Cdd:TIGR00955 116 VREHL------MFQAHLRMPRRVTK-----------KEKRERVDEVLQA-------LGLRKCANTRiGVPG---RVKGLS 168
|
170 180 190
....*....|....*....|....*....|.
gi 2788209839 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDA 195
Cdd:TIGR00955 169 GGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
324-500 |
1.96e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.56 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGeTVKLASVDQ-----FRDS- 397
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-TAPLAEAREdtrlmFQDAr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 398 MDNSKTVWEEVSGGLDimkiGNTEMPSR---AYVGRFNfkgvdqgkRVGE----LSGGERGRLHLAKLLQVGGNMLLLDE 470
Cdd:PRK11247 92 LLPWKKVIDNVGLGLK----GQWRDAALqalAAVGLAD--------RANEwpaaLSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190
....*....|....*....|....*....|....
gi 2788209839 471 PTNDLD----IETLRALENALLEFPGCAMVISHD 500
Cdd:PRK11247 160 PLGALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-218 |
2.10e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.28 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEA--RPQP---------DIKIGYLPQepQLNPEH- 84
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIllDAQPleswsskafARKVAYLPQ--QLPAAEg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 -TVRESIEEAVSEVVNALKRLDevyalyadpdadfdklAAEQGRLEEIIQAhdghnlnVQLERAADalRLPDwdakiaNL 163
Cdd:PRK10575 100 mTVRELVAIGRYPWHGALGRFG----------------AADREKVEEAISL-------VGLKPLAH--RLVD------SL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD 218
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHRLSQERGLTVIAVLHD 207
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-218 |
2.54e-14 |
|
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: 72.65 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDIKIGYLPQEPQLNpehTVRESieeavsevvn 99
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVN---TVFQN---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 100 alkrldevYALYadPDAD-FDKLA---AEQGRLEEIIQahdghnlnvqlERAADALRLPDWDA----KIANLSGGERRRV 171
Cdd:cd03300 81 --------YALF--PHLTvFENIAfglRLKKLPKAEIK-----------ERVAEALDLVQLEGyanrKPSQLSGGQQQRV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 172 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLE---RFLHDFEG-TVVAITHD 218
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQlelKRLQKELGiTFVFVTHD 190
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
324-484 |
2.73e-14 |
|
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: 72.72 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGD-RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRDSMD-- 399
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdGEDIREQDPVELRRKIGyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 400 -------NSKTVWEEVSGGLDIMK-------------IGNTEMPSRAYVGRFNfkgvdqgkrvGELSGGERGRLHLAKLL 459
Cdd:cd03295 81 iqqiglfPHMTVEENIALVPKLLKwpkekireradelLALVGLDPAEFADRYP----------HELSGGQQQRVGVARAL 150
|
170 180
....*....|....*....|....*
gi 2788209839 460 QVGGNMLLLDEPTNDLDIETLRALE 484
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQ 175
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-477 |
3.17e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.33 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 9 HRVGKVVPPKRhILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE----ARPQ----------PDIKIGYl 74
Cdd:PRK11288 8 DGIGKTFPGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSilidGQEMrfasttaalaAGVAIIY- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 75 pQEPQLNPEHTVRESIeeavsevvnALKRLDEVYALyadpdADFDKLAAEQGRleeiiqahdghnlnvQLERAADALrlp 154
Cdd:PRK11288 86 -QELHLVPEMTVAENL---------YLGQLPHKGGI-----VNRRLLNYEARE---------------QLEHLGVDI--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 155 DWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVA-ITH--DRYFLDNVAGWI 229
Cdd:PRK11288 133 DPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELraEGRVILyVSHrmEEIFALCDAITV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 230 LeldrgegipwegnysswleqKDQRLAQEASQEAA-RRKSIEKELewvrqgtKGRqskgkarlarfeELNSTeYQKRnet 308
Cdd:PRK11288 213 F--------------------KDGRYVATFDDMAQvDRDQLVQAM-------VGR------------EIGDI-YGYR--- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 309 nelfippgPR-LGDKVLEVSNLRksyGDRLLiDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETV 386
Cdd:PRK11288 250 --------PRpLGEVRLRLDGLK---GPGLR-EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKPI 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 387 KLASV-DQFRDSM-----DNSK-------TVWEEVS---------GGLDIMKIGNTEMPSRaYVGRFNFKGVDQGKRVGE 444
Cdd:PRK11288 318 DIRSPrDAIRAGImlcpeDRKAegiipvhSVADNINisarrhhlrAGCLINNRWEAENADR-FIRSLNIKTPSREQLIMN 396
|
490 500 510
....*....|....*....|....*....|...
gi 2788209839 445 LSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDI 477
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
320-500 |
3.44e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.88 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 320 GDKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRDSM 398
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIPAMSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 DNSKTVWEevSGGL--DIMKIGNTEMPSRAY------------------VGrfnFKGVDQGKRvGELSGGERGRLHLAKL 458
Cdd:PRK11831 84 KRMSMLFQ--SGALftDMNVFDNVAYPLREHtqlpapllhstvmmkleaVG---LRGAAKLMP-SELSGGMARRAALARA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2788209839 459 LQVGGNMLLLDEPTNDLDIETLRALENALLEFPGC----AMVISHD 500
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlgvtCVVVSHD 203
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-241 |
3.64e-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 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: 72.85 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE--------ARPQ--PDI--KIGYLPQepqlNPEH- 84
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKvtvdgldtLDEEnlWEIrkKVGMVFQ----NPDNq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 ----TVRESI-----------EEAVSEVVNALKRldevyalyadpdadfdklaaeqgrleeiiqahdghnlnVQLERAAD 149
Cdd:TIGR04520 90 fvgaTVEDDVafglenlgvprEEMRKRVDEALKL--------------------------------------VGMEDFRD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 150 alRLPdwdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLERFLHDFEG-TVVAITHDryfLDNV 225
Cdd:TIGR04520 132 --REP------HLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGrkeVLETIRKLNKEEGiTVISITHD---MEEA 200
|
250 260
....*....|....*....|..
gi 2788209839 226 --AGWILELDRG----EGIPWE 241
Cdd:TIGR04520 201 vlADRVIVMNKGkivaEGTPRE 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
321-508 |
4.46e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 72.84 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSYG---DRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRD 396
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 SM-------DNS---KTVWEEVSGGLDIMKIGNTEMPSR-----AYVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQV 461
Cdd:PRK13650 82 KIgmvfqnpDNQfvgATVEDDVAFGLENKGIPHEEMKERvnealELVGMQDFK----EREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 462 GGNMLLLDEPTNDLD----IETLRALENALLEFPGCAMVISHDrwfLDRIA 508
Cdd:PRK13650 158 RPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
323-476 |
4.96e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.67 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRDSMDNS 401
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 402 --------KTVWEEVSGGLDIMKIGNTEMPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTN 473
Cdd:PRK10247 87 aqtptlfgDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
...
gi 2788209839 474 DLD 476
Cdd:PRK10247 167 ALD 169
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-476 |
5.01e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.74 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKS-TLLRIMAGIDKdiEGEARPQPDI---------------------KIGYLPQ 76
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPS--PPVVYPSGDIrfhgesllhaseqtlrgvrgnKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 77 EP--QLNPEHTVResieeavsevvnalKRLDEVYALYADpdadfdkLAAEQGRlEEIIQAHDghnlNVQLERAADalRLP 154
Cdd:PRK15134 100 EPmvSLNPLHTLE--------------KQLYEVLSLHRG-------MRREAAR-GEILNCLD----RVGIRQAAK--RLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 155 DWDAKianLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG----TVVAITHD----RYFLDNVA 226
Cdd:PRK15134 152 DYPHQ---LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNlsivRKLADRVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 227 gwILELDRGegipwegnysswLEQKDQRLAQEASQEAARRKSIEKELEwvrqgtkgrqskGKArlarfeelnsteyqkrn 306
Cdd:PRK15134 229 --VMQNGRC------------VEQNRAATLFSAPTHPYTQKLLNSEPS------------GDP----------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 307 etnelfiPPGPRLGDKVLEVSNLRKSY-----------GDRLLIDDLSFSIPKGAIVGIIGPNGAGKST----LFRMISG 371
Cdd:PRK15134 266 -------VPLPEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 372 QeqpdsGTITL-GETVKLASVDQ-----------FRD---SMDNSKTVWEEVSGGLDI-MKIGNTEMPSRAYVGRFNFKG 435
Cdd:PRK15134 339 Q-----GEIWFdGQPLHNLNRRQllpvrhriqvvFQDpnsSLNPRLNVLQIIEEGLRVhQPTLSAAQREQQVIAVMEEVG 413
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2788209839 436 VDQGKR---VGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:PRK15134 414 LDPETRhryPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
324-383 |
5.08e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 72.43 E-value: 5.08e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 324 LEVSNLRKSYG-----DRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG 383
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID 66
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-511 |
6.40e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 71.69 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGET----------VKL-- 388
Cdd:COG4674 8 GPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTdltgldeheiARLgi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 389 ------ASVdqFRD---------SMDNSKTVWEEVSGGL---------DIMK-IGNTEmpsrayvgrfnfkgvDQGKRVG 443
Cdd:COG4674 88 grkfqkPTV--FEEltvfenlelALKGDRGVFASLFARLtaeerdrieEVLEtIGLTD---------------KADRLAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 444 ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDL-DIETLR--ALENALLEfpGCA-MVISHDRWFLDRIATHI 511
Cdd:COG4674 151 LLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMtDAETERtaELLKSLAG--KHSvVVVEHDMEFVRQIARKV 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-490 |
6.52e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 70.15 E-value: 6.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 320 GDKVLEVSNLRKSYGdrllIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRD-- 396
Cdd:cd03215 1 GEPVLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVTRRSPRDAIRag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 ----SMDNSKTvweevsGGLDIMKIG-NTEMPSRayvgrfnfkgvdqgkrvgeLSGGERGRLHLAKLLQVGGNMLLLDEP 471
Cdd:cd03215 77 iayvPEDRKRE------GLVLDLSVAeNIALSSL-------------------LSGGNQQKVVLARWLARDPRVLILDEP 131
|
170
....*....|....*....
gi 2788209839 472 TNDLDIETLRALENALLEF 490
Cdd:cd03215 132 TRGVDVGAKAEIYRLIREL 150
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
328-521 |
6.89e-14 |
|
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: 73.22 E-value: 6.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 328 NLRKSYGDRLLidDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVkLASVDQFRDSMDNSKT---V 404
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRT-LFDSRKGIFLPPEKRRigyV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 405 WEE--------VSGGLdimKIGNTEmpSRAYVGRFNFKGVDQ--------GKRVGELSGGERGRLHLAKLLQVGGNMLLL 468
Cdd:TIGR02142 81 FQEarlfphlsVRGNL---RYGMKR--ARPSERRISFERVIEllgighllGRLPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2788209839 469 DEPTNDLDI----ETLRALENALLEFPGCAMVISHDRWFLDRIATHILDYQDeGKVE 521
Cdd:TIGR02142 156 DEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED-GRVA 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
321-500 |
7.08e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.08 E-value: 7.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSY--GDRLLiDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTIT-LGETV----------K 387
Cdd:PRK13647 2 DNIIEVEDLHFRYkdGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvMGREVnaenekwvrsK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 388 LASVDQFRDSMDNSKTVWEEVSGGLDIMKIGNTEMPSRA-----YVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVG 462
Cdd:PRK13647 81 VGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVeealkAVRMWDFR----DKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2788209839 463 GNMLLLDEPTNDLD---IETLRALENALLEFPGCAMVISHD 500
Cdd:PRK13647 157 PDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
335-520 |
7.17e-14 |
|
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: 70.96 E-value: 7.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 335 DRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETV----------KLASVDQfrDSMDNSKT 403
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdGKPIsqyehkylhsKVSLVGQ--EPVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 404 VWEEVSGGL---DIMKIgnTEMPSRAYVGRFNFK-----GVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDL 475
Cdd:cd03248 104 LQDNIAYGLqscSFECV--KEAAQKAHAHSFISElasgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2788209839 476 DIETLRALENALLEFPG--CAMVISHDRWFLDRiATHILdYQDEGKV 520
Cdd:cd03248 182 DAESEQQVQQALYDWPErrTVLVIAHRLSTVER-ADQIL-VLDGGRI 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
21-217 |
7.23e-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: 70.77 E-value: 7.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR-------PQPDIKIGYLPQEPQLNPEHTVRE----- 88
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldIAARNRIGYLPEERGLYPKMKVIDqlvyl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 89 ------SIEEAVSEVVNALKRLDevyalyadpdadfdklaaeqgrleeiIQAHdghnlnvqleraadalrlpdWDAKIAN 162
Cdd:cd03269 95 aqlkglKKEEARRRIDEWLERLE--------------------------LSEY--------------------ANKRVEE 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG---TVVAITH 217
Cdd:cd03269 129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTH 186
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
325-489 |
7.84e-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: 71.10 E-value: 7.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 325 EVSNLRKSY-GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL----GETVKLAS-------VD 392
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgidIRDISRKSlrsmigvVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 393 Q----FRDS-MDN--------SKTVWEEVS---GGLD-IMKIGNtempsrayvgrfnfkGVDQ--GKRVGELSGGERGRL 453
Cdd:cd03254 84 QdtflFSGTiMENirlgrpnaTDEEVIEAAkeaGAHDfIMKLPN---------------GYDTvlGENGGNLSQGERQLL 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 2788209839 454 HLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLE 489
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEK 184
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
324-513 |
7.94e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.09 E-value: 7.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDR--LLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRDSM-- 398
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLnGQPIADYSEAALRQAIsv 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 -------------DNSK------------TVWEEVsgGLDimKIGNTEMPSRAYVGrfnfkgvdQGKRvgELSGGERGRL 453
Cdd:PRK11160 419 vsqrvhlfsatlrDNLLlaapnasdealiEVLQQV--GLE--KLLEDDKGLNAWLG--------EGGR--QLSGGEQRRL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788209839 454 HLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEFpgCA----MVISHDRWFL---DRIatHILD 513
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH--AQnktvLMITHRLTGLeqfDRI--CVMD 547
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
288-488 |
8.56e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 74.39 E-value: 8.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 288 KARLA--RFEE--LNSTEYQKRNETNELFIPpgprLGDkvLEVSNLRKSYG-DRLLIDDLSFSIPKGAIVGIIGPNGAGK 362
Cdd:TIGR01193 440 AARVAnnRLNEvyLVDSEFINKKKRTELNNL----NGD--IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGK 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 363 STLFRMISGQEQPDSGTITLGETvKLASVD--QFRDS---------------MDN------SKTVWEEVSGGLDIMKI-G 418
Cdd:TIGR01193 514 STLAKLLVGFFQARSGEILLNGF-SLKDIDrhTLRQFinylpqepyifsgsiLENlllgakENVSQDEIWAACEIAEIkD 592
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 419 NTEMPSRAYVGRFNFKGvdqgkrvGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALL 488
Cdd:TIGR01193 593 DIENMPLGYQTELSEEG-------SSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLL 655
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-251 |
8.57e-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: 71.11 E-value: 8.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GID-KDIE-GEARPQpdikIGYLPQEPQLNPEhT 85
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPrfydvdsgrilidGHDvRDYTlASLRRQ----IGLVSQDVFLFND-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIeeavsevvnalkrldevyaLYADPDADfdklaaeqgrLEEIIQAhdghnlnvqlERAADAL----RLPD-WDAKI 160
Cdd:cd03251 92 VAENI-------------------AYGRPGAT----------REEVEEA----------ARAANAHefimELPEgYDTVI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 161 A----NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDfeGTVVAITHDRYFLDNvAGWILEL 232
Cdd:cd03251 133 GergvKLSGGQRQRIAIARALLKDPPILILDEATSALDTESerlvQAALERLMKN--RTTFVIAHRLSTIEN-ADRIVVL 209
|
250
....*....|....*....
gi 2788209839 233 DRGEgIPWEGNYSSWLEQK 251
Cdd:cd03251 210 EDGK-IVERGTHEELLAQG 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-490 |
8.58e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 71.48 E-value: 8.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRM------------ISGQEQPDSGTITLGETVKLAS 390
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 391 VDQFRDSMDN---SKTVWEEVSGGLDIMKIGNT--EMPSRAYVGRFNFKGVDQGKR-----VGELSGGERGRLHLAKLLQ 460
Cdd:PRK14247 83 RVQMVFQIPNpipNLSIFENVALGLKLNRLVKSkkELQERVRWALEKAQLWDEVKDrldapAGKLSGGQQQRLCIARALA 162
|
170 180 190
....*....|....*....|....*....|
gi 2788209839 461 VGGNMLLLDEPTNDLDIETLRALENALLEF 490
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLEL 192
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-257 |
8.67e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.09 E-value: 8.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAgidkdiegeaRpqpdikiGYLPQEPQ--LN-------PEHTVRESI 90
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT----------R-------AWDPQQGEilLNgqpiadySEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 91 EeavseVVNalKRLDeVYA-------LYADPDADFDKLAA--EQGRLEEIIQAHDGhnLNVQLeraADALRLpdwdakia 161
Cdd:PRK11160 417 S-----VVS--QRVH-LFSatlrdnlLLAAPNASDEALIEvlQQVGLEKLLEDDKG--LNAWL---GEGGRQ-------- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 162 nLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawlER----FLHDF--EGTVVAITHDRYFLDNVAGWILeLDRG 235
Cdd:PRK11160 476 -LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET----ERqileLLAEHaqNKTVLMITHRLTGLEQFDRICV-MDNG 549
|
250 260
....*....|....*....|..
gi 2788209839 236 EGIPwEGNYSSwLEQKDQRLAQ 257
Cdd:PRK11160 550 QIIE-QGTHQE-LLAQQGRYYQ 569
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
324-500 |
8.89e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 8.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLrkSYGDRLLidDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQeQPDSGTITLG----ETVKLASVDQFRD--- 396
Cdd:PRK03695 1 MQLNDV--AVSTRLG--PLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAgqplEAWSAAELARHRAyls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 -------SMDnsktVWEEVSggLDIMKIGNTEMPSRA--YVGRFnFKGVDQ-GKRVGELSGGERGRLHLAK-LLQV---- 461
Cdd:PRK03695 76 qqqtppfAMP----VFQYLT--LHQPDKTRTEAVASAlnEVAEA-LGLDDKlGRSVNQLSGGEWQRVRLAAvVLQVwpdi 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2788209839 462 --GGNMLLLDEPTNDLDIETLRALENALLEFP--GCAMVIS-HD 500
Cdd:PRK03695 149 npAGQLLLLDEPMNSLDVAQQAALDRLLSELCqqGIAVVMSsHD 192
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
325-482 |
9.20e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 72.53 E-value: 9.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 325 EVSNLRKSY--GDRLLI--DDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG--ETVKLASVD--QFRD 396
Cdd:PRK11153 3 ELKNISKVFpqGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDgqDLTALSEKElrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 SMD---------NSKTVWEEVSGGLDIMKIGNTEMPSR-----AYVGRfnfkgVDQGKRV-GELSGGERGRLHLAKLLQV 461
Cdd:PRK11153 83 QIGmifqhfnllSSRTVFDNVALPLELAGTPKAEIKARvtellELVGL-----SDKADRYpAQLSGGQKQRVAIARALAS 157
|
170 180
....*....|....*....|.
gi 2788209839 462 GGNMLLLDEPTNDLDIETLRA 482
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRS 178
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-194 |
9.99e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.77 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 26 SLSFFPGAKIGVLGLNGAGKSTLLRIMAGI------DKDIEGE--------ARPqpdikIGYLPQEPQLNPEHTVRESIe 91
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFltpasgSLTLNGQdhtttppsRRP-----VSMLFQENNLFSHLTVAQNI- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 92 eavsevvnalkrldevyALYADPDAdfdKLAAEQ-GRLEEIIQahdghnlNVQLEraaDAL-RLPdwdakiANLSGGERR 169
Cdd:PRK10771 93 -----------------GLGLNPGL---KLNAAQrEKLHAIAR-------QMGIE---DLLaRLP------GQLSGGQRQ 136
|
170 180
....*....|....*....|....*
gi 2788209839 170 RVALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:PRK10771 137 RVALARCLVREQPILLLDEPFSALD 161
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-472 |
1.13e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.01 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 9 HRVGKVVPpkrhiLKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-----------IDKDIeGEARPQPDI--KIGYLP 75
Cdd:NF033858 9 HRYGKTVA-----LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarkiqqgrvevLGGDM-ADARHRRAVcpRIAYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 76 QE--PQLNPEHTVRESIEeavsevvnALKRLdevyalyadpdadFDKLAAE-QGRLEEIIQAHDghnLNVQLERAAdalr 152
Cdd:NF033858 83 QGlgKNLYPTLSVFENLD--------FFGRL-------------FGQDAAErRRRIDELLRATG---LAPFADRPA---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 153 lpdwdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA--W--LERFLHDFEG-TVVAITHdryFLDNVAG 227
Cdd:NF033858 135 --------GKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRqfWelIDRIRAERPGmSVLVATA---YMEEAER 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 228 --WILELDRGegipwegnysswleqkdQRLAQEASQEaarrksiekelewVRQGTkGRQSKGKARLARFEElnsteyQKR 305
Cdd:NF033858 204 fdWLVAMDAG-----------------RVLATGTPAE-------------LLART-GADTLEAAFIALLPE------EKR 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 306 NETNELFIPPGPRLGDK--VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL- 382
Cdd:NF033858 247 RGHQPVVIPPRPADDDDepAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLf 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 383 GETVKlasvdqfRDSMDNSKTV---------WEE--VSGGLD----IMKIGNTEMPSR--AYVGRFNFKGVdQGKRVGEL 445
Cdd:NF033858 327 GQPVD-------AGDIATRRRVgymsqafslYGEltVRQNLElharLFHLPAAEIAARvaEMLERFDLADV-ADALPDSL 398
|
490 500
....*....|....*....|....*..
gi 2788209839 446 SGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:NF033858 399 PLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
324-487 |
1.16e-13 |
|
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: 70.72 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGD--RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRDSMDN 400
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 401 --------SKTVWEEVSGG---------LDIMKIGN-----TEMPsrayvgrfnfKGVDQ--GKRVGELSGGERGRLHLA 456
Cdd:cd03251 81 vsqdvflfNDTVAENIAYGrpgatreevEEAARAANahefiMELP----------EGYDTviGERGVKLSGGQRQRIAIA 150
|
170 180 190
....*....|....*....|....*....|.
gi 2788209839 457 KLLQVGGNMLLLDEPTNDLDIETLRALENAL 487
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAAL 181
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
339-500 |
1.17e-13 |
|
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: 70.57 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQ---FRD-SMDNSKTVWEEVSGGLD 413
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQITEPGPDRmvvFQNySLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 414 IMKIGNTEMPSRAYVgRFNFKGVD----QGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLE 489
Cdd:TIGR01184 81 RVLPDLSKSERRAIV-EEHIALVGlteaADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170
....*....|....*.
gi 2788209839 490 F-----PGCAMViSHD 500
Cdd:TIGR01184 160 IweehrVTVLMV-THD 174
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-218 |
1.21e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.02 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdKDIEGEA----RPQPDIKI-------GYLPQ--EPQLN------- 81
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEIllngRPLSDWSAaelarhrAYLSQqqSPPFAmpvfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 82 ----PEHTVRESIEEAVSEVVNALKrLDevyalyadpdadfDKLaaeqgrleeiiqahdGHNLNvqleraadalrlpdwd 157
Cdd:COG4138 91 alhqPAGASSEAVEQLLAQLAEALG-LE-------------DKL---------------SRPLT---------------- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 158 akiaNLSGGERRRVALCRLLLE-----KPD--MLLLDEPTNHLD-AESVA---WLERFlHDFEGTVVAITHD 218
Cdd:COG4138 126 ----QLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPMNSLDvAQQAAldrLLREL-CQQGITVVMSSHD 192
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
321-522 |
1.26e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 73.30 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLR-KSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKL----------- 388
Cdd:COG4178 360 DGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVlflpqrpylpl 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 389 ----------ASVDQFRDsmDNSKTVWEEVsgGLDimkigntempsrAYVGRFnfkgvDQGKRVG-ELSGGERGRLHLAK 457
Cdd:COG4178 440 gtlreallypATAEAFSD--AELREALEAV--GLG------------HLAERL-----DEEADWDqVLSLGEQQRLAFAR 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788209839 458 LLQVGGNMLLLDEPTNDLDIETLRALENALL-EFPGCAMV-ISHdRWFLDRIATHILDYQDEGKVEF 522
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQLLReELPGTTVIsVGH-RSTLAAFHDRVLELTGDGSWQL 564
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-197 |
1.30e-13 |
|
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: 73.70 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---ID-KDIegearpqPDIK-------IGYLPQEP 78
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfrfydvtSGrilIDgQDI-------RDVTqaslraaIGIVPQDT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 79 QL-NpeHTVRESIeeavsevvnalkrldevyaLYADPDADFDKL--AAEQGRLEEIIQahdghnlnvqleraadalRLPD 155
Cdd:COG5265 442 VLfN--DTIAYNI-------------------AYGRPDASEEEVeaAARAAQIHDFIE------------------SLPD 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2788209839 156 -WDAKIA----NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 197
Cdd:COG5265 483 gYDTRVGerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
323-516 |
1.37e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.59 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVK--LASVDQ------ 393
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKkdLCTYQKqlcfvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 FRDSMDNSKTVWEEV-------SGGLDImkignTEMPSRAYVGRF-NFKgvdqgkrVGELSGGERGRLHLAKLLQVGGNM 465
Cdd:PRK13540 81 HRSGINPYLTLRENClydihfsPGAVGI-----TELCRLFSLEHLiDYP-------CGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 466 LLLDEPTNDLD---IETLRALENALLEFPGCAMVISHDRWFLDRIathilDYQD 516
Cdd:PRK13540 149 WLLDEPLVALDelsLLTIITKIQEHRAKGGAVLLTSHQDLPLNKA-----DYEE 197
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
324-483 |
1.37e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.93 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLAS---------VDQF 394
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 395 RD---------SMDNSKTVWEEVSGGLDIMK---IGNTEMPSRAYVGRFNFKGVDQG--KRvgeLSGGERGRLHLAKLLQ 460
Cdd:PRK11264 84 RQhvgfvfqnfNLFPHRTVLENIIEGPVIVKgepKEEATARARELLAKVGLAGKETSypRR---LSGGQQQRVAIARALA 160
|
170 180 190
....*....|....*....|....*....|
gi 2788209839 461 VGGNMLLLDEPTNDLDIE-------TLRAL 483
Cdd:PRK11264 161 MRPEVILFDEPTSALDPElvgevlnTIRQL 190
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
323-476 |
1.42e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.69 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG-ETVKLASVDQF------- 394
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdEDISLLPLHARarrgigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 395 ---RDSMDNSKTVWEEVSGGLDIMKIGNTEM-PSRAYVGRFNFKGVDQGKRVGE-LSGGERGRLHLAKLLQVGGNMLLLD 469
Cdd:PRK10895 83 lpqEASIFRRLSVYDNLMAVLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQsLSGGERRRVEIARALAANPKFILLD 162
|
....*..
gi 2788209839 470 EPTNDLD 476
Cdd:PRK10895 163 EPFAGVD 169
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-251 |
1.48e-13 |
|
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: 70.94 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DKDI---EGEARPQPDIKIGYLPQepqlNPEH 84
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLlkptsgtvtidGRDItakKKKKLKDLRKKVGLVFQ----FPEH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 -----TVRESIEEA-----VSEvvnalkrldevyalyadpdadfdklaaeqgrlEEIiqahdghnlnvqLERAADALRLP 154
Cdd:TIGR04521 94 qlfeeTVYKDIAFGpknlgLSE--------------------------------EEA------------EERVKEALELV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 155 DWDAKIA-----NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES-VAWLERF--LHDFEG-TVVAITHDryfLDNV 225
Cdd:TIGR04521 130 GLDEEYLerspfELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGrKEILDLFkrLHKEKGlTVILVTHS---MEDV 206
|
250 260 270
....*....|....*....|....*....|....
gi 2788209839 226 AGW---ILELDRG----EGIPWE-GNYSSWLEQK 251
Cdd:TIGR04521 207 AEYadrVIVMHKGkivlDGTPREvFSDVDELEKI 240
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-236 |
1.89e-13 |
|
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: 69.83 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKST----LLRIMAG------ID-KDIEGEARPQPDIKIGYLPQEPQLNpEHTVRES 89
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVELssgsilIDgVDISKIGLHDLRSRISIIPQDPVLF-SGTIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 90 I----EEAVSEVVNALKRLdevyalyadpdadfdklaaeqgRLEEIIQAHDGHNlnvqleraadalrlpdwDAKIA---- 161
Cdd:cd03244 98 LdpfgEYSDEELWQALERV----------------------GLKEFVESLPGGL-----------------DTVVEegge 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITH--------DRyfldnvagwILE 231
Cdd:cd03244 139 NLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAHrldtiidsDR---------ILV 209
|
....*
gi 2788209839 232 LDRGE 236
Cdd:cd03244 210 LDKGR 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-236 |
2.22e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.60 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEA--RPQPDIKigylpqepqlnpeHTVREsIEEAVSE 96
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVliRGEPITK-------------ENIRE-VRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 97 VVNALKrlDEVYALYADPDADFDKLaaEQGRLEEIIqAHdghnlnvQLERAADALRLPDWDAKIAN-LSGGERRRVALCR 175
Cdd:PRK13652 83 VFQNPD--DQIFSPTVEQDIAFGPI--NLGLDEETV-AH-------RVSSALHMLGLEELRDRVPHhLSGGEKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 176 LLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG----TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDKGR 215
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
324-532 |
2.58e-13 |
|
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: 69.60 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQE--QPDSGTITLGETVKLA------------ 389
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPsyEVTSGTILFKGQDLLElepderaraglf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 390 ------------SVDQFRDSMDNSKTVwEEVSGGLDIM---KIGNTEMPSRAYVGRFNFKGVDQGkrvgeLSGGERGRLH 454
Cdd:TIGR01978 81 lafqypeeipgvSNLEFLRSALNARRS-ARGEEPLDLLdfeKLLKEKLALLDMDEEFLNRSVNEG-----FSGGEKKRNE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 455 LAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEF--PGCAM-VISHDRWFLDRIA---THILdyqDEGKVeFFEGNFT 528
Cdd:TIGR01978 155 ILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrePDRSFlIITHYQRLLNYIKpdyVHVL---LDGRI-VKSGDVE 230
|
....
gi 2788209839 529 EYEE 532
Cdd:TIGR01978 231 LAKE 234
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
324-499 |
2.89e-13 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 72.44 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYG--DRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG----ETVKLAS------- 390
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghdlADYTLASlrrqval 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 391 VDQfrDSMDNSKTVWEEVSGGlDIMKIGNTEMPS---RAYVGRF---NFKGVDQ--GKRVGELSGGERGRLHLAKLLQVG 462
Cdd:TIGR02203 411 VSQ--DVVLFNDTIANNIAYG-RTEQADRAEIERalaAAYAQDFvdkLPLGLDTpiGENGVLLSGGQRQRLAIARALLKD 487
|
170 180 190
....*....|....*....|....*....|....*....
gi 2788209839 463 GNMLLLDEPTNDLDIETLRALENALLEF-PG-CAMVISH 499
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLmQGrTTLVIAH 526
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
324-520 |
2.90e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.02 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETV-KLASVDQFRD----- 396
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIqHYASKEVARRiglla 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 ---SMDNSKTVWEEVSGGldimKIGNTEMPSR-------AYVGRFNFKGVDQ--GKRVGELSGGERGRLHLAKLLQVGGN 464
Cdd:PRK10253 88 qnaTTPGDITVQELVARG----RYPHQPLFTRwrkedeeAVTKAMQATGITHlaDQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 465 MLLLDEPTNDLDIE---TLRALENALLEFPGCAM-VISHDRWFLDRIATHILDYQDeGKV 520
Cdd:PRK10253 164 IMLLDEPTTWLDIShqiDLLELLSELNREKGYTLaAVLHDLNQACRYASHLIALRE-GKI 222
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
324-512 |
2.95e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 69.71 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQE--QPDSGTITL-GETVKLASVDQ------- 393
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLdGEDILELSPDEraragif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 ----------------FRDSMDNSKTvwEEVSGGLDIMKIGNTEMP----SRAYVGRfnfkGVDQGkrvgeLSGGERGRL 453
Cdd:COG0396 81 lafqypveipgvsvsnFLRTALNARR--GEELSAREFLKLLKEKMKelglDEDFLDR----YVNEG-----FSGGEKKRN 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 454 HLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEF--PGCAM-VISHDRWFLDRIA---THIL 512
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrsPDRGIlIITHYQRILDYIKpdfVHVL 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-218 |
3.09e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.42 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 2 AQFVYTMHRVGKVVPPKRH---ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR--PQPDIKIGYlPQ 76
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlvGQPLHQMDE-EA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 77 EPQLNPEHT--VRESIeeAVSEVVNALKRLDEVYALYADPDADFDKLAAEqgrleeiiqahdghnLNVQLERAADALRLP 154
Cdd:PRK10584 82 RAKLRAKHVgfVFQSF--MLIPTLNALENVELPALLRGESSRQSRNGAKA---------------LLEQLGLGKRLDHLP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 155 dwdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL----HDFEGTVVAITHD 218
Cdd:PRK10584 145 ------AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-64 |
3.76e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.34 E-value: 3.76e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR 64
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-218 |
3.98e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.07 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEA--RPQP-------------DIKIGYLPQEPQLNPEHT 85
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifNGQPmsklssaakaelrNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIeeAVSEVVNALKRldevyalyadpdadfdklAAEQGRLEEIIQAhdghnlnVQLERAADAlrlpdwdaKIANLSG 165
Cdd:PRK11629 104 ALENV--AMPLLIGKKKP------------------AEINSRALEMLAA-------VGLEHRANH--------RPSELSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2788209839 166 GERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDFEGTV-VAITHD 218
Cdd:PRK11629 149 GERQRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTAfLVVTHD 205
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
324-488 |
4.76e-13 |
|
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: 71.62 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSY-GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGEtVKLASVDQ--------- 393
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG-VPVSSLDQdevrrrvsv 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 -------FRDSMDNSKTVW------EEVSGGLDIMKIGNtemPSRAYVGRFNFKGVDQGKRvgeLSGGERGRLHLAKLLQ 460
Cdd:TIGR02868 414 caqdahlFDTTVRENLRLArpdatdEELWAALERVGLAD---WLRALPDGLDTVLGEGGAR---LSGGERQRLALARALL 487
|
170 180
....*....|....*....|....*...
gi 2788209839 461 VGGNMLLLDEPTNDLDIETLRALENALL 488
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLL 515
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
339-381 |
4.89e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.12 E-value: 4.89e-13
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2788209839 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTIT 381
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
317-483 |
5.20e-13 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 68.45 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 317 PRLGDKVLEVSNLRKSygdRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPD---SGTITL-GETVK----- 387
Cdd:cd03234 4 LPWWDVGLKAKNWNKY---ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFnGQPRKpdqfq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 388 --LASVDQFrDSMDNSKTVWEEVSGGLdIMKIGNtEMPSRAYVGRFNFKGVDQ-------GKRVGELSGGERGRLHLAKL 458
Cdd:cd03234 81 kcVAYVRQD-DILLPGLTVRETLTYTA-ILRLPR-KSSDAIRKKRVEDVLLRDlaltrigGNLVKGISGGERRRVSIAVQ 157
|
170 180 190
....*....|....*....|....*....|..
gi 2788209839 459 LQVGGNMLLLDEPTNDLD-------IETLRAL 483
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDsftalnlVSTLSQL 189
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-190 |
5.84e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.20 E-value: 5.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR----------PQPDIK--IGYLPQEPQ---LNPE 83
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvrirsPRDAIRagIAYVPEDRKgegLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 84 HTVRESIeeavseVVNALKRLdeVYALYADPdadfdklAAEQGRLEEIIQAhdghnLNVqleraadalRLPDWDAKIANL 163
Cdd:COG1129 345 LSIRENI------TLASLDRL--SRGGLLDR-------RRERALAEEYIKR-----LRI---------KTPSPEQPVGNL 395
|
170 180
....*....|....*....|....*..
gi 2788209839 164 SGGERRRVALCRLLLEKPDMLLLDEPT 190
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-508 |
6.12e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKS----TLLRIMAGIDKDIEGEA-----RPQPDIKIGYLP----------------Q 76
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKmllrrRSRQVIELSEQSaaqmrhvrgadmamifQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 77 EP--QLNPEHTVRESIEEAVsevvnalkrldevyalyadpdadfdKLAAEQGRLEEIIQAhdghnlnvqlERAADALRLP 154
Cdd:PRK10261 112 EPmtSLNPVFTVGEQIAESI-------------------------RLHQGASREEAMVEA----------KRMLDQVRIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 155 DWDAKIA----NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHDRYFLDNVA 226
Cdd:PRK10261 157 EAQTILSryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMGVIFITHDMGVVAEIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 227 GWILELDRGEGIpwEGNYSSWLEQKDQRLAQEASQEAARRKSIEKELEWVRqgtkgrqskgkarlaRFEELNSTEYQKRN 306
Cdd:PRK10261 237 DRVLVMYQGEAV--ETGSVEQIFHAPQHPYTRALLAAVPQLGAMKGLDYPR---------------RFPLISLEHPAKQE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 307 ETNE--LFIPpgprlGDKVLEVSNL------RKSYGDRL-----LIDDLSFSIPKGAIVGIIGPNGAGKST----LFRMI 369
Cdd:PRK10261 300 PPIEqdTVVD-----GEPILQVRNLvtrfplRSGLLNRVtrevhAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 370 SGQEqpdsGTITL-GETVKLASVDQ-----------FRD---SMDNSKTVWEEVSGGLDIMKIGNTEMPSRA---YVGRF 431
Cdd:PRK10261 375 ESQG----GEIIFnGQRIDTLSPGKlqalrrdiqfiFQDpyaSLDPRQTVGDSIMEPLRVHGLLPGKAAAARvawLLERV 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 432 NFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALL----EFPGCAMVISHDRWFLDRI 507
Cdd:PRK10261 451 GLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLdlqrDFGIAYLFISHDMAVVERI 530
|
.
gi 2788209839 508 A 508
Cdd:PRK10261 531 S 531
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
323-498 |
6.65e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 69.06 E-value: 6.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSY-GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFR----- 395
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREVRkfvgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 -----DSMDNSKTVWEEVSGGLDIMKIGNTEMPSRAYVGRFNFKGVDQGKRV-GELSGGERGRLHLAKLLQVGGNMLLLD 469
Cdd:PRK13652 83 vfqnpDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVpHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190
....*....|....*....|....*....|..
gi 2788209839 470 EPTNDLDIETLRAL---ENALLEFPGCAMVIS 498
Cdd:PRK13652 163 EPTAGLDPQGVKELidfLNDLPETYGMTVIFS 194
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
341-498 |
6.67e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 341 DLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTIT-LGETVKLASVDQFRDSMDNSKTV-W------EEV---- 408
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISiLGQPTRQALQKNLVAYVPQSEEVdWsfpvlvEDVvmmg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 409 ----SGGLDIMKIGNTEMPSRAY--VGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRA 482
Cdd:PRK15056 105 ryghMGWLRRAKKRDRQIVTAALarVDMVEFR----HRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170
....*....|....*...
gi 2788209839 483 LENALLEF--PGCAMVIS 498
Cdd:PRK15056 181 IISLLRELrdEGKTMLVS 198
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
329-508 |
6.90e-13 |
|
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: 68.82 E-value: 6.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 329 LRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRD------SMDNS 401
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIdGQDIAAMSRKELRElrrkkiSMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 402 K-------TVWEEVSGGLDIMKIGNTEMPSRA-----YVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNMLLLD 469
Cdd:cd03294 110 SfallphrTVLENVAFGLEVQGVPRAEREERAaealeLVGLEGWE----HKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788209839 470 EPTNDLDIETLRALENALL----EFPGCAMVISHDrwfL-------DRIA 508
Cdd:cd03294 186 EAFSALDPLIRREMQDELLrlqaELQKTIVFITHD---LdealrlgDRIA 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-228 |
7.86e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.99 E-value: 7.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdkdiegearpqpdikigYLPQepqlnpehtvRESIEEAVSEVVN 99
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI-----------------YLPQ----------RGRVKVMGREVNA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 100 ALKRL--DEVYALYADPDAD-FDKLAAEQGRLEEIIQAHDGHNLNVQLERAADALRLPDWDAKIA-NLSGGERRRVALCR 175
Cdd:PRK13647 72 ENEKWvrSKVGLVFQDPDDQvFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPyHLSYGQKKRVAIAG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2788209839 176 LLLEKPDMLLLDEPTNHLD----AESVAWLERfLHDFEGTVVAITHDryfLDNVAGW 228
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDprgqETLMEILDR-LHNQGKTVIVATHD---VDLAAEW 204
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
334-529 |
9.43e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 70.76 E-value: 9.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 334 GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GE---TVKLASVDQ-----FRDSMDNSKTV 404
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTdirTVTRASLRRniavvFQDAGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 405 WEEVSGGldimKIGNT--EM---PSRAYVGRF---NFKGVDQ--GKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTND 474
Cdd:PRK13657 426 EDNIRVG----RPDATdeEMraaAERAQAHDFierKPDGYDTvvGERGRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 475 LDIETLRALENALlefpGCAM------VISHdRWFLDRIATHILdYQDEGK-VEffEGNFTE 529
Cdd:PRK13657 502 LDVETEAKVKAAL----DELMkgrttfIIAH-RLSTVRNADRIL-VFDNGRvVE--SGSFDE 555
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-217 |
9.49e-13 |
|
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: 70.93 E-value: 9.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 14 VVPPKRHILKNiSLSF-FP-GAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDIKIGYLPQEPQLNpEHTVRESIe 91
Cdd:TIGR00954 459 LVTPNGDVLIE-SLSFeVPsGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMT-LGTLRDQI- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 92 eavsevvnalkrldevyaLYADPDADFDKLAAEQGRLEEIIQAHDGHNLnVQLERAADALRlpDWdakIANLSGGERRRV 171
Cdd:TIGR00954 536 ------------------IYPDSSEDMKRRGLSDKDLEQILDNVQLTHI-LEREGGWSAVQ--DW---MDVLSGGEKQRI 591
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2788209839 172 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITH 217
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-236 |
1.19e-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: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID-KDIEGEARPQPDIKIGYLPQEPQLNpEH 84
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRfyvpengrvlVDgHDLALADPAWLRRQVGVVLQENVLF-NR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 TVRESIeeavsevvnalkrldevyALyADPDADFDklaaeqgRLEEIIQAHDGHNLNVQLERAADALRlpdwDAKIANLS 164
Cdd:cd03252 91 SIRDNI------------------AL-ADPGMSME-------RVIEAAKLAGAHDFISELPEGYDTIV----GEQGAGLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAITHdRYFLDNVAGWILELDRGE 236
Cdd:cd03252 141 GGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAH-RLSTVKNADRIIVMEKGR 213
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
321-529 |
1.24e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 68.34 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSYGDRL-LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGET---------VKL-A 389
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglMKLrE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 390 SVDQFRDSMDN---SKTVWEEVSGGLDIMKIGNTEMPSRayVGRFNFK-GVD--QGKRVGELSGGERGRLHLAKLLQVGG 463
Cdd:PRK13636 83 SVGMVFQDPDNqlfSASVYQDVSFGAVNLKLPEDEVRKR--VDNALKRtGIEhlKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 464 NMLLLDEPTNDLD---IETLRALENALLEFPGCAMVishdrwfldrIATHILD----------YQDEGKVeFFEGNFTE 529
Cdd:PRK13636 161 KVLVLDEPTAGLDpmgVSEIMKLLVEMQKELGLTII----------IATHDIDivplycdnvfVMKEGRV-ILQGNPKE 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
323-483 |
1.29e-12 |
|
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: 66.81 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRK------SYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQ--EQPDSGTITL-GETVKLAS--- 390
Cdd:cd03213 3 TLSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLInGRPLDKRSfrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 391 ----VDQfRDSMDNSKTVWE--EVSGGLdimkigntempsrayvgrfnfKGvdqgkrvgeLSGGERGRLHLAKLLQVGGN 464
Cdd:cd03213 83 iigyVPQ-DDILHPTLTVREtlMFAAKL---------------------RG---------LSGGERKRVSIALELVSNPS 131
|
170 180
....*....|....*....|....*.
gi 2788209839 465 MLLLDEPTNDLD-------IETLRAL 483
Cdd:cd03213 132 LLFLDEPTSGLDsssalqvMSLLRRL 157
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
324-487 |
1.61e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSY-GDRLLiDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVdqfRDSMDN- 400
Cdd:PRK11288 5 LSFDGIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMRFAST---TAALAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 401 ------------SKTVWEEVSGGldimkigntEMPSRA---------YVGRFNFKG----VDQGKRVGELSGGERGRLHL 455
Cdd:PRK11288 81 vaiiyqelhlvpEMTVAENLYLG---------QLPHKGgivnrrllnYEAREQLEHlgvdIDPDTPLKYLSIGQRQMVEI 151
|
170 180 190
....*....|....*....|....*....|....*
gi 2788209839 456 AKLLQVGGNMLLLDEPTNDL---DIETLRALENAL 487
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLsarEIEQLFRVIREL 186
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-238 |
1.81e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.56 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLR-----IMAGIDKDIEGEARP------QPDI-------KIGYLPQEPQLN 81
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLfgrniySPDVdpievrrEVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 82 PEHTVRESIEEAVSevvnalkrldevyalyadpdadFDKLAAEQGRLEEIIQAhdghnlnvQLERAA--DAL--RLPDWD 157
Cdd:PRK14267 98 PHLTIYDNVAIGVK----------------------LNGLVKSKKELDERVEW--------ALKKAAlwDEVkdRLNDYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 158 AkiaNLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:PRK14267 148 S---NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTHSPAQAARVSDYVAFLYLG 224
|
...
gi 2788209839 236 EGI 238
Cdd:PRK14267 225 KLI 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
322-499 |
1.92e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.43 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 322 KVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGE------TVKLA-----S 390
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynklDHKLAaqlgiG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 391 VDQFRDSMDNSKTVWEEVS-GGLDIMK------IGNTEMPSRAYV--GRFNFKgVDQGKRVGELSGGERGRLHLAKLLQV 461
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYiGRHLTKKvcgvniIDWREMRVRAAMmlLRVGLK-VDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2788209839 462 GGNMLLLDEPTNDL---DIETLRALENALLEfPGCAMV-ISH 499
Cdd:PRK09700 163 DAKVIIMDEPTSSLtnkEVDYLFLIMNQLRK-EGTAIVyISH 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
328-500 |
2.19e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.52 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 328 NLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGetvklasvDQFRDSMDNSK----- 402
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--------EKRMNDVPPAErgvgm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 403 -----------TVWEEVSGGLDIMKIGNTEMPSRayvgrfnfkgVDQGKRV-----------GELSGGERGRLHLAKLLQ 460
Cdd:PRK11000 80 vfqsyalyphlSVAENMSFGLKLAGAKKEEINQR----------VNQVAEVlqlahlldrkpKALSGGQRQRVAIGRTLV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2788209839 461 VGGNMLLLDEPTNDLD--------IETLRaLENALlefpGCAMV-ISHD 500
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDaalrvqmrIEISR-LHKRL----GRTMIyVTHD 193
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
21-218 |
2.22e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 67.03 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-IDKDiEGEAR---------PQPDI--KIGYLPQEPQLNPEHTVRe 88
Cdd:COG4604 16 VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRlLPPD-SGEVLvdgldvattPSRELakRLAILRQENHINSRLTVR- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 89 sieEAVSevvnalkrldevyalyadpdadFDKLAAEQGRLEEIIQAHdghnlnvqLERAADALRLPDW-DAKIANLSGGE 167
Cdd:COG4604 94 ---ELVA----------------------FGRFPYSKGRLTAEDREI--------IDEAIAYLDLEDLaDRYLDELSGGQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 168 RRRVALCRLLLEKPDMLLLDEPTNHLD-AESVAW---LERFLHDFEGTVVAITHD 218
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDmKHSVQMmklLRRLADELGKTVVIVLHD 195
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
230-297 |
2.67e-12 |
|
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: 62.59 E-value: 2.67e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 230 LELDRGEGIPWEGNYSSWLEQKDQRLAQEASQEAARRKSIEKELEWVRQ----GTKGRQSKGKA-RLARFEEL 297
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRfrakASKAKQAQSRIkALEKMERI 73
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-241 |
2.73e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 67.35 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdkdiegeARPQP-DIKIGYLPqepqLNPEhTVREsIEEAVSE 96
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL-------LLPEAgTITVGGMV----LSEE-TVWD-VRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 97 VvnalkrldevyalYADPDADF------DKLAAEqgrLEEIIQAHDghnlnVQLERAADALRL----PDWDAKIANLSGG 166
Cdd:PRK13635 86 V-------------FQNPDNQFvgatvqDDVAFG---LENIGVPRE-----EMVERVDQALRQvgmeDFLNREPHRLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHDFEG-TVVAITHDryfLDNVAGW--ILELDRG----E 236
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPrgrREVLETVRQLKEQKGiTVLSITHD---LDEAAQAdrVIVMNKGeileE 221
|
....*
gi 2788209839 237 GIPWE 241
Cdd:PRK13635 222 GTPEE 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-90 |
3.14e-12 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 66.02 E-value: 3.14e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK----DIEGEARPQPDIKIGYlpqepQLNPEHTVRESI 90
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpdsgTVTVRGRVSSLLGLGG-----GFNPELTGRENI 105
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-246 |
3.29e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.10 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK-----DIEGEARPQPDIK-----IGYLPQEPQLnPEHTVRESI 90
Cdd:PRK11174 365 LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslKINGIELRELDPEswrkhLSWVGQNPQL-PHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 91 eeavsevvnalkrldevyaLYADPDADFDKL--AAEQGRLEEIIQAHDgHNLNVQL-ERAAdalrlpdwdakiaNLSGGE 167
Cdd:PRK11174 444 -------------------LLGNPDASDEQLqqALENAWVSEFLPLLP-QGLDTPIgDQAA-------------GLSVGQ 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD--FEGTVVAITHDryfLDNVAGW--ILELDRGEgIPWEGN 243
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAasRRQTTLMVTHQ---LEDLAQWdqIWVMQDGQ-IVQQGD 566
|
...
gi 2788209839 244 YSS 246
Cdd:PRK11174 567 YAE 569
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
323-507 |
3.80e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.99 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGD-RLLID---DLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTI--------TLGETVK--- 387
Cdd:PRK11629 5 LLQCDNLCKRYQEgSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsKLSSAAKael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 388 ----LASVDQFRDSMDNSkTVWEEVSGGLDIMKIGNTEMPSRAyvgRFNFKGVDQGKRV----GELSGGERGRLHLAKLL 459
Cdd:PRK11629 85 rnqkLGFIYQFHHLLPDF-TALENVAMPLLIGKKKPAEINSRA---LEMLAAVGLEHRAnhrpSELSGGERQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 460 QVGGNMLLLDEPTNDLDIETLRALENALLEF---PGCA-MVISHDRWFLDRI 507
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELnrlQGTAfLVVTHDLQLAKRM 212
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-477 |
3.88e-12 |
|
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: 68.70 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI------DKDI--EGEARPQPDIK------IGYLPQEPQLNPEHTVR 87
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwDGEIywSGSPLKASNIRdteragIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 88 ESIEEAvsevvnalkrldevyalyadpdadfDKLAAEQGRLEEIIQAHDGHNLNVQLERAADALRLPdwdakIANLSGGE 167
Cdd:TIGR02633 97 ENIFLG-------------------------NEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRP-----VGDYGGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVagwileldrgegipwegnyssw 247
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEV---------------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 248 leqkdqrlaqeasqeaarrKSIEKELEWVRQGtkgrQSKGKARLARFEELNSTEYQKRNETNELFiPPGPR-LGDKVLEV 326
Cdd:TIGR02633 205 -------------------KAVCDTICVIRDG----QHVATKDMSTMSEDDIITMMVGREITSLY-PHEPHeIGDVILEA 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 327 SNLRKSYGD---RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISG-------------QEQPDSGTITLGETVKLAS 390
Cdd:TIGR02633 261 RNLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvfinGKPVDIRNPAQAIRAGIAM 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 391 V--DQFRDSMDNSKTVWEEVS-------GGLDIMKIGNTEMPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQV 461
Cdd:TIGR02633 341 VpeDRKRHGIVPILGVGKNITlsvlksfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLT 420
|
490
....*....|....*.
gi 2788209839 462 GGNMLLLDEPTNDLDI 477
Cdd:TIGR02633 421 NPRVLILDEPTRGVDV 436
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
324-520 |
4.02e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.19 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTIT-------LGETVKLASVDQFRD 396
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdFSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 S--MDNSK-------TVWEE-VSGGLDIMKIGNTEMPSRA-----------YVGRFNFkgvdqgkrvgELSGGERGRLHL 455
Cdd:PRK11124 83 NvgMVFQQynlwphlTVQQNlIEAPCRVLGLSKDQALARAekllerlrlkpYADRFPL----------HLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 456 AKLLQVGGNMLLLDEPTNDLDIETLRALENALLEFPGCAM---VISHDRWFLDRIATHILdYQDEGKV 520
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVEVARKTASRVV-YMENGHI 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-217 |
4.16e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.98 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE----ARPQPDI-------KIGYLPQEPQLNpEHT 85
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQvlldGVPLVQYdhhylhrQVALVGQEPVLF-SGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIeeavsevvnalkrldeVYALYADPDADFDKLAAEQGRLEEIIQAHDGHNLNVqleraadalrlpdwDAKIANLSG 165
Cdd:TIGR00958 571 VRENI----------------AYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEV--------------GEKGSQLSG 620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 166 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITH 217
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
336-483 |
5.04e-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: 65.97 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 336 RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTItLGETVKLASVDQ----------FRDSMDNSKTVW 405
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-LVDGHDLALADPawlrrqvgvvLQENVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 406 EEVSggldimkIGNTEMPSRAYV------GRFNF-----KGVDQ--GKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:cd03252 94 DNIA-------LADPGMSMERVIeaaklaGAHDFiselpEGYDTivGEQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170
....*....|.
gi 2788209839 473 NDLDIETLRAL 483
Cdd:cd03252 167 SALDYESEHAI 177
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
324-520 |
5.96e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 65.80 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG-------ETVKLASVDQFRD 396
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAghqfdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 S----------------MDNSktvweeVSGGLDIMKIGNTEMPSRA-----------YVGRFNFkgvdqgkrvgELSGGE 449
Cdd:COG4161 83 KvgmvfqqynlwphltvMENL------IEAPCKVLGLSKEQAREKAmkllarlrltdKADRFPL----------HLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 450 RGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEFPGCAM---VISHDRWFLDRIATHILdYQDEGKV 520
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVV-YMEKGRI 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-228 |
6.80e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.65 E-value: 6.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEarpqpdIKIGYLPQEPQlnpehTVRESIEEAVSEVVNAL 101
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGT------IEWIFKDEKNK-----KKTKEKEKVLEKLVIQK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 102 KRLDEV------------------YALYadpdadfdklaaEQGRLEEII--QAHDGHNLNVQLERAADALRLPDWDAKIA 161
Cdd:PRK13651 92 TRFKKIkkikeirrrvgvvfqfaeYQLF------------EQTIEKDIIfgPVSMGVSKEEAKKRAAKYIELVGLDESYL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 162 -----NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA-WLERF--LHDFEGTVVAITHDryfLDNVAGW 228
Cdd:PRK13651 160 qrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKeILEIFdnLNKQGKTIILVTHD---LDNVLEW 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
322-384 |
6.85e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 65.78 E-value: 6.85e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 322 KVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGE 384
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG 66
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
341-485 |
6.87e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.30 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 341 DLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETV---------------KLASVDQFRDSMDNSKTVW 405
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkeikpvrkKVGVVFQFPESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 406 EEVSGGLDIMKIGNTEMPSRAyVGRFNFKGVDQ---GKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD----IE 478
Cdd:PRK13643 104 KDVAFGPQNFGIPKEKAEKIA-AEKLEMVGLADefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDpkarIE 182
|
....*..
gi 2788209839 479 TLRALEN 485
Cdd:PRK13643 183 MMQLFES 189
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
321-509 |
6.93e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 66.27 E-value: 6.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSY---GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETV---------- 386
Cdd:PRK13642 2 NKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLtaenvwnlrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 387 KLASVDQFRDSMDNSKTVWEEVSGGLDIMKIGNTEMPSRAYVGRFNFKGVD-QGKRVGELSGGERGRLHLAKLLQVGGNM 465
Cdd:PRK13642 82 KIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDfKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788209839 466 LLLDEPTNDLD----IETLRALENALLEFPGCAMVISHDrwfLDRIAT 509
Cdd:PRK13642 162 IILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD---LDEAAS 206
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-477 |
7.02e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.65 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 1 MAQFVYTMHRVGKVVPPKRhILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI------DKDI--EGEARPQPDIK-- 70
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyEGEIifEGEELQASNIRdt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 71 ----IGYLPQEPQLNPEHTVRESIEEAVSEVVNALKRLDEVYalyadpdADFDKLaaeqgrLEEIiqahdghNLNVqler 146
Cdd:PRK13549 80 eragIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMY-------LRAQKL------LAQL-------KLDI---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 147 aadalrlpDWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVA---ITHDryfLD 223
Cdd:PRK13549 136 --------NPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIAciyISHK---LN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 224 NV---AGWILELDRGEGIpwegnysswleqkDQRLAQEASQEAARRKSIEKELewvrqgtkgrqskgkarlarfeelnst 300
Cdd:PRK13549 205 EVkaiSDTICVIRDGRHI-------------GTRPAAGMTEDDIITMMVGREL--------------------------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 301 eyqkrnetNELFiPPGPR-LGDKVLEVSNL---RKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPD 376
Cdd:PRK13549 245 --------TALY-PREPHtIGEVILEVRNLtawDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGR 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 377 S-GTITL-GETVKLASVdqfRDSMDNSKTVWEE---VSGGLDIMKIG-NTEMPS-------------------RAYVGRF 431
Cdd:PRK13549 316 WeGEIFIdGKPVKIRNP---QQAIAQGIAMVPEdrkRDGIVPVMGVGkNITLAAldrftggsriddaaelktiLESIQRL 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2788209839 432 NFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDI 477
Cdd:PRK13549 393 KVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
336-476 |
7.24e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 66.20 E-value: 7.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 336 RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETV---------------KLASVDQFRDSMDN 400
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkplrkKVGIVFQFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 401 SKTVWEEVSGGldIMKIGNTEMPSRAyvgrfnfKGVDQGKRVG-----------ELSGGERGRLHLAKLLQVGGNMLLLD 469
Cdd:PRK13634 100 EETVEKDICFG--PMNFGVSEEDAKQ-------KAREMIELVGlpeellarspfELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
....*..
gi 2788209839 470 EPTNDLD 476
Cdd:PRK13634 171 EPTAGLD 177
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-218 |
7.98e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 66.65 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR-----PQPDiKIGYLP-------QEPQLNPEHTVRES 89
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvPFKR-RKEFARrigvvfgQRSQLWWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 90 ieeavsevvnaLKRLDEVYALyadPDADFDKlaaeqgRLEEIIQAHD-GHNLNVQLeRaadalrlpdwdakiaNLSGGER 168
Cdd:COG4586 117 -----------FRLLKAIYRI---PDAEYKK------RLDELVELLDlGELLDTPV-R---------------QLSLGQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 169 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD----FEGTVVAITHD 218
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynreRGTTILLTSHD 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
323-487 |
8.41e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.80 E-value: 8.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFR----MISGQEQPDSGTITLGETVKLAS-------- 390
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRTVQREGrlardirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 391 --------VDQFrdSMDNSKTVWEEV-SGGLDIMKIGNT-------EMPSRAY-----VGRFNFKgvdqGKRVGELSGGE 449
Cdd:PRK09984 84 srantgyiFQQF--NLVNRLSVLENVlIGALGSTPFWRTcfswftrEQKQRALqaltrVGMVHFA----HQRVSTLSGGQ 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 2788209839 450 RGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENAL 487
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTL 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
324-499 |
9.79e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.52 E-value: 9.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQ--PDSGTI--------------------- 380
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 381 ---TLGETVKLASVDQFrdsmDNSKTVWEEVSGGLDIM------------KIGNT--EMPSRAYVGRFN-------FKGV 436
Cdd:TIGR03269 81 pcpVCGGTLEPEEVDFW----NLSDKLRRRIRKRIAIMlqrtfalygddtVLDNVleALEEIGYEGKEAvgravdlIEMV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 437 DQGKRVG----ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEF---PGCAMVI-SH 499
Cdd:TIGR03269 157 QLSHRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkaSGISMVLtSH 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-239 |
9.99e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.38 E-value: 9.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGearpqpdiKIGYLPQEPQLnpehtVRES---IEEAVSEV 97
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEG--------SIVVNGQTINL-----VRDKdgqLKVADKNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 98 VNALK-RLDEVYALYadpdadfdKLAAEQGRLEEIIQAHD---GHNLNVQLERAADALRLPDWDAKI-----ANLSGGER 168
Cdd:PRK10619 87 LRLLRtRLTMVFQHF--------NLWSHMTVLENVMEAPIqvlGLSKQEARERAVKYLAKVGIDERAqgkypVHLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 169 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFLDNVAGWILELDRG----EGIP 239
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaeEGkTMVVVTHEMGFARHVSSHVIFLHQGkieeEGAP 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-223 |
1.00e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGidkdiegEARPQPDIKIGYLPQEpQLNPEHTVRESIeeavsev 97
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-------ALKGTPVAGCVDVPDN-QFGREASLIDAI------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 98 vnalkrldevyALYADPDADFDKLAAeqgrleeiiqahdghnlnVQLeraADAlrlPDWDAKIANLSGGERRRVALCRLL 177
Cdd:COG2401 107 -----------GRKGDFKDAVELLNA------------------VGL---SDA---VLWLRRFKELSTGQKFRFRLALLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788209839 178 LEKPDMLLLDEPTNHLD---AESVAW-LERFLHDFEGTVVAITHDRYFLD 223
Cdd:COG2401 152 AERPKLLVIDEFCSHLDrqtAKRVARnLQKLARRAGITLVVATHHYDVID 201
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-490 |
1.08e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.25 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGEtVKLASVDQFRDSMDNSK- 402
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGE-VRLFGRNIYSPDVDPIEv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 403 -----------------TVWEEVSGGLDIMKI--GNTEMPSRAyvgRFNFKGVDQGKRV--------GELSGGERGRLHL 455
Cdd:PRK14267 84 rrevgmvfqypnpfphlTIYDNVAIGVKLNGLvkSKKELDERV---EWALKKAALWDEVkdrlndypSNLSGGQRQRLVI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 2788209839 456 AKLLQVGGNMLLLDEPTNDLDIETLRALENALLEF 490
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL 195
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-242 |
1.17e-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: 64.44 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 26 SLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE---------ARPQPDIKIGYLPQEPQLNPEHTVRESIEEAVSE 96
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRvlingvdvtAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 97 VVnalkRLDEVyalyadpdadfdklaaEQGRLEEIIQahdghnlnvQLERAADALRLPDwdakiaNLSGGERRRVALCRL 176
Cdd:cd03298 98 GL----KLTAE----------------DRQAIEVALA---------RVGLAGLEKRLPG------ELSGGERQRVALARV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 177 LLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEgIPWEG 242
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR-IAAQG 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
335-485 |
1.24e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 67.44 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 335 DRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETV----------KLASVDQFRDSMdnSKT 403
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLdGVPLvqydhhylhrQVALVGQEPVLF--SGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 404 VWEEVSGGLDIM---KIGNTEMPSRA--YVGRFNfKGVDQ--GKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:TIGR00958 571 VRENIAYGLTDTpdeEIMAAAKAANAhdFIMEFP-NGYDTevGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
....*....
gi 2788209839 477 IETLRALEN 485
Cdd:TIGR00958 650 AECEQLLQE 658
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-218 |
1.25e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGidkDIEGEARPQPDIKIGylpqEPQLNPEHTVRESIEEavsevv 98
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG---DLTGGGAPRGARVTG----DVTLNGEPLAAIDAPR------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 99 naLKRLDEVYALYADPDADF--DKLAAeQGRLEEIIQA-----HDGHNLNVQLERA-ADALRLPDwdakIANLSGGERRR 170
Cdd:PRK13547 81 --LARLRAVLPQAAQPAFAFsaREIVL-LGRYPHARRAgalthRDGEIAWQALALAgATALVGRD----VTTLSGGELAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 171 VALCRLLLE---------KPDMLLLDEPTNHLD-------AESVAWLERflhDFEGTVVAITHD 218
Cdd:PRK13547 154 VQFARVLAQlwpphdaaqPPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVHD 214
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
339-522 |
1.37e-11 |
|
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: 63.11 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMI---SGQEQPDSGTITLGETvKLASVDQFRDSMDNsktvweevsgGLDIM 415
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGlyaSGKARLISFLPKFSRN-KLIFIDQLQFLIDV----------GLGYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 416 KIGNtEMPSrayvgrfnfkgvdqgkrvgeLSGGERGRLHLAKLLQVG--GNMLLLDEPTNDLDIETLRALENALLEFPGC 493
Cdd:cd03238 80 TLGQ-KLST--------------------LSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLLEVIKGLIDL 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 2788209839 494 A---MVISHDRWFLDRiATHILDY-----QDEGKVEF 522
Cdd:cd03238 139 GntvILIEHNLDVLSS-ADWIIDFgpgsgKSGGKVVF 174
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
323-383 |
1.77e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.07 E-value: 1.77e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTIT-LG 383
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLG 62
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-219 |
1.83e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.51 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 10 RVGKVVppkrhILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE-----------ARPQPDIKIGYlpQEP 78
Cdd:PRK11432 15 RFGSNT-----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQifidgedvthrSIQQRDICMVF--QSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 79 QLNPEHTVRESIEeavsevvnalkrldevYALyadpdadfdKLaaeQGRLEEIIQahdghnlnvqlERAADALRLPDW-- 156
Cdd:PRK11432 88 ALFPHMSLGENVG----------------YGL---------KM---LGVPKEERK-----------QRVKEALELVDLag 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 157 --DAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAEsvawLERFLHD--------FEGTVVAITHDR 219
Cdd:PRK11432 129 feDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN----LRRSMREkirelqqqFNITSLYVTHDQ 197
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-236 |
2.16e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.44 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGearpqpDIKIGylpqepqlnpehtvresiEEAVSEVVN 99
Cdd:PRK11000 17 VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG------DLFIG------------------EKRMNDVPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 100 ALKRLDEV---YALY-----ADPDADFDKLAAEQGRleEIIQahdghnlnvQLERAADALRLPDW-DAKIANLSGGERRR 170
Cdd:PRK11000 73 AERGVGMVfqsYALYphlsvAENMSFGLKLAGAKKE--EINQ---------RVNQVAEVLQLAHLlDRKPKALSGGQRQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 171 VALCRLLLEKPDMLLLDEPTNHLDAE-------SVAWLERFLhdfEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSNLDAAlrvqmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-217 |
2.22e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.28 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 37 VLGLNGAGKSTLLRIMAGIDKDIEGEAR---------------PQPDIKIGYLPQEPQLNPEHTVRESIEeavsevvnal 101
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVlngrvlfdaekgiclPPEKRRIGYVFQDARLFPHYKVRGNLR---------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 102 krldevYALYADPDADFDKLAaeqgRLEEIiqahdGHNLNvqleraadalRLPdwdakiANLSGGERRRVALCRLLLEKP 181
Cdd:PRK11144 99 ------YGMAKSMVAQFDKIV----ALLGI-----EPLLD----------RYP------GSLSGGEKQRVAIGRALLTAP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2788209839 182 DMLLLDEPTNHLDA----ESVAWLERFLHDFEGTVVAITH 217
Cdd:PRK11144 148 ELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSH 187
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-218 |
2.56e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.34 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID-KDIEGearpQPDIK----IGYLPQEPQLN-- 81
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGslppdsgsilIDgKDVTK----LPEYKrakyIGRVFQDPMMGta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 82 PEHTVREsieeavsevvN---ALKR----------LDEVYALYADpdadfdklaaeqgRLEEiiqahdghnLNVQLERaa 148
Cdd:COG1101 95 PSMTIEE----------NlalAYRRgkrrglrrglTKKRRELFRE-------------LLAT---------LGLGLEN-- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 149 dalRLpdwDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWL-ERFLHDFEGTVVAITHD 218
Cdd:COG1101 141 ---RL---DTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktAALVLELtEKIVEENNLTTLMVTHN 208
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-229 |
2.81e-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: 63.92 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 31 PGAKIGVLGLNGAGKSTLLRIMAGidkdiegEARPQpdikIGYLPQEPQLnpehtvRESIEE-AVSEVVNALKRL--DEV 107
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAG-------KLKPN----LGKFDDPPDW------DEILDEfRGSELQNYFTKLleGDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 108 YAL----YAD--PdadfdklAAEQGRLEEIIQAHDGHNlnvQLERAADALRL-PDWDAKIANLSGGERRRVALCRLLLEK 180
Cdd:cd03236 88 KVIvkpqYVDliP-------KAVKGKVGELLKKKDERG---KLDELVDQLELrHVLDRNIDQLSGGELQRVAIAAALARD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 181 PDMLLLDEPTNHLDAE---SVAWLERFLHDFEGTVVAITHDRYFLDNVAGWI 229
Cdd:cd03236 158 ADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-218 |
2.83e-11 |
|
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: 63.86 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 10 RVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRImagIDKDIE---GE-------ARPQPDI----KIGYLP 75
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKM---INRLIEptsGEifidgedIREQDPVelrrKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 76 QEPQLNPEHTVRESIEeavseVVNALKRLDEvyalyadpdadfdklAAEQGRLEEIIQAhdghnlnVQLERAADALRLPD 155
Cdd:cd03295 82 QQIGLFPHMTVEENIA-----LVPKLLKWPK---------------EKIRERADELLAL-------VGLDPAEFADRYPH 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 156 wdakiaNLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA-------ESVAWLERFLHDfegTVVAITHD 218
Cdd:cd03295 135 ------ELSGGQQQRVGVARALAADPPLLLMDEPFGALDPitrdqlqEEFKRLQQELGK---TIVFVTHD 195
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
321-489 |
3.16e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 63.90 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFR-------MISGQEQpdSGTITL-GETVKLASVD 392
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLdGEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 393 QF----RDSM-------------DN-----------SKTV--------------WEEVSGGLDimkigntempsrayvgr 430
Cdd:COG1117 87 VVelrrRVGMvfqkpnpfpksiyDNvayglrlhgikSKSEldeiveeslrkaalWDEVKDRLK----------------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 431 fnfkgvdqgKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD-IETLRaLENALLE 489
Cdd:COG1117 150 ---------KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILE 199
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
324-520 |
4.15e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.55 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSY---------GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTIT-LGETV-KLASVD 392
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwRGEPLaKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 393 Q----------FRDS---MDNSKTVWEEVSGGL-DIMKIGNTEMPSRAyvgRFNFKGVD-----QGKRVGELSGGERGRL 453
Cdd:PRK10419 84 RkafrrdiqmvFQDSisaVNPRKTVREIIREPLrHLLSLDKAERLARA---SEMLRAVDlddsvLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 454 HLAKLLQVGGNMLLLDEPTNDLDI----ETLRALENALLEFPGCAMVISHDRWFLDRIATHILdYQDEGKV 520
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVM-VMDNGQI 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-235 |
4.95e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.58 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGearpqpdiKIGYLPQEpqlnpehtvresIEEAVSEVV 98
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAG--------KIWFSGHD------------ITRLKNREV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 99 NALKRldEVYALYADPDADFDKLAAEQGRLEEIIQAHDGHNLNVQLERAADALRLPDwdaKIAN----LSGGERRRVALC 174
Cdd:PRK10908 75 PFLRR--QIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLD---KAKNfpiqLSGGEQQRVGIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 175 RLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG---TVVAITHDRYFLDNVAGWILELDRG 235
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
339-476 |
4.97e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.53 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL------GETVKLAS-------VDQFRDSMDNSKTVW 405
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditDKKVKLSDirkkvglVFQYPEYQLFEETIE 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 406 EEVSGGLDIMKIGNTEMPSRAYVGrFNFKGVD----QGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRA-MNIVGLDyedyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-243 |
5.53e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 62.80 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 1 MAQFVYTMHRVGKVVppkrhILKNISLSFFPGAKIGVLGLNGAGKSTLLR-------------IMAGIDkdIEGEARPQP 67
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ-----VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdlIVDGLK--VNDPKVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 68 DIKI--GYLPQEPQLNPEHTVRESIEEAVSEVVNALKrldevyalyadpdADFDKLAAEqgrleeiiqahdghnLNVQLE 145
Cdd:PRK09493 74 LIRQeaGMVFQQFYLFPHLTALENVMFGPLRVRGASK-------------EEAEKQARE---------------LLAKVG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 146 RAADALRLPdwdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHDRYFL 222
Cdd:PRK09493 126 LAERAHHYP------SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLaeEGmTMVIVTHEIGFA 199
|
250 260
....*....|....*....|.
gi 2788209839 223 DNVAGWILELDRGeGIPWEGN 243
Cdd:PRK09493 200 EKVASRLIFIDKG-RIAEDGD 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
343-489 |
6.10e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.68 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 343 SFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRDSM---DNS----KTVWEEVSGGLDi 414
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDHTTTPPSRRPVSMlfqENNlfshLTVAQNIGLGLN- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 415 mkigntemPSRAYVGRFNFKGVDQGKRVG----------ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDietlRALE 484
Cdd:PRK10771 98 --------PGLKLNAAQREKLHAIARQMGiedllarlpgQLSGGQRQRVALARCLVREQPILLLDEPFSALD----PALR 165
|
....*
gi 2788209839 485 NALLE 489
Cdd:PRK10771 166 QEMLT 170
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
324-522 |
6.57e-11 |
|
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: 62.13 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGD--RLLIDDLSFSIPKGAIVGIIGPNGAGKST----LFRMIsgqeQPDSGTITLGEtVKLASVD--QFR 395
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDG-VDISKIGlhDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 DSMD-----------------------------------NSKTVWEEVSGGLDIMKIGNTEmpsrayvgrfNFkgvdqgk 440
Cdd:cd03244 78 SRISiipqdpvlfsgtirsnldpfgeysdeelwqalervGLKEFVESLPGGLDTVVEEGGE----------NL------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 441 rvgelSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENAL-LEFPGCAMV-ISHdrwfldRIAThILDYQ--- 515
Cdd:cd03244 141 -----SVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIrEAFKDCTVLtIAH------RLDT-IIDSDril 208
|
250
....*....|
gi 2788209839 516 --DEGKV-EF 522
Cdd:cd03244 209 vlDKGRVvEF 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
321-484 |
6.95e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.88 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFR-------MISGQEQpdSGTITL-GETVKLASVD 392
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFhGKNLYAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 393 Q----------FRDSMDNSKTVWEEVSGGLDI--MKIGNTEMPSRAYVGRFNFKGV-DQGKRVG-ELSGGERGRLHLAKL 458
Cdd:PRK14243 86 PvevrrrigmvFQKPNPFPKSIYDNIAYGARIngYKGDMDELVERSLRQAALWDEVkDKLKQSGlSLSGGQQQRLCIARA 165
|
170 180
....*....|....*....|....*..
gi 2788209839 459 LQVGGNMLLLDEPTNDLD-IETLRALE 484
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDpISTLRIEE 192
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-195 |
7.31e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 62.96 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEAR------PQPDIKIGYLPQEPQLNPEHTVRESIEE 92
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITldgvpvTGPGADRGVVFQKDALLPWLNVLDNVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 93 AVsevvnalkRLDEVyalyadpdadfdKLAAEQGRLEEIIQAhdghnlnVQLERAADAlrlpdwdaKIANLSGGERRRVA 172
Cdd:COG4525 100 GL--------RLRGV------------PKAERRARAEELLAL-------VGLADFARR--------RIWQLSGGMRQRVG 144
|
170 180
....*....|....*....|...
gi 2788209839 173 LCRLLLEKPDMLLLDEPTNHLDA 195
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDA 167
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-217 |
7.56e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.49 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLR-------------IMAGIDKDIEGEARPQPDI-----KIGYLPQEPq 79
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRsinrmndlnpevtITGSIVYNGHNIYSPRTDTvdlrkEIGMVFQQP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 80 lNPehtVRESIEEAVsevvnalkrldeVYALyadpdadfdklaaeqgRLEEIiqaHDGHNLNVQLERAADALRLpdWD-- 157
Cdd:PRK14239 96 -NP---FPMSIYENV------------VYGL----------------RLKGI---KDKQVLDEAVEKSLKGASI--WDev 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788209839 158 -----AKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAITH 217
Cdd:PRK14239 139 kdrlhDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTR 205
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
314-489 |
9.08e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.33 E-value: 9.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 314 PPGPRLGDKVLEVSNLRKSYGDR-----LLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETV-- 386
Cdd:PRK13631 12 VPNPLSDDIILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYig 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 387 ------------------------KLAS-VDQFRDSMDNSKTVWEEVSGGLDIMKIGNTEMPSRA--YVGRFNFKGVDQG 439
Cdd:PRK13631 92 dkknnhelitnpyskkiknfkelrRRVSmVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAkfYLNKMGLDDSYLE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788209839 440 KRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLE 489
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
321-476 |
9.47e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.46 E-value: 9.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSY-GDR-LLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGEtvKLASVDQFRD-- 396
Cdd:PRK13648 5 NSIIVFKNVSFQYqSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN--QAITDDNFEKlr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 --------SMDNS---KTVWEEVSGGLDIMKIGNTEMPSRAyvgRFNFKGVDQGKRVGE----LSGGERGRLHLAKLLQV 461
Cdd:PRK13648 83 khigivfqNPDNQfvgSIVKYDVAFGLENHAVPYDEMHRRV---SEALKQVDMLERADYepnaLSGGQKQRVAIAGVLAL 159
|
170
....*....|....*
gi 2788209839 462 GGNMLLLDEPTNDLD 476
Cdd:PRK13648 160 NPSVIILDEATSMLD 174
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
344-511 |
1.01e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.42 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 344 FSIP---KGAIVGIIGPNGAGKSTLFRMISGQEQPDsgtitLGETVKLASVDQ-------------FRDSMDNSKTVwee 407
Cdd:COG1245 91 YGLPvpkKGKVTGILGPNGIGKSTALKILSGELKPN-----LGDYDEEPSWDEvlkrfrgtelqdyFKKLANGEIKV--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 408 vsggldIMKIGNTEMPSRAYVGRFN--FKGVDQ-----------------GKRVGELSGGERGRLHLAKLLQVGGNMLLL 468
Cdd:COG1245 163 ------AHKPQYVDLIPKVFKGTVRelLEKVDErgkldelaeklglenilDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2788209839 469 DEPTNDLDI-ETLRA--LENALLEFPGCAMVISHDRWFLDRIATHI 511
Cdd:COG1245 237 DEPSSYLDIyQRLNVarLIRELAEEGKYVLVVEHDLAILDYLADYV 282
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
324-499 |
1.09e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 64.27 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSY--GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETV---KLAS------- 390
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdGHDLrdyTLASlrnqval 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 391 VDQ----FRDSMDNSKT-VWEEVSGGLDIMKIGntEMpsrAYVGRFnFKGVDQG--KRVGE----LSGGERGRLHLAKLL 459
Cdd:PRK11176 422 VSQnvhlFNDTIANNIAyARTEQYSREQIEEAA--RM---AYAMDF-INKMDNGldTVIGEngvlLSGGQRQRIAIARAL 495
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2788209839 460 QVGGNMLLLDEPTNDLDIETLRALENALLEFPG--CAMVISH 499
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH 537
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-218 |
1.17e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKST----LLRIMAGI------DKDIEGEARPQ-----PDIKIGYlpQEPQ--LNP 82
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQgeiwfdGQPLHNLNRRQllpvrHRIQVVF--QDPNssLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 83 EHTVRESIEEAVsevvnalkrldEVYalyadpdadFDKLAAEQgRLEEIIQAHDGHNLNvqlerAADALRLPdwdakiAN 162
Cdd:PRK15134 378 RLNVLQIIEEGL-----------RVH---------QPTLSAAQ-REQQVIAVMEEVGLD-----PETRHRYP------AE 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD 218
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHD 485
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-217 |
1.23e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 64.48 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 15 VPPKR-HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG------IDKDIEGEARPQPD---IKI-GYLPQEPQLNPE 83
Cdd:PLN03140 888 VTEDRlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGrktggyIEGDIRISGFPKKQetfARIsGYCEQNDIHSPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 84 HTVRESIeeavsevvnalkrldeVYALyadpdadFDKLAAEQGRLEEIIQAHDGHNLnVQLERAADAL-RLPDwdakIAN 162
Cdd:PLN03140 968 VTVRESL----------------IYSA-------FLRLPKEVSKEEKMMFVDEVMEL-VELDNLKDAIvGLPG----VTG 1019
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLH---DFEGTVVAITH 217
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRntvDTGRTVVCTIH 1077
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-218 |
1.46e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 25 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdKDIEGEAR---------PQPDIKI--GYLPQE--PQLN---------- 81
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQfagqpleawSAAELARhrAYLSQQqtPPFAmpvfqyltlh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 82 -PEHTVRESIEEAVSEVVNALKrLDevyalyadpdadfDKLaaeqGRleeiiqahdghnlnvqleraadalrlpdwdaKI 160
Cdd:PRK03695 94 qPDKTRTEAVASALNEVAEALG-LD-------------DKL----GR-------------------------------SV 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 161 ANLSGGERRRVALCRLLLE-----KPD--MLLLDEPTNHLDAESVAWLERFLHDFE---GTVVAITHD 218
Cdd:PRK03695 125 NQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-236 |
1.60e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 60.89 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTL-LRIMAGIDKD-----IEGEarpqpDI----------KIGYLPQEPQLNpEH 84
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLiLALFRFLEAEegkieIDGI-----DIstipledlrsSLTIIPQDPTLF-SG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 85 TVResieeavsevvNALKRLDEvyalYADPDAdFDKLAAEQGRLeeiiqahdghnlnvqleraadalrlpdwdakiaNLS 164
Cdd:cd03369 97 TIR-----------SNLDPFDE----YSDEEI-YGALRVSEGGL---------------------------------NLS 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD-FEG-TVVAITHDryfLDNVAGW--ILELDRGE 236
Cdd:cd03369 128 QGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREeFTNsTILTIAHR---LRTIIDYdkILVMDAGE 200
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
21-194 |
2.20e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 62.66 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQpDIKIGYLPqePQLNPEHTVRESieeavsevvna 100
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-GQDITHVP--AENRHVNTVFQS----------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 101 lkrldevYALYadPDAD-FDKLA---AEQGRLEEIIQahdghnlnvqlERAADALR---LPDW-DAKIANLSGGERRRVA 172
Cdd:PRK09452 95 -------YALF--PHMTvFENVAfglRMQKTPAAEIT-----------PRVMEALRmvqLEEFaQRKPHQLSGGQQQRVA 154
|
170 180
....*....|....*....|..
gi 2788209839 173 LCRLLLEKPDMLLLDEPTNHLD 194
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALD 176
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-236 |
2.27e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.56 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdkdiegeARPQpdiKIGYLPQEPQLNPEHTVRESIEEAVSEVVNA 100
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL-------LRPQ---KGAVLWQGKPLDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 101 lkrlDEVYALYADPDADFDKLAAEQGRLEEIIQahdghnlnvqlERAADALRLPDWD----AKIANLSGGERRRVALCRL 176
Cdd:PRK13638 86 ----PEQQIFYTDIDSDIAFSLRNLGVPEAEIT-----------RRVDEALTLVDAQhfrhQPIQCLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 177 LLEKPDMLLLDEPTNHLD----AESVAWLERFLHdfEGTVVAI-THDRYFLDNVAGWILELDRGE 236
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDpagrTQMIAIIRRIVA--QGNHVIIsSHDIDLIYEISDAVYVLRQGQ 213
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
18-198 |
2.50e-10 |
|
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: 61.12 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK----------------DIEGEARPQPDIKIGYlpQEPQLN 81
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyevtsgtilfkgqdllELEPDERARAGLFLAF--QYPEEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 82 PEHTVRESIEEAVsevvNALKRLDEVYALyadPDADFDKLAAEQGRLEEIIQAHDGHNLNVqleraadalrlpdwdakia 161
Cdd:TIGR01978 90 PGVSNLEFLRSAL----NARRSARGEEPL---DLLDFEKLLKEKLALLDMDEEFLNRSVNE------------------- 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV 198
Cdd:TIGR01978 144 GFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDAL 180
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-218 |
2.69e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 61.25 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARpqpdIKigylpqepqlnpehtvRESIEEAVSEVVNAL 101
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL----IK----------------GEPIKYDKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 102 KRldeVYALYADPDadfDKLAAEqgRLEEIIqAHDGHNLNVQLE----RAADALR---LPDWDAKIAN-LSGGERRRVAL 173
Cdd:PRK13639 78 KT---VGIVFQNPD---DQLFAP--TVEEDV-AFGPLNLGLSKEevekRVKEALKavgMEGFENKPPHhLSGGQKKRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788209839 174 CRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EG-TVVAITHD 218
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGiTIIISTHD 196
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-198 |
2.98e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.68 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DKDI-----EGEARPqpdiKIGYLPQEPQLNP 82
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvprdagniiidDEDIsllplHARARR----GIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 83 EHTVRESIeEAVSEVVnalkrldevyalyadpdadfDKLAAEQ--GRLEEIIQAHDGHNLNVQLERAadalrlpdwdaki 160
Cdd:PRK10895 92 RLSVYDNL-MAVLQIR--------------------DDLSAEQreDRANELMEEFHIEHLRDSMGQS------------- 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 2788209839 161 anLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV 198
Cdd:PRK10895 138 --LSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-197 |
3.13e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.97 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-------IDKDIEGEARPQPDI--KIGYLPQEPQLNPEHTVRE 88
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriqgnnfTGTILANNRKPTKQIlkRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 89 SIeeavseVVNALKRLDEvyALYADpdadfDKLAAEQGRLEEIIQAHDGHNLNvqleraadalrlpdWDAKIANLSGGER 168
Cdd:PLN03211 160 TL------VFCSLLRLPK--SLTKQ-----EKILVAESVISELGLTKCENTII--------------GNSFIRGISGGER 212
|
170 180
....*....|....*....|....*....
gi 2788209839 169 RRVALCRLLLEKPDMLLLDEPTNHLDAES 197
Cdd:PLN03211 213 KRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
339-476 |
3.27e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.38 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETV--------------KLASVDQFRDSMDNSKT 403
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHItpetgnknlkklrkKVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 404 VWEEVSGGldIMKIGNTEMPSRAyvgrfnfKGVDQGKRVG-----------ELSGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:PRK13641 103 VLKDVEFG--PKNFGFSEDEAKE-------KALKWLKKVGlsedliskspfELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
....
gi 2788209839 473 NDLD 476
Cdd:PRK13641 174 AGLD 177
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-218 |
3.88e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 61.63 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 11 VGKVVPPKR---HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK------DIEGEarpqpDI------------ 69
Cdd:COG1135 7 LSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERptsgsvLVDGV-----DLtalserelraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 70 -KIGYLPQEPQLNPEHTVRESIEeavsevvnalkrldevYALYAdpdADFDKLAAEQgRLEEIIQahdghnLnVQLERAA 148
Cdd:COG1135 82 rKIGMIFQHFNLLSSRTVAENVA----------------LPLEI---AGVPKAEIRK-RVAELLE------L-VGLSDKA 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 149 DALrlPdwdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDFEG-TVVAITHD 218
Cdd:COG1135 135 DAY--P------SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPEttrSILDLLKDINRELGlTIVLITHE 200
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-218 |
4.18e-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: 60.74 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKD------IEGEarpqpDI--------------KIGYLPQEPQLN 81
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPtsgkvlIDGQ-----DIaamsrkelrelrrkKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 82 PEHTVRESIEeavsevvnalkrldevYALyadpdadfdklaaeqgrleEIiqahDGHNLNVQLERAADALR---LPDW-D 157
Cdd:cd03294 115 PHRTVLENVA----------------FGL-------------------EV----QGVPRAEREERAAEALElvgLEGWeH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 158 AKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD 218
Cdd:cd03294 156 KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHD 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-218 |
4.60e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.43 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARpqpdikigylpqepqlnpehTVRESIEEAVSEVVNA 100
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYR--------------------VAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 101 LKR-----LDEVYALYAdpdadfdKLAAEQGrlEEIIQAHDGHNLNVQLERAADAL-RL---PDWDAKIANLSGGERRRV 171
Cdd:PRK10535 83 LRRehfgfIFQRYHLLS-------HLTAAQN--VEVPAVYAGLERKQRLLRAQELLqRLgleDRVEYQPSQLSGGQQQRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788209839 172 ALCRLLLEKPDMLLLDEPTNHLDAES---VAWLERFLHDFEGTVVAITHD 218
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-240 |
6.00e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.93 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMagiDKDIE--GEARPQPDIkigYLPQEPQLNPEHTVRESIEEAVSEVV 98
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVF---NRLIElyPEARVSGEV---YLDGQDIFKMDVIELRRRVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 99 NALKRLD--EVYALyadpDADFDKLAAEQGRLEEIIQAhdghnlnvQLERAADALRLPD-WDAKIANLSGGERRRVALCR 175
Cdd:PRK14247 92 NPIPNLSifENVAL----GLKLNRLVKSKKELQERVRW--------ALEKAQLWDEVKDrLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788209839 176 LLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITHDRYFLDNVAGWILELDRGEGIPW 240
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELkkDMTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
328-484 |
6.41e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.11 E-value: 6.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 328 NLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLA-SVDQFRDSMDNSKTVWE 406
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGrSIFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 407 --EVSGGLDIMKIGNTEMPSRAY--VGRFNFKGVDQGK--RVG--------------ELSGGERGRLHLAKLLQVGGNML 466
Cdd:PRK14271 106 lfQRPNPFPMSIMDNVLAGVRAHklVPRKEFRGVAQARltEVGlwdavkdrlsdspfRLSGGQQQLLCLARTLAVNPEVL 185
|
170
....*....|....*...
gi 2788209839 467 LLDEPTNDLDIETLRALE 484
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIE 203
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-218 |
6.79e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.11 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGearpqpdikigylpqepqlnpehTVRESIEEAVSEVVNAL 101
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG-----------------------KVKIDGELLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 102 KRldEVYALYADPDADFDKLAAE---------QG-RLEEIIQahdghnlnvQLERAADALRLPDWDAK-IANLSGGERRR 170
Cdd:PRK13642 80 RR--KIGMVFQNPDNQFVGATVEddvafgmenQGiPREEMIK---------RVDEALLAVNMLDFKTRePARLSGGQKQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 171 VALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG----TVVAITHD 218
Cdd:PRK13642 149 VAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyqlTVLSITHD 200
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-275 |
6.91e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.00 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKdiegearpqpdikigylPQEPQLnpehtVRESIEEAVSEVVNAL 101
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLR-----------------PQKGKV-----LVSGIDTGDFSKLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 102 KRLdeVYALYADPDADFdklaaeQGRLEEIIQAHDGHNLNV-------QLERAADALRLPDWDAKI-ANLSGGERRRVAL 173
Cdd:PRK13644 76 RKL--VGIVFQNPETQF------VGRTVEEDLAFGPENLCLppieirkRVDRALAEIGLEKYRHRSpKTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 174 CRLLLEKPDMLLLDEPTNHLDAES-VAWLERF--LHDFEGTVVAITHDRYFLdNVAGWILELDRG----EGIPweGNYSS 246
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSgIAVLERIkkLHEKGKTIVYITHNLEEL-HDADRIIVMDRGkivlEGEP--ENVLS 224
|
250 260 270
....*....|....*....|....*....|
gi 2788209839 247 WLEQKDQRLAQEASQEAARR-KSIEKELEW 275
Cdd:PRK13644 225 DVSLQTLGLTPPSLIELAENlKMHGVVIPW 254
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-226 |
7.29e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 60.52 E-value: 7.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 24 NISLSFFPGAKIGVLGLNGAGKSTLLRIMAGID-----------KDI----EGEARP-QPDIKIGYlpQEPQ--LNPEHT 85
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEeptsgeilfdgQDItglsGRELRPlRRRMQMVF--QDPYasLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIEEA--VSEVVNALKRLDEVYALyadpdadfdklaaeqgrLEEiiqahdghnlnVQLeRAADALRLPdwdakiANL 163
Cdd:COG4608 114 VGDIIAEPlrIHGLASKAERRERVAEL-----------------LEL-----------VGL-RPEHADRYP------HEF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD----RYFLDNVA 226
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQVLNLLEDLQDELGLTYLFISHDlsvvRHISDRVA 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-241 |
8.03e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 59.76 E-value: 8.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEA--RPQP-------DIK--IGYLPQepqlNPEhtvresi 90
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfyNNQAitddnfeKLRkhIGIVFQ----NPD------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 91 eeavSEVVNALKRLDEVYAL--YADPDADFDKLAAEQgrLEEIiqahdghnlnVQLERAadalrlpdwDAKIANLSGGER 168
Cdd:PRK13648 94 ----NQFVGSIVKYDVAFGLenHAVPYDEMHRRVSEA--LKQV----------DMLERA---------DYEPNALSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 169 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLH----DFEGTVVAITHDryfLDNVAG--WILELDRG----EGI 238
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRkvksEHNITIISITHD---LSEAMEadHVIVMNKGtvykEGT 225
|
...
gi 2788209839 239 PWE 241
Cdd:PRK13648 226 PTE 228
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
324-386 |
8.09e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 60.63 E-value: 8.09e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 324 LEVSNLRKSY-GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETV 386
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV 67
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-241 |
8.11e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.25 E-value: 8.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQpDIKIGylpqePQLNPEHTVRESIEEAVSEVVNA 100
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG-DIYIG-----DKKNNHELITNPYSKKIKNFKEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 101 LKRLDEV-----YALYAD---PDADFDKLAAEQGRLEEIIQAhdghnlNVQLERAAdaLRLPDWDAKIANLSGGERRRVA 172
Cdd:PRK13631 115 RRRVSMVfqfpeYQLFKDtieKDIMFGPVALGVKKSEAKKLA------KFYLNKMG--LDDSYLERSPFGLSGGQKRRVA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 173 LCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG---TVVAITHDRYFLDNVAGWILELDRGE----GIPWE 241
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMDKGKilktGTPYE 262
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
324-501 |
8.82e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.85 E-value: 8.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSY--GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTL----FRMIS--GQEQPDS---GTITLGETVKLASV- 391
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLSteGEIQIDGvswNSVTLQTWRKAFGVi 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 392 --------DQFRDSMD-----NSKTVW---EEVsgGLDIMkigntempSRAYVGRFNFKGVDQGKRvgeLSGGERGRLHL 455
Cdd:TIGR01271 1298 pqkvfifsGTFRKNLDpyeqwSDEEIWkvaEEV--GLKSV--------IEQFPDKLDFVLVDGGYV---LSNGHKQLMCL 1364
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2788209839 456 AKLLQVGGNMLLLDEPTNDLDIETLRALENALLE-FPGCAMVISHDR 501
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQsFSNCTVILSEHR 1411
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
320-511 |
9.49e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.29 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 320 GDKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFR-DSM 398
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQiDAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 DNSK---TVWEEVSGGLDIMKIGNTEMPSRAY----------VGRFNFKGVDQGKRV--------GELSGGERGRLHLAK 457
Cdd:PRK14246 87 KLRKevgMVFQQPNPFPHLSIYDNIAYPLKSHgikekreikkIVEECLRKVGLWKEVydrlnspaSQLSGGQQQRLTIAR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 458 LLQVGGNMLLLDEPTNDLDIETLRALENALLEFPG--CAMVISHDRWFLDRIATHI 511
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-228 |
9.52e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 59.75 E-value: 9.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQpDIKIGYLPQEPQLNPehtVREsieeavs 95
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG-DIVVSSTSKQKEIKP---VRK------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 96 evvnalkrldEVYALYADPDADFdklaAEQGRLEEIiqAHDGHNLNVQLERA----ADALRLPD-----WDAKIANLSGG 166
Cdd:PRK13643 85 ----------KVGVVFQFPESQL----FEETVLKDV--AFGPQNFGIPKEKAekiaAEKLEMVGladefWEKSPFELSGG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAES-VAWLERF--LHDFEGTVVAITHdryFLDNVAGW 228
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKArIEMMQLFesIHQSGQTVVLVTH---LMDDVADY 210
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
325-487 |
9.55e-10 |
|
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: 59.09 E-value: 9.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 325 EVSNLRKSYGDR---LLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRDSM-- 398
Cdd:cd03249 2 EFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRDLNLRWLRSQIgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 -------------------DNSKTVWEEVSGGLD------IMKI---GNTEMpsrayvgrfnfkgvdqGKRVGELSGGER 450
Cdd:cd03249 82 vsqepvlfdgtiaenirygKPDATDEEVEEAAKKanihdfIMSLpdgYDTLV----------------GERGSQLSGGQK 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 2788209839 451 GRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENAL 487
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEAL 182
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
338-516 |
1.12e-09 |
|
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: 58.25 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 338 LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVklASVDQ--------------FRDSMDNSKt 403
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQepwiqngtirenilFGKPFDEER- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 404 vWEEV------SGGLDIMKIG-NTEmpsrayvgrfnfkgvdqgkrVGE----LSGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:cd03250 97 -YEKVikacalEPDLEILPDGdLTE--------------------IGEkginLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788209839 473 NDLDIETLRAL-ENAL---LEFPGCAMVISHDRWFLDRiATHILDYQD 516
Cdd:cd03250 156 SAVDAHVGRHIfENCIlglLLNNKTRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-194 |
1.22e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.46 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPdiKIGYLPQEPQLNPeHTVRESIEEAVSevvna 100
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RISFSPQTSWIMP-GTIKDNIIFGLS----- 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 101 lkrLDEVyalyadpdadfdklaaeqgRLEEIIQAhdghnlnVQLERaaDALRLPDWDAKI-----ANLSGGERRRVALCR 175
Cdd:TIGR01271 513 ---YDEY-------------------RYTSVIKA-------CQLEE--DIALFPEKDKTVlgeggITLSGGQRARISLAR 561
|
170
....*....|....*....
gi 2788209839 176 LLLEKPDMLLLDEPTNHLD 194
Cdd:TIGR01271 562 AVYKDADLYLLDSPFTHLD 580
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-225 |
1.25e-09 |
|
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: 57.92 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG------IDKDI--EGEarpqpDIKigylpqepQLNPEHTVRES 89
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkyevTEGEIlfKGE-----DIT--------DLPPEERARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 90 I------EEAVSEVVNAlkrldevyalyadpdaDFDKlaaeqgrleeiiqahdghNLNVqleraadalrlpdwdakiaNL 163
Cdd:cd03217 79 IflafqyPPEIPGVKNA----------------DFLR------------------YVNE-------------------GF 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDFEGTVVAITHDRYFLDNV 225
Cdd:cd03217 106 SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVinkLREEGKSVLIITHYQRLLDYI 170
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-227 |
1.47e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.74 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 24 NISLSffPGAKIGVLGLNGAGKS-TLLRIMAGIDKD--IEGEARPQPDiKIGYLPqEPQLNpehtvresieeavsevvna 100
Cdd:PRK09473 36 NFSLR--AGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGR-EILNLP-EKELN------------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 101 LKRLDEVYALYADPDADFDKLAAEQGRLEEIIQAHDGHNLNVQLE---RAADALRLPDWDAKIA----NLSGGERRRVAL 173
Cdd:PRK09473 93 KLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEesvRMLDAVKMPEARKRMKmyphEFSGGMRQRVMI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 174 CRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHDryfLDNVAG 227
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD---LGVVAG 227
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
329-517 |
1.52e-09 |
|
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: 57.20 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 329 LRKSYGD-RLLIDDLSFSipKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGtitlgetvklasvdqfrdsmdnsKTVWEE 407
Cdd:cd03222 6 CVKRYGVfFLLVELGVVK--EGEVIGIVGPNGTGKTTAVKILAGQLIPNGD-----------------------NDEWDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 408 VSGGLDIMKIgntempsrayvgrfnfkgvdqgkrvgELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIE----TLRAL 483
Cdd:cd03222 61 ITPVYKPQYI--------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAI 114
|
170 180 190
....*....|....*....|....*....|....
gi 2788209839 484 ENALLEFPGCAMVISHDRWFLDRIATHILDYQDE 517
Cdd:cd03222 115 RRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
323-480 |
1.69e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQeQPD---SGTITL-GETVKLASVdqfRDSM 398
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFeGEELQASNI---RDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 DN-------------SKTVWEEVSGGLDIMKIGNT---EMPSRAY--VGRFNFkGVDQGKRVGELSGGERGRLHLAKLLQ 460
Cdd:PRK13549 81 RAgiaiihqelalvkELSVLENIFLGNEITPGGIMdydAMYLRAQklLAQLKL-DINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180
....*....|....*....|...
gi 2788209839 461 VGGNMLLLDEPTNDL---DIETL 480
Cdd:PRK13549 160 KQARLLILDEPTASLtesETAVL 182
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
317-520 |
1.81e-09 |
|
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: 57.81 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 317 PRLGDkvLEVSNLRKSYGDRL--LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLgetvklasvdqf 394
Cdd:cd03369 2 PEHGE--IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 395 rDSMDNSKTVWEEVSGGLDIMKIGNTEMPS--RAYVGRFNFKGVDQ---GKRVGE----LSGGERGRLHLAKLLQVGGNM 465
Cdd:cd03369 68 -DGIDISTIPLEDLRSSLTIIPQDPTLFSGtiRSNLDPFDEYSDEEiygALRVSEgglnLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 466 LLLDEPTNDLDIETLRALENALLE-FPGCAMV-ISHdrwfldRIAThILDYQ-----DEGKV 520
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREeFTNSTILtIAH------RLRT-IIDYDkilvmDAGEV 201
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-216 |
1.83e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.49 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 7 TMHRVGKVVPPKRH--ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdkdIEGEARPQPDIKI--------GYLPQ 76
Cdd:PRK09984 3 TIIRVEKLAKTFNQhqALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGSHIELlgrtvqreGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 77 EPQLNPEHTvrESIEEAVSeVVNALKRLDEVY--ALYADP--DADFDKLAAEQGR-----LEEIIQAHDGHNlnvqlera 147
Cdd:PRK09984 80 DIRKSRANT--GYIFQQFN-LVNRLSVLENVLigALGSTPfwRTCFSWFTREQKQralqaLTRVGMVHFAHQ-------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 148 adalrlpdwdaKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF---EGTVVAIT 216
Cdd:PRK09984 149 -----------RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqnDGITVVVT 209
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
22-236 |
2.18e-09 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 58.47 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVL-GLNGAGKSTLLRIMA----GIDKDIEGEARPQPDIKIGylpqepQLNPEHTV-------RES 89
Cdd:COG3950 14 FEDLEIDFDNPPRLTVLvGENGSGKTTLLEAIAlalsGLLSRLDDVKFRKLLIRNG------EFGDSAKLilyygtsRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 90 IEEAVSEVVNALKRLDEVYALYA---DPDADFDKLAAEQGRLEEIIQAHDGHNLNVQLERAADALR--LPDWDA------ 158
Cdd:COG3950 88 LDGPLKKLERLKEEYFSRLDGYDsllDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVREALNklLPDFKDiridrd 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 159 --------------KIANLSGGERRRVALC-----RLLLEKPDM---------LLLDEPTNHLdaeSVAWLERFLHDFEG 210
Cdd:COG3950 168 pgrlvildkngeelPLNQLSDGERSLLALVgdlarRLAELNPALenplegegiVLIDEIDLHL---HPKWQRRILPDLRK 244
|
250 260 270
....*....|....*....|....*....|..
gi 2788209839 211 T-----VVAITHDRYFLDNV-AGWILELDRGE 236
Cdd:COG3950 245 IfpniqFIVTTHSPLILSSLeDEEVIVLERDE 276
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-216 |
2.37e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE-----ARPQPDI-------KIGYLPQEPQLnpehtVRE 88
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDiiindSHNLKDInlkwwrsKIGVVSQDPLL-----FSN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 89 SIEEAVSEVVNALKRLDEV--------YALYADPDADFDKLAAEQGRLEEIIQAHDGHNL-----NVQLERAADALR--- 152
Cdd:PTZ00265 475 SIKNNIKYSLYSLKDLEALsnyynedgNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELiemrkNYQTIKDSEVVDvsk 554
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 153 ----------LPD-WDAKI----ANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAIT 216
Cdd:PTZ00265 555 kvlihdfvsaLPDkYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
346-512 |
2.44e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 346 IPK-GAIVGIIGPNGAGKSTLFRMISGQEQPDsgtitLGETVKLASVDQ-------------FRDSMDNSKTVweevsgg 411
Cdd:PRK13409 95 IPKeGKVTGILGPNGIGKTTAVKILSGELIPN-----LGDYEEEPSWDEvlkrfrgtelqnyFKKLYNGEIKV------- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 412 ldIMKIGNTEMPSRAYVGRFN--FKGVDQ-----------------GKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:PRK13409 163 --VHKPQYVDLIPKVFKGKVRelLKKVDErgkldevverlglenilDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2788209839 473 NDLDI-ETLRAlENALLEF-PGCA-MVISHDRWFLDRIA--THIL 512
Cdd:PRK13409 241 SYLDIrQRLNV-ARLIRELaEGKYvLVVEHDLAVLDYLAdnVHIA 284
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
21-235 |
2.98e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 57.84 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGIDK--DIEGEA-RP---------QPDIKIGYLPQEPQLN 81
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRvgDITIDTaRSlsqqkglirQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 82 PEHTVRESIEEAvSEVVNALKRLDevyalyadpdadfdklAAEQGRleEIIQahdghnlNVQLERAADALrlPdwdakiA 161
Cdd:PRK11264 98 PHRTVLENIIEG-PVIVKGEPKEE----------------ATARAR--ELLA-------KVGLAGKETSY--P------R 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLE---RFLHDFEGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:PRK11264 144 RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLntiRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
323-499 |
3.02e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTIT-LGETVKLASVdqfRDSMD-- 399
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGP---KSSQEag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 400 -----------NSKTVWEEVSGGLDIM----KIGNTEMPSRA--YVGRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVG 462
Cdd:PRK10762 81 igiihqelnliPQLTIAENIFLGREFVnrfgRIDWKKMYAEAdkLLARLNLRFSSD-KLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2788209839 463 GNMLLLDEPTNDL-DIETlRALENAL--LEFPGCAMV-ISH 499
Cdd:PRK10762 160 SKVIIMDEPTDALtDTET-ESLFRVIreLKSQGRGIVyISH 199
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
321-535 |
3.08e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMIS--GQEQPdsgTITLGETVKLASVDQFR--- 395
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNP---EVTITGSIVYNGHNIYSprt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 DSMDNSK--------------TVWEEVSGGLDIMKIGNTEMPSRAyVGRfNFKGVDQGKRVGE--------LSGGERGRL 453
Cdd:PRK14239 80 DTVDLRKeigmvfqqpnpfpmSIYENVVYGLRLKGIKDKQVLDEA-VEK-SLKGASIWDEVKDrlhdsalgLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 454 HLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEFPG--CAMVISHDRWFLDRIAThildyqdegKVEFF-EGNFTEY 530
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQQASRISD---------RTGFFlDGDLIEY 228
|
....*
gi 2788209839 531 EEYKK 535
Cdd:PRK14239 229 NDTKQ 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-218 |
3.13e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 58.08 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEarpqpdIKI-GYlpqepQLNpehtvRESIEEAv 94
Cdd:PRK13632 19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGE------IKIdGI-----TIS-----KENLKEI- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 95 sevvnalkrLDEVYALYADPDADFDKLAAE-------------QGRLEEIIqahDGHNLNVQLERAADalRLPDwdakia 161
Cdd:PRK13632 82 ---------RKKIGIIFQNPDNQFIGATVEddiafglenkkvpPKKMKDII---DDLAKKVGMEDYLD--KEPQ------ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG----TVVAITHD 218
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrkkTLISITHD 202
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-217 |
3.85e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 57.74 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI----------------DKDIEGEARPQPDI--KIGYLPQEPq 79
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipgarvegeilldGEDIYDPDVDVVELrrRVGMVFQKP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 80 lNP-EHTVRESIeeavsevvnalkrldeVYALyadpdadfdKLA--AEQGRLEEIIQAHdghnlnvqLERAA------Da 150
Cdd:COG1117 102 -NPfPKSIYDNV----------------AYGL---------RLHgiKSKSELDEIVEES--------LRKAAlwdevkD- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 151 lRLpdwDAKIANLSGGERRRvaLC--RLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAITH 217
Cdd:COG1117 147 -RL---KKSALGLSGGQQQR--LCiaRALAVEPEVLLMDEPTSALDPISTAKIEELILELKKdyTIVIVTH 211
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
321-507 |
4.03e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEqpdSGTITLGETVklasvdqFRDSMDN 400
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHP---AYKILEGDIL-------FKGESIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 401 SKTVWEEVSGGL--------DIMKIGNTEMPSRAYVGRFNFKGVDQ------------------------GKRVGE-LSG 447
Cdd:CHL00131 75 DLEPEERAHLGIflafqypiEIPGVSNADFLRLAYNSKRKFQGLPEldplefleiineklklvgmdpsflSRNVNEgFSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 448 GERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALE---NALLEFPGCAMVISHDRWFLDRI 507
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAegiNKLMTSENSIILITHYQRLLDYI 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
324-476 |
4.90e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.97 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSY--GDRLL--IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGtitlgeTVKLASVDQFRDSMD 399
Cdd:PRK10535 5 LELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSG------TYRVAGQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 400 NSKTVWEEVSGGL--------DIMKIGNTEMP--------------SRAYVGRFNFkgvdqGKRV----GELSGGERGRL 453
Cdd:PRK10535 79 ALAQLRREHFGFIfqryhllsHLTAAQNVEVPavyaglerkqrllrAQELLQRLGL-----EDRVeyqpSQLSGGQQQRV 153
|
170 180
....*....|....*....|...
gi 2788209839 454 HLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALD 176
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-194 |
6.29e-09 |
|
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: 58.60 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE----ARPQPDIK-------IGYLPQEPQL------- 80
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEillnGFSLKDIDrhtlrqfINYLPQEPYIfsgsile 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 81 -----NPEHTVRESIEEAVSevvnalkrldevyalYADPDADFDKLAaeqgrleeiiqahdghnLNVQLERAADAlrlpd 155
Cdd:TIGR01193 567 nlllgAKENVSQDEIWAACE---------------IAEIKDDIENMP-----------------LGYQTELSEEG----- 609
|
170 180 190
....*....|....*....|....*....|....*....
gi 2788209839 156 wdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:TIGR01193 610 -----SSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
314-487 |
7.02e-09 |
|
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: 58.29 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 314 PPGPR---LGDKVLEVSNLRKSY-GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG----ET 385
Cdd:COG5265 345 APDAPplvVGGGEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDgqdiRD 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 386 VKLAS-------VDQ----FRDSM---------DNSKtvwEEVsggldimkignTEMPSRAYVGRFnFKGVDQG--KRVG 443
Cdd:COG5265 425 VTQASlraaigiVPQdtvlFNDTIayniaygrpDASE---EEV-----------EAAARAAQIHDF-IESLPDGydTRVG 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788209839 444 E----LSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENAL 487
Cdd:COG5265 490 ErglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAAL 537
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
338-522 |
7.55e-09 |
|
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: 58.61 E-value: 7.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 338 LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQ--------FRDSM----------- 398
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQrpymtlgtLRDQIiypdssedmkr 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 -DNSKTVWEEVSGGLDIMKIGNTEMpsrayvgrfNFKGVDQGKRVgeLSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDI 477
Cdd:TIGR00954 547 rGLSDKDLEQILDNVQLTHILEREG---------GWSAVQDWMDV--LSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2788209839 478 ETLRALENALLEFPGCAMVISHdRWFLDRIATHILDYQDEGKVEF 522
Cdd:TIGR00954 616 DVEGYMYRLCREFGITLFSVSH-RKSLWKYHEYLLYMDGRGGYQF 659
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
323-383 |
8.66e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 8.66e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG 383
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-223 |
9.75e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 56.23 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK------DI--EGEarpqpDIK-----------IGYLPQEPQLN 81
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyevtsgSIllDGE-----DILelspderaragIFLAFQYPVEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 82 PEHTVRESIEEAVSEVvnalkRLDEVYALyadpdaDFDKLAAEQGRLEEIIQAHdghnlnvqLERAADAlrlpdwdakia 161
Cdd:COG0396 90 PGVSVSNFLRTALNAR-----RGEELSAR------EFLKLLKEKMKELGLDEDF--------LDRYVNE----------- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLERFLHDFEGTVVAITHDRYFLD 223
Cdd:COG0396 140 GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDAlriVAEGVNKLRSPDRGILIITHYQRILD 204
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-218 |
9.78e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 9.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDkDIEGEARPQPdiKIGYLPQ---EPQLNpehtvresieeavsev 97
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVRVEG--RVEFFNQniyERRVN---------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 98 VNALKRldEVYALYADPD----ADFDKLAAEQgrleEIIQAHDGHNLNVQLERAADALRLpdWDA------KIA-NLSGG 166
Cdd:PRK14258 83 LNRLRR--QVSMVHPKPNlfpmSVYDNVAYGV----KIVGWRPKLEIDDIVESALKDADL--WDEikhkihKSAlDLSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF----EGTVVAITHD 218
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHN 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-194 |
1.01e-08 |
|
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: 56.79 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPdiKIGYLPQEPQLNPeHTVRESIEEAVSevvna 100
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQFSWIMP-GTIKENIIFGVS----- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 101 lkrldevYALYadpdadfdklaaeqgRLEEIIQAhdghnlnVQLERaaDALRLPDWDAKI-----ANLSGGERRRVALCR 175
Cdd:cd03291 124 -------YDEY---------------RYKSVVKA-------CQLEE--DITKFPEKDNTVlgeggITLSGGQRARISLAR 172
|
170
....*....|....*....
gi 2788209839 176 LLLEKPDMLLLDEPTNHLD 194
Cdd:cd03291 173 AVYKDADLYLLDSPFGYLD 191
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
324-507 |
1.18e-08 |
|
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: 55.31 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRkSYGDRLLIDdlsFSIPkgaIVGIIGPNGAGKSTLFRMI-------------SGQEQPDsgtiTLGETVKLAS 390
Cdd:cd03240 4 LSIRNIR-SFHERSEIE---FFSP---LTLIVGQNGAGKTTIIEALkyaltgelppnskGGAHDPK----LIREGEVRAQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 391 VD-QFRDSMDNSKTVWEEVSGGLDIMKIGNTEMPSRAYVGRfnfkgvdqgkrvGELSGGERG------RLHLAKLLQVGG 463
Cdd:cd03240 73 VKlAFENANGKKYTITRSLAILENVIFCHQGESNWPLLDMR------------GRCSGGEKVlasliiRLALAETFGSNC 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2788209839 464 NMLLLDEPTNDLDIETLR-----ALENALLEFPGCAMVISHDRWFLDRI 507
Cdd:cd03240 141 GILALDEPTTNLDEENIEeslaeIIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-236 |
1.23e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 56.35 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdkdiegearpqpdikigYLPQEpqlNPEHTVRESIEEAVSEV 97
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL-----------------LLPDD---NPNSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 98 VNALKrlDEVYALYADPDADF------DKLA-------AEQGRLEEIIQahdghnlnvqlERAADALRLPDWDAKIANLS 164
Cdd:PRK13640 79 VWDIR--EKVGIVFQNPDNQFvgatvgDDVAfglenraVPRPEMIKIVR-----------DVLADVGMLDYIDSEPANLS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHDryfLD--NVAGWILELDRGE 236
Cdd:PRK13640 146 GGQKQRVAIAGILAVEPKIIILDESTSMLDPAGkeqiLKLIRKLKKKNNLTVISITHD---IDeaNMADQVLVLDDGK 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-219 |
1.24e-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: 58.00 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGIDKDIEGEARPQPDIKI-------GYLPQEPQLNpEHTVRe 88
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAllrLLSTEGEIQIDGVSWNSVTLqtwrkafGVIPQKVFIF-SGTFR- 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 89 sieeavsevvnalKRLDEvYALYAdpDADFDKLAAEQGrLEEIIQAHDGhNLNVQLERAADAlrlpdwdakianLSGGER 168
Cdd:TIGR01271 1310 -------------KNLDP-YEQWS--DEEIWKVAEEVG-LKSVIEQFPD-KLDFVLVDGGYV------------LSNGHK 1359
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 169 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL-HDFEGTVVAITHDR 219
Cdd:TIGR01271 1360 QLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLkQSFSNCTVILSEHR 1411
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
341-476 |
1.34e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.29 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 341 DLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETV---------------KLASVDQFRDSMDNSKTVW 405
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirkKVGLVFQFPESQLFEETVL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 406 EEVSGGLDIMKIGNTEMPSRAYvGRFNFKGVDQ---GKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:PRK13649 105 KDVAFGPQNFGVSQEEAEALAR-EKLALVGISEslfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-240 |
1.46e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.82 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMagiDKDIE-GEARPQPDIKIGYLPQEpqlnpehTVResieeavsev 97
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL---NRLIEiYDSKIKVDGKVLYFGKD-------IFQ---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 98 VNALKRLDEVYALYADPD-----ADFDKLA---AEQGRLE--EIIQAHDGHNLNVQL-ERAADALRLPdwdakIANLSGG 166
Cdd:PRK14246 83 IDAIKLRKEVGMVFQQPNpfphlSIYDNIAyplKSHGIKEkrEIKKIVEECLRKVGLwKEVYDRLNSP-----ASQLSGG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITHDRYFLDNVAGWILELDRGEGIPW 240
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVADYVAFLYNGELVEW 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-249 |
1.61e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.87 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRhILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGiDKDIEgEARPQPDIKIGYLPQEPQ-LNPehTVRESIeeavs 95
Cdd:PTZ00243 672 PKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS-QFEIS-EGRVWAERSIAYVPQQAWiMNA--TVRGNI----- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 96 evvnalkrldevyaLYADPDadfdklaaEQGRLEEIIQAhdghnlnVQLEraADALRLP-----DWDAKIANLSGGERRR 170
Cdd:PTZ00243 742 --------------LFFDEE--------DAARLADAVRV-------SQLE--ADLAQLGggletEIGEKGVNLSGGQKAR 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 171 VALCRLLLEKPDMLLLDEPTNHLDAEsVAwlERFLHD-FEG-----TVVAITHDRYFLDNvAGWILELDRGEgIPWEGNY 244
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPLSALDAH-VG--ERVVEEcFLGalagkTRVLATHQVHVVPR-ADYVVALGDGR-VEFSGSS 865
|
....*
gi 2788209839 245 SSWLE 249
Cdd:PTZ00243 866 ADFMR 870
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
320-544 |
1.81e-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: 57.61 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 320 GDKVLEVSNLrKSYGDRLLiDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASvdQFRDSMD 399
Cdd:TIGR01271 425 GDDGLFFSNF-SLYVTPVL-KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSP--QTSWIMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 400 NskTVWEEVSGGLDIMKIGNTEMPSRAYVGRFNFKGVDQGKRV-GE----LSGGERGRLHLAKLLQVGGNMLLLDEPTND 474
Cdd:TIGR01271 501 G--TIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVlGEggitLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 475 LDIETlralENALLEFPGCAMVISHDRWFLDRIATHiLDYQD------EGkVEFFEGNFTEYE----EYKKRTLGADALE 544
Cdd:TIGR01271 579 LDVVT----EKEIFESCLCKLMSNKTRILVTSKLEH-LKKADkilllhEG-VCYFYGTFSELQakrpDFSSLLLGLEAFD 652
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
324-501 |
1.85e-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: 55.63 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSY--GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLF----RMIS--GQEQPDS---GTITLGETVKLASV- 391
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLNteGDIQIDGvswNSVPLQKWRKAFGVi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 392 --------DQFRDSMD-----NSKTVW---EEVSggldiMKIGNTEMPsrayvGRFNFKGVDQGKrvgELSGGERGRLHL 455
Cdd:cd03289 83 pqkvfifsGTFRKNLDpygkwSDEEIWkvaEEVG-----LKSVIEQFP-----GQLDFVLVDGGC---VLSHGHKQLMCL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2788209839 456 AKLLQVGGNMLLLDEPTNDLDIETLRALENALLE-FPGCAMVISHDR 501
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQaFADCTVILSEHR 196
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-200 |
1.93e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLL-----RIMAGI----DKDIEGEARPQP-DIKIGYLPQEPQLNPEHTVR 87
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVitggDRLVNGRPLDSSfQRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 88 ESIEEAVsevvnALKRLDEVyalyadPDADFDKLaaeqgrLEEIIQAhdghnlnVQLERAADAL-RLPDwdakiANLSGG 166
Cdd:TIGR00956 855 ESLRFSA-----YLRQPKSV------SKSEKMEY------VEEVIKL-------LEMESYADAVvGVPG-----EGLNVE 905
|
170 180 190
....*....|....*....|....*....|....*
gi 2788209839 167 ERRRVALCRLLLEKPDMLL-LDEPTNHLDAESvAW 200
Cdd:TIGR00956 906 QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT-AW 939
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-272 |
1.95e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.89 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---ID-KDIEGEARPQPDIKIGYLPQEPQL-Npe 83
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGrilIDgTDIRTVTRASLRRNIAVVFQDAGLfN-- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 84 HTVRESI----EEAV-SEVVNALKRLdEVYALYADPDADFDKLAAEQGRleeiiqahdghnlnvqleraadalrlpdwda 158
Cdd:PRK13657 423 RSIEDNIrvgrPDATdEEMRAAAERA-QAHDFIERKPDGYDTVVGERGR------------------------------- 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 159 kiaNLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF-EG-TVVAITHDryfLDNV--AGWILELDR 234
Cdd:PRK13657 471 ---QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELmKGrTTFIIAHR---LSTVrnADRILVFDN 544
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2788209839 235 GEGIPwEGNYSSwLEQKDQRLAQEA-----SQEAARRKSIEKE 272
Cdd:PRK13657 545 GRVVE-SGSFDE-LVARGGRFAALLraqgmLQEDERRKQPAAE 585
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
321-489 |
2.13e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.57 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSYGDRL---------LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLgETVKLASV 391
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI-DDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 392 DQ----------FRDSmDNSKTVWEEVSGGLDIMKIGNTEMPSRAYVGRFNfkgvDQGKRVG-----------ELSGGER 450
Cdd:PRK15112 81 DYsyrsqrirmiFQDP-STSLNPRQRISQILDFPLRLNTDLEPEQREKQII----ETLRQVGllpdhasyyphMLAPGQK 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 2788209839 451 GRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLE 489
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLE 194
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-195 |
2.23e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.01 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 11 VGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEarpqpdIKIGylpqepqlnpehtvresi 90
Cdd:PRK11650 9 VRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE------IWIG------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 91 eeavSEVVNALKRLD-------EVYALYadPDAD-FDKLA-----AEQGRlEEIIQahdghnlnvQLERAADALRL-PDW 156
Cdd:PRK11650 65 ----GRVVNELEPADrdiamvfQNYALY--PHMSvRENMAyglkiRGMPK-AEIEE---------RVAEAARILELePLL 128
|
170 180 190
....*....|....*....|....*....|....*....
gi 2788209839 157 DAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 195
Cdd:PRK11650 129 DRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
285-396 |
2.88e-08 |
|
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: 56.34 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 285 SKGKARLARFEELNSTEYQKRNETNELFIPPGPRLGDKvLEVSNLRKSYGDRlliDD--------LSFSIPKGAIVGIIG 356
Cdd:COG4615 290 SRANVALRKIEELELALAAAEPAAADAAAPPAPADFQT-LELRGVTYRYPGE---DGdegftlgpIDLTIRRGELVFIVG 365
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2788209839 357 PNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRD 396
Cdd:COG4615 366 GNGSGKSTLAKLLTGLYRPESGEILLdGQPVTADNREAYRQ 406
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-526 |
3.19e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.04 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKST----LFRM--ISGQEQPDSGTITLGETV--KLASVDQFR 395
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTflkcLNRMneLESEVRVEGRVEFFNQNIyeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 D--SMDNSK------TVWEEVSGGLDIM----KIGNTEMPSRAYVGRFNFKGVDQG--KRVGELSGGERGRLHLAKLLQV 461
Cdd:PRK14258 88 RqvSMVHPKpnlfpmSVYDNVAYGVKIVgwrpKLEIDDIVESALKDADLWDEIKHKihKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 462 GGNMLLLDEPTNDLD------IETLraLENALLEFPGCAMVISHDRWFLDRIAthilDYqdegkVEFFEGN 526
Cdd:PRK14258 168 KPKVLLMDEPCFGLDpiasmkVESL--IQSLRLRSELTMVIVSHNLHQVSRLS----DF-----TAFFKGN 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
17-218 |
3.81e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 54.71 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK------DIEGEARPQPDIKIGYLPQEPQLNPEHTVRESI 90
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 91 EeavsevvnalkrldevyalyadpdadFDKLAAEQGRLEeiiqahdghnlnvQLERAADALRLPDWDA----KIANLSGG 166
Cdd:PRK11248 92 A--------------------------FGLQLAGVEKMQ-------------RLEIAHQMLKKVGLEGaekrYIWQLSGG 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL----HDFEGTVVAITHD 218
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHD 188
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
320-500 |
4.03e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.36 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 320 GDKVLEVSNLRKSY--------GDRLL--IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKL 388
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 389 ASVDQFRD--------------SMDNSKTVWEEVSGGLDImkigNTEMPS---RAyvgrfnfKGVDQGKRVG---E---- 444
Cdd:PRK11308 82 ADPEAQKLlrqkiqivfqnpygSLNPRKKVGQILEEPLLI----NTSLSAaerRE-------KALAMMAKVGlrpEhydr 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 445 ----LSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIeTLRALENALL-----EFpGCAMV-ISHD 500
Cdd:PRK11308 151 yphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQAQVLNLMmdlqqEL-GLSYVfISHD 214
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
331-476 |
4.07e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 54.11 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 331 KSY-GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG--ETVKLASVDQ----------FRDS 397
Cdd:PRK10908 9 KAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghDITRLKNREVpflrrqigmiFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 398 ---MDnsKTVWEEVSGGLDIMKIGNTEMPSRAYVGRFNFKGVDQGKRVG-ELSGGERGRLHLAKLLQVGGNMLLLDEPTN 473
Cdd:PRK10908 89 hllMD--RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPiQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
...
gi 2788209839 474 DLD 476
Cdd:PRK10908 167 NLD 169
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
323-472 |
4.36e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.11 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG-------ETVKL-----AS 390
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkditdwQTAKImreavAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 391 VDQFRDSMdNSKTVWEEVS-GGLDIMKIGNTEMPSRAYvGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLD 469
Cdd:PRK11614 85 VPEGRRVF-SRMTVEENLAmGGFFAERDQFQERIKWVY-ELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
...
gi 2788209839 470 EPT 472
Cdd:PRK11614 163 EPS 165
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
323-500 |
4.57e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.45 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQ----EQPDSGTITLGETVK---LASVDQFR 395
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltggGAPRGARVTGDVTLNgepLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 dsMDNSKTVWEEVS------GGLDIMKIGNTEMPSRAYVGRFNFKGVDQ------------GKRVGELSGGERGRLHLAK 457
Cdd:PRK13547 81 --LARLRAVLPQAAqpafafSAREIVLLGRYPHARRAGALTHRDGEIAWqalalagatalvGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 458 LL---------QVGGNMLLLDEPTNDLD-------IETLRALENallEFPGCAMVISHD 500
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVHD 214
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-236 |
4.58e-08 |
|
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: 56.11 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQ----PDI-------KIGYLPQEPQLNpEHTVRES 89
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDglniAKIglhdlrfKITIIPQDPVLF-SGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 90 IEEavsevvnalkrldevYALYADPDAdfdKLAAEQGRLEEIIQAHDGhNLNVQLERAADalrlpdwdakiaNLSGGERR 169
Cdd:TIGR00957 1380 LDP---------------FSQYSDEEV---WWALELAHLKTFVSALPD-KLDHECAEGGE------------NLSVGQRQ 1428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788209839 170 RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLH-DFEG-TVVAITHDryfLDNVAGW--ILELDRGE 236
Cdd:TIGR00957 1429 LVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRtQFEDcTVLTIAHR---LNTIMDYtrVIVLDKGE 1496
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-205 |
5.24e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 31 PGAKIGVLGLNGAGKSTLLRIMAG--------IDKDIEGEARPQPDIKIGYLPQEPQLNPEhtvresieeavsevVNALK 102
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGllhvesgqIQIDGKTATRGDRSRFMAYLGHLPGLKAD--------------LSTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 103 RLDEVYALyadpdadfdklaaeQGRLEeiiQAHDGHNLN-VQLERAADALrlpdwdakIANLSGGERRRVALCRLLLEKP 181
Cdd:PRK13543 102 NLHFLCGL--------------HGRRA---KQMPGSALAiVGLAGYEDTL--------VRQLSAGQKKRLALARLWLSPA 156
|
170 180
....*....|....*....|....
gi 2788209839 182 DMLLLDEPTNHLDAESVAWLERFL 205
Cdd:PRK13543 157 PLWLLDEPYANLDLEGITLVNRMI 180
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
339-520 |
5.31e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.63 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQ----------------------FRD 396
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikevkrlrkeiglvfqfpeyqlFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 SMD------------NSKTVWEEVSGGLDIMKIgntempSRAYVGRFNFkgvdqgkrvgELSGGERGRLHLAKLLQVGGN 464
Cdd:PRK13645 107 TIEkdiafgpvnlgeNKQEAYKKVPELLKLVQL------PEDYVKRSPF----------ELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 465 MLLLDEPTNDLDIETLRALENALL----EFPGCAMVISHDRWFLDRIATHILdYQDEGKV 520
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFErlnkEYKKRIIMVTHNMDQVLRIADEVI-VMHEGKV 229
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
323-515 |
5.91e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRDSMDNS 401
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRGDRSRFMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 402 KTVWEEVSgGLDIMKIGN-------TEMPSRAY--VGrfnFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:PRK13543 91 PGLKADLS-TLENLHFLCglhgrraKQMPGSALaiVG---LAGYED-TLVRQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2788209839 473 NDLDIETLRALENAL---LEFPGCAMVISHDRWFLDRIATHILDYQ 515
Cdd:PRK13543 166 ANLDLEGITLVNRMIsahLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
339-380 |
6.08e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.28 E-value: 6.08e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2788209839 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTI 380
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-226 |
6.25e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 54.35 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRImagIDKDIEGEArpqPDIKIgylpqEPQLNPEHTVREsIEEAVSEVv 98
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRL---IDGLLEAES---GQIII-----DGDLLTEENVWD-IRHKIGMV- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 99 nalkrldevyalYADPDADFDKLAAEQG---RLEeiiqaHDGHNLNVQLERAADALRLPDW----DAKIANLSGGERRRV 171
Cdd:PRK13650 87 ------------FQNPDNQFVGATVEDDvafGLE-----NKGIPHEEMKERVNEALELVGMqdfkEREPARLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 172 ALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHDryfLDNVA 226
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGrlelIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-218 |
1.16e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.56 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 1 MAQFVYTMHRVGKVVppkrhiLKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGeARPQPDI----------- 69
Cdd:PRK14271 22 MAAVNLTLGFAGKTV------LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVllggrsifnyr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 70 -------KIGYLPQEPQLNPEhtvreSIEEAVSEVVNALKRLdevyalyadPDADFDKLAaeQGRLEEIiqahdghnlnv 142
Cdd:PRK14271 95 dvlefrrRVGMLFQRPNPFPM-----SIMDNVLAGVRAHKLV---------PRKEFRGVA--QARLTEV----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 143 qleRAADAL--RLPDWDAKianLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAITHD 218
Cdd:PRK14271 148 ---GLWDAVkdRLSDSPFR---LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-477 |
1.17e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEarpqpdikIGYLPQEPQLnpeHTVRESIEEAVSEV---V 98
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGS--------ILFQGKEIDF---KSSKEALENGISMVhqeL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 99 NALKR---LDEVY--------------ALYADPDADFDKLaaeqgrleeiiqahdghNLNVqleraadalrlpDWDAKIA 161
Cdd:PRK10982 83 NLVLQrsvMDNMWlgryptkgmfvdqdKMYRDTKAIFDEL-----------------DIDI------------DPRAKVA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEgtvvaithdryfldnvagwilelDRGEGIPwe 241
Cdd:PRK10982 134 TLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLK-----------------------ERGCGIV-- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 242 gnYSSWLEQKDQRLAQEASqeaarrksIEKELEWVR-QGTKGRQSKGKARLARFEELNSTEYQKRNETNELfippgprlg 320
Cdd:PRK10982 189 --YISHKMEEIFQLCDEIT--------ILRDGQWIAtQPLAGLTMDKIIAMMVGRSLTQRFPDKENKPGEV--------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 dkVLEVSNLrkSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDqfrDSMD 399
Cdd:PRK10982 250 --ILEVRNL--TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLhGKKINNHNAN---EAIN 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 400 NS-KTVWEE-----VSGGLDI-------------MKIG---NTEMPS--RAYVGRFNFKGVDQGKRVGELSGGERGRLHL 455
Cdd:PRK10982 323 HGfALVTEErrstgIYAYLDIgfnslisnirnykNKVGlldNSRMKSdtQWVIDSMRVKTPGHRTQIGSLSGGNQQKVII 402
|
490 500
....*....|....*....|..
gi 2788209839 456 AKLLQVGGNMLLLDEPTNDLDI 477
Cdd:PRK10982 403 GRWLLTQPEILMLDEPTRGIDV 424
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
326-476 |
1.18e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.50 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 326 VSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDS--GTI----------------------- 380
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTIlannrkptkqilkrtgfvtqddi 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 381 -----TLGETVKLASVDQFRDSM--DNSKTVWEEVSGGLDIMKIGNTempsraYVGRFNFKGVdqgkrvgelSGGERGRL 453
Cdd:PLN03211 151 lyphlTVRETLVFCSLLRLPKSLtkQEKILVAESVISELGLTKCENT------IIGNSFIRGI---------SGGERKRV 215
|
170 180
....*....|....*....|...
gi 2788209839 454 HLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:PLN03211 216 SIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-219 |
1.35e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.41 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE--------ARPQPDI---KIGYLPQEPQLNPEhTVRES 89
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTllfegediSTLKPEIyrqQVSYCAQTPTLFGD-TVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 90 IeeavseVVNALKRLDEVyalyadpdaDFDKLAAEQGRLEeiiqahdghnlnvqleraadalrLPD--WDAKIANLSGGE 167
Cdd:PRK10247 101 L------IFPWQIRNQQP---------DPAIFLDDLERFA-----------------------LPDtiLTKNIAELSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLH----DFEGTVVAITHDR 219
Cdd:PRK10247 143 KQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHryvrEQNIAVLWVTHDK 198
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
9-217 |
1.40e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.10 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 9 HRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEarpqpdIKIGYLPQEPQLNPEHtvre 88
Cdd:PRK13634 10 HRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGT------VTIGERVITAGKKNKK---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 89 sieeavsevvnaLKRL-DEVYALYADPDADFdklaaeqgrLEEIIQ---AHDGHNLNVQ----LERAADALRLPDWDAKI 160
Cdd:PRK13634 80 ------------LKPLrKKVGIVFQFPEHQL---------FEETVEkdiCFGPMNFGVSeedaKQKAREMIELVGLPEEL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788209839 161 A-----NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLERfLHDFEG-TVVAITH 217
Cdd:PRK13634 139 LarspfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPkgrkEMMEMFYK-LHKEKGlTTVLVTH 204
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-219 |
1.57e-07 |
|
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: 52.93 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGIDKDIEGEARPQPDIKI-------GYLPQEPQLNpEHTVResi 90
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAflrLLNTEGDIQIDGVSWNSVPLqkwrkafGVIPQKVFIF-SGTFR--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 91 eeavsevvnalKRLDEvYALYAdpDADFDKLAAEQGrLEEIIQAHDGHnLNVQLERAADAlrlpdwdakianLSGGERRR 170
Cdd:cd03289 95 -----------KNLDP-YGKWS--DEEIWKVAEEVG-LKSVIEQFPGQ-LDFVLVDGGCV------------LSHGHKQL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788209839 171 VALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL-HDFEGTVVAITHDR 219
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLkQAFADCTVILSEHR 196
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
317-477 |
1.67e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 317 PRLGDKVLEVSNLR---KSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQE--QPDSGTITL-GETVKLAS 390
Cdd:NF040905 251 PKIGEVVFEVKNWTvyhPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKdGKEVDVST 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 391 VdqfRDSMDNS-KTVWEEVSG-GL----DIMKigNTEMPS-------------------RAYVGRFNFK--GVDQGkrVG 443
Cdd:NF040905 331 V---SDAIDAGlAYVTEDRKGyGLnlidDIKR--NITLANlgkvsrrgvideneeikvaEEYRKKMNIKtpSVFQK--VG 403
|
170 180 190
....*....|....*....|....*....|....
gi 2788209839 444 ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDI 477
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
348-515 |
1.91e-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: 50.45 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 348 KGAIVGIIGPNGAGKSTLFRMISGQEQPDSGtitlgeTVKLASVDQFRDsmdnsktvweevsggldimkigntempsray 427
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG------GVIYIDGEDILE------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 428 VGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIET---------LRALENALLEFPGCAMVIS 498
Cdd:smart00382 44 EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTT 123
|
170
....*....|....*...
gi 2788209839 499 HDR-WFLDRIATHILDYQ 515
Cdd:smart00382 124 NDEkDLGPALLRRRFDRR 141
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
323-476 |
1.93e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.70 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTI-------------TLGETVKLA 389
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldyskrgLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 390 SVDQFRDSMDNSKTVWEEVSGGLDIMKIGNTEMPSRAYVGrfnFKGVD-QGKR---VGELSGGERGRLHLAKLLQVGGNM 465
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEA---LTLVDaQHFRhqpIQCLSHGQKKRVAIAGALVLQARY 157
|
170
....*....|.
gi 2788209839 466 LLLDEPTNDLD 476
Cdd:PRK13638 158 LLLDEPTAGLD 168
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-194 |
2.00e-07 |
|
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: 53.53 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 12 GKVVPPKRhILKNISLSFFPGAKIGVLGLNGAGKSTL----LRIMAG------IDKDIEG----EARP-QPDIKIGYlpQ 76
Cdd:COG4172 293 RRTVGHVK-AVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPSegeirfDGQDLDGlsrrALRPlRRRMQVVF--Q 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 77 EP--QLNPEHTVRESIEE--AVSEVvnalkrldevyalyadpdadfdKLAAEQgRLEEIIQAHDGhnlnVQLErAADALR 152
Cdd:COG4172 370 DPfgSLSPRMTVGQIIAEglRVHGP----------------------GLSAAE-RRARVAEALEE----VGLD-PAARHR 421
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2788209839 153 LPdwdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:COG4172 422 YP------HEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
346-511 |
2.20e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.37 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 346 IPK-GAIVGIIGPNGAGKSTLFRMISGQEQPDSG------------------------TITLGETVKLASVDQFRDSMdn 400
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildefrgselqnyfTKLLEGDVKVIVKPQYVDLI-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 401 SKTVWEEVSGGLDimKIGNTEMPSRaYVGRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIE-- 478
Cdd:cd03236 100 PKAVKGKVGELLK--KKDERGKLDE-LVDQLELRHVLD-RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqr 175
|
170 180 190
....*....|....*....|....*....|....
gi 2788209839 479 -TLRALENALLEFPGCAMVISHDRWFLDRIATHI 511
Cdd:cd03236 176 lNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
324-485 |
2.32e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.78 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRL-----LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLgetvklasvdQFRDSM 398
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW----------IFKDEK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 DNSKTVWEEVSGGLDIM------KIGNTEmPSRAYVGR-FNFK--------------------GVDQG----------KR 441
Cdd:PRK13651 73 NKKKTKEKEKVLEKLVIqktrfkKIKKIK-EIRRRVGVvFQFAeyqlfeqtiekdiifgpvsmGVSKEeakkraakyiEL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 442 VG-----------ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD----IETLRALEN 485
Cdd:PRK13651 152 VGldesylqrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDN 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
323-488 |
2.77e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYG--DRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVD-------- 392
Cdd:TIGR01257 1937 ILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISdvhqnmgy 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 393 --QFrDSMDNSKT------VWEEVSG--GLDIMKIGNTEMPS---RAYVGRFnfkgvdqgkrVGELSGGERGRLHLAKLL 459
Cdd:TIGR01257 2017 cpQF-DAIDDLLTgrehlyLYARLRGvpAEEIEKVANWSIQSlglSLYADRL----------AGTYSGGNKRKLSTAIAL 2085
|
170 180
....*....|....*....|....*....
gi 2788209839 460 QVGGNMLLLDEPTNDLDIETLRALENALL 488
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-214 |
3.52e-07 |
|
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: 52.80 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMA---GIDK-DIEGEARPQPDIKIGYLPQEPQLNPEHTV--RESIEE 92
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPrfyEPDSgQILLDGHDLADYTLASLRRQVALVSQDVVlfNDTIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 93 AVsevvnALKRLDEVyalyadPDADFDKlAAEQGRLEEIIqahDGHNLNVQLERAADAlrlpdwdakiANLSGGERRRVA 172
Cdd:TIGR02203 425 NI-----AYGRTEQA------DRAEIER-ALAAAYAQDFV---DKLPLGLDTPIGENG----------VLLSGGQRQRLA 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2788209839 173 LCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVA 214
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESerlvQAALERLMQGRTTLVIA 525
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
320-476 |
3.63e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 52.01 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 320 GDKVLEVSNLRKSYGD------RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLG--ETVKLASV 391
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDglDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 392 DQFRDSM-------DN---SKTVWEEVSGGLDIMKIGNTEMPSRayvgrfnfkgVDQG-KRVGE----------LSGGER 450
Cdd:PRK13633 81 WDIRNKAgmvfqnpDNqivATIVEEDVAFGPENLGIPPEEIRER----------VDESlKKVGMyeyrrhaphlLSGGQK 150
|
170 180
....*....|....*....|....*.
gi 2788209839 451 GRLHLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-217 |
3.68e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 52.11 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 9 HRVGKVVP-PKRHI--LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE------------------ARPQp 67
Cdd:PRK11153 5 KNISKVFPqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRvlvdgqdltalsekelrkARRQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 68 dikIGYLPQEPQLNPEHTVRESIeeavsevvnALkrldevyALYAD--PDADFDKlaaeqgRLEEIIQAhdghnlnVQLE 145
Cdd:PRK11153 84 ---IGMIFQHFNLLSSRTVFDNV---------AL-------PLELAgtPKAEIKA------RVTELLEL-------VGLS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 146 RAADalRLPdwdakiANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SV-AWLERFLHDFEGTVVAITH 217
Cdd:PRK11153 132 DKAD--RYP------AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAttrSIlELLKDINRELGLTIVLITH 199
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
297-489 |
4.13e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.92 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 297 LNSTEYQKRNETNELFIPPGPRLGDKVLEVsnlrKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRM-------- 368
Cdd:PRK11174 328 LETPLAHPQQGEKELASNDPVTIEAEDLEI----LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAllgflpyq 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 369 ----ISGQE--------------------QPDSGTI----TLGEtvKLASVDQFRDSMDNSKtVWEEVSG---GLDIMkI 417
Cdd:PRK11174 404 gslkINGIElreldpeswrkhlswvgqnpQLPHGTLrdnvLLGN--PDASDEQLQQALENAW-VSEFLPLlpqGLDTP-I 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 418 GntempsrayvgrfnfkgvDQGKRvgeLSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLE 489
Cdd:PRK11174 480 G------------------DQAAG---LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA 530
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
162-217 |
4.15e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 4.15e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF----EGTVVAITH 217
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdkaDKTIITIAH 1417
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-198 |
4.72e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEA----------RPQPDIKIGYLPQEPQLNPEHTVRESI 90
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferqsikkdLCTYQKQLCFVGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 91 EEAVSEVVNALKrLDEVYALYadpdadfdklaaeqgRLEEIIqahdghnlnvqleraadalrlpdwDAKIANLSGGERRR 170
Cdd:PRK13540 96 LYDIHFSPGAVG-ITELCRLF---------------SLEHLI------------------------DYPCGLLSSGQKRQ 135
|
170 180
....*....|....*....|....*...
gi 2788209839 171 VALCRLLLEKPDMLLLDEPTNHLDAESV 198
Cdd:PRK13540 136 VALLRLWMSKAKLWLLDEPLVALDELSL 163
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
324-500 |
5.11e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 50.39 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRkSYGDRLLIDdlsfsIPKGaIVGIIGPNGAGKSTLF------------RMISGQEQ-----PDSGTITL---- 382
Cdd:COG0419 5 LRLENFR-SYRDTETID-----FDDG-LNLIVGPNGAGKSTILeairyalygkarSRSKLRSDlinvgSEEASVELefeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 383 -----------GETVKLAS---------------VDQFRDSMDNSKTVWEEVSGGLDimKIGNTEMPSRAYVGRFN-FKG 435
Cdd:COG0419 78 ggkryrierrqGEFAEFLEakpserkealkrllgLEIYEELKERLKELEEALESALE--ELAELQKLKQEILAQLSgLDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 436 VDQgkrvgeLSGGERGRLHLAKLLQvggnmLLLDepTNDLDIETLRALENALLEfpgcAMVISHD 500
Cdd:COG0419 156 IET------LSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-251 |
6.06e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 52.33 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKST---LLRIMAGIDkdiEGEarpqpdIKI-GYLPQEPQLNpehTVRESIEeAVSEV 97
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTianLLTRFYDID---EGE------ILLdGHDLRDYTLA---SLRNQVA-LVSQN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 98 VNalkrldevyaLYADPDADFDKLAA-EQGRLEEIIQAhdghnlnvqlERAADAL----RLPD-WDAKI----ANLSGGE 167
Cdd:PRK11176 426 VH----------LFNDTIANNIAYARtEQYSREQIEEA----------ARMAYAMdfinKMDNgLDTVIgengVLLSGGQ 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 168 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG--TVVAITHDRYFLDNvAGWILELDRGEgIPWEGNYS 245
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAHRLSTIEK-ADEILVVEDGE-IVERGTHA 563
|
....*.
gi 2788209839 246 SWLEQK 251
Cdd:PRK11176 564 ELLAQN 569
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-198 |
6.18e-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: 50.34 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI---DKDIEG----------EARPQPDIKIGYLPQEPQLNPE 83
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGdihyngipykEFAEKYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 84 HTVRESIEEAVSevvnalkrldevyalyadpdadfdklaaEQGrleeiiqahdghnlnvqleraadalrlpdwDAKIANL 163
Cdd:cd03233 98 LTVRETLDFALR----------------------------CKG------------------------------NEFVRGI 119
|
170 180 190
....*....|....*....|....*....|....*
gi 2788209839 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV 198
Cdd:cd03233 120 SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-286 |
6.51e-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: 52.64 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKrhiLKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPdiKIGYLPQEPQLNPEhTVRESIeeavs 95
Cdd:TIGR00957 651 PPT---LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--SVAYVPQQAWIQND-SLRENI----- 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 96 evvnalkrldevyaLYADPdadfdklaAEQGRLEEIIQAhdghnlnvqLERAADALRLPDWD-----AKIANLSGGERRR 170
Cdd:TIGR00957 720 --------------LFGKA--------LNEKYYQQVLEA---------CALLPDLEILPSGDrteigEKGVNLSGGQKQR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 171 VALCRLLLEKPDMLLLDEPTNHLDA-------ESVAWLERFLHDfeGTVVAITHDRYFLDNVaGWILELDRGEgIPWEGN 243
Cdd:TIGR00957 769 VSLARAVYSNADIYLFDDPLSAVDAhvgkhifEHVIGPEGVLKN--KTRILVTHGISYLPQV-DVIIVMSGGK-ISEMGS 844
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2788209839 244 YSSWLeQKDQRLAQEASQEAARRKSIEKELEWVR-QGTKGRQSK 286
Cdd:TIGR00957 845 YQELL-QRDGAFAEFLRTYAPDEQQGHLEDSWTAlVSGEGKEAK 887
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
323-499 |
6.59e-07 |
|
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: 52.13 E-value: 6.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISG---QEQPDSGTITLGETVKLASVdqfRDS-- 397
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvypHGTWDGEIYWSGSPLKASNI---RDTer 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 398 -----------MDNSKTVWEEVSGGLDIMKIGN----TEMPSRAY--VGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQ 460
Cdd:TIGR02633 78 agiviihqeltLVPELSVAENIFLGNEITLPGGrmayNAMYLRAKnlLRELQLDADNVTRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2788209839 461 VGGNMLLLDEPTNDLDIETLRALENAL--LEFPGCAMV-ISH 499
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIrdLKAHGVACVyISH 199
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
22-197 |
8.10e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE-----------ARPQpdikIGYLPQEPQLNPEHTVRESi 90
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNiyykncninniAKPY----CTYIGHNLGLKLEMTVFEN- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 91 eeavsevvnaLKRLDEVYalyadpdadfdklaaeqgrleeiiqahdghNLNVQLERAADALRLPDW-DAKIANLSGGERR 169
Cdd:PRK13541 91 ----------LKFWSEIY------------------------------NSAETLYAAIHYFKLHDLlDEKCYSLSSGMQK 130
|
170 180
....*....|....*....|....*...
gi 2788209839 170 RVALCRLLLEKPDMLLLDEPTNHLDAES 197
Cdd:PRK13541 131 IVAIARLIACQSDLWLLDEVETNLSKEN 158
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-235 |
8.18e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.02 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEG---------------EARPQPDIKIGYLPQEPQLnpehtV 86
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsnknesepsfeATRSRNRYSVAYAAQKPWL-----L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 87 RESIEEAVSevvnalkrldevyalYADPdadFDKlaaeqGRLEEIIQAhdghnlnVQLERAADALRLPDwDAKIA----N 162
Cdd:cd03290 92 NATVEENIT---------------FGSP---FNK-----QRYKAVTDA-------CSLQPDIDLLPFGD-QTEIGergiN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 163 LSGGERRRVALCRLLLEKPDMLLLDEP--------TNHLDAESVAwleRFLHDFEGTVVAITHDRYFLDNvAGWILELDR 234
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPfsaldihlSDHLMQEGIL---KFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKD 216
|
.
gi 2788209839 235 G 235
Cdd:cd03290 217 G 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-238 |
1.06e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.60 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEarpqpdIKI-GYlpqepQLNPEHTVResieeavsevvnA 100
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGT------ITIaGY-----HITPETGNK------------N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 101 LKRL-DEVYALYADPDADFdklaAEQGRLEEIiqAHDGHNLNVQLERAADA----LRLPDWDAKIAN-----LSGGERRR 170
Cdd:PRK13641 80 LKKLrKKVSLVFQFPEAQL----FENTVLKDV--EFGPKNFGFSEDEAKEKalkwLKKVGLSEDLISkspfeLSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788209839 171 VALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG---TVVAITHDryfLDNVAGW---ILELDRGEGI 238
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHN---MDDVAEYaddVLVLEHGKLI 224
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
324-499 |
1.20e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 51.26 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSY-GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTI--------TLGETV---KLASV 391
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrplsSLSHSVlrqGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 392 DQfrDSMDNSKTVWEEVSGGLDIMKIG---NTEMPSRAYVGRFNFKGVDQgkRVGE----LSGGERGRLHLAKLLQVGGN 464
Cdd:PRK10790 421 QQ--DPVVLADTFLANVTLGRDISEEQvwqALETVQLAELARSLPDGLYT--PLGEqgnnLSVGQKQLLALARVLVQTPQ 496
|
170 180 190
....*....|....*....|....*....|....*..
gi 2788209839 465 MLLLDEPTNDLDIETLRALENALLEFPGCA--MVISH 499
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTtlVVIAH 533
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
339-520 |
1.31e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 50.16 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETV---------------KLASVDQFRDSMDNSKT 403
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyirpvrkRIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 404 VWEEVSGGLDIMKIGNTEMPSRAY--VGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD----I 477
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVKNYAHrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqskR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2788209839 478 ETLRALENALLEFPGCAMVISHDrwfLDRIAThildYQDEGKV 520
Cdd:PRK13646 183 QVMRLLKSLQTDENKTIILVSHD---MNEVAR----YADEVIV 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-194 |
1.33e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.35 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE--------ARPQPDI------KIGYLPQEP--QLNPEHT 85
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGElyyqgqdlLKADPEAqkllrqKIQIVFQNPygSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 86 VRESIEEAVseVVNAlkrldevyalyadpdadfdKLAAEQgRLEEIIQ--AHdghnlnVQLeRAADALRLPDWdakianL 163
Cdd:PRK11308 111 VGQILEEPL--LINT-------------------SLSAAE-RREKALAmmAK------VGL-RPEHYDRYPHM------F 155
|
170 180 190
....*....|....*....|....*....|.
gi 2788209839 164 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
327-476 |
1.36e-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: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 327 SNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPD---SGTITL-GETVKLASVDQFRDSMDNSK 402
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYnGIPYKEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 403 --------TVWEEVSGGLDiMKiGNtempsrAYVgrfnfKGVdqgkrvgelSGGERGRLHLAKLLQVGGNMLLLDEPTND 474
Cdd:cd03233 91 edvhfptlTVRETLDFALR-CK-GN------EFV-----RGI---------SGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
..
gi 2788209839 475 LD 476
Cdd:cd03233 149 LD 150
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-226 |
1.36e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 50.23 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE----ARPQPDIKIGYLPQEPQL-----NPEHTV-RES 89
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRilfdGKPIDYSRKGLMKLRESVgmvfqDPDNQLfSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 90 IEEAVS-EVVNALKRLDEVyalyadpdadfdklaaeQGRLEEIiqahdghnlnvqLERAADAlrlPDWDAKIANLSGGER 168
Cdd:PRK13636 100 VYQDVSfGAVNLKLPEDEV-----------------RKRVDNA------------LKRTGIE---HLKDKPTHCLSFGQK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788209839 169 RRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHDryfLDNVA 226
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD---IDIVP 206
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-194 |
1.97e-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: 50.59 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 14 VVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-DKDIEGEA----------RPQPDI--KIGYLPQEPQ- 79
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVfingkpvdirNPAQAIraGIAMVPEDRKr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 80 --LNPEHTVRESIEEAVSEVVNALKRLDEvyalyadpdadfdklAAEQGRLEEIIQahdghnlnvQLERAADALRLPdwd 157
Cdd:TIGR02633 348 hgIVPILGVGKNITLSVLKSFCFKMRIDA---------------AAELQIIGSAIQ---------RLKVKTASPFLP--- 400
|
170 180 190
....*....|....*....|....*....|....*..
gi 2788209839 158 akIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:TIGR02633 401 --IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
336-500 |
2.05e-06 |
|
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: 47.74 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 336 RLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMIsgqeqpdsGTITLGETVKLASVDQFrdsmdnsktvweevsggldim 415
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAI--------GLALGGAQSATRRRSGV--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 416 KIGNTEMPSRAyvgRFNFkgvdqgkRVGELSGGERGRLHLAKLLQ----VGGNMLLLDEPTNDLDIETLRALENALLEF- 490
Cdd:cd03227 59 KAGCIVAAVSA---ELIF-------TRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHl 128
|
170
....*....|..
gi 2788209839 491 -PGC-AMVISHD 500
Cdd:cd03227 129 vKGAqVIVITHL 140
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
339-476 |
2.49e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 50.71 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVklASVDQfrDSMDNSKTVWEEVSGGLDIMK-- 416
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV--AYVPQ--QAWIQNDSLRENILFGKALNEky 729
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 417 ----------IGNTEM-PS--RAYVGRfnfKGVDqgkrvgeLSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:TIGR00957 730 yqqvleacalLPDLEIlPSgdRTEIGE---KGVN-------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-213 |
2.57e-06 |
|
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: 47.81 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE--------ARPQP----DIKIGYLPQEPQ---LNPEHTV 86
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEitldgkpvTRRSPrdaiRAGIAYVPEDRKregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 87 RESIeeavsevvnALKRLdevyalyadpdadfdklaaeqgrleeiiqahdghnlnvqleraadalrlpdwdakianLSGG 166
Cdd:cd03215 96 AENI---------ALSSL----------------------------------------------------------LSGG 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2788209839 167 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVV 213
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELadAGKAV 157
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-194 |
2.65e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.10 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLL----RIMAGIDKDIEGEARPQPDIKI-------GYLPQEPQLNPEhTVRES 89
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLsliqRHFDVSEGDIRFHDIPLTKLQLdswrsrlAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 90 IeeavsevvnALKRldevyalyadPDadfdklaAEQGRLEEIIQAHDGHNlnvqleraaDALRLPD-WDAKIAN----LS 164
Cdd:PRK10789 409 I---------ALGR----------PD-------ATQQEIEHVARLASVHD---------DILRLPQgYDTEVGErgvmLS 453
|
170 180 190
....*....|....*....|....*....|
gi 2788209839 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:PRK10789 454 GGQKQRISIARALLLNAEILILDDALSAVD 483
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-236 |
2.79e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 49.28 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK-----------DIEGEARPQPDI--KIGYLPQEP--QL 80
Cdd:PRK13637 17 PFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKptsgkiiidgvDITDKKVKLSDIrkKVGLVFQYPeyQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 81 NpEHTVRESIE-------EAVSEVVNALKRLDEVYALyadpdaDFDKLAaeqgrleeiiqahdghnlnvqleraadalrl 153
Cdd:PRK13637 97 F-EETIEKDIAfgpinlgLSEEEIENRVKRAMNIVGL------DYEDYK------------------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 154 pdwDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHD-FEGTVVAITHDRYFLDNVAGWI 229
Cdd:PRK13637 139 ---DKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrDEILNKIKELHKeYNMTIILVSHSMEDVAKLADRI 215
|
....*..
gi 2788209839 230 LELDRGE 236
Cdd:PRK13637 216 IVMNKGK 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
163-226 |
3.47e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.97 E-value: 3.47e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788209839 163 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDFEGTVVAITHdryFLDNVA 226
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLfkkLHQSGMTIVLVTH---LMDDVA 209
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-218 |
3.65e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 48.62 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFfPGAKI-GVLGLNGAGKSTLLRIMAGIDKDIEGeARPQPdiKIGYLPQE---PQLNPehtvresieeavsev 97
Cdd:PRK14243 26 VKNVWLDI-PKNQItAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEG--KVTFHGKNlyaPDVDP--------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 98 VNALKRLDEVYAL-YADPDADFDKLA------AEQGRLEEIIQAhdghnlnvQLERAA------DALRlpdwDAKIAnLS 164
Cdd:PRK14243 87 VEVRRRIGMVFQKpNPFPKSIYDNIAygarinGYKGDMDELVER--------SLRQAAlwdevkDKLK----QSGLS-LS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITHD 218
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTHN 209
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-236 |
4.07e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.59 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEArpqpdikigYLPQEPQlnpehtvresieeavsevvnAL 101
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI---------LLDGKPV--------------------TA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 102 KRLDEVYALYADPDAD---FDKLAAEQGrleeiiQAHDGHNLNVQLER--AADALRLPDWdaKIAN--LSGGERRRVALC 174
Cdd:PRK10522 390 EQPEDYRKLFSAVFTDfhlFDQLLGPEG------KPANPALVEKWLERlkMAHKLELEDG--RISNlkLSKGQKKRLALL 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 175 RLLLEKPDMLLLDEPTNHLDAEsvawLERF--------LHDFEGTVVAITHDRYFLDNvAGWILELDRGE 236
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPH----FRREfyqvllplLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQ 526
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
326-516 |
4.37e-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: 50.01 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 326 VSNLRKSY--GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFRDSMD---- 399
Cdd:TIGR01257 931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGmcpq 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 400 -----NSKTV--------------WEEVSGGLDIMkIGNTEMPSRayvgrfnfkgvdQGKRVGELSGGERGRLHLAKLLQ 460
Cdd:TIGR01257 1011 hnilfHHLTVaehilfyaqlkgrsWEEAQLEMEAM-LEDTGLHHK------------RNEEAQDLSGGMQRKLSVAIAFV 1077
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 461 VGGNMLLLDEPTNDLDIETLRALENALLEFPGCAMVIshdrwfldrIATHILDYQD 516
Cdd:TIGR01257 1078 GDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTII---------MSTHHMDEAD 1124
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
327-499 |
4.75e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 327 SNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTIT-LGETVKLASVdqfRDSMDNS-KTV 404
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILfQGKEIDFKSS---KEALENGiSMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 405 WEEVSGGLDIMKIGNTempsraYVGRFNFKG--VDQGK--------------------RVGELSGGERGRLHLAKLLQVG 462
Cdd:PRK10982 79 HQELNLVLQRSVMDNM------WLGRYPTKGmfVDQDKmyrdtkaifdeldididpraKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2788209839 463 GNMLLLDEPTNDL---DIETLRALENALLEfPGCAMV-ISH 499
Cdd:PRK10982 153 AKIVIMDEPTSSLtekEVNHLFTIIRKLKE-RGCGIVyISH 192
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
13-226 |
5.16e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 48.24 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 13 KVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQpDIKIGYLPQEPQLNPehtVResiee 92
Cdd:PRK13646 14 KGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDKYIRP---VR----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 93 avsevvnalKRLDEVYALyadPDADFDKLAAEQgrleEIIQAHDGHNLNVQ--LERAADALRLPDWDAKIANLS-----G 165
Cdd:PRK13646 85 ---------KRIGMVFQF---PESQLFEDTVER----EIIFGPKNFKMNLDevKNYAHRLLMDLGFSRDVMSQSpfqmsG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 166 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFE----GTVVAITHDryfLDNVA 226
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHD---MNEVA 210
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
160-223 |
5.43e-06 |
|
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: 47.22 E-value: 5.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 160 IANLSGGERR------RVALCRLLLEKPDMLLLDEPTNHLDAESVAW-----LERFLHDFEGTVVAITHDRYFLD 223
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVD 187
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
321-500 |
6.39e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 48.49 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 321 DKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFRD--- 396
Cdd:PRK10070 26 EQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIdGVDIAKISDAELREvrr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 397 ----------SMDNSKTVWEEVSGGLDIMKIGNTEMPSRAyvgrfnfkgVDQGKRVG----------ELSGGERGRLHLA 456
Cdd:PRK10070 106 kkiamvfqsfALMPHMTVLDNTAFGMELAGINAEERREKA---------LDALRQVGlenyahsypdELSGGMRQRVGLA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788209839 457 KLLQVGGNMLLLDEPTNDLDIETLRALENALLEFPG----CAMVISHD 500
Cdd:PRK10070 177 RALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAkhqrTIVFISHD 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
323-485 |
9.99e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 47.29 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRL-LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-----GETVKLASVD---- 392
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtGDFSKLQGIRklvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 393 ---QFRDSMDNSKTVWEEVSGGLDIMKIGNTEMPSR-----AYVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGN 464
Cdd:PRK13644 81 ivfQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRvdralAEIGLEKYR----HRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180
....*....|....*....|..
gi 2788209839 465 MLLLDEPTNDLDIETLRA-LEN 485
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAvLER 178
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
322-395 |
1.07e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.04 E-value: 1.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 322 KVLEVSNLRKSYGDR-LLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL-GETVKLASVDQFR 395
Cdd:PRK10522 321 QTLELRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPVTAEQPEDYR 396
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-241 |
1.20e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.39 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdkdiegearpqpdikigYLPQEPQLNPEhTVRESIEEAVSEVVNAL 101
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL-----------------LIPSEGKVYVD-GLDTSDEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 102 KrldevyALYADPDadfDKLAAEQgrLEEIIqAHDGHNLNVQLE----RAADAL-RLPDWDAKIAN---LSGGERRRVAL 173
Cdd:PRK13633 88 G------MVFQNPD---NQIVATI--VEEDV-AFGPENLGIPPEeireRVDESLkKVGMYEYRRHAphlLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 174 CRLLLEKPDMLLLDEPTNHLDA----ESVAWLERFLHDFEGTVVAITHdryFLDNV--AGWILELDRG----EGIPWE 241
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPsgrrEVVNTIKELNKKYGITIILITH---YMEEAveADRIIVMDSGkvvmEGTPKE 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
13-241 |
1.57e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.92 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 13 KVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----DKDIEGEARPQPDIK-----------IGYLPQ 76
Cdd:PRK13645 18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetGQTIVGDYAIPANLKkikevkrlrkeIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 77 EPQLnpeHTVRESIEEAVS-EVVNALKRLDEVYAlyadpdadfdklaaeqgRLEEIIqahdghnlnvqleraaDALRLPD 155
Cdd:PRK13645 98 FPEY---QLFQETIEKDIAfGPVNLGENKQEAYK-----------------KVPELL----------------KLVQLPE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 156 WDAKIA--NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDFEGTVVAITHDRYFLDNVAGWI 229
Cdd:PRK13645 142 DYVKRSpfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEV 221
|
250
....*....|....*.
gi 2788209839 230 LELDRGE----GIPWE 241
Cdd:PRK13645 222 IVMHEGKvisiGSPFE 237
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-218 |
1.82e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.41 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFfPGAKIGVL-GLNGAGKSTLLRIMAGIDKDIEGEAR--PQPDIK------IGYLPQEPQlnpehtVRESIEE 92
Cdd:PRK15056 23 LRDASFTV-PGGSIAALvGVNGSGKSTLFKALMGFVRLASGKISilGQPTRQalqknlVAYVPQSEE------VDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 93 AVSEVVnALKRLDEVYALyadpdadfdklaaeqgrleEIIQAHDGHNLNVQLERAaDALRLPDwdAKIANLSGGERRRVA 172
Cdd:PRK15056 96 LVEDVV-MMGRYGHMGWL-------------------RRAKKRDRQIVTAALARV-DMVEFRH--RQIGELSGGQKKRVF 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2788209839 173 LCRLLLEKPDMLLLDEPTNHLDAESVAW---LERFLHDFEGTVVAITHD 218
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARiisLLRELRDEGKTMLVSTHN 201
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
324-479 |
2.07e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 324 LEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAG--KSTLFRMISGqeqPDSGTITLGETVKLASVDQFRDSMDNS 401
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 402 KTV----WEEVSGGLDIMKIGNTEMPSRA--------YVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLD 469
Cdd:NF000106 91 RPVr*grRESFSGRENLYMIGR*LDLSRKdararadeLLERFSLTEA-AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170
....*....|
gi 2788209839 470 EPTNDLDIET 479
Cdd:NF000106 170 EPTTGLDPRT 179
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
339-381 |
2.22e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 2.22e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2788209839 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTIT 381
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
323-380 |
2.46e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 2.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 323 VLEVSNLRKSYGDRLLIDdLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTI 380
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI 57
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
162-226 |
3.36e-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: 44.49 E-value: 3.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE----SVAWLERFLHDFEGTVVAITHDRYFLDNVA 226
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLS 139
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
341-518 |
4.08e-05 |
|
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: 45.30 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 341 DLSFSIPKGAIVGIIGPNGAGKSTLF----------RMISGQEQPDSGT-ITLGETV-KLASVDQ-------------FR 395
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarRLHLKKEQPGNHDrIEGLEHIdKVIVIDQspigrtprsnpatYT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 396 DSMDNSKTVWEEVSGG-------LDIMKIGNT-----EMPsrAYVGRFNFKGVDQGKR-------VG-----------EL 445
Cdd:cd03271 93 GVFDEIRELFCEVCKGkrynretLEVRYKGKSiadvlDMT--VEEALEFFENIPKIARklqtlcdVGlgyiklgqpatTL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 446 SGGERGRLHLAKLLQ---VGGNMLLLDEPTNDL---DIETLRALENALLEFPGCAMVISHDrwfLD--RIATHILDYQDE 517
Cdd:cd03271 171 SGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLhfhDVKKLLEVLQRLVDKGNTVVVIEHN---LDviKCADWIIDLGPE 247
|
.
gi 2788209839 518 G 518
Cdd:cd03271 248 G 248
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
328-523 |
4.33e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.02 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 328 NLRKSYGDRLLidDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVkLASVDQ-------------- 393
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV-LFDAEKgiclppekrrigyv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 FRDS---------------MDNSKTV-WEEVSGGLDIMKIgntempsrayVGRFNfkgvdqgkrvGELSGGERGRLHLAK 457
Cdd:PRK11144 82 FQDArlfphykvrgnlrygMAKSMVAqFDKIVALLGIEPL----------LDRYP----------GSLSGGEKQRVAIGR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788209839 458 LLQVGGNMLLLDEPTNDLDI----ETLRALENALLEFPGCAMVISHDrwfLD---RIATHILdYQDEGKVEFF 523
Cdd:PRK11144 142 ALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHS---LDeilRLADRVV-VLEQGKVKAF 210
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
120-223 |
4.43e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 120 KLAAEQGRLEEIIQAHDGhnlNVQLERAADALRLPDWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA 199
Cdd:smart00382 21 ALARELGPPGGGVIYIDG---EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
90 100 110
....*....|....*....|....*....|...
gi 2788209839 200 WL---------ERFLHDFEGTVVAITHDRYFLD 223
Cdd:smart00382 98 LLllleelrllLLLKSEKNLTVILTTNDEKDLG 130
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
22-225 |
4.45e-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: 45.76 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGakIGVL-GLNGAGKSTLLRIMAGIdkdIEGEARPQPDIKIGYLPQEPQLnPEHTVRESIEEAVSEVVNA 100
Cdd:COG3593 14 IKDLSIELSDD--LTVLvGENNSGKSSILEALRLL---LGPSSSRKFDEEDFYLGDDPDL-PEIEIELTFGSLLSRLLRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 101 L---KRLDEVYALYADPDADFDKLAAE-QGRLEEII-QAHDGHNLNVQLERAADA-------LRLPDWDA-KIANLSGGE 167
Cdd:COG3593 88 LlkeEDKEELEEALEELNEELKEALKAlNELLSEYLkELLDGLDLELELSLDELEdllkslsLRIEDGKElPLDRLGSGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788209839 168 RRRV--ALCRLLLE-----KPDMLLLDEPTNHLDAESVAWLERFLHDFEGT---VVAITHDRYFLDNV 225
Cdd:COG3593 168 QRLIllALLSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKpnqVIITTHSPHLLSEV 235
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
159-238 |
5.74e-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: 43.85 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 159 KIANLSGGERRRVALCRLLLE--KPDMLLLDEPTNHLDAESvawLERFLHDFEG------TVVAITHDRYFLDNvAGWIL 230
Cdd:cd03238 84 KLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQD---INQLLEVIKGlidlgnTVILIEHNLDVLSS-ADWII 159
|
....*...
gi 2788209839 231 ELDRGEGI 238
Cdd:cd03238 160 DFGPGSGK 167
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
35-218 |
8.63e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.85 E-value: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 35 IGVLGLNGAGKSTLLR-IMAGIDKDIEGEARPQPDIkIGYLPQEPQLN--------------PEHTVRESIEEAVSEVVN 99
Cdd:COG0419 26 NLIVGPNGAGKSTILEaIRYALYGKARSRSKLRSDL-INVGSEEASVElefehggkryrierRQGEFAEFLEAKPSERKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 100 ALKRL--DEVYalyadpdadfDKLAAEQGRLEEIIQAHDGHNLNVQLERAADALRLPDWDAkIANLSGGERRRVALCRLL 177
Cdd:COG0419 105 ALKRLlgLEIY----------EELKERLKELEEALESALEELAELQKLKQEILAQLSGLDP-IETLSGGERLRLALADLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2788209839 178 lekpdMLLLDepTNHLDAESvawLERFLHDFEGTVVaITHD 218
Cdd:COG0419 174 -----SLILD--FGSLDEER---LERLLDALEELAI-ITHV 203
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
323-514 |
8.90e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQE--QPDSGTITL--GETVKLASVDQFRDSM 398
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFkgKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 DNSKTVWEEVSGGLDIMKIGNTEMPSRAYVG-----RFNFKGVDQGK---------------RVGeLSGGERGRLHLAKL 458
Cdd:PRK09580 81 FMAFQYPVEIPGVSNQFFLQTALNAVRSYRGqepldRFDFQDLMEEKiallkmpedlltrsvNVG-FSGGEKKRNDILQM 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788209839 459 LQVGGNMLLLDEPTNDLDIETLRALENallefpGCAMVISHDRWFLdrIATH---ILDY 514
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVAD------GVNSLRDGKRSFI--IVTHyqrILDY 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
298-392 |
1.40e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 298 NSTEYQKRNE-TNELF----IPP-------GPRLGD-KVLEVSNLRKSYGDRLLID---DLSFSIPKGAIVGIIGPNGAG 361
Cdd:PTZ00265 344 NITEYMKSLEaTNSLYeiinRKPlvennddGKKLKDiKKIQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCG 423
|
90 100 110
....*....|....*....|....*....|.
gi 2788209839 362 KSTLFRMISGQEQPDSGTITLGETVKLASVD 392
Cdd:PTZ00265 424 KSTILKLIERLYDPTEGDIIINDSHNLKDIN 454
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-218 |
1.41e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.96 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 24 NISLSFFPGAKIGVLGLNGAGKS-TLLRIMAGID--------------KDI----EGEARPQPDIKIGYLPQEP--QLNP 82
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgrvmaeklefngQDLqrisEKERRNLVGAEVAMIFQDPmtSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 83 EHTVRESIEEAvsevvnalkrldevyalyadpdadfdklaaeqgrleeiIQAHDGHNLNVQLERAADALRL---PDWDAK 159
Cdd:PRK11022 105 CYTVGFQIMEA--------------------------------------IKVHQGGNKKTRRQRAIDLLNQvgiPDPASR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788209839 160 IAN----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEG----TVVAITHD 218
Cdd:PRK11022 147 LDVyphqLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkenmALVLITHD 213
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
334-381 |
1.43e-04 |
|
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: 43.00 E-value: 1.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2788209839 334 GDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEqpDSGTIT 381
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK--TAGVIT 63
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
163-241 |
1.97e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 163 LSGGERRRVALCRLLLEK---PDMLLLDEPTNHLDAESVAWLERFLH---DFEGTVVAITHDryfLD--NVAGWILEL-- 232
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQrlvDKGNTVVVIEHN---LDviKTADYIIDLgp 906
|
90
....*....|....*..
gi 2788209839 233 ---DRG-----EGIPWE 241
Cdd:TIGR00630 907 eggDGGgtvvaSGTPEE 923
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
19-218 |
2.68e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 42.99 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGidkdiegeaRPQPDI-KIGYLPQEPQLNPEHTVRESIEEAvsev 97
Cdd:PRK11701 19 RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA---------RLAPDAgEVHYRMRDGQLRDLYALSEAERRR---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 98 vnaLKRLDEVYaLYADPdADFDKLAAEQG-----RLEEIIQAHDGhNLNVQ----LERAA-DALRLPDwdaKIANLSGGE 167
Cdd:PRK11701 86 ---LLRTEWGF-VHQHP-RDGLRMQVSAGgnigeRLMAVGARHYG-DIRATagdwLERVEiDAARIDD---LPTTFSGGM 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2788209839 168 RRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD 218
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRGLVRELGLAVVIVTHD 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-218 |
3.01e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.48 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GID--KDIEGEARPQPDIKIGYLPQEPQLNPEHTV 86
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNrlieptrgqvlidGVDiaKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 87 RESIEEAVsevvnalkrldevyalyadpdaDFDKLAAEQGRleeiiqahdghnlnvqlERAADALR----------LPDw 156
Cdd:PRK10070 124 LDNTAFGM----------------------ELAGINAEERR-----------------EKALDALRqvglenyahsYPD- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 157 dakiaNLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDFEGTVVAITHD 218
Cdd:PRK10070 164 -----ELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
19-251 |
3.30e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.55 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE----ARPQPDIKIGYLPQEPQLNPEHTV-------- 86
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEirldGRPLSSLSHSVLRQGVAMVQQDPVvladtfla 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 87 -----RESIEEAVSEVVNALKRLDEVYALyadPDADFDKLAaEQGRleeiiqahdghnlnvqleraadalrlpdwdakia 161
Cdd:PRK10790 434 nvtlgRDISEEQVWQALETVQLAELARSL---PDGLYTPLG-EQGN---------------------------------- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDF--EGTVVAITHDryfLDNV--AGWILELDRGEG 237
Cdd:PRK10790 476 NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHR---LSTIveADTILVLHRGQA 552
|
250
....*....|....
gi 2788209839 238 IPwEGNYSSWLEQK 251
Cdd:PRK10790 553 VE-QGTHQQLLAAQ 565
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
21-173 |
3.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 21 ILKNISLSFFPGAKIgVLGLNGAGKSTLLR-IMAGIDKDIEGEA----RPQPDIKIGYLPQEPQLNPEHTVRESIEEAVS 95
Cdd:COG4717 13 KFRDRTIEFSPGLNV-IYGPNEAGKSTLLAfIRAMLLERLEKEAdelfKPQGRKPELNLKELKELEEELKEAEEKEEEYA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 96 EVVNALKRLDEvyaLYADPDADFDKLAAEQGRLEEIIQAHDGHNLNVQLERAADAL--RLPDWDAKIANLSGGERRRVAL 173
Cdd:COG4717 92 ELQEELEELEE---ELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELpeRLEELEERLEELRELEEELEEL 168
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
323-371 |
4.17e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 4.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2788209839 323 VLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISG 371
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-200 |
7.92e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 42.32 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGE--------ARPQP----DIKIGYLPQEPQ---LNPEHTV 86
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSirldgediTGLSPrerrRLGVAYIPEDRLgrgLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 87 RESIeeavsevvnALKRLDEvyalyaDPDA-----DFDKLAAeqgRLEEIIQAHDghnlnvqleraadaLRLPDWDAKIA 161
Cdd:COG3845 354 AENL---------ILGRYRR------PPFSrggflDRKAIRA---FAEELIEEFD--------------VRTPGPDTPAR 401
|
170 180 190
....*....|....*....|....*....|....*....
gi 2788209839 162 NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAW 200
Cdd:COG3845 402 SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEF 440
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
322-363 |
8.82e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 40.53 E-value: 8.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2788209839 322 KVLEVSNLrKSYGDRLLIDdlsfsIPKGaIVGIIGPNGAGKS 363
Cdd:cd03278 2 KKLELKGF-KSFADKTTIP-----FPPG-LTAIVGPNGSGKS 36
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-54 |
8.83e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.17 E-value: 8.83e-04
10 20 30
....*....|....*....|....*....|....
gi 2788209839 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG 54
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-194 |
1.03e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--IDKDIEGEARpqpdiKIGylpQEPQLNpehTVRESIEEAV 94
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVF-----KDG---KEVDVS---TVSDAIDAGL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 95 SEVVNALKRldevYALYADPD-------ADFDKLAaEQG---RLEEIIQAHDghnlnvqlERAADALRLPDWDAKIANLS 164
Cdd:NF040905 340 AYVTEDRKG----YGLNLIDDikrnitlANLGKVS-RRGvidENEEIKVAEE--------YRKKMNIKTPSVFQKVGNLS 406
|
170 180 190
....*....|....*....|....*....|
gi 2788209839 165 GGERRRVALCRLLLEKPDMLLLDEPTNHLD 194
Cdd:NF040905 407 GGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
323-508 |
1.20e-03 |
|
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: 41.59 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 323 VLEVSNLRKSYGD----RLLIDDLSFSIPKGAIVGIIGPNGAGKS----TLFRMISGQEQPDSGTITL-GETVKLASVDQ 393
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFdGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 394 FRD------SMdnsktVWEEVSGGLD-IMKIGN---------TEMPSRAYVGRfnfkGVDQGKRVG-------------E 444
Cdd:COG4172 86 LRRirgnriAM-----IFQEPMTSLNpLHTIGKqiaevlrlhRGLSGAAARAR----ALELLERVGipdperrldayphQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788209839 445 LSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIeTLRA--LEnaLL-----EFpGCAMV-ISHD----RWFLDRIA 508
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQAqiLD--LLkdlqrEL-GMALLlITHDlgvvRRFADRVA 228
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
160-223 |
1.26e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.22 E-value: 1.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 160 IANLSGGERR---RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL---HDFEGTVVAITHDRYFLD 223
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLkelSRNGAQLILTTHSPLLLD 303
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-63 |
2.12e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.64 E-value: 2.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDK------DIEGEA 63
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMpnkgtvDIKGSA 87
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-91 |
3.32e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 3.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDIKIgyLPQEPQLNPEHTVRESIE 91
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV--IAISAGLSGQLTGIENIE 107
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
445-518 |
3.65e-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: 40.38 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 445 LSGGERGRLHLAKLLQ---VGGNMLLLDEPTNDL---DIETLRALENALLEFPGCAMVISHDrwfLDRI--ATHILDYQD 516
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLhfdDIKKLLEVLQRLVDKGNTVVVIEHN---LDVIktADYIIDLGP 906
|
..
gi 2788209839 517 EG 518
Cdd:TIGR00630 907 EG 908
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
335-479 |
5.11e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 39.70 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 335 DRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGET-----------VKLASVDQ----FRDSM- 398
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpltklqldswrSRLAVVSQtpflFSDTVa 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 --------DNSKTVWEEV----SGGLDIMKignteMPsrayvgrfnfkgvdQG--KRVGE----LSGGERGRLHLAKLLQ 460
Cdd:PRK10789 407 nnialgrpDATQQEIEHVarlaSVHDDILR-----LP--------------QGydTEVGErgvmLSGGQKQRISIARALL 467
|
170
....*....|....*....
gi 2788209839 461 VGGNMLLLDEPTNDLDIET 479
Cdd:PRK10789 468 LNAEILILDDALSAVDGRT 486
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
439-513 |
5.42e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 439 GKRVGELSGGERGRLHLAKllQVG----GNMLLLDEPT-------NDLDIET---LRALENALLefpgcamVISHDRWFL 504
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLAT--QIGsgltGVLYVLDEPSiglhqrdNRRLINTlkrLRDLGNTLI-------VVEHDEDTI 553
|
....*....
gi 2788209839 505 dRIATHILD 513
Cdd:TIGR00630 554 -RAADYVID 561
|
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
330-501 |
6.96e-03 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 39.12 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 330 RKSYGDRL--LIddLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITL---------GETVKLASVDQFRDSM 398
Cdd:COG4928 10 RKKYAESLanLI--KSSDADEPLVIGLDGEWGSGKTSFLNLIEKELESNEKVIVVyfnawlydgEEDLLAALLSEIAAEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 399 DNSKTVWEEVSGGldIMKIGNTEMPSRAYVGRFNFKGVDQGKRVGEL--SGGERGRLHLAKLLQVGGNML--LLDEPT-- 472
Cdd:COG4928 88 EKKKKKDKKAAKK--LKKYAKRLSKLALKAGLLGGPAEAVAEALKALlkKEYKSKKKSIEAFREELEELLkeLKGKRLvv 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 2788209839 473 --NDLD-------IETLRALeNALLEFPGCAMVISHDR 501
Cdd:COG4928 166 fiDDLDrcepdeaIEVLELI-KLFFDFPNVVFVLAFDR 202
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
144-218 |
8.65e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 38.05 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788209839 144 LERAA---DALRLPDWDAKIA-NLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFL----HDFEGTVVAI 215
Cdd:PRK11300 131 LDRAAtwlERVGLLEHANRQAgNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelrNEHNVTVLLI 210
|
...
gi 2788209839 216 THD 218
Cdd:PRK11300 211 EHD 213
|
|
| |
