|
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: 1208.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 1 MAQYVYSMLRVGKIVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPKL 80
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 81 NPEHTVREAVEEAVSELKNALNRLDEVYAAYADPDADFDKLAKEQGQLEAIIQSHDGHNLENQLERAAEALRLPEWDAKI 160
Cdd:PRK11819 82 DPEKTVRENVEEGVAEVKAALDRFNEIYAAYAEPDADFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPWDAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 161 EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPW 240
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 241 EGNYSSWLEQKDARLEQEAATEAARHKSIQKELEWIRQNPKGRQAKGKARLARFEELNSVDYQKRNETSELFIPPGPRLG 320
Cdd:PRK11819 242 EGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYEELLSEEYQKRNETNEIFIPPGPRLG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRDSMDD 400
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 401 SKTVWEEVSGGQDIMRIGNFEIPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETL 480
Cdd:PRK11819 402 NKTVWEEISGGLDIIKVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETL 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 481 RALENALLEFPGCAMVISHDRWFLDRIATHIIDYQDEGKVEFFEGNFTEYEEYKKRTLGNDAIQPRRMKYKRMSK 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: 1141.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 2 AQYVYSMLRVGKIVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPKLN 81
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 PEHTVREAVEEAVSELKNALNRLDEVYAAYADPDADFDKLAKEQGQLEAIIQSHDGHNLENQLERAAEALRLPEWDAKIE 161
Cdd:TIGR03719 81 PTKTVRENVEEGVAEIKDALDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDADVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPWE 241
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 242 GNYSSWLEQKDARLEQEAATEAARHKSIQKELEWIRQNPKGRQAKGKARLARFEELNSVDYQKRNETSELFIPPGPRLGD 321
Cdd:TIGR03719 241 GNYSSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRNETAEIYIPPGPRLGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 322 KVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRDSMDDS 401
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 402 KTVWEEVSGGQDIMRIGNFEIPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLR 481
Cdd:TIGR03719 401 KTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLR 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739061588 482 ALENALLEFPGCAMVISHDRWFLDRIATHIIDYQDEGKVEFFEGNFTEYEEYKKRTLGNDAIQPRRMKYKRM 553
Cdd:TIGR03719 481 ALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEEDKKRRLGEDADQPHRIKYKKL 552
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
17-533 |
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: 722.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPKLNPEHTVREAVEEAVSE 96
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLDTVLDGDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 97 LKNALNRLDEVYAAYADPDADFDKLAKEQGQLEAiiqsHDGHNLENQLERAAEALRLPE--WDAKIEKLSGGERRRVAIC 174
Cdd:COG0488 89 LRALEAELEELEAKLAEPDEDLERLAELQEEFEA----LGGWEAEARAEEILSGLGFPEedLDRPVSELSGGWRRRVALA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 175 RLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQKDAR 254
Cdd:COG0488 165 RALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQRAER 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 255 LEQEAATEAARHKSIQKELEWIRQN-PKGRQAK-GKARLARFEELNSVDYQKRNETSELFIPPGPRLGDKVLEINNLTKS 332
Cdd:COG0488 245 LEQEAAAYAKQQKKIAKEEEFIRRFrAKARKAKqAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKVLELEGLSKS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 333 YGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRDSMDDSKTVWEEVSGGQ 412
Cdd:COG0488 325 YGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTVLDELRDGA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 413 DimriGNFEIPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEFPG 492
Cdd:COG0488 405 P----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPG 480
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 739061588 493 CAMVISHDRWFLDRIATHIIDYQDeGKVEFFEGNFTEYEEY 533
Cdd:COG0488 481 TVLLVSHDRYFLDRVATRILEFED-GGVREYPGGYDDYLEK 520
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-527 |
3.82e-105 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 329.22 E-value: 3.82e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-IDTDiEGEARPQPGIKIGYLPQEPKLNPEHTVREAVEEAVSELKN 99
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGeVLLD-DGRIIYEQDLIVARLQQDPPRNVEGTVYDFVAEGIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 100 ALNRLDEVYAAYA-DPDadfDKLAKEQGQLEAIIQSHDGHNLENQLERAAEALRLPEwDAKIEKLSGGERRRVAICRLLL 178
Cdd:PRK11147 97 YLKRYHDISHLVEtDPS---EKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP-DAALSSLSGGWLRKAALGRALV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 179 EKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQKDARLEQE 258
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALRVE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 259 AATEAARHKSIQKELEWIRQNPKGRQAKGKARLARFEELNSVDYQKRNE--TSELFIPPGPRLGDKVLEINNLTKSYGDR 336
Cdd:PRK11147 253 ELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVmgTAKMQVEEASRSGKIVFEMENVNYQIDGK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 337 VLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRDSMDDSKTVWEEVS-GGQDIM 415
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNLAeGKQEVM 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 416 RIGNfeipSR---AYVGRFNFkgvdQGKR----VGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALL 488
Cdd:PRK11147 413 VNGR----PRhvlGYLQDFLF----HPKRamtpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLD 484
|
490 500 510
....*....|....*....|....*....|....*....
gi 739061588 489 EFPGCAMVISHDRWFLDRIATHIIDYQDEGKVEFFEGNF 527
Cdd:PRK11147 485 SYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGY 523
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
24-530 |
1.53e-77 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 254.05 E-value: 1.53e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 24 NISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPKLNPEHTVREAVEEAVSELKNALNR 103
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVIMGHTELWEVKQE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 104 LDEVYAAYADPDADFDKLAkeqgQLEAIIQSHDGHNLENqleRAAEALRlpEWDAKIEKLSG-------GERRRVAICRL 176
Cdd:PRK15064 99 RDRIYALPEMSEEDGMKVA----DLEVKFAEMDGYTAEA---RAGELLL--GVGIPEEQHYGlmsevapGWKLRVLLAQA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 177 LLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQKDARLE 256
Cdd:PRK15064 170 LFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQARE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 257 QEAATEAARHKSIQKELEWIRQ----NPKGRQAKGKARLARFEELNSVDYQKRNETSELFiPPGPRLGDKVLEINNLTKS 332
Cdd:PRK15064 250 RLLADNAKKKAQIAELQSFVSRfsanASKAKQATSRAKQIDKIKLEEVKPSSRQNPFIRF-EQDKKLHRNALEVENLTKG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 333 YGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLA-----SVDQFRDSMD--DSKTVW 405
Cdd:PRK15064 329 FDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGyyaqdHAYDFENDLTlfDWMSQW 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 406 EEVSGGQDIMRignfeipsrAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALEN 485
Cdd:PRK15064 409 RQEGDDEQAVR---------GTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNM 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 739061588 486 ALLEFPGCAMVISHDRWFLDRIATHIIDYQDEGkVEFFEGNFTEY 530
Cdd:PRK15064 480 ALEKYEGTLIFVSHDREFVSSLATRIIEITPDG-VVDFSGTYEEY 523
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-533 |
2.19e-68 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 232.37 E-value: 2.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 5 VYSMLRVGKIVppkRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-IDTDIEGEARPQpGIKIGYLPQE-PKLnp 82
Cdd:PRK10636 3 VFSSLQIRRGV---RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNeISADGGSYTFPG-NWQLAWVNQEtPAL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 83 EHTVREAVEEAVSELKNALNRLDEvyaayADPDADFDKLAKEQGQLEAI----IQSHdGHNLENQLERAAEALRLPewda 158
Cdd:PRK10636 77 PQPALEYVIDGDREYRQLEAQLHD-----ANERNDGHAIATIHGKLDAIdawtIRSR-AASLLHGLGFSNEQLERP---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 159 kIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGI 238
Cdd:PRK10636 147 -VSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 239 PWEGNYSSWLEQKDARLEQEAA---TEAARHKSIQKELEWIR-QNPKGRQAKGKARLARFEELNS---VDyqkrNETSEL 311
Cdd:PRK10636 226 EYTGNYSSFEVQRATRLAQQQAmyeSQQERVAHLQSYIDRFRaKATKAKQAQSRIKMLERMELIApahVD----NPFHFS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 312 FIPPgPRLGDKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASV 391
Cdd:PRK10636 302 FRAP-ESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 392 DQFRDSM---DDSKTvweevsggQDIMRIGNFEIPS--RAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNML 466
Cdd:PRK10636 381 AQHQLEFlraDESPL--------QHLARLAPQELEQklRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLL 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 467 LLDEPTNDLDVETLRALENALLEFPGCAMVISHDRWFLdRIATHIIDYQDEGKVEFFEGNFTEYEEY 533
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLL-RSTTDDLYLVHDGKVEPFDGDLEDYQQW 518
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
326-534 |
6.32e-67 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 225.71 E-value: 6.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 326 INNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQfRDSMDDSKTVW 405
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQ-EPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 406 EEVSGG----------------------QDIMRIGN----------FEIPSRA--YVGRFNFKGVDQGKRVGELSGGERG 451
Cdd:COG0488 80 DTVLDGdaelraleaeleeleaklaepdEDLERLAElqeefealggWEAEARAeeILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 452 RLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEFPGCAMVISHDRWFLDRIATHIIDYqDEGKVEFFEGNFTEYE 531
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILEL-DRGKLTLYPGNYSAYL 238
|
...
gi 739061588 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 |
2.42e-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: 185.73 E-value: 2.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQfrdsmddskt 403
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 404 vweevsggqdimrignfeipsrayvgrfnfkgvdqgkrvgeLSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRAL 483
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 739061588 484 ENALLEFPGCAMVISHDRWFLDRIATHIIDYQDEG 518
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
25-538 |
4.79e-51 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 186.60 E-value: 4.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 25 ISLSFfpGAKIGVLGLNGAGKSTLLRIMA-----GIDTD-----IEGEArpqPGIKIGYLP------QEPKLNPEHTVRE 88
Cdd:PLN03073 198 VTLAF--GRHYGLVGRNGTGKTTFLRYMAmhaidGIPKNcqilhVEQEV---VGDDTTALQcvlntdIERTQLLEEEAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 89 AVEEAVSELKNALNRLDEVYAAYADPDADFDKLAKEQGQLEAIiqshDGHNLEnqlERAAEALR----LPEWDAKIEK-L 163
Cdd:PLN03073 273 VAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELI----DAYTAE---ARAASILAglsfTPEMQVKATKtF 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 164 SGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGN 243
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGD 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 244 YSSWLEQKDARLE-QEAATEA-ARHKS-IQKELEWIRQNPKgRQAKGKARLARFEELNSVDyQKRNETSELFIPPGP--R 318
Cdd:PLN03073 426 YDTFERTREEQLKnQQKAFESnERSRShMQAFIDKFRYNAK-RASLVQSRIKALDRLGHVD-AVVNDPDYKFEFPTPddR 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 319 LGDKVLEINNLTKSY-GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFR-D 396
Cdd:PLN03073 504 PGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHvD 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 397 SMDDSKTVWEEvsggqdIMRI--GNFEIPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTND 474
Cdd:PLN03073 584 GLDLSSNPLLY------MMRCfpGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNH 657
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 475 LDVETLRALENALLEFPGCAMVISHDRwfldriatHIIDYQ-------DEGKVEFFEGNFTEYeeykKRTL 538
Cdd:PLN03073 658 LDLDAVEALIQGLVLFQGGVLMVSHDE--------HLISGSvdelwvvSEGKVTPFHGTFHDY----KKTL 716
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
18-236 |
1.17e-48 |
|
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: 165.31 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQepklnpehtvreaveeavsel 97
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 98 knalnrldevyaayadpdadfdklakeqgqleaiiqshdghnlenqleraaealrlpewdakiekLSGGERRRVAICRLL 177
Cdd:cd03221 71 -----------------------------------------------------------------LSGGEKMRLALAKLL 85
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 178 LEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-512 |
3.78e-47 |
|
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: 172.01 E-value: 3.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI--------------DTDIEGEARPQPGIKIGYLPQEPK--LNP 82
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphggrisgevlldGRDLLELSEALRGRRIGMVFQDPMtqLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 83 eHTVREAVEEAvseLKNalnrldevyaayadpdadfDKLAKEQGQLEAIiqshdghnlenqleRAAEALRLPE-WDAKIE 161
Cdd:COG1123 99 -VTVGDQIAEA---LEN-------------------LGLSRAEARARVL--------------ELLEAVGLERrLDRYPH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEG 237
Cdd:COG1123 142 QLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 238 IpwegnysswleqkdarlEQEAATEaarhksiqkelewIRQNPKGRQAKGKARLARFEElnsvdyqkrnetselfiPPGP 317
Cdd:COG1123 222 V-----------------EDGPPEE-------------ILAAPQALAAVPRLGAARGRA-----------------APAA 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 318 RLGDKVLEINNLTKSY-----GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTVKLASV 391
Cdd:COG1123 255 AAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSiLFDGKDLTKLSR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 392 DQFRD--------------SMDDSKTVWEEVSGGQDIMRIGNF-EIPSRAY-----VG---RFnfkgvdQGKRVGELSGG 448
Cdd:COG1123 335 RSLRElrrrvqmvfqdpysSLNPRMTVGDIIAEPLRLHGLLSRaERRERVAellerVGlppDL------ADRYPHELSGG 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739061588 449 ERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEF---PGCAMV-ISHDRWFLDRIATHII 512
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqreLGLTYLfISHDLAVVRYIADRVA 476
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
19-236 |
8.19e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.71 E-value: 8.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA----RPQPGI-------KIGYLPQEPKLnPEHTVR 87
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMpppewrrQVAYVPQEPAL-WGGTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 88 EAveeavselknalnrldevyaayadpdadfdklakeqgqLEAIIQSHDGHNLENQLERAAEALRLPE--WDAKIEKLSG 165
Cdd:COG4619 92 DN--------------------------------------LPFPFQLRERKFDRERALELLERLGLPPdiLDKPVERLSG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 166 GERRRVAICRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG4619 134 GERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
324-520 |
1.81e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 135.58 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTVKLASVDQFRD--SMDD 400
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEvRVLGEDVARDPAEVRRRigYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 401 SKTVWEEVSGGQ------DIMRIGNFEIPSRA--YVGRFNFKGVdQGKRVGELSGGERGRLHLAKLL----QVggnmLLL 468
Cdd:COG1131 81 EPALYPDLTVREnlrffaRLYGLPRKEARERIdeLLELFGLTDA-ADRKVGTLSGGMKQRLGLALALlhdpEL----LIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 469 DEPTNDLDVETLRALENALLEF--PGCAMVIS-HDRWFLDRIATHIIdYQDEGKV 520
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVA-IIDKGRI 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
321-512 |
7.26e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.06 E-value: 7.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL-VLGDTVKLAS-----VDQF 394
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrLFGKPPRRARrrigyVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 395 RDSMDDSK-TVWEEVSGGQDImRIGNFEIPSRAY----------VGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGG 463
Cdd:COG1121 84 AEVDWDFPiTVRDVVLMGRYG-RRGLFRRPSRADreavdealerVGLEDLA----DRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739061588 464 NMLLLDEPTNDLDVETLRALENALLEFP--GCAM-VISHDRWFLDRIATHII 512
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRreGKTIlVVTHDLGAVREYFDRVL 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-191 |
4.09e-35 |
|
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: 128.92 E-value: 4.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-----------ARPQPGIKIGYLPQEPKLNPEHTVREAV 90
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqdltddERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 91 EEAvselknalnrldevyaayadpdadfdklakeqgqleAIIQSHDGHNLENQLERAAEALRLPEW-----DAKIEKLSG 165
Cdd:pfam00005 81 RLG------------------------------------LLLKGLSKREKDARAEEALEKLGLGDLadrpvGERPGTLSG 124
|
170 180
....*....|....*....|....*.
gi 739061588 166 GERRRVAICRLLLEKPDMLLLDEPTN 191
Cdd:pfam00005 125 GQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-225 |
6.98e-35 |
|
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: 130.29 E-value: 6.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE----------ARPQPGIKIGYLPQEPKLNPEHTVRE 88
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEvlwngepirdAREDYRRRLAYLGHADGLKPELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 89 AVEeavselknalnrldeVYAAYADPDADfdklakeqgqleaiiqshdghnlENQLERAAEALRLPE-WDAKIEKLSGGE 167
Cdd:COG4133 95 NLR---------------FWAALYGLRAD-----------------------REAIDEALEAVGLAGlADLPVRQLSAGQ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 168 RRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAITHDRYFLDNV 225
Cdd:COG4133 137 KRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
325-512 |
2.70e-34 |
|
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: 128.81 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 325 EINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL-VLG-----DTVKLASVDQFRDSM 398
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrVFGkplekERKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 399 DDSK-TVWEEVSGGQDImRIGNFEIPSRAY----------VGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNMLL 467
Cdd:cd03235 81 RDFPiSVRDVVLMGLYG-HKGLFRRLSKADkakvdealerVGLSELA----DRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 739061588 468 LDEPTNDLDVETLRALENALLEF--PGCAM-VISHDRWFLDRIATHII 512
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELrrEGMTIlVVTHDLGLVLEYFDRVL 203
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
323-520 |
4.44e-34 |
|
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: 129.21 E-value: 4.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRDSM---- 398
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIgvlp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 399 -----DDSKTVWEEVSGGQDIMRIGNFEIPSRA--YVGRFNFkGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEP 471
Cdd:COG4555 81 derglYDRLTVRENIRYFAELYGLFDEELKKRIeeLIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739061588 472 TNDLDVETLRALENALLEF---PGCAMVISHDRWFLDRIATHIIdYQDEGKV 520
Cdd:COG4555 160 TNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVV-ILHKGKV 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
339-473 |
6.92e-34 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 125.84 E-value: 6.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDT-----------VKLASVDQFrDSMDDSKTVWEE 407
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrKEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 408 VSGGQDIMRIGNFEIPSRAYVGRFNFKGVDQGKRV-----GELSGGERGRLHLAKLLQVGGNMLLLDEPTN 473
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
323-512 |
9.85e-34 |
|
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: 128.62 E-value: 9.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTV-----------KLASV 391
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 392 DQFRDSMDDSkTVWEEVSGGqdimR---IGNFEIPSR----------AYVGRFNFKgvdqGKRVGELSGGERGRLHLAKL 458
Cdd:COG1120 81 PQEPPAPFGL-TVRELVALG----RyphLGLFGRPSAedreaveealERTGLEHLA----DRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739061588 459 LQVGGNMLLLDEPTNDLD----VETLRALEnALLEFPGCAMVIS-HDrwfLD---RIATHII 512
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDlahqLEVLELLR-RLARERGRTVVMVlHD---LNlaaRYADRLV 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
325-516 |
3.74e-33 |
|
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: 123.89 E-value: 3.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 325 EINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLgdtvklasvdqfrdsmddsktv 404
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 405 weevsGGQDIMRIGNFEIpsRAYVGrfnfkgvdqgkRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALE 484
Cdd:cd00267 59 -----DGKDIAKLPLEEL--RRRIG-----------YVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 739061588 485 NALLEF--PGCAMV-ISHDRWFLDRIATHIIDYQD 516
Cdd:cd00267 121 ELLRELaeEGRTVIiVTHDPELAELAADRVIVLKD 155
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
324-512 |
6.36e-33 |
|
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: 123.66 E-value: 6.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTVKLASVDQFR------- 395
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEiKVLGKDIKKEPEEVKRrigylpe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 -DSMDDSKTVWEevsggqdimrignfeipsrayvgrfNFKgvdqgkrvgeLSGGERGRLHLAKLLQVGGNMLLLDEPTND 474
Cdd:cd03230 81 ePSLYENLTVRE-------------------------NLK----------LSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 739061588 475 LDVETLRALENALLEFP--GCAMVI-SHDRWFLDRIATHII 512
Cdd:cd03230 126 LDPESRREFWELLRELKkeGKTILLsSHILEEAERLCDRVA 166
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
17-218 |
8.35e-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: 125.93 E-value: 8.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE----------------ARpqpgiKIGYLPQEPKL 80
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvlldgrdlaslsrrelAR-----RIAYVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 81 NPEHTVREAVeeavselknALNRLdevyaAYADPdadfdkLAKEQGQLEAIIqshdghnlenqlERAAEALRLPEW-DAK 159
Cdd:COG1120 87 PFGLTVRELV---------ALGRY-----PHLGL------FGRPSAEDREAV------------EEALERTGLEHLaDRP 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 160 IEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLD-AESVAWLE--RFLHDYEG-TVVAITHD 218
Cdd:COG1120 135 VDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDlAHQLEVLEllRRLARERGrTVVMVLHD 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
325-512 |
3.20e-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: 122.16 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 325 EINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLgdtvklasvdqfrdsmddsktv 404
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 405 weevsGGQDIMRIGNFEI-PSRAYV-------GRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:cd03214 59 -----DGKDLASLSPKELaRKIAYVpqalellGLAHLA----DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 739061588 477 V-------ETLRALENALlefpGCAMVIS-HDRWFLDRIATHII 512
Cdd:cd03214 130 IahqiellELLRRLARER----GKTVVMVlHDLNLAARYADRVI 169
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
324-513 |
3.45e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.00 E-value: 3.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL--------------------- 382
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdgkplsampppewrrqvayvp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 383 ------GDTVK--LASVDQFRDSMDDSKTVweevsggqdimrignfeipsRAYVGRFNFKGVDQGKRVGELSGGERGRLH 454
Cdd:COG4619 81 qepalwGGTVRdnLPFPFQLRERKFDRERA--------------------LELLERLGLPPDILDKPVERLSGGERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 455 LAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEFP----GCAMVISHDRWFLDRIATHIID 513
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLT 203
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-236 |
4.48e-32 |
|
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: 122.58 E-value: 4.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE---------ARPQPGI--KIGYLPQepklNPEH-- 84
Cdd:cd03225 13 ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvlvdgkdltKLSLKELrrKVGLVFQ----NPDDqf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 ---TVREavEEAVSeLKNalnrldevyaayadpdadfdklakeqgqleaiiQSHDGHNLENQLERAAEALRLPEW-DAKI 160
Cdd:cd03225 89 fgpTVEE--EVAFG-LEN---------------------------------LGLPEEEIEERVEEALELVGLEGLrDRSP 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 161 EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03225 133 FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-235 |
4.70e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 123.66 E-value: 4.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR------PQPGIKIGYLPQEPKLNPEH--TVREA 89
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQRAEVDWDFpiTVRDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 90 VeeavselknALNRLDEVYAayadpdadFDKLAKEQgqleaiiqshdghnlenqLERAAEALR----LPEWDAKIEKLSG 165
Cdd:COG1121 98 V---------LMGRYGRRGL--------FRRPSRAD------------------REAVDEALErvglEDLADRPIGELSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 166 GERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDRYFLDNVAGWILELDRG 235
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
18-236 |
1.51e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 122.09 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR----------PQPGIKIGYLPQEPKLNPEHTVR 87
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvardpAEVRRRIGYVPQEPALYPDLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 88 EAVEeavselknalnrldeVYAAYADpdadfdklakeqgqleaiiqsHDGHNLENQLERAAEALRLPEW-DAKIEKLSGG 166
Cdd:COG1131 92 ENLR---------------FFARLYG---------------------LPRKEARERIDELLELFGLTDAaDRKVGTLSGG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 167 ERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG1131 136 MKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaEGkTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
323-513 |
1.88e-31 |
|
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: 120.66 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFR------- 395
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRrrlaylg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 --DSMDDSKTVWEEVSGGQDIMRIGNFEIPSRAYVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTN 473
Cdd:COG4133 82 haDGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739061588 474 DLDVETLRALENALLEFP---GCAMVISHDRwfLDRIATHIID 513
Cdd:COG4133 161 ALDAAGVALLAELIAAHLargGAVLLTTHQP--LELAAARVLD 201
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-236 |
1.98e-31 |
|
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: 121.29 E-value: 1.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQepklNPEH 84
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLlkptsgevlvdGKDITKKNLRELRRKVGLVFQ----NPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 -----TVREaveeavselknalnrldEVyaAYAdPdadfdklaKEQGQLEAIIQshdghnlenqlERAAEALR---LPEW 156
Cdd:COG1122 87 qlfapTVEE-----------------DV--AFG-P--------ENLGLPREEIR-----------ERVEEALElvgLEHL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 157 -DAKIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDRYFLDNVAGWILEL 232
Cdd:COG1122 128 aDRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVL 207
|
....
gi 739061588 233 DRGE 236
Cdd:COG1122 208 DDGR 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
325-512 |
1.51e-30 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 118.34 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 325 EINNLTKSYGD--RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTVKLASVDQFR------ 395
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvLVDGKDLTKLSLKELRrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 ----DSMDDSKTVWEEVSGGQDIMRIGNFEIPSRA--YVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLD 469
Cdd:cd03225 81 fqnpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVeeALELVGLEGL-RDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 739061588 470 EPTNDLDVETLRALENALLEFPGCAM---VISHDRWFLDRIATHII 512
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKtiiIVTHDLDLLLELADRVI 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-512 |
5.30e-30 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 124.15 E-value: 5.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 31 PGAKIGVLGLNGAGKSTLLRIMAGI--------------DTDIE----------------GEARPqpGIKIGYLPQEPKl 80
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGElipnlgdyeeepswDEVLKrfrgtelqnyfkklynGEIKV--VHKPQYVDLIPK- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 81 npehtvreAVEEAVSELknaLNRLDEVYAayadpdadFDKLAKEQgqleaiiqshdghNLENQLERaaealrlpewdaKI 160
Cdd:PRK13409 175 --------VFKGKVREL---LKKVDERGK--------LDEVVERL-------------GLENILDR------------DI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 161 EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDyEGTVVAITHDRYFLDNVAGWILELdrgEG 237
Cdd:PRK13409 211 SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRqrlNVARLIRELAE-GKYVLVVEHDLAVLDYLADNVHIA---YG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 238 IPweGNYSSWLEQKDAR------LEQEAATEAARhksiqkelewIRQNPkgrqakgkarlARFEELNSVDYQKRnetsel 311
Cdd:PRK13409 287 EP--GAYGVVSKPKGVRvgineyLKGYLPEENMR----------IRPEP-----------IEFEERPPRDESER------ 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 312 fippgprlgDKVLEINNLTKSYGDRVLIDDLSFsIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLgdTVKLA-- 389
Cdd:PRK13409 338 ---------ETLVEYPDLTKKLGDFSLEVEGGE-IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--ELKISyk 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 390 ----------SVDQFRDSMDD---SKTVWEEVSGGQDIMRIgnFEipsrayvgrfnfkgvdqgKRVGELSGGERGRLHLA 456
Cdd:PRK13409 406 pqyikpdydgTVEDLLRSITDdlgSSYYKSEIIKPLQLERL--LD------------------KNVKDLSGGELQRVAIA 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 457 KLLQVGGNMLLLDEPTNDLDVE----TLRALENALLEFPGCAMVISHDRWFLDRIATHII 512
Cdd:PRK13409 466 ACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
324-532 |
1.12e-29 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 116.66 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSY-GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTVKLASVDQFRDSM--- 398
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEvLVDGKDITKKNLRELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 399 ----DD---SKTVWEEVSGGQDIMRIGNFEIPSR-----AYVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNML 466
Cdd:COG1122 81 fqnpDDqlfAPTVEEDVAFGPENLGLPREEIRERveealELVGLEHLA----DRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 467 LLDEPTNDLDVETLRALENALLEFP--GCAMV-ISHDRWFLDRIATHIIdYQDEGKVeFFEGN----FTEYEE 532
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNkeGKTVIiVTHDLDLVAELADRVI-VLDDGRI-VADGTprevFSDYEL 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
324-508 |
1.17e-29 |
|
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: 116.08 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRD------- 396
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNigmvfqd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 397 -SMDDSKTVWEEVSGGQDIMRIGNFEIPSRAY-----VGRFNFkgvdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDE 470
Cdd:cd03259 81 yALFPHLTVAENIAFGLKLRGVPKAEIRARVRellelVGLEGL----LNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 739061588 471 PTNDLDVET---LRALENALLEFPGCAMV-ISHDR----WFLDRIA 508
Cdd:cd03259 157 PLSALDAKLreeLREELKELQRELGITTIyVTHDQeealALADRIA 202
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-236 |
1.48e-29 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 114.42 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA--------RPQPGIK--IGYLPQEPKLNPEHTVR 87
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdikKEPEEVKrrIGYLPEEPSLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 88 EaveeavselknalnrldevyaayadpdadfdklakeqgqleaiiqshdghNLenqleraaealrlpewdakieKLSGGE 167
Cdd:cd03230 92 E--------------------------------------------------NL---------------------KLSGGM 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739061588 168 RRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03230 101 KQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-235 |
2.94e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 114.94 E-value: 2.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR--PQPGIK----IGYLPQEPKLNPEH--TVREAV 90
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfGKPLEKerkrIGYVPQRRSIDRDFpiSVRDVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 91 eeavselknALNRLDEVYAayadpdadFDKLAKEQgqleaiiqshdghnlenqLERAAEALRLPE----WDAKIEKLSGG 166
Cdd:cd03235 92 ---------LMGLYGHKGL--------FRRLSKAD------------------KAKVDEALERVGlselADRQIGELSGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739061588 167 ERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDYEGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELlreLRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
324-512 |
6.28e-29 |
|
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: 113.05 E-value: 6.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGdtvklasvdqfrdsmddskt 403
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 404 vweevsgGQDIMRIGNFEIPSRAYVG----RFN-FKGVDQGKRVGE-LSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDV 477
Cdd:cd03229 61 -------GEDLTDLEDELPPLRRRIGmvfqDFAlFPHLTVLENIALgLSGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 739061588 478 ET---LRALENALLEFPGCAMV-ISHDRWFLDRIATHII 512
Cdd:cd03229 134 ITrreVRALLKSLQAQLGITVVlVTHDLDEAARLADRVV 172
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-236 |
1.13e-28 |
|
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: 114.13 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD------IEGEARPQPGIK-----IGYLPQEPK--LNPEH 84
Cdd:COG1124 17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPwsgevtFDGRPVTRRRRKafrrrVQMVFQDPYasLHPRH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 TVREAVEEAvseLKNalnrldevyaayadpdadfdklakeqgqleaiiqshdgHNLENQLERAAEALRL----PEW-DAK 159
Cdd:COG1124 97 TVDRILAEP---LRI--------------------------------------HGLPDREERIAELLEQvglpPSFlDRY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 160 IEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:COG1124 136 PHQLSGGQRQRVAIARALILEPELLLLDEPTSALDvsvqAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNG 215
|
.
gi 739061588 236 E 236
Cdd:COG1124 216 R 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-512 |
2.32e-28 |
|
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: 119.12 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 31 PGAKIGVLGLNGAGKSTLLRIMAGidtdiegEARPQPGIkigylpqepkLNPEHTVREAVEE-AVSELKNALNRL--DEV 107
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSG-------ELKPNLGD----------YDEEPSWDEVLKRfRGTELQDYFKKLanGEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 108 YAAYadpdadfdklaKEQgQLEAIIQSHDGhNLENQLERA---------AEALRL-PEWDAKIEKLSGGERRRVAICRLL 177
Cdd:COG1245 161 KVAH-----------KPQ-YVDLIPKVFKG-TVRELLEKVdergkldelAEKLGLeNILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 178 LEKPDMLLLDEPTNHLDAE---SVAWLERFLHDYEGTVVAITHDRYFLDNVAGWIlELDRGEgipwEGNYSSWLEQKDAR 254
Cdd:COG1245 228 LRDADFYFFDEPSSYLDIYqrlNVARLIRELAEEGKYVLVVEHDLAILDYLADYV-HILYGE----PGVYGVVSKPKSVR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 255 ------LEQEAATEAARhksiqkelewIRQNPkgrqakgkarlARFEELNSVDYQKRnetselfippgprlgDKVLEINN 328
Cdd:COG1245 303 vginqyLDGYLPEENVR----------IRDEP-----------IEFEVHAPRREKEE---------------ETLVEYPD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 329 LTKSYGDRVLIDDlSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGtlVLGDTVKLA------------SVDQF-- 394
Cdd:COG1245 347 LTKSYGGFSLEVE-GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG--EVDEDLKISykpqyispdydgTVEEFlr 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 395 ---RDSMDDSKtVWEEVSGGQDIMRIgnFEipsrayvgrfnfkgvdqgKRVGELSGGERGRLHLAKLLQVGGNMLLLDEP 471
Cdd:COG1245 424 sanTDDFGSSY-YKTEIIKPLGLEKL--LD------------------KNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 739061588 472 TNDLDVE----TLRALENALLEFPGCAMVISHDRWFLDRIATHII 512
Cdd:COG1245 483 SAHLDVEqrlaVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
324-512 |
2.37e-28 |
|
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: 112.31 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLG-DTVKLASVDQFRDSMDDS 401
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEiTFDGkSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 402 KTVWEEVSGGQdimrigNFEIPSRAYvgRFNFKGVDQ-----------GKRVGELSGGERGRLHLAKLLQVGGNMLLLDE 470
Cdd:cd03268 81 PGFYPNLTARE------NLRLLARLL--GIRKKRIDEvldvvglkdsaKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 739061588 471 PTNDLDVETLRALENALLEFP--GCAMVI-SHDRWFLDRIATHII 512
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRdqGITVLIsSHLLSEIQKVADRIG 197
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
19-251 |
3.56e-28 |
|
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: 118.72 E-value: 3.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQEPklnpeH--- 84
Cdd:COG4987 348 RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFldpqsgsitlgGVDLRDLDEDDLRRRIAVVPQRP-----Hlfd 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 -TVREaveeavselknalN-RLdevyaayADPDADfdklakeqgqleaiiqshdghnlENQLERAAEALRLPEW------ 156
Cdd:COG4987 423 tTLRE-------------NlRL-------ARPDAT-----------------------DEELWAALERVGLGDWlaalpd 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 157 --DAKI----EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESV-AWLERFLHDYEG-TVVAITHDRYFLDNVAGw 228
Cdd:COG4987 460 glDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEqALLADLLEALAGrTVLLITHRLAGLERMDR- 538
|
250 260
....*....|....*....|...
gi 739061588 229 ILELDRGEGIPwEGNYSSWLEQK 251
Cdd:COG4987 539 ILVLEDGRIVE-QGTHEELLAQN 560
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
324-511 |
3.82e-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: 3.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGD--RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRDSM--- 398
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 399 --DDskTVWEEVSGGQDIM------RIGNFEIPSRA--YVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLqVGGN-MLL 467
Cdd:cd03263 81 pqFD--ALFDELTVREHLRfyarlkGLPKSEIKEEVelLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIAL-IGGPsVLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 739061588 468 LDEPTNDLDVETLRALENALLEF-PGCAMVI-SHDRWFLDRIATHI 511
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVrKGRSIILtTHSMDEAEALCDRI 202
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-236 |
4.11e-28 |
|
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: 112.64 E-value: 4.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--------IDTDIEGEARPQPGIK--IGYLPQEPKLNPEHTVR 87
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGllkpdsgsILIDGEDVRKEPREARrqIGVLPDERGLYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 88 EAVEEAvselkNALNRLDevyaayadpdadfdklakeqgqleaiiqshdGHNLENQLERAAEALRLPEW-DAKIEKLSGG 166
Cdd:COG4555 93 ENIRYF-----AELYGLF-------------------------------DEELKKRIEELIELLGLEEFlDRRVGELSTG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 167 ERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG4555 137 MKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGK 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-251 |
8.22e-28 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 118.01 E-value: 8.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIK-----------------IGYLPQEP 78
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR------ILidgidlrqidpaslrrqIGVVLQDV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 79 KLNPEhTVREAVeeavselknalnrldevyaAYADPDADFDKL--AKEQGQLEAIIQSH-DGhnLENQL-ERAAealrlp 154
Cdd:COG2274 559 FLFSG-TIRENI-------------------TLGDPDATDEEIieAARLAGLHDFIEALpMG--YDTVVgEGGS------ 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 155 ewdakieKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG--TVVAITHDRYFLDNvAGWILEL 232
Cdd:COG2274 611 -------NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-ADRIIVL 682
|
250
....*....|....*....
gi 739061588 233 DRGEgIPWEGNYSSWLEQK 251
Cdd:COG2274 683 DKGR-IVEDGTHEELLARK 700
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-237 |
1.58e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 116.45 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-ARPqPGIKIGYLPQEPKLnPEHTVREAVeeav 94
Cdd:COG4178 373 PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRiARP-AGARVLFLPQRPYL-PLGTLREAL---- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 95 selknalnrldevyaAYADPDADFDklakeQGQLEAIIQSHdghNLENQLERAAEALRlpeWDakiEKLSGGERRRVAIC 174
Cdd:COG4178 447 ---------------LYPATAEAFS-----DAELREALEAV---GLGHLAERLDEEAD---WD---QVLSLGEQQRLAFA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 175 RLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD--YEGTVVAITHdRYFLDNVAGWILELDRGEG 237
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGDGS 561
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
320-529 |
4.15e-27 |
|
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: 109.68 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 320 GDKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTVKLASVDQFR--- 395
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEiLVDGQDITGLSEKELYelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 -------------DSMddskTVWEEV--------SGGQDIMRignfEIpSRAYVGRFNFKGVdQGKRVGELSGGERGRLH 454
Cdd:COG1127 82 rrigmlfqggalfDSL----TVFENVafplrehtDLSEAEIR----EL-VLEKLELVGLPGA-ADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 455 LAKLLQVGGNMLLLDEPTNDLDVETLRALENALLE----FPGCAMVISHDRWFLDRIATHIIdYQDEGKVEfFEGNFTE 529
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIADRVA-VLADGKII-AEGTPEE 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
18-236 |
4.46e-27 |
|
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: 108.73 E-value: 4.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGI----------------KIGYLPQEPKLN 81
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD-GTdisklsekelaafrrrHIGFVFQSFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 PEHTVREAVEeavselknalnrldevyaayadpdadfdklakeqgqLEAIIQSHDGHNLENQLERAAEALRLPE-WDAKI 160
Cdd:cd03255 95 PDLTALENVE------------------------------------LPLLLAGVPKKERRERAEELLERVGLGDrLNHYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 161 EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHDRyFLDNVAGWILELDRGE 236
Cdd:cd03255 139 SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
324-520 |
6.28e-27 |
|
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: 108.35 E-value: 6.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGD----RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTvklaSVDQFRDSMD 399
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGT----DISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 400 DSK------------------TVWEEVSGGQDIMRIGNFEIPSRA-----YVG---RFNfkgvdqgKRVGELSGGERGRL 453
Cdd:cd03255 77 AAFrrrhigfvfqsfnllpdlTALENVELPLLLAGVPKKERRERAeelleRVGlgdRLN-------HYPSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 454 HLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEF---PGCAMVI-SHDRwFLDRIATHIIDYQDeGKV 520
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkeAGTTIVVvTHDP-ELAEYADRIIELRD-GKI 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
17-236 |
1.32e-26 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 105.79 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARpqpgikigYLPQEPKLNPEHTVREAVeeavse 96
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL--------IDGKDIAKLPLEELRRRI------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 97 lknalnrldevyaAYadpdadfdklakeqgqleaIIQshdghnlenqleraaealrlpewdakiekLSGGERRRVAICRL 176
Cdd:cd00267 76 -------------GY-------------------VPQ-----------------------------LSGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 177 LLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELaeEGrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-251 |
1.35e-26 |
|
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: 113.70 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-----------ARPQPGIKIGYLPQEPKLnPEH 84
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSilingvdlsdlDPASWRRQIAWVPQNPYL-FAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 TVREaveeavselknalN-RLdevyaayADPDADfdklakeqgqleaiiqshdghnlENQLERAAEAL-------RLPE- 155
Cdd:COG4988 426 TIRE-------------NlRL-------GRPDAS-----------------------DEELEAALEAAgldefvaALPDg 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 156 WDAKIE----KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY-EG-TVVAITHDRYFLDNvAGWI 229
Cdd:COG4988 463 LDTPLGeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaKGrTVILITHRLALLAQ-ADRI 541
|
250 260
....*....|....*....|..
gi 739061588 230 LELDRGEGIPwEGNYSSWLEQK 251
Cdd:COG4988 542 LVLDDGRIVE-QGTHEELLAKN 562
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
324-512 |
1.97e-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: 107.52 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQ--------- 393
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFdGEDITGLPPHEiarlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 ------FRDSmddskTVWEEV--------SGGQDIMRIGNFEIPSRAYVGRF-NFKGVD--QGKRVGELSGGERGRLHLA 456
Cdd:cd03219 81 fqiprlFPEL-----TVLENVmvaaqartGSGLLLARARREEREARERAEELlERVGLAdlADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 457 KLLQVGGNMLLLDEPT---NDLDVETLRALENALLEFpGCA-MVISHDRWFLDRIATHII 512
Cdd:cd03219 156 RALATDPKLLLLDEPAaglNPEETEELAELIRELRER-GITvLLVEHDMDVVMSLADRVT 214
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
324-544 |
2.46e-26 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 113.51 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQfrD-SMDDSK 402
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQ--DpPRNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 403 TVWEEVSGG---------------------------------QDIMRIGN---FEIPSRAYVGRFnfkGVDQGKRVGELS 446
Cdd:PRK11147 82 TVYDFVAEGieeqaeylkryhdishlvetdpseknlnelaklQEQLDHHNlwqLENRINEVLAQL---GLDPDAALSSLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 447 GGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEFPGCAMVISHDRWFLDRIATHIIDYqDEGKVEFFEGN 526
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDL-DRGKLVSYPGN 237
|
250
....*....|....*...
gi 739061588 527 FTEYEEYKKRTLGNDAIQ 544
Cdd:PRK11147 238 YDQYLLEKEEALRVEELQ 255
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
17-218 |
3.54e-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: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQepklnpeht 85
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLlkpssgeilldGKDLASLSPKELARKIAYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 86 vreaveeavselknALNRLdevyaayadpdadfdklakeqgqleaiiqshdghNLENQLERaaealrlpewdaKIEKLSG 165
Cdd:cd03214 81 --------------ALELL----------------------------------GLAHLADR------------PFNELSG 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 166 GERRRVAICRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD 218
Cdd:cd03214 101 GERQRVLLARALAQEPPILLLDEPTSHLDiahqIELLELLRRLARERGKTVVMVLHD 157
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
320-512 |
3.83e-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: 107.43 E-value: 3.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 320 GDKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLG--DTVKLASVDQFR-- 395
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgrDITGLPPHRIARlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 -----------DSMddskTVWEEV-SGGQDIMRIGNFEIPSRAYVGRFNFKGVDQ---------------GKRVGELSGG 448
Cdd:COG0411 81 iartfqnprlfPEL----TVLENVlVAAHARLGRGLLAALLRLPRARREEREAREraeellervgladraDEPAGNLSYG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739061588 449 ERGRLHLAKLLQVGGNMLLLDEPT---NDLDVETLRALENALLEFPGCAMV-ISHDRWFLDRIATHII 512
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGITILlIEHDMDLVMGLADRIV 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
303-483 |
6.24e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 108.76 E-value: 6.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 303 QKRNETSELFIPPGPRLGDKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL-V 381
Cdd:PRK13536 21 RKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 382 LGDTV---------KLASVDQFrDSMDDSKTVWEE--VSGGQDIMRIGNFE--IPSRAYVGRFNFKGvdqGKRVGELSGG 448
Cdd:PRK13536 101 LGVPVpararlaraRIGVVPQF-DNLDLEFTVRENllVFGRYFGMSTREIEavIPSLLEFARLESKA---DARVSDLSGG 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 739061588 449 ERGRLHLAKLLQVGGNMLLLDEPTNDLDV-------ETLRAL 483
Cdd:PRK13536 177 MKRRLTLARALINDPQLLILDEPTTGLDPharhliwERLRSL 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
18-226 |
7.06e-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: 105.67 E-value: 7.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEG---EARPQPGIKIGYLPQEP--KLN 81
Cdd:cd03257 17 SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLlkptsgsiifdGKDLLKlsrRLRKIRRKEIQMVFQDPmsSLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 PEHTVREAVEEAVSELKnalnrldevyaayadpdadfdKLAKEQGQLEAIIQshdghnLENQLERAAEAL-RLPEWdaki 160
Cdd:cd03257 97 PRMTIGEQIAEPLRIHG---------------------KLSKKEARKEAVLL------LLVGVGLPEEVLnRYPHE---- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739061588 161 ekLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD----YEGTVVAITHD----RYFLDNVA 226
Cdd:cd03257 146 --LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHDlgvvAKIADRVA 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
323-508 |
7.84e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.39 E-value: 7.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGD-------TVKLAsvdQFR 395
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwsPAELA---RRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 DSMDDSKTVW-----EEVsggqdiMRIGnfeipsrAYVGRFNFKGVDQ---------------GKRVGELSGGERGRLHL 455
Cdd:PRK13548 79 AVLPQHSSLSfpftvEEV------VAMG-------RAPHGLSRAEDDAlvaaalaqvdlahlaGRDYPQLSGGEQQRVQL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739061588 456 AKLL-QV-----GGNMLLLDEPTNDLDV----ETLRALENALLEFPGCAMVISHD-----RWfLDRIA 508
Cdd:PRK13548 146 ARVLaQLwepdgPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHDlnlaaRY-ADRIV 212
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
325-523 |
1.27e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.94 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 325 EINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGtlvlgdTVKLASVDQFR-DSMDDSKT 403
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSG------EVLVDGLDVATtPSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 404 VweevsggqDIMRIGNFeIPSRAYV------GRFNF-KG---------VDQ-----------GKRVGELSGGERGRLHLA 456
Cdd:COG4604 77 L--------AILRQENH-INSRLTVrelvafGRFPYsKGrltaedreiIDEaiayldledlaDRYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739061588 457 KLLQVGGNMLLLDEPTNDLD----VETLRALENALLEFpGCAMVIS-HDRWFLDRIATHIIDYQDeGKVEFF 523
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADEL-GKTVVIVlHDINFASCYADHIVAMKD-GRVVAQ 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
324-512 |
2.05e-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: 102.85 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDR--VLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLgdtvklasvdqfrdsmdds 401
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 402 ktvweevsGGQDIMRIGNFEIPSR-AYVG----------RFNFkgvdqgkrvgeLSGGERGRLHLAKLLQVGGNMLLLDE 470
Cdd:cd03228 62 --------DGVDLRDLDLESLRKNiAYVPqdpflfsgtiRENI-----------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 739061588 471 PTNDLDVETLRALENALLEFPGCAMV--ISHdRWFLDRIATHII 512
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVivIAH-RLSTIRDADRII 165
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
324-489 |
3.89e-25 |
|
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: 103.32 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDR----VLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTVKLASVD-----Q 393
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEvLVDGEPVTGPGPDrgyvfQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 frdsmDDS----KTVWEEVSGGQDIMRIGNFEIPSRA--YVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLL 467
Cdd:cd03293 81 -----QDAllpwLTVLDNVALGLELQGVPKAEARERAeeLLELVGLSGF-ENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180
....*....|....*....|..
gi 739061588 468 LDEPTNDLDVETLRALENALLE 489
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLD 176
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
19-218 |
6.07e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 104.02 E-value: 6.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD------IEGEARPQPGIKIGYLPQEPKLNPEHTVREAVEE 92
Cdd:COG1116 24 VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPtsgevlVDGKPVTGPGPDRGVVFQEPALLPWLTVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 93 AVselknalnrldevyaayadpdaDFDKLAKEQGQleaiiqshdghnlenqlERAAEALR---LPEW-DAKIEKLSGGER 168
Cdd:COG1116 104 GL----------------------ELRGVPKAERR-----------------ERARELLElvgLAGFeDAYPHQLSGGMR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739061588 169 RRVAICRLLLEKPDMLLLDEPTNHLDAESVA----WLERFLHDYEGTVVAITHD 218
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRErlqdELLRLWQETGKTVLFVTHD 198
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
332-500 |
1.19e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.16 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 332 SYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQfRDSMDDS--KTVWEEVS 409
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-RSEVPDSlpLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 410 GG--QDIMRIGNFEIPSRAYVG----RFNFKGVDqGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRAL 483
Cdd:NF040873 80 MGrwARRGLWRRLTRDDRAAVDdaleRVGLADLA-GRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180
....*....|....*....|
gi 739061588 484 ENALLEFPG---CAMVISHD 500
Cdd:NF040873 159 IALLAEEHArgaTVVVVTHD 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
324-523 |
1.51e-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: 102.19 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLG-DTVKLASVDQFR------ 395
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEvLIDGeDISGLSEAELYRlrrrmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 ---------DSMddskTVWEEVS---------GGQDIMRIGNFEIpsrayvGRFNFKGVDQgKRVGELSGGERGRLHLAK 457
Cdd:cd03261 81 mlfqsgalfDSL----TVFENVAfplrehtrlSEEEIREIVLEKL------EAVGLRGAED-LYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 458 LLQVGGNMLLLDEPTNDLDVETLRALENALL----EFPGCAMVISHDRWFLDRIATHIIdYQDEGKVEFF 523
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRslkkELGLTSIMVTHDLDTAFAIADRIA-VLYDGKIVAE 218
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-251 |
1.63e-24 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 107.28 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEpklnpeHTvreaveeavSELKNA 100
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQD------HA---------YDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 101 LNRLDEVyAAYADPDADfdklakEQ---GQLEAIIQSHDghnlenqleraaealrlpEWDAKIEKLSGGERRRVAICRLL 177
Cdd:PRK15064 399 LTLFDWM-SQWRQEGDD------EQavrGTLGRLLFSQD------------------DIKKSVKVLSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739061588 178 LEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQK 251
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
315-529 |
2.10e-24 |
|
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: 107.15 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 315 PGPRLGDKVLEINNLTKSYGD-RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDtVKLASVDQ 393
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING-VDLSDLDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 frdsmddsKTVWEEVSG-GQ----------DIMRIGNFEIPS--------RAYVGRFnFKGVDQG--KRVGE----LSGG 448
Cdd:COG4988 407 --------ASWRRQIAWvPQnpylfagtirENLRLGRPDASDeeleaaleAAGLDEF-VAALPDGldTPLGEggrgLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 449 ERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEFPG--CAMVISHdRWFLDRIATHIIDYQDEGKVEffEGN 526
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITH-RLALLAQADRILVLDDGRIVE--QGT 554
|
...
gi 739061588 527 FTE 529
Cdd:COG4988 555 HEE 557
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-226 |
2.61e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 106.53 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGID--------------TDIEGEARPQPGIKIGYLPQEPK-- 79
Cdd:COG1123 275 KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLrptsgsilfdgkdlTKLSRRSLRELRRRVQMVFQDPYss 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 80 LNPEHTVREAVEEAvseLKNalnrldevyaayadpdadfdklakeqgqleaiiqsHDGHNLENQLERAAEALR---LPE- 155
Cdd:COG1123 355 LNPRMTVGDIIAEP---LRL-----------------------------------HGLLSRAERRERVAELLErvgLPPd 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 156 -WDAKIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAeSVAW-----LERFLHDYEGTVVAITHD----RYFLDNV 225
Cdd:COG1123 397 lADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAqilnlLRDLQRELGLTYLFISHDlavvRYIADRV 475
|
.
gi 739061588 226 A 226
Cdd:COG1123 476 A 476
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-477 |
2.81e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.26 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD------IEGEARPQPGIK------IGYLPQEPKLNPEHTVREA 89
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPdsgeilLDGEPVRFRSPRdaqaagIAIIHQELNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 90 VeeavselknALNRLdevyaayadpdadfdklakeqgqleaiIQSHDGHNLENQLERAAEAL-RL-----PewDAKIEKL 163
Cdd:COG1129 100 I---------FLGRE---------------------------PRRGGLIDWRAMRRRARELLaRLgldidP--DTPVGDL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 164 SGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHdryFLDNvagwILEL-DR----- 234
Cdd:COG1129 142 SVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLkaQGvAIIYISH---RLDE----VFEIaDRvtvlr 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 235 -GEGIpwegnysswleqkdarlEQEAATEAARHKSIQKELewirqnpkGRqakgkarlarfeelnsvdyqkrnETSELFI 313
Cdd:COG1129 215 dGRLV-----------------GTGPVAELTEDELVRLMV--------GR-----------------------ELEDLFP 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 314 PPGPRLGDKVLEINNLTksygDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVd 392
Cdd:COG1129 247 KRAAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdGKPVRIRSP- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 393 qfRDSMD--------DSKTvwEEVSGGQDIM---------RIGNFEIPSRA--------YVGRFNFKGVDQGKRVGELSG 447
Cdd:COG1129 322 --RDAIRagiayvpeDRKG--EGLVLDLSIRenitlasldRLSRGGLLDRRreralaeeYIKRLRIKTPSPEQPVGNLSG 397
|
490 500 510
....*....|....*....|....*....|
gi 739061588 448 GERGRLHLAKLLQVGGNMLLLDEPTNDLDV 477
Cdd:COG1129 398 GNQQKVVLAKWLATDPKVLILDEPTRGIDV 427
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
20-218 |
2.94e-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: 101.01 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD------IEGEARPQPGIKIGYLPQEPKLNPEHTVREaveea 93
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPtsgevlVDGEPVTGPGPDRGYVFQQDALLPWLTVLD----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 94 vselkNALNRLDEVYAAYADPDADFDKLAKEQGqleaiiqshdghnlenqLERAAealrlpewDAKIEKLSGGERRRVAI 173
Cdd:cd03293 93 -----NVALGLELQGVPKAEARERAEELLELVG-----------------LSGFE--------NAYPHQLSGGMRQRVAL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 739061588 174 CRLLLEKPDMLLLDEPTNHLDA---ESV-AWLERFLHDYEGTVVAITHD 218
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDAltrEQLqEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
324-513 |
5.40e-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: 99.96 E-value: 5.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGaIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRD------- 396
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrigylpq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 397 --SMDDSKTVWEEVSGGQDIMRIGNFEIPSRA-----YVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNMLLLD 469
Cdd:cd03264 80 efGVYPNFTVREFLDYIAWLKGIPSKEVKARVdevleLVNLGDRA----KKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 739061588 470 EPTNDLDVETLRALENALLEfpgcamvISHDRWFLdrIATHIID 513
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSE-------LGEDRIVI--LSTHIVE 190
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
17-196 |
6.31e-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: 99.96 E-value: 6.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAkIGVLGLNGAGKSTLLRIMAGIDTDIEG-------EARPQPGI---KIGYLPQEPKLNPEHTV 86
Cdd:cd03264 11 GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGtiridgqDVLKQPQKlrrRIGYLPQEFGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 87 REAVEeavselknalnrldevYAAYAD--PDADFDKLAkeQGQLEAIiqshdghNLENQLERaaealrlpewdaKIEKLS 164
Cdd:cd03264 90 REFLD----------------YIAWLKgiPSKEVKARV--DEVLELV-------NLGDRAKK------------KIGSLS 132
|
170 180 190
....*....|....*....|....*....|..
gi 739061588 165 GGERRRVAICRLLLEKPDMLLLDEPTNHLDAE 196
Cdd:cd03264 133 GGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
324-483 |
7.32e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 100.96 E-value: 7.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTvklaSVDQFRD------- 396
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR----PLAAWSPwelarrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 397 -------SMDDSKTVWEEVSGGqdimRIGNF-------EIPSRA--------YVGRFnfkgvdqgkrVGELSGGERGRLH 454
Cdd:COG4559 78 avlpqhsSLAFPFTVEEVVALG----RAPHGssaaqdrQIVREAlalvglahLAGRS----------YQTLSGGEQQRVQ 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 739061588 455 LAK-LLQV------GGNMLLLDEPTNDLDV----ETLRAL 483
Cdd:COG4559 144 LARvLAQLwepvdgGPRWLFLDEPTSALDLahqhAVLRLA 183
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
18-218 |
9.09e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 99.73 E-value: 9.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARpqpgI-------------------KIGYLPQEP 78
Cdd:COG1136 20 EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVL----IdgqdisslserelarlrrrHIGFVFQFF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 79 KLNPEHTVREAVEeavselknalnrldevyaayadpdadfdklakeqgqLEAIIQSHDGHNLENQLERAAEALRLPEW-D 157
Cdd:COG1136 96 NLLPELTALENVA------------------------------------LPLLLAGVSRKERRERARELLERVGLGDRlD 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 158 AKIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHD 218
Cdd:COG1136 140 HRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHD 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-508 |
1.36e-23 |
|
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: 104.50 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDtdiegEARPQPGIKIGYLpqepKLNPEHTVREAVEEAVSELKNA 100
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMD-----QYEPTSGRIIYHV----ALCEKCGYVERPSKVGEPCPVC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 101 LNRLDEVYAAYADPD----ADFDK-----------LAKEQGQLEAIIQS-HD-GHNLENQLERAAEALRLPEWDAKI--- 160
Cdd:TIGR03269 86 GGTLEPEEVDFWNLSdklrRRIRKriaimlqrtfaLYGDDTVLDNVLEAlEEiGYEGKEAVGRAVDLIEMVQLSHRIthi 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 161 -EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESV----AWLERFLHDYEGTVVAITHDRYFLDNVAgwileldrg 235
Cdd:TIGR03269 166 aRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLS--------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 236 egipwegNYSSWLEQKDARLEQEAATEAARHKSIQKELEwirqnpkgrqakgkarlaRFEELnsvdyqkrnetselfipp 315
Cdd:TIGR03269 237 -------DKAIWLENGEIKEEGTPDEVVAVFMEGVSEVE------------------KECEV------------------ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 316 gpRLGDKVLEINNLTKSYG--DRVLI---DDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL--VLG----D 384
Cdd:TIGR03269 274 --EVGEPIIKVRNVSKRYIsvDRGVVkavDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGdewvD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 385 TVKLASVDQFRD-----------SMDDSKTVWEEVSGGqdimrIG---NFEIPSRAYVGRFNFKGVDQGKRVG------- 443
Cdd:TIGR03269 352 MTKPGPDGRGRAkryigilhqeyDLYPHRTVLDNLTEA-----IGlelPDELARMKAVITLKMVGFDEEKAEEildkypd 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 444 ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALL----EFPGCAMVISHDRWFL----DRIA 508
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkareEMEQTFIIVSHDMDFVldvcDRAA 499
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
323-479 |
1.48e-23 |
|
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: 99.19 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDR----VLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLG-DTVKL--ASVDQF 394
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSvLVDGtDLTLLsgKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 395 RDSMD---------DSKTVWEEVSGGQDIMRIGNFEIPSRAY-----VGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQ 460
Cdd:cd03258 81 RRRIGmifqhfnllSSRTVFENVALPLEIAGVPKAEIEERVLellelVGLEDKA----DAYPAQLSGGQKQRVGIARALA 156
|
170
....*....|....*....
gi 739061588 461 VGGNMLLLDEPTNDLDVET 479
Cdd:cd03258 157 NNPKVLLCDEATSALDPET 175
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-235 |
2.06e-23 |
|
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: 98.43 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIE----GEARPQpgikIGYLPQEPKLNp 82
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLykptsgsvlldGTDIRqldpADLRRN----IGYVPQDVTLF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 83 EHTVREAVeeavselknalnrldevyaAYADPDADFDKL--AKEQGQLEAIIQSHdGHNLENQL-ERAAEalrlpewdak 159
Cdd:cd03245 91 YGTLRDNI-------------------TLGAPLADDERIlrAAELAGVTDFVNKH-PNGLDLQIgERGRG---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 160 iekLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVawlERFLHDYEG-----TVVAITHdRYFLDNVAGWILELDR 234
Cdd:cd03245 141 ---LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE---ERLKERLRQllgdkTLIIITH-RPSLLDLVDRIIVMDS 213
|
.
gi 739061588 235 G 235
Cdd:cd03245 214 G 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
323-394 |
2.59e-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: 2.59e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTVKLASVDQF 394
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEvLWDGEPLDPEDRRRI 73
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-236 |
2.87e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 98.20 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 8 MLR---VGKIVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR---------PQPGI-----K 70
Cdd:COG2884 1 MIRfenVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrlKRREIpylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 71 IGYLPQEPKLNPEHTVREAVeeavselknalnrldevyaAYAdpdadfdklakeqgqLEAIiqshdGHNLENQLERAAEA 150
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENV-------------------ALP---------------LRVT-----GKSRKEIRRRVREV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 151 LrlpEW-------DAKIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESvAW-----LERFlHDYEGTVVAITHD 218
Cdd:COG2884 122 L---DLvglsdkaKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPET-SWeimelLEEI-NRRGTTVLIATHD 196
|
250
....*....|....*...
gi 739061588 219 RYFLDNVAGWILELDRGE 236
Cdd:COG2884 197 LELVDRMPKRVLELEDGR 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
324-507 |
3.89e-23 |
|
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: 98.41 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGD-RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDT----VKLASVDQFRDSM 398
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinkLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 399 ddsKTVW------EEVSGGQDIM--RIGnfEIPS-RAYVGRFN-------FKGVDQ-------GKRVGELSGGERGRLHL 455
Cdd:cd03256 81 ---GMIFqqfnliERLSVLENVLsgRLG--RRSTwRSLFGLFPkeekqraLAALERvglldkaYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 456 AKLLQVGGNMLLLDEPTNDLDVETLRALENALLEFP---GCAMVIS-HD----RWFLDRI 507
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreeGITVIVSlHQvdlaREYADRI 215
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-288 |
3.99e-23 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 103.49 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 10 RVGKIV---------PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAgidtdieGEARPQPG-IKIG------Y 73
Cdd:PRK11147 314 RSGKIVfemenvnyqIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLML-------GQLQADSGrIHCGtklevaY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 74 LPQ-EPKLNPEHTVREAVEEavselknalnrldevyaayadpdadfdklakeqGQLEAIIQSHDGH---NLENQL---ER 146
Cdd:PRK11147 387 FDQhRAELDPEKTVMDNLAE---------------------------------GKQEVMVNGRPRHvlgYLQDFLfhpKR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 147 AaealRLPewdakIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVA 226
Cdd:PRK11147 434 A----MTP-----VKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTV 504
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 227 --GWILEldrGEGIpWE---GNYSswleqkDARlEQEAATEAARHKSIQKELEWIRQNPKGRQAKGK 288
Cdd:PRK11147 505 teCWIFE---GNGK-IGryvGGYH------DAR-QQQAQYLALKQPAVKKKEEAAAPKAETVKRSSK 560
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
325-520 |
4.05e-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: 97.33 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 325 EINNLTKSYGDRVLI-DDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDtVKLASVDQFRDS---MDD 400
Cdd:cd03226 1 RIENISFSYKKGTEIlDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-KPIKAKERRKSIgyvMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 401 ------SKTVWEEVSGGQDIMRIGNFEIpsRAYVGRFN-FKGVDQGKRvgELSGGERGRLHLAKLLQVGGNMLLLDEPTN 473
Cdd:cd03226 80 vdyqlfTDSVREELLLGLKELDAGNEQA--ETVLKDLDlYALKERHPL--SLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 739061588 474 DLDVETLRALENALLEFP--GCAM-VISHDRWFLDRIATHIIdYQDEGKV 520
Cdd:cd03226 156 GLDYKNMERVGELIRELAaqGKAViVITHDYEFLAKVCDRVL-LLANGAI 204
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
323-508 |
4.08e-23 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 97.96 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSY----GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRD-- 396
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 397 -------------SMDDSKTVWEEVsggQDIMRIGNFEIPSRAY--VGRFNFKGVDQGKRV-----GELSGGERGRLHLA 456
Cdd:cd03257 81 rkeiqmvfqdpmsSLNPRMTIGEQI---AEPLRIHGKLSKKEARkeAVLLLLVGVGLPEEVlnrypHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739061588 457 KLLQVGGNMLLLDEPTNDLDV-------ETLRALENALlefpGCAMV-ISHD----RWFLDRIA 508
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVsvqaqilDLLKKLQEEL----GLTLLfITHDlgvvAKIADRVA 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
324-520 |
1.41e-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: 96.06 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVklasvdqfrdsMDDSKT 403
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLK-----------LTDDKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 404 VWEEVsggqdimrignfeipsRAYVG----RFNF-----------------KGVDQG----------KRVG--------- 443
Cdd:cd03262 70 NINEL----------------RQKVGmvfqQFNLfphltvlenitlapikvKGMSKAeaeeralellEKVGladkadayp 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 444 -ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEFP--GCAMVI-SHDRWFLDRIATHIIdYQDEGK 519
Cdd:cd03262 134 aQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAeeGMTMVVvTHEMGFAREVADRVI-FMDDGR 212
|
.
gi 739061588 520 V 520
Cdd:cd03262 213 I 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-236 |
1.41e-22 |
|
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: 94.76 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID----TDIEGEARPQpgiKIGYLPQEPKLNPEh 84
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRlydptsgeilIDgvdlRDLDLESLRK---NIAYVPQDPFLFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 TVREaveeavselknalnrldevyaayadpdadfdklakeqgqleaiiqshdghNLenqleraaealrlpewdakiekLS 164
Cdd:cd03228 91 TIRE--------------------------------------------------NI----------------------LS 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739061588 165 GGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG--TVVAITHdRYFLDNVAGWILELDRGE 236
Cdd:cd03228 99 GGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-235 |
1.45e-22 |
|
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: 101.36 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 14 IVPP--KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQEPKL 80
Cdd:COG4618 338 VVPPgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVwpptagsvrldGADLSQWDREELGRHIGYLPQDVEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 81 NPEhTVREaveeavselknalN--RLDEvyaayADPdadfdklakeqgqlEAIIQshdghnlenqlerAAEA-------L 151
Cdd:COG4618 418 FDG-TIAE-------------NiaRFGD-----ADP--------------EKVVA-------------AAKLagvhemiL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 152 RLPE-WDAKIE----KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD--YEG-TVVAITHDRYFLd 223
Cdd:COG4618 452 RLPDgYDTRIGeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlkARGaTVVVITHRPSLL- 530
|
250
....*....|..
gi 739061588 224 NVAGWILELDRG 235
Cdd:COG4618 531 AAVDKLLVLRDG 542
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-219 |
1.50e-22 |
|
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: 96.05 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE---------ARPQPGIKIGYLPQEPKLNPEHTVREAV 90
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEilidgrdvtGVPPERRNIGMVFQDYALFPHLTVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 91 eeaVSELKNAlnrldevyaayadpdadfdKLAKEQgqleaiiqshdghnLENQLERAAEALRLPEW-DAKIEKLSGGERR 169
Cdd:cd03259 94 ---AFGLKLR-------------------GVPKAE--------------IRARVRELLELVGLEGLlNRYPHELSGGQQQ 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739061588 170 RVAICRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHDR 219
Cdd:cd03259 138 RVALARALAREPSLLLLDEPLSALDAKLreelREELKELQRELGITTIYVTHDQ 191
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
324-490 |
1.52e-22 |
|
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: 96.10 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISG-----QEQPDSGTLVL-GDTVKLASVDQ---- 393
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLdGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 ------FRDSMDDSKTVWEEVSGGQDIMRI-GNFEIPSRAYVGrfnFKGVDQGKRV------GELSGGERGRLHLAKLLQ 460
Cdd:cd03260 81 rrvgmvFQKPNPFPGSIYDNVAYGLRLHGIkLKEELDERVEEA---LRKAALWDEVkdrlhaLGLSGGQQQRLCLARALA 157
|
170 180 190
....*....|....*....|....*....|
gi 739061588 461 VGGNMLLLDEPTNDLDVETLRALENALLEF 490
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAEL 187
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
17-219 |
1.65e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 99.07 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT-D-----IEGE---------ARpqpgiKIGYLPQEPKLN 81
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETpDsgrivLNGRdlftnlpprER-----RVGFVFQHYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 PEHTVREAVEEAVSELKNalnrldevyaayadPDADFDKLAKEQgqLEAIiqshdghnlenQLERAAEalRLPEwdakie 161
Cdd:COG1118 88 PHMTVAENIAFGLRVRPP--------------SKAEIRARVEEL--LELV-----------QLEGLAD--RYPS------ 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAeSVA-----WLERFLHDYEGTVVAITHDR 219
Cdd:COG1118 133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDA-KVRkelrrWLRRLHDELGGTTVFVTHDQ 194
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
19-218 |
1.81e-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: 96.81 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQEPKLNPEHTVR 87
Cdd:TIGR03873 14 RLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGAlrpdagtvdlaGVDLHGLSRRARARRVALVEQDSDTAVPLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 88 EAVeeavselknALNRLDEVYAAYADPDADFDKLAKEQGQLEAiiqshdghnlenqleraaEALRLPEWDAkiekLSGGE 167
Cdd:TIGR03873 94 DVV---------ALGRIPHRSLWAGDSPHDAAVVDRALARTEL------------------SHLADRDMST----LSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739061588 168 RRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG---TVVAITHD 218
Cdd:TIGR03873 143 RQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHD 196
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
324-479 |
1.96e-22 |
|
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: 95.90 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLG--DTVKLAS--------VDQ 393
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghDVVREPRevrrrigiVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 FRdSMDDSKTVWEEVSGGQDIMRIGNFEIPSRA-----YVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNMLLL 468
Cdd:cd03265 81 DL-SVDDELTGWENLYIHARLYGVPGAERRERIdelldFVGLLEAA----DRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170
....*....|.
gi 739061588 469 DEPTNDLDVET 479
Cdd:cd03265 156 DEPTIGLDPQT 166
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
315-513 |
2.79e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 100.44 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 315 PGPRLGDKVLEINNLTKSYGDR-VLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDtVKLASVDQ 393
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG-VPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 frDSMDDS------------KTVWEEVSGGQ-----DIMRignfEIPSRAYVGRFnFKGVDQG--KRVGE----LSGGER 450
Cdd:TIGR02857 392 --DSWRDQiawvpqhpflfaGTIAENIRLARpdasdAEIR----EALERAGLDEF-VAALPQGldTPIGEggagLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 451 GRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEFPGCAMV--ISHDRWFLDRiATHIID 513
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVllVTHRLALAAL-ADRIVV 528
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
324-484 |
2.90e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.15 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTV----------KLASVD 392
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTvLVAGDDVealsaraasrRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 393 QfRDSMDDSKTVWEEVSGGQD--IMRIGNFEIPSRAYVGR-FNFKGVDQ--GKRVGELSGGERGRLHLAKLLQVGGNMLL 467
Cdd:PRK09536 84 Q-DTSLSFEFDVRQVVEMGRTphRSRFDTWTETDRAAVERaMERTGVAQfaDRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170
....*....|....*...
gi 739061588 468 LDEPTNDLDV-ETLRALE 484
Cdd:PRK09536 163 LDEPTASLDInHQVRTLE 180
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
323-501 |
3.91e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.37 E-value: 3.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLgDTVKLASVDQFR---DSMD 399
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLSHVPPYQrpiNMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 400 DSKTVWEEVSGGQDIM------RIGNFEIPSR-----AYVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNMLLL 468
Cdd:PRK11607 98 QSYALFPHMTVEQNIAfglkqdKLPKAEIASRvnemlGLVHMQEFA----KRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 739061588 469 DEPTNDLDvETLR---ALENA-LLEFPG--CAMViSHDR 501
Cdd:PRK11607 174 DEPMGALD-KKLRdrmQLEVVdILERVGvtCVMV-THDQ 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
323-476 |
4.26e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.80 E-value: 4.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTV---------KLASVD 392
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVpsrarharqRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 393 QFrDSMDDSKTVWEevsggqDIMRIGN-FEIPS---RAYV-GRFNFKGVDQ--GKRVGELSGGERGRLHLAKLLQVGGNM 465
Cdd:PRK13537 87 QF-DNLDPDFTVRE------NLLVFGRyFGLSAaaaRALVpPLLEFAKLENkaDAKVGELSGGMKRRLTLARALVNDPDV 159
|
170
....*....|.
gi 739061588 466 LLLDEPTNDLD 476
Cdd:PRK13537 160 LVLDEPTTGLD 170
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
288-500 |
4.82e-22 |
|
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: 100.29 E-value: 4.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 288 KARLARFEELnsVDYQKRNETSELFIPPGPRLGDkvLEINNLTKSYGDRV--LIDDLSFSIPKGAIVGIIGPNGAGKSTL 365
Cdd:COG2274 442 KIALERLDDI--LDLPPEREEGRSKLSLPRLKGD--IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 366 FRMISGQEQPDSGTLVLGDT-VKLASVDQFRDSM-----DD---SKTVWEEVSGG------QDIMR------IGNFeIPS 424
Cdd:COG2274 518 LKLLLGLYEPTSGRILIDGIdLRQIDPASLRRQIgvvlqDVflfSGTIRENITLGdpdatdEEIIEaarlagLHDF-IEA 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 425 RAyvgrfnfKGVDQgkRVGE----LSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLE-FPGCAM-VIS 498
Cdd:COG2274 597 LP-------MGYDT--VVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRlLKGRTViIIA 667
|
..
gi 739061588 499 HD 500
Cdd:COG2274 668 HR 669
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
324-477 |
5.17e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.47 E-value: 5.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTV-----------KLASVD 392
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 393 QFRDSMDDSkTVWEEVSGGQDimrignfeiPSRAYVGRFNFKG---VDQG-----------KRVGELSGGERGRLHLAKL 458
Cdd:PRK11231 83 QHHLTPEGI-TVRELVAYGRS---------PWLSLWGRLSAEDnarVNQAmeqtrinhladRRLTDLSGGQRQRAFLAMV 152
|
170
....*....|....*....
gi 739061588 459 LQVGGNMLLLDEPTNDLDV 477
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDI 171
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-218 |
6.52e-22 |
|
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: 94.94 E-value: 6.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 11 VGKIVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDI---EGEARPQPGIKIGYLPQ 76
Cdd:cd03256 6 LSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLveptsgsvlidGTDInklKGKALRQLRRQIGMIFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 77 EPKLNPEHTVreaveeavseLKNALN-RLDEVyaayadpdadfdklakeqgqleAIIQSHDGHNLENQLERAAEALR--- 152
Cdd:cd03256 86 QFNLIERLSV----------LENVLSgRLGRR----------------------STWRSLFGLFPKEEKQRALAALErvg 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 153 -LPEWDAKIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDYEG-TVVAITHD 218
Cdd:cd03256 134 lLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDpasSRQVMDLLKRINREEGiTVIVSLHQ 204
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
324-499 |
7.21e-22 |
|
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: 92.49 E-value: 7.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVdqfRDSMDdsk 402
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEVSFASP---RDARR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 403 tvweevsggqdiMRIGnfeipsrayvgrfnfkgvdqgkRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDV----- 477
Cdd:cd03216 75 ------------AGIA----------------------MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPaever 120
|
170 180
....*....|....*....|....*
gi 739061588 478 --ETLRALENAllefpGCAMV-ISH 499
Cdd:cd03216 121 lfKVIRRLRAQ-----GVAVIfISH 140
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
320-499 |
8.15e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.56 E-value: 8.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 320 GDKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASvdqFRDSM 398
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdGKPVRIRS---PRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 399 D-------------DSKTVWEEVSGGQDIMRIGNF-------EIpsRAYVGRFNFKgVDQGKRVGELSGGERGRLHLAKL 458
Cdd:COG3845 79 AlgigmvhqhfmlvPNLTVAENIVLGLEPTKGGRLdrkaaraRI--RELSERYGLD-VDPDAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 739061588 459 LQVGGNMLLLDEPT--------NDLdVETLRALENAllefpGCAMV-ISH 499
Cdd:COG3845 156 LYRGARILILDEPTavltpqeaDEL-FEILRRLAAE-----GKSIIfITH 199
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
324-501 |
8.24e-22 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 94.33 E-value: 8.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDtvKLASVDQFRD------- 396
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG--EDATDVPVQErnvgfvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 397 ---SMDDSKTVWEEVSGGQDIMRIGnfEIPSRAYVGR-----FNFKGVDQ-GKRV-GELSGGERGRLHLAKLLQVGGNML 466
Cdd:cd03296 81 qhyALFRHMTVFDNVAFGLRVKPRS--ERPPEAEIRAkvhelLKLVQLDWlADRYpAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 739061588 467 LLDEPTNDLDVETLRALENALLEFpgcamvisHDR 501
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRL--------HDE 185
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-236 |
8.33e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 99.08 E-value: 8.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID-TDIE----GEARPQpgikIGYLPQEPKL 80
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfydptsgrilIDgVDIRdltlESLRRQ----IGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 81 NPEhTVREAVeeavselknalnrldevyaAYADPDADFDklakeqgqleaiiqshdghnlenQLERAAEA-------LRL 153
Cdd:COG1132 426 FSG-TIRENI-------------------RYGRPDATDE-----------------------EVEEAAKAaqahefiEAL 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 154 PE-WDAKIE----KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAW----LERFLHDYegTVVAITH------- 217
Cdd:COG1132 463 PDgYDTVVGergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALiqeaLERLMKGR--TTIVIAHrlstirn 540
|
250 260
....*....|....*....|
gi 739061588 218 -DRyfldnvagwILELDRGE 236
Cdd:COG1132 541 aDR---------ILVLDDGR 551
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-218 |
1.47e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.30 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPKLNPEH--TVREAVEEAV 94
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLplTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 95 SELKNALNRLDevyaayadpdADfDKLAkeqgqleaiiqshdghnlenqLERAAEALRLPEW-DAKIEKLSGGERRRVAI 173
Cdd:NF040873 83 WARRGLWRRLT----------RD-DRAA---------------------VDDALERVGLADLaGRQLGELSGGQRQRALL 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 739061588 174 CRLLLEKPDMLLLDEPTNHLDAESVAWLE---RFLHDYEGTVVAITHD 218
Cdd:NF040873 131 AQGLAQEADLLLLDEPTTGLDAESRERIIallAEEHARGATVVVVTHD 178
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-238 |
3.53e-21 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 91.55 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------ARPQPGIKIGYLPQEPKlnpehtvR 87
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSillngkpiKAKERRKSIGYVMQDVD-------Y 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 88 EAVEEAVSElknalnrldEVYaaYADPDADfdklaKEQGQLEAIIQshdghnlenQLERAAEALRLPeWDakiekLSGGE 167
Cdd:cd03226 83 QLFTDSVRE---------ELL--LGLKELD-----AGNEQAETVLK---------DLDLYALKERHP-LS-----LSGGQ 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739061588 168 RRRVAICRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGI 238
Cdd:cd03226 132 KQRLAIAAALLSGKDLLIFDEPTSGLDYknmERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-217 |
4.04e-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: 91.07 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--IDTDIEGE----ARPQPGIK----IGYLPQEPKLNPEHTVR 87
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEvlinGRPLDKRSfrkiIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 88 EAVEeavselknalnrldevYAayadpdadfdklakeqgqleaiiqshdghnlenqleraaealrlpewdAKIEKLSGGE 167
Cdd:cd03213 101 ETLM----------------FA------------------------------------------------AKLRGLSGGE 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 739061588 168 RRRVAICRLLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDYEGTVVAITH 217
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDsssALQVMSLLRRLADTGRTIICSIH 169
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-234 |
4.23e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 96.59 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE----ARPQPGIK-------IGYLPQEPKLnPEH 84
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavnGVPLADADadswrdqIAWVPQHPFL-FAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 TVREAVeeavselknalnrldevyaAYADPDADfdklakeqgqleaiiqshdGHNLENQLERA--AEALR-LPE-WDAKI 160
Cdd:TIGR02857 411 TIAENI-------------------RLARPDAS-------------------DAEIREALERAglDEFVAaLPQgLDTPI 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 161 ----EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG--TVVAITHDRyfldnvaGWILELDR 234
Cdd:TIGR02857 453 geggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL-------ALAALADR 525
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-215 |
4.41e-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: 91.51 E-value: 4.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR---------PQPGIKIGYLPQEPKLNPEHTVRE 88
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksyqknIEALRRIGALIEAPGFYPNLTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 89 AVEEAVSELKNALNRLDEVyaayadpdadfdklakeqgqLEAIIQSHDGHNlenqleraaealrlpewdaKIEKLSGGER 168
Cdd:cd03268 92 NLRLLARLLGIRKKRIDEV--------------------LDVVGLKDSAKK-------------------KVKGFSLGMK 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 739061588 169 RRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAI 215
Cdd:cd03268 133 QRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLrdQGITVLI 181
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-396 |
4.96e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 96.25 E-value: 4.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT-D-----IEGEAR----PQPGIK--IGYLPQEPKLNPEHTVREA 89
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQpDsgeilIDGKPVrirsPRDAIAlgIGMVHQHFMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 90 VEEAVSELKNALNRLDEVyaayadpdadfdklakeqgqleaiiqshdghnlENQLERAAEALRLP-EWDAKIEKLSGGER 168
Cdd:COG3845 101 IVLGLEPTKGGRLDRKAA---------------------------------RARIRELSERYGLDvDPDAKVEDLSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 169 RRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDryfLDNVagwiLEL-DR------GEGI 238
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITHK---LREV----MAIaDRvtvlrrGKVV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 239 pwegnysswleqkdARLEQEAATEAarhksiqkELewirqnpkgrqAK---GKARLARFEelnsvdyqkrnetselfiPP 315
Cdd:COG3845 221 --------------GTVDTAETSEE--------EL-----------AElmvGREVLLRVE------------------KA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 316 GPRLGDKVLEINNLT-KSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQ 393
Cdd:COG3845 250 PAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLdGEDITGLSPRE 329
|
...
gi 739061588 394 FRD 396
Cdd:COG3845 330 RRR 332
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
323-471 |
6.68e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.01 E-value: 6.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTV--KL------------ 388
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDitHLpmhkrarlgigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 389 ----ASVdqFRDSmddskTVWEevsggqDIMRIGNFEIPSRA--------YVGRFNFKGVdQGKRVGELSGGERGRLHLA 456
Cdd:COG1137 83 lpqeASI--FRKL-----TVED------NILAVLELRKLSKKereerleeLLEEFGITHL-RKSKAYSLSGGERRRVEIA 148
|
170
....*....|....*
gi 739061588 457 KLLQVGGNMLLLDEP 471
Cdd:COG1137 149 RALATNPKFILLDEP 163
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
324-481 |
7.37e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 94.01 E-value: 7.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVkLASV--DQ------FR 395
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD-VTGLppEKrnvgmvFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 D-----SMddskTVWEEVSGGQDIMRIGNFEIPSRA--YVGRFNFKGVdQGKRVGELSGGERGRLHLAKLL----QVggn 464
Cdd:COG3842 85 DyalfpHL----TVAENVAFGLRMRGVPKAEIRARVaeLLELVGLEGL-ADRYPHQLSGGQQQRVALARALapepRV--- 156
|
170
....*....|....*..
gi 739061588 465 mLLLDEPTNDLDVEtLR 481
Cdd:COG3842 157 -LLLDEPLSALDAK-LR 171
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
323-511 |
9.92e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.32 E-value: 9.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL----GDTVKLASVDQF---R 395
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdggdIDDPDVAEACHYlghR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 DSMDDSKTVWEEVSGGQDIMriGNFEIPSRAYVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDL 475
Cdd:PRK13539 82 NAMKPALTVAENLEFWAAFL--GGEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 739061588 476 DVETLRALENAL---LEFPGcaMVIshdrwfldrIATHI 511
Cdd:PRK13539 159 DAAAVALFAELIrahLAQGG--IVI---------AATHI 186
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
323-512 |
1.37e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 90.50 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSY-GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGD----TVKLASVDQFRDS 397
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 398 M-----D----DSKTVWEEVSGGQDIMRIGNFEIPSRA-----YVGRFNFKgvdqGKRVGELSGGERGRLHLA------- 456
Cdd:COG2884 81 IgvvfqDfrllPDRTVYENVALPLRVTGKSRKEIRRRVrevldLVGLSDKA----KALPHELSGGEQQRVAIAralvnrp 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 457 KLlqvggnmLLLDEPTNDLDVETLRALENALLEF--PGCAMVI-SHDRWFLDRIATHII 512
Cdd:COG2884 157 EL-------LLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRMPKRVL 208
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
315-512 |
1.40e-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: 95.22 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 315 PGPRLGDKVLEINNLTKSY--GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDtVKLASVD 392
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG-VDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 393 QfrdsmddsKTVWEEVSG-GQDI----------MRIGNfeiPS-----------RAYVGRFnFKGVDQG--KRVGE---- 444
Cdd:COG4987 404 E--------DDLRRRIAVvPQRPhlfdttlrenLRLAR---PDatdeelwaaleRVGLGDW-LAALPDGldTWLGEggrr 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 445 LSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLE-FPGCAMV-ISHDRWFLDRiATHII 512
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEaLAGRTVLlITHRLAGLER-MDRIL 540
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-218 |
1.46e-20 |
|
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: 90.05 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSF-FPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR---------------PQPGIKIGYLPQEPKLN 81
Cdd:cd03297 8 KRLPDFTLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkinlPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 PEHTVREAVEEAVSELKNALNRLdevyaayadpdadfdklakeqgQLEAIIQSHDGHNLENQleraaealrlpewdaKIE 161
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNREDRI----------------------SVDELLDLLGLDHLLNR---------------YPA 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHD 218
Cdd:cd03297 131 QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHD 191
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
324-513 |
1.47e-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: 90.50 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDR----VLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSG-TLVLG-DTVK-----LASVD 392
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGfATVDGfDVVKepaeaRRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 393 QFRDSMD--DSKTVWEEVS--GGQDIMRIGNFEIPSRAYVGRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLL 468
Cdd:cd03266 82 FVSDSTGlyDRLTARENLEyfAGLYGLKGDELTARLEELADRLGMEELLD-RRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 739061588 469 DEPTNDLDVETLRALENALLEF--PGCAMVIShdrwfldriaTHIID 513
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLraLGKCILFS----------THIMQ 197
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
324-471 |
1.61e-20 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 90.68 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLG--DTVKL------------- 388
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqDITKLpmhkrarlgigyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 389 ---ASVdqFRDsmddsKTVWEEVSGGQDIMRIGNFEIPSR--AYVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGG 463
Cdd:cd03218 81 pqeASI--FRK-----LTVEENILAVLEIRGLSKKEREEKleELLEEFHITHL-RKSKASSLSGGERRRVEIARALATNP 152
|
....*...
gi 739061588 464 NMLLLDEP 471
Cdd:cd03218 153 KFLLLDEP 160
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-238 |
2.09e-20 |
|
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: 88.36 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 14 IVPPKRHIL-KNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPKLnPEHTVREAVee 92
Cdd:cd03223 8 LATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYL-PLGTLREQL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 93 avselknalnrldevyaAYAdpdadfdklakeqgqleaiiqshdghnlenqleraaealrlpeWDakiEKLSGGERRRVA 172
Cdd:cd03223 85 -----------------IYP-------------------------------------------WD---DVLSGGEQQRLA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 173 ICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHdRYFLDNVAGWILELDRGEGI 238
Cdd:cd03223 102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGEGGW 166
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
323-516 |
3.61e-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: 89.42 E-value: 3.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSY-----GDRVL--IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL---GDTVKLASVD 392
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 393 QfrdsmddsktvweevsggQDIMRIGNFEIpsrAYVGRF-----------------NFKGVDQG---KRVGEL------- 445
Cdd:COG4778 84 P------------------REILALRRRTI---GYVSQFlrviprvsaldvvaeplLERGVDREearARARELlarlnlp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 446 -----------SGGERGRLHLAKLLQVGGNMLLLDEPTNDLD-------VETLRALENAllefpGCAMV-ISHDRWFLDR 506
Cdd:COG4778 143 erlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDaanravvVELIEEAKAR-----GTAIIgIFHDEEVREA 217
|
250
....*....|
gi 739061588 507 IATHIIDYQD 516
Cdd:COG4778 218 VADRVVDVTP 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
18-236 |
4.69e-20 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 87.63 E-value: 4.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-------------ARPQPGIKIGYLPQEPKLNPEH 84
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSilidgedltdledELPPLRRRIGMVFQDFALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 TVREAVEEAvselknalnrldevyaayadpdadfdklakeqgqleaiiqshdghnlenqleraaealrlpewdakiekLS 164
Cdd:cd03229 92 TVLENIALG---------------------------------------------------------------------LS 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 165 GGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDYEG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03229 103 GGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALlksLQAQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
324-489 |
6.47e-20 |
|
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: 88.11 E-value: 6.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTVKLASVDQFrDSMDDSK 402
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEvLFDGKPLDIAARNRI-GYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 403 TVWEEVSGGQDIMRIGNF------EIPSRA--YVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTND 474
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLkglkkeEARRRIdeWLERLELSEY-ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170
....*....|....*
gi 739061588 475 LDVETLRALENALLE 489
Cdd:cd03269 159 LDPVNVELLKDVIRE 173
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
324-481 |
9.85e-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: 88.45 E-value: 9.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDtVKLASVDQFRDSMD---- 399
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG-KDITNLPPHKRPVNtvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 400 -----DSKTVWEEVSGGQDIMRIGNFEIPSRA--YVGRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:cd03300 80 nyalfPHLTVFENIAFGLRLKKLPKAEIKERVaeALDLVQLEGYAN-RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
....*....
gi 739061588 473 NDLDVEtLR 481
Cdd:cd03300 159 GALDLK-LR 166
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
323-524 |
1.16e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 88.13 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTvklasvdqfrdSMDDSK 402
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGE-----------DLTDSK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 403 TvweevsggqDIMRIgnfeipsRAYVG----RFN-F----------------KGVDQG----------KRVG-------- 443
Cdd:COG1126 70 K---------DINKL-------RRKVGmvfqQFNlFphltvlenvtlapikvKKMSKAeaeeramellERVGladkaday 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 444 --ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVE-------TLRALENAllefpGCAMVI-SHDRWFLDRIATHIId 513
Cdd:COG1126 134 paQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPElvgevldVMRDLAKE-----GMTMVVvTHEMGFAREVADRVV- 207
|
250
....*....|....*...
gi 739061588 514 YQDEGKV-------EFFE 524
Cdd:COG1126 208 FMDGGRIveegppeEFFE 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
321-499 |
1.21e-19 |
|
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: 88.60 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSG-TL-VLGDTVKLASV------- 391
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVrLFGERRGGEDVwelrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 392 --------DQFRDSMddskTVWEEV-SGGQDImrIGNFEIPSRAYVGR----FNFKGVDQ--GKRVGELSGGERGRLHLA 456
Cdd:COG1119 81 glvspalqLRFPRDE----TVLDVVlSGFFDS--IGLYREPTDEQRERarelLELLGLAHlaDRPFGTLSQGEQRRVLIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 739061588 457 KLLQVGGNMLLLDEPTNDLDV---ETLRALENALLEFPGCAMV-ISH 499
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLgarELLLALLDKLAAEGAPTLVlVTH 201
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
323-521 |
1.39e-19 |
|
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: 91.89 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSY--GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPD---SGTLVLGDTVKLASVDQFR-- 395
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 -------DSMD--DSKTVWEEVSGGQDIMRIGNFEIPSRAyVGRFNFKGVDQ--GKRVGELSGGERGRLHLAKLLQVGGN 464
Cdd:COG1123 84 rigmvfqDPMTqlNPVTVGDQIAEALENLGLSRAEARARV-LELLEAVGLERrlDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 465 MLLLDEPTNDLDVETLR---ALENALLEFPGCAMV-ISHDRWFLDRIATHIIDYQDEGKVE 521
Cdd:COG1123 163 LLIADEPTTALDVTTQAeilDLLRELQRERGTTVLlITHDLGVVAEIADRVVVMDDGRIVE 223
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
323-530 |
1.52e-19 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 91.88 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLA--SVDQFR----- 395
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGklRQDQFAfeeft 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 --DS--MDDSKtVWE------------EVSgGQDIMRIGNFEipsrayvGRF-NFKGVDQGKRVGEL------------- 445
Cdd:PRK15064 81 vlDTviMGHTE-LWEvkqerdriyalpEMS-EEDGMKVADLE-------VKFaEMDGYTAEARAGELllgvgipeeqhyg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 446 -----SGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEFpGCAMV-ISHDRWFLDRIATHIIDYqDEGK 519
Cdd:PRK15064 152 lmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNER-NSTMIiISHDRHFLNSVCTHMADL-DYGE 229
|
250
....*....|.
gi 739061588 520 VEFFEGNFTEY 530
Cdd:PRK15064 230 LRVYPGNYDEY 240
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-190 |
1.73e-19 |
|
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: 87.49 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEG---EARPQPGikIGYLPQEPKLNPEHT 85
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLlpprsgsirfdGRDITGlppHERARAG--IGYVPEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 86 VREAVEEAVSELKNALN--RLDEVYAAyadpdadFDKLAkeqgqleaiiqshdghnlenqlERaaealrlpeWDAKIEKL 163
Cdd:cd03224 92 VEENLLLGAYARRRAKRkaRLERVYEL-------FPRLK----------------------ER---------RKQLAGTL 133
|
170 180
....*....|....*....|....*..
gi 739061588 164 SGGERRRVAICRLLLEKPDMLLLDEPT 190
Cdd:cd03224 134 SGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
37-371 |
1.79e-19 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 91.61 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 37 VLGLNGAGKSTLLRIMAGIDTDIEGEARPQPgikigylpqepklnpEHTVR---EAVEEAVSE--LKNALNRLDEvyaay 111
Cdd:PRK10938 34 FVGANGSGKSALARALAGELPLLSGERQSQF---------------SHITRlsfEQLQKLVSDewQRNNTDMLSP----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 112 aDPDaDFDKLAKEqgqleaIIQshDGHNLENQLERAAEALRL-PEWDAKIEKLSGGERRRVAICRLLLEKPDMLLLDEPT 190
Cdd:PRK10938 94 -GED-DTGRTTAE------IIQ--DEVKDPARCEQLAQQFGItALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 191 NHLDAESVAWLERFLHDYEGTVVAIthdryfldnvagwILELDRGEGIPwegnysswleqkdarleqeaatEAARHKSIQ 270
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQSGITL-------------VLVLNRFDEIP----------------------DFVQFAGVL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 271 KELEWIRQNPKGR--QAKGKARLARFEELNSVDYQKRNETS-ELFIPPG-PRlgdkvLEINNLTKSYGDRVLIDDLSFSI 346
Cdd:PRK10938 209 ADCTLAETGEREEilQQALVAQLAHSEQLEGVQLPEPDEPSaRHALPANePR-----IVLNNGVVSYNDRPILHNLSWQV 283
|
330 340
....*....|....*....|....*
gi 739061588 347 PKGAIVGIIGPNGAGKSTLFRMISG 371
Cdd:PRK10938 284 NPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-218 |
2.87e-19 |
|
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: 90.88 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE---------ARPQPGIK--IGYLPQEPKLNpEH 84
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEvtldgvpvsSLDQDEVRrrVSVCAQDAHLF-DT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 TVREAVeeavselknalnRLdevyaayADPDADfdklakeqgqleaiiqshdghnlENQLERAAEALRLPEWDAKIE--- 161
Cdd:TIGR02868 424 TVRENL------------RL-------ARPDAT-----------------------DEELWAALERVGLADWLRALPdgl 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739061588 162 ---------KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHD 218
Cdd:TIGR02868 462 dtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAlsGRTVVLITHH 529
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
324-476 |
3.17e-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: 86.15 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTV--KLASVDqfRD----- 396
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtDLPPKD--RDiamvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 397 ---SMDDSKTVWEEVSGGQDIMRIGNFEIPSRAY-VGRfnFKGVDQ--GKRVGELSGGERGRLHLAKLLQVGGNMLLLDE 470
Cdd:cd03301 79 qnyALYPHMTVYDNIAFGLKLRKVPKDEIDERVReVAE--LLQIEHllDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
....*.
gi 739061588 471 PTNDLD 476
Cdd:cd03301 157 PLSNLD 162
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
323-507 |
3.35e-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: 86.64 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGD-----RVLiDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLG-DTVKLASVD--- 392
Cdd:TIGR02211 1 LLKCENLGKRYQEgkldtRVL-KGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEvLFNGqSLSKLSSNErak 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 393 ----------QFRDSMDDSkTVWEEVSGGqdiMRIGNF---EIPSRAYVgrfNFKGVDQGKRV----GELSGGERGRLHL 455
Cdd:TIGR02211 80 lrnkklgfiyQFHHLLPDF-TALENVAMP---LLIGKKsvkEAKERAYE---MLEKVGLEHRInhrpSELSGGERQRVAI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 456 AKLLQVGGNMLLLDEPTNDLDVETLRALENALLEF---PGCAMVI-SHDRWFLDRI 507
Cdd:TIGR02211 153 ARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELnreLNTSFLVvTHDLELAKKL 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
324-501 |
3.43e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 89.01 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQfRD------ 396
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDVTHRSIQQ-RDicmvfq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 397 --SMDDSKTVWEEVSGGQDIMRIGNFEIPSR-----AYV--GRFNFKGVDQgkrvgeLSGGERGRLHLAKLLQVGGNMLL 467
Cdd:PRK11432 86 syALFPHMSLGENVGYGLKMLGVPKEERKQRvkealELVdlAGFEDRYVDQ------ISGGQQQRVALARALILKPKVLL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 739061588 468 LDEPTNDLDVETLRALENALLE----FPGCAMVISHDR 501
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRElqqqFNITSLYVTHDQ 197
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
324-499 |
3.65e-19 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 84.96 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGD--RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQFRDSMdd 400
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDPNELGDHV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 401 sktvweevsgG---QDIMRignfeipsrayvgrfnFKGVdqgkrVGE--LSGGERGRLHLAKLLQVGGNMLLLDEPTNDL 475
Cdd:cd03246 79 ----------GylpQDDEL----------------FSGS-----IAEniLSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180
....*....|....*....|....*..
gi 739061588 476 DVETLRALENALLEFPGC---AMVISH 499
Cdd:cd03246 128 DVEGERALNQAIAALKAAgatRIVIAH 154
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
323-520 |
3.92e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 86.69 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVD--------- 392
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdGLKVNDPKVDerlirqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 393 ----QFrdSMDDSKTVWEEVSGGQDIMRiGNFEIPSRAyVGRFNFKGVDQGKRVG----ELSGGERGRLHLAKLLQVGGN 464
Cdd:PRK09493 81 mvfqQF--YLFPHLTALENVMFGPLRVR-GASKEEAEK-QARELLAKVGLAERAHhypsELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 465 MLLLDEPTNDLDV----ETLRALENALLEfpGCAMVI-SHDRWFLDRIATHIIdYQDEGKV 520
Cdd:PRK09493 157 LMLFDEPTSALDPelrhEVLKVMQDLAEE--GMTMVIvTHEIGFAEKVASRLI-FIDKGRI 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-217 |
9.66e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 85.91 E-value: 9.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------GIDTDIEGEARPQPGI-----KIGYLPQE--PKLNPEH 84
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgdlpptyGNDVRLFGERRGGEDVwelrkRIGLVSPAlqLRFPRDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 TVREAVeeaVSELKNALNRldevyaaYADPDadfdklakeqgqleaiiqshdghnlENQLERAAEALRLPEWDAKIEK-- 162
Cdd:COG1119 96 TVLDVV---LSGFFDSIGL-------YREPT-------------------------DEQRERARELLELLGLAHLADRpf 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 163 --LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITH 217
Cdd:COG1119 141 gtLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
21-266 |
1.16e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 85.45 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-----------ARPQPGI------KIGYLPQEPKLNPE 83
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQlniaghqfdfsQKPSEKAirllrqKVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 84 HTVREAVEEAVSELKnalnrldevyaayadpdadfdKLAKEQGQLEAIiqshdghNLENQLERAAEALRLPEwdakieKL 163
Cdd:COG4161 97 LTVMENLIEAPCKVL---------------------GLSKEQAREKAM-------KLLARLRLTDKADRFPL------HL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 164 SGGERRRVAICRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIpw 240
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEitaQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII-- 220
|
250 260
....*....|....*....|....*.
gi 739061588 241 egnysswlEQKDARLEQEAATEAARH 266
Cdd:COG4161 221 --------EQGDASHFTQPQTEAFAH 238
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-235 |
1.23e-18 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 89.33 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 14 IVPP--KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQEPKL 80
Cdd:TIGR01842 324 IVPPggKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIwpptsgsvrldGADLKQWDRETFGKHIGYLPQDVEL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 81 NPeHTVREAV----EEAVSElknalnrldEVYAAyadpdadfdklAKEQGQLEAIiqshdghnlenqleraaeaLRLPE- 155
Cdd:TIGR01842 404 FP-GTVAENIarfgENADPE---------KIIEA-----------AKLAGVHELI-------------------LRLPDg 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 156 WDAKI----EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYE---GTVVAITHdRYFLDNVAGW 228
Cdd:TIGR01842 444 YDTVIgpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITH-RPSLLGCVDK 522
|
....*..
gi 739061588 229 ILELDRG 235
Cdd:TIGR01842 523 ILVLQDG 529
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
324-520 |
1.42e-18 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 84.38 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVL-IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDT----VKLASVDQFRDSM 398
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 399 ----DDSK-----TVWEEVSGGQDIMRIGNFEIPSRAyVGRFNFKGVDQGKRV--GELSGGERGRLHLAKLLQVGGNMLL 467
Cdd:cd03292 81 gvvfQDFRllpdrNVYENVAFALEVTGVPPREIRKRV-PAALELVGLSHKHRAlpAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 468 LDEPTNDLDVETLRALENALLEF--PGCAMVIS-HDRWFLDRIATHIIDYQDeGKV 520
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKInkAGTTVVVAtHAKELVDTTRHRVIALER-GKL 214
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-239 |
3.43e-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: 87.92 E-value: 3.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 32 GAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEArpQPGIKIGYLPQEPKLNPEHTVREAVEEAVSElknalnRLDEVYAay 111
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGTVEEFLRSANTD------DFGSSYY-- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 112 adpdadfdklakeqgQLEaIIQshdGHNLENQLERaaealrlpewdaKIEKLSGGERRRVAICRLLLEKPDMLLLDEPTN 191
Cdd:COG1245 436 ---------------KTE-IIK---PLGLEKLLDK------------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 192 HLDAE---SVA-WLERFLHDYEGTVVAITHDRYFLDNVAgwilelDRG---EGIP 239
Cdd:COG1245 485 HLDVEqrlAVAkAIRRFAENRGKTAMVVDHDIYLIDYIS------DRLmvfEGEP 533
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-236 |
3.65e-18 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 83.23 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 8 MLRVGKIVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT--------------DIEGEARPQPGIKIGY 73
Cdd:cd03292 3 FINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELptsgtirvngqdvsDLRGRAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 74 LPQEPKLNPEHTVREAVeeavselknalnrldevyaAYAdpdadfdklakeqgqLEAIiqshdGHNLENQLERAAEALRL 153
Cdd:cd03292 83 VFQDFRLLPDRNVYENV-------------------AFA---------------LEVT-----GVPPREIRKRVPAALEL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 154 PEWDAKI----EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFL---HDYEGTVVAITHDRYFLDNVA 226
Cdd:cd03292 124 VGLSHKHralpAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLkkiNKAGTTVVVATHAKELVDTTR 203
|
250
....*....|
gi 739061588 227 GWILELDRGE 236
Cdd:cd03292 204 HRVIALERGK 213
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
21-219 |
3.69e-18 |
|
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: 83.56 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgikIGYLPQEpklnpehtVREAVEEAVSELKNa 100
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGE--------VLFNGQS--------LSKLSSNERAKLRN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 101 lNRLDEVYAaYADPDADFDKLakEQGQLEAIIQshdGHNLENQLERAAEALRLPEWDAKIEK----LSGGERRRVAICRL 176
Cdd:TIGR02211 83 -KKLGFIYQ-FHHLLPDFTAL--ENVAMPLLIG---KKSVKEAKERAYEMLEKVGLEHRINHrpseLSGGERQRVAIARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 739061588 177 LLEKPDMLLLDEPTNHLD---AESVAWLERFLHDYEGT-VVAITHDR 219
Cdd:TIGR02211 156 LVNQPSLVLADEPTGNLDnnnAKIIFDLMLELNRELNTsFLVVTHDL 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
323-499 |
3.95e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.93 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRDSM---- 398
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 399 -----DDSKTVWE------EVSGGQDimrigNFEIpsRAYVGRFNFKGVDQGKrVGELSGGERGRLHLAKLLQVGGNMLL 467
Cdd:PRK13538 81 hqpgiKTELTALEnlrfyqRLHGPGD-----DEAL--WEALAQVGLAGFEDVP-VRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*
gi 739061588 468 LDEPTNDLD---VETLRALENALLEFPGCAMVISH 499
Cdd:PRK13538 153 LDEPFTAIDkqgVARLEALLAQHAEQGGMVILTTH 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
18-194 |
4.11e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.01 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIGYLPQEPKLNPehTVREAVEEAVsEL 97
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDT--TLPLTVNRFL-RL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 98 KNALNRLDevyaayadpdadfdklakeqgQLEAIIQSHDGHNLenqleraaealrlpewDAKIEKLSGGERRRVAICRLL 177
Cdd:PRK09544 93 RPGTKKED---------------------ILPALKRVQAGHLI----------------DAPMQKLSGGETQRVLLARAL 135
|
170
....*....|....*..
gi 739061588 178 LEKPDMLLLDEPTNHLD 194
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVD 152
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
324-479 |
5.20e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 85.51 E-value: 5.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSY----GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLG--DTVKLASVD--QFR 395
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDgvDLTALSERElrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 DSMD---------DSKTVWE------EVSGgqdimrignfeipsrayvgrfnFKGVDQGKRVGE---------------- 444
Cdd:COG1135 82 RKIGmifqhfnllSSRTVAEnvalplEIAG----------------------VPKAEIRKRVAEllelvglsdkadayps 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 739061588 445 -LSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVET 479
Cdd:COG1135 140 qLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-226 |
5.28e-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: 5.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 28 SFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEArPQPGIKIGYLPQEPKLNPEHTVREAVEEAVSELKNALNRLDEV 107
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-EIELDTVSYKPQYIKADYEGTVRDLLSSITKDFYTHPYFKTEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 108 yaayADPdadfdklakeqGQLEAIIQShdghnlenqleraaealRLPEwdakiekLSGGERRRVAICRLLLEKPDMLLLD 187
Cdd:cd03237 100 ----AKP-----------LQIEQILDR-----------------EVPE-------LSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739061588 188 EPTNHLDAE----SVAWLERFLHDYEGTVVAITHDRYFLDNVA 226
Cdd:cd03237 141 EPSAYLDVEqrlmASKVIRRFAENNEKTAFVVEHDIIMIDYLA 183
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
324-482 |
5.41e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 85.51 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTV--KLASVDqfRD-SMD- 399
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtDLPPKD--RNiAMVf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 400 ------DSKTVWEEVSGGQDIMRIGNFEIPSRayvgrfnfkgVDQ-----------GKRVGELSGGERGRLHLAKLL--- 459
Cdd:COG3839 82 qsyalyPHMTVYENIAFPLKLRKVPKAEIDRR----------VREaaellgledllDRKPKQLSGGQRQRVALGRALvre 151
|
170 180
....*....|....*....|....
gi 739061588 460 -QVggnmLLLDEPTNDLDVEtLRA 482
Cdd:COG3839 152 pKV----FLLDEPLSNLDAK-LRV 170
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
20-219 |
5.53e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 85.53 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEG---EARPqpgikIGYLPQEPKLNPEHT 85
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFetpdsgrilldGRDVTGlppEKRN-----VGMVFQDYALFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 86 VREAVEEAvseLKnalnrldevyaayadpdadFDKLAKEQgqleaiiqshdghnlenQLERAAEAL---RLPEW-DAKIE 161
Cdd:COG3842 94 VAENVAFG---LR-------------------MRGVPKAE-----------------IRARVAELLelvGLEGLaDRYPH 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDA---ESV-AWLERFLHDYEGTVVAITHDR 219
Cdd:COG3842 135 QLSGGQQQRVALARALAPEPRVLLLDEPLSALDAklrEEMrEELRRLQRELGITFIYVTHDQ 196
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
18-236 |
5.56e-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: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT------DIEGEARPQPGI-------KIGYLPQEPKLNPEH 84
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiIIDGLKLTDDKKninelrqKVGMVFQQFNLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 TVREAVEEAVSELKnalnrldevyaayadpdadfdKLAKEQGQleaiiqshdghnlenqlERAAEALR---LPEW-DAKI 160
Cdd:cd03262 92 TVLENITLAPIKVK---------------------GMSKAEAE-----------------ERALELLEkvgLADKaDAYP 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 161 EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD--YEG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03262 134 AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlaEEGmTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
313-490 |
6.14e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 82.70 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 313 IPPGPRLGDkVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQE--QPDSGTLVLGDtvklas 390
Cdd:COG2401 21 LDLSERVAI-VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 391 vDQFrdsmddsktvWEEVSGGQDIMRIGNF----EIPSRA-YVGRFNFKgvdqgKRVGELSGGERGRLHLAKLLQVGGNM 465
Cdd:COG2401 94 -NQF----------GREASLIDAIGRKGDFkdavELLNAVgLSDAVLWL-----RRFKELSTGQKFRFRLALLLAERPKL 157
|
170 180
....*....|....*....|....*
gi 739061588 466 LLLDEPTNDLDVETLRALENALLEF 490
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKL 182
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-242 |
6.60e-18 |
|
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: 82.93 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT-----------DIEG--EARPQP-GIKIGYLPQEPKLNPEH 84
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpdsgevlidgeDISGlsEAELYRlRRRMGMLFQSGALFDSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 TVREAVEEAVSELknalnrldevyaaYADPDADFDKLAKEQgqLEAIiqshdghNLEnqleraAEALRLPEwdakieKLS 164
Cdd:cd03261 93 TVFENVAFPLREH-------------TRLSEEEIREIVLEK--LEAV-------GLR------GAEDLYPA------ELS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 165 GGERRRVAICRLLLEKPDMLLLDEPTNHLD---AESVAWLERFLHDYEG-TVVAITHDRYFLDNVAGWILELDRGEgIPW 240
Cdd:cd03261 139 GGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIADRIAVLYDGK-IVA 217
|
..
gi 739061588 241 EG 242
Cdd:cd03261 218 EG 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
333-490 |
6.69e-18 |
|
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: 83.15 E-value: 6.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 333 YGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRDS----MDDSKTVWEEV 408
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRigvvFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 409 SGG------QDIMRIGNFEIPSRA-------YVGRFnfkgVDQGKRvgELSGGERGRLHLAKLLQVGGNMLLLDEPTNDL 475
Cdd:cd03267 111 PVIdsfyllAAIYDLPPARFKKRLdelsellDLEEL----LDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170
....*....|....*
gi 739061588 476 DVETLRALENALLEF 490
Cdd:cd03267 185 DVVAQENIRNFLKEY 199
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
324-490 |
7.35e-18 |
|
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: 81.59 E-value: 7.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYG--DRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRDSMdds 401
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 402 kTVweevsggqdimrignfeIPSRAYVgrFNFKGVDQ-GKRvgeLSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETL 480
Cdd:cd03247 78 -SV-----------------LNQRPYL--FDTTLRNNlGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170
....*....|
gi 739061588 481 RALENALLEF 490
Cdd:cd03247 135 RQLLSLIFEV 144
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-477 |
7.54e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.64 E-value: 7.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT------DIEGEAR----PQPGIKIG-YL-PQEPKLNPEHTVRE 88
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPpdsgtlEIGGNPCarltPAKAHQLGiYLvPQEPLLFPNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 89 aveeavselkNALNRLdevyaayADPDADFDKLAkeqgQLEAIIQSHdghnlenqleraaeaLRLpewDAKIEKLSGGER 168
Cdd:PRK15439 106 ----------NILFGL-------PKRQASMQKMK----QLLAALGCQ---------------LDL---DSSAGSLEVADR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 169 RRVAICRLLLEKPDMLLLDEPTNHLD-AESVAWLERF--LHDYEGTVVAITHDRYFLDNVAGWILELdRGEGIPWEGNYS 245
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTpAETERLFSRIreLLAQGVGIVFISHKLPEIRQLADRISVM-RDGTIALSGKTA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 246 SWleqKDARLEQeAATEAARHKSIQKELEWIRQNPKGR--QAKGKARLaRFEELnsvdyqkrneTSELFIppgprlgdkv 323
Cdd:PRK15439 226 DL---STDDIIQ-AITPAAREKSLSASQKLWLELPGNRrqQAAGAPVL-TVEDL----------TGEGFR---------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 leinnltksygdrvlidDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDtvKLASVDQFRDSMD---- 399
Cdd:PRK15439 281 -----------------NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG--KEINALSTAQRLArglv 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 400 -------------DSKTVWEEVSGGQDimRIGNFEIPSR--AYVGRF------NFKGVDQGkrVGELSGGERGRLHLAKL 458
Cdd:PRK15439 342 ylpedrqssglylDAPLAWNVCALTHN--RRGFWIKPARenAVLERYrralniKFNHAEQA--ARTLSGGNQQKVLIAKC 417
|
490
....*....|....*....
gi 739061588 459 LQVGGNMLLLDEPTNDLDV 477
Cdd:PRK15439 418 LEASPQLLIVDEPTRGVDV 436
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
323-511 |
1.06e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.84 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGD-RVLiDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVdqfRDSMD- 399
Cdd:COG1129 4 LLEMRGISKSFGGvKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVRFRSP---RDAQAa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 400 ------------DSKTVWEEVSGGQDIMRIGNFEIP-----SRAYVGRFNFKgVDQGKRVGELSGGERGRLHLAKLLQVG 462
Cdd:COG1129 80 giaiihqelnlvPNLSVAENIFLGREPRRGGLIDWRamrrrARELLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 463 GNMLLLDEPT---NDLDVETLRALENALLEfPGCAMV-ISHdrwFLD---RIATHI 511
Cdd:COG1129 159 ARVLILDEPTaslTEREVERLFRIIRRLKA-QGVAIIyISH---RLDevfEIADRV 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-218 |
1.16e-17 |
|
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: 82.13 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD------IEGEARPQPGIKIGYLPQEPKLNPEHTVREAVEEAVS 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPtsggviLEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 96 ELKNALNRldevyaayadpdadfdklakeqGQLEAIIQSHdgHNLENqLERAAealrlpewDAKIEKLSGGERRRVAICR 175
Cdd:TIGR01184 81 RVLPDLSK----------------------SERRAIVEEH--IALVG-LTEAA--------DKRPGQLSGGMKQRVAIAR 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 739061588 176 LLLEKPDMLLLDEPTNHLDAESVAWLE----RFLHDYEGTVVAITHD 218
Cdd:TIGR01184 128 ALSIRPKVLLLDEPFGALDALTRGNLQeelmQIWEEHRVTVLMVTHD 174
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
285-509 |
1.19e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 86.37 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 285 AKGKARLARFEELnsvdyqkRNETSELFIPPGPRLGDKV---LEINNLTKSY-GDRVLIDDLSFSIPKGAIVGIIGPNGA 360
Cdd:COG1132 305 QRALASAERIFEL-------LDEPPEIPDPPGAVPLPPVrgeIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 361 GKSTLFRMISGQEQPDSGTLVLGDT-VKLASVDQFRDSM-----DD---SKTVWEEVsggqdimRIGNFEIP-------- 423
Cdd:COG1132 378 GKSTLVNLLLRFYDPTSGRILIDGVdIRDLTLESLRRQIgvvpqDTflfSGTIRENI-------RYGRPDATdeeveeaa 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 424 SRAYVGRF--NF-KGVDQgkRVGE----LSGGERGRLHLAKLL----QVggnmLLLDEPTNDLDVETLRALENALLEF-P 491
Cdd:COG1132 451 KAAQAHEFieALpDGYDT--VVGErgvnLSGGQRQRIAIARALlkdpPI----LILDEATSALDTETEALIQEALERLmK 524
|
250
....*....|....*....
gi 739061588 492 GCAM-VISHdrwfldRIAT 509
Cdd:COG1132 525 GRTTiVIAH------RLST 537
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
20-218 |
1.57e-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: 81.71 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGearpqpgikigylpqepklnpehTVREAVEEavselkn 99
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSG-----------------------TVRLAGQD------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 100 aLNRLDEvyaayadpdadfDKLAKEQGQLEAII-QSHdgH------NLENQL------------ERAAEAL-------RL 153
Cdd:COG4181 76 -LFALDE------------DARARLRARHVGFVfQSF--QllptltALENVMlplelagrrdarARARALLervglghRL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 154 pewDAKIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHDYEG-TVVAITHD 218
Cdd:COG4181 141 ---DHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAatgEQIIDLLFELNRERGtTLVLVTHD 206
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-218 |
1.59e-17 |
|
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: 82.00 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARpqpgiKIGYLPQEPKlnPEHTVREAVeeaVSELKNAL 101
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR-----VAGLVPWKRR--KKFLRRIGV---VFGQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 102 nrldevyaAYADPDADFDKLakeqgqLEAIIQSHDGHNLENqLERAAEALRL-PEWDAKIEKLSGGERRRVAICRLLLEK 180
Cdd:cd03267 107 --------WWDLPVIDSFYL------LAAIYDLPPARFKKR-LDELSELLDLeELLDTPVRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 739061588 181 PDMLLLDEPTNHLDAESVAWLERFLHDY----EGTVVAITHD 218
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHY 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
341-500 |
2.02e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 81.19 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 341 DLSFSIPkGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRDSMDDSK--------------TVWE 406
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKiglvfqqyalfphlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 407 EVSGGQDIMRIGNFEIPSRAYVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENA 486
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170
....*....|....*...
gi 739061588 487 LLE----FPGCAMVISHD 500
Cdd:cd03297 174 LKQikknLNIPVIFVTHD 191
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-218 |
2.92e-17 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 81.07 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGI-------KIGYLPQEPk 79
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipgapdegEVLLDGKDIYDLDVdvlelrrRVGMVFQKP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 80 lNPEH-TVREAVeeavselknalnrldevyaAYAdpdadfdklAKEQGqleaiiqSHDGHNLEnqlERAAEALRLPE-WD 157
Cdd:cd03260 91 -NPFPgSIYDNV-------------------AYG---------LRLHG-------IKLKEELD---ERVEEALRKAAlWD 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739061588 158 -----AKIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHD 218
Cdd:cd03260 132 evkdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-235 |
3.57e-17 |
|
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: 80.85 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD------IEGEARPQPGIK---IGYLPQEPKLNPEHTVREAVEE 92
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdsgtilFGGEDATDVPVQernVGFVFQHYALFRHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 93 AVsELKNALNRldevyaayaDPDADFDKLAKEQGQLEaiiqshdghnlenQLERAAEalRLPEwdakieKLSGGERRRVA 172
Cdd:cd03296 98 GL-RVKPRSER---------PPEAEIRAKVHELLKLV-------------QLDWLAD--RYPA------QLSGGQRQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 173 ICRLLLEKPDMLLLDEPTNHLDA----ESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
324-487 |
3.85e-17 |
|
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: 79.84 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTvklaSVDQFRDSMDDS-- 401
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG----PLDFQRDSIARGll 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 402 --------KTVWEEVSGGQDIMRIGNFEIPSRAyVGRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTN 473
Cdd:cd03231 77 ylghapgiKTTLSVLENLRFWHADHSDEQVEEA-LARVGLNGFED-RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170
....*....|....
gi 739061588 474 DLDVETLRALENAL 487
Cdd:cd03231 155 ALDKAGVARFAEAM 168
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-218 |
4.22e-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: 80.84 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR-------PQPGIK--IGYLPQEPKLNPEHTVREAVEE 92
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditNLPPEKrdISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 93 AVSELKNalnrldevyaayadPDADFDKLAKEQGQLEAIiqshdGHNLenqleraaealrlpewDAKIEKLSGGERRRVA 172
Cdd:cd03299 95 GLKKRKV--------------DKKEIERKVLEIAEMLGI-----DHLL----------------NRKPETLSGGEQQRVA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 739061588 173 ICRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHD-YEGTVVAITHD 218
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVrtkEKLREELKKIRKeFGVTVLHVTHD 189
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
324-501 |
4.68e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.82 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLG--DTVKLASVDQ-------- 393
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgtDVSRLHARDRkvgfvfqh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 ---FRdSMddskTVWEEVSGGQDIM--RignfEIPSRAYVGRFNFKGVD--QGKRVGE-----LSGGERGRLHLAKLLQV 461
Cdd:PRK10851 83 yalFR-HM----TVFDNIAFGLTVLprR----ERPNAAAIKAKVTQLLEmvQLAHLADrypaqLSGGQKQRVALARALAV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 739061588 462 GGNMLLLDEPTNDLDVET-------LRALENallEFPGCAMVISHDR 501
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVrkelrrwLRQLHE---ELKFTSVFVTHDQ 197
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-218 |
4.84e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.35 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQEPKLNPEHTVREA 89
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTltptagtvlvaGDDVEALSARAASRRVASVPQDTSLSFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 90 VEEAVSELKNALNRLDEVyaayadpdadfDKLAKEQgqleAIiqshdghnleNQLERAAEAlrlpewDAKIEKLSGGERR 169
Cdd:PRK09536 98 VEMGRTPHRSRFDTWTET-----------DRAAVER----AM----------ERTGVAQFA------DRPVTSLSGGERQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739061588 170 RVAICRLLLEKPDMLLLDEPTNHLDA-ESVAWLE--RFLHDYEGTVVAITHD 218
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDInHQVRTLElvRRLVDDGKTAVAAIHD 198
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-189 |
5.49e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.46 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGE---ARPQPGIkiGYLPQEP----K 79
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLvkpdsgrifldGEDITHLpmhKRARLGI--GYLPQEAsifrK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 80 LnpehTVREAVeEAVSELknalnrldevyaayadpdADFDKLAKEQgQLEAIIQshdghnlENQLERaaeaLRlpewDAK 159
Cdd:COG1137 93 L----TVEDNI-LAVLEL------------------RKLSKKEREE-RLEELLE-------EFGITH----LR----KSK 133
|
170 180 190
....*....|....*....|....*....|
gi 739061588 160 IEKLSGGERRRVAICRLLLEKPDMLLLDEP 189
Cdd:COG1137 134 AYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
324-500 |
6.07e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 80.74 E-value: 6.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL-------VLGDTVKLASVDQFRD 396
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgQLRDLYALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 397 SMDDSKTVWE--------EVSGGQDI----MRIGNfeipsRAYvGRFNFKGVDQGKRV-----------GELSGGERGRL 453
Cdd:PRK11701 87 LRTEWGFVHQhprdglrmQVSAGGNIgerlMAVGA-----RHY-GDIRATAGDWLERVeidaariddlpTTFSGGMQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 454 HLAKLLQVGGNMLLLDEPTNDLDV-------ETLRALENALlefpGCAMVI-SHD 500
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVsvqarllDLLRGLVREL----GLAVVIvTHD 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
322-379 |
6.19e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.51 E-value: 6.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 322 KVLEINNLTKSY----------------------GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT 379
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
324-472 |
6.34e-17 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 79.79 E-value: 6.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDT----------VK--LASV 391
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppherARagIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 392 DQFRD---SMddskTVWEE-VSGGQDIMRIGNFEIPSRAYvGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLL 467
Cdd:cd03224 81 PEGRRifpEL----TVEENlLLGAYARRRAKRKARLERVY-ELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
....*
gi 739061588 468 LDEPT 472
Cdd:cd03224 156 LDEPS 160
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-225 |
6.48e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.31 E-value: 6.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR-------PQPGIKIGYLPQEPKLNPEHTVREAV 90
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgepldPEDRRRIGYLPEERGLYPKMKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 91 eeavselknalnrldeVYaayadpdadfdkLAKEQGQLEAIIQshdgHNLENQLERaaeaLRLPEW-DAKIEKLSGGERR 169
Cdd:COG4152 93 ----------------VY------------LARLKGLSKAEAK----RRADEWLER----LGLGDRaNKKVEELSKGNQQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 170 RVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDryfLDNV 225
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGtTVIFSSHQ---MELV 192
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
324-520 |
6.59e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.18 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLidDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQFRDSM---D 399
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWnGQDLTALPPAERPVSMlfqE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 400 D----SKTVWEEVS-GGQDIMRIGNFEipsRAYV----GRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLLDE 470
Cdd:COG3840 80 NnlfpHLTVAQNIGlGLRPGLKLTAEQ---RAQVeqalERVGLAGLLD-RLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 471 PTNDLD----------VETLRALENALLefpgcaMVISHDrwfLD---RIATHIIdYQDEGKV 520
Cdd:COG3840 156 PFSALDpalrqemldlVDELCRERGLTV------LMVTHD---PEdaaRIADRVL-LVADGRI 208
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
324-507 |
6.60e-17 |
|
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: 79.11 E-value: 6.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGqeqpDSGTLVLGDTVKLasvdqfrdsmddskt 403
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----HPKYEVTEGEILF--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 404 vweevsGGQDIMrigNFEIPSRAYVGRF---------------NF-KGVDQGkrvgeLSGGERGRLHLAKLLQVGGNMLL 467
Cdd:cd03217 62 ------KGEDIT---DLPPEERARLGIFlafqyppeipgvknaDFlRYVNEG-----FSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739061588 468 LDEPTNDLDVETLRALENALLEF--PGCAM-VISHDRWFLDRI 507
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLreEGKSVlIITHYQRLLDYI 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
324-507 |
7.21e-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: 79.56 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGD--RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTlVLGDTVKLASVD--------- 392
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGS-VLLDGTDIRQLDpadlrrnig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 393 ---Q----FRDSMDDSKTVWEEVSGGQDIMRIGNFeipsrAYVGRF---NFKGVDqgKRVGE----LSGGERGRLHLAKL 458
Cdd:cd03245 82 yvpQdvtlFYGTLRDNITLGAPLADDERILRAAEL-----AGVTDFvnkHPNGLD--LQIGErgrgLSGGQRQAVALARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739061588 459 LQVGGNMLLLDEPTNDLDVETLRALENALLEFPG--CAMVISHDRWFL---DRI 507
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLdlvDRI 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-236 |
7.29e-17 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 80.17 E-value: 7.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGE---ARPQPGikIGYLPQEPKLNPEHT 85
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFlrptsgsvlfdGEDITGLpphEIARLG--IGRTFQIPRLFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 86 VREAVEeavselknalnrldevyaayadpdadfdkLAKEQGQLEAIIQSHDGHNLENQLERAAEALRL----PEWDAKIE 161
Cdd:cd03219 92 VLENVM-----------------------------VAAQARTGSGLLLARARREEREARERAEELLERvglaDLADRPAG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLLLDEPT---NHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-218 |
7.75e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 79.80 E-value: 7.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 8 MLRVGKIVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------------ARPqpgIKIgy 73
Cdd:COG3840 1 MLRLDDLTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRilwngqdltalppaERP---VSM-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 74 LPQEPKLNPEHTVREAVeeavselknALNRldevyaayaDPDAdfdKL-AKEQGQLEAIIQSHdghNLENQLERaaealr 152
Cdd:COG3840 76 LFQENNLFPHLTVAQNI---------GLGL---------RPGL---KLtAEQRAQVEQALERV---GLAGLLDR------ 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 153 LPEwdakieKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD 218
Cdd:COG3840 126 LPG------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-217 |
8.65e-17 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 79.97 E-value: 8.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---ID-TDIEGEARPQPGIKIGYLPQEpklnpeh 84
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvsSGsilIDgQDIREVTLDSLRRAIGVVPQD------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 TVreaveeavseLKNalnrlDEVYA--AYADPDADfdklakeqgqleaiiqshdghnlENQLERAAEA-------LRLPE 155
Cdd:cd03253 84 TV----------LFN-----DTIGYniRYGRPDAT-----------------------DEEVIEAAKAaqihdkiMRFPD 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 156 -WDAKI-E---KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG--TVVAITH 217
Cdd:cd03253 126 gYDTIVgErglKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAH 194
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-241 |
1.22e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.82 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAgidtdieGEARPQPG-IKI-----------------GYLPQEPK 79
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS-------GELSPDSGeVRLngrpladwspaelarrrAVLPQHSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 80 LNPEHTVREAVeeavselknALNRLDevyaayadpdadfdkLAKEQGQLEAIIQShdghnlenQLERA-AEALRlpewDA 158
Cdd:PRK13548 87 LSFPFTVEEVV---------AMGRAP---------------HGLSRAEDDALVAA--------ALAQVdLAHLA----GR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 159 KIEKLSGGERRRVAICRLLL------EKPDMLLLDEPTNHLD---AESVAWLER-FLHDYEGTVVAITHD-----RYfld 223
Cdd:PRK13548 131 DYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDlahQHHVLRLARqLAHERGLAVIVVLHDlnlaaRY--- 207
|
250 260
....*....|....*....|..
gi 739061588 224 nvAGWILELDRG----EGIPWE 241
Cdd:PRK13548 208 --ADRIVLLHQGrlvaDGTPAE 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
324-479 |
1.26e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.72 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRDSMDDS-- 401
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDArl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 402 ---KTVWEEVSGGQDimriGNFEIPSR---AYVGRFNfkgvdqgkRVGE----LSGGERGRLHLAKLLQVGGNMLLLDEP 471
Cdd:PRK11247 93 lpwKKVIDNVGLGLK----GQWRDAALqalAAVGLAD--------RANEwpaaLSGGQKQRVALARALIHRPGLLLLDEP 160
|
....*...
gi 739061588 472 TNDLDVET 479
Cdd:PRK11247 161 LGALDALT 168
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
345-512 |
1.52e-16 |
|
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: 79.37 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 345 SIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSG-TLVLGDTVKL----------ASVDQFRDSMDDSKTV---WEevsg 410
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdIEIELDTVSYkpqyikadyeGTVRDLLSSITKDFYThpyFK---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 411 gQDIMRIGNFEipsrayvgrfnfKGVDQgkRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVE----TLRALENA 486
Cdd:cd03237 97 -TEIAKPLQIE------------QILDR--EVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKVIRRF 161
|
170 180
....*....|....*....|....*.
gi 739061588 487 LLEFPGCAMVISHDRWFLDRIATHII 512
Cdd:cd03237 162 AENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
16-217 |
1.65e-16 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 78.56 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHI--LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdtdiegeARPQPGIKI--GYlpqepklnpehtvreave 91
Cdd:cd03266 13 DVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL-------LEPDAGFATvdGF------------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 92 EAVSELKNALNRLDEVYAAyadpDADFDKL-AKEQGQLEAIIQSHDGHNLENQLERAAEALRLPEW-DAKIEKLSGGERR 169
Cdd:cd03266 68 DVVKEPAEARRRLGFVSDS----TGLYDRLtARENLEYFAGLYGLKGDELTARLEELADRLGMEELlDRRVGGFSTGMRQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 739061588 170 RVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITH 217
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLraLGkCILFSTH 194
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-226 |
1.72e-16 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 80.92 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 30 FPGAKIGVL-GLNGAGKSTLLRIMAGIDTDIEG--------------------EARPqpgikIGYLPQEPKLNPEHTVRE 88
Cdd:COG4148 22 LPGRGVTALfGPSGSGKTTLLRAIAGLERPDSGrirlggevlqdsargiflppHRRR-----IGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 89 aveeavsELKNALNRldevyAAYADPDADFDKLAKEQGqleaiiqshdghnLENQLERaaealrlpewdaKIEKLSGGER 168
Cdd:COG4148 97 -------NLLYGRKR-----APRAERRISFDEVVELLG-------------IGHLLDR------------RPATLSGGER 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 169 RRVAICRLLLEKPDMLLLDEPTNHLD----AESVAWLERfLHDYEGT-VVAITHDryfLDNVA 226
Cdd:COG4148 140 QRVAIGRALLSSPRLLLMDEPLAALDlarkAEILPYLER-LRDELDIpILYVSHS---LDEVA 198
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-220 |
1.90e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 79.29 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQEPkLNPEH-T 85
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLltpqsgtvflgDKPISMLSSRQLARRLALLPQHH-LTPEGiT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 86 VREAVEEAVSELKNALNRLdevyaayadpdadfdklakeqgqleaiiqSHDGHNLenqLERAAEALRLPEW-DAKIEKLS 164
Cdd:PRK11231 93 VRELVAYGRSPWLSLWGRL-----------------------------SAEDNAR---VNQAMEQTRINHLaDRRLTDLS 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 165 GGERRRVAICRLLLEKPDMLLLDEPTNHLD----AESVAwLERFLHDYEGTVVAITHD-----RY 220
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDinhqVELMR-LMRELNTQGKTVVTVLHDlnqasRY 204
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-217 |
2.06e-16 |
|
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: 77.78 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------IDTDIEGEARPQPGIKIGYLPQEPKLNPEHTVRE 88
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGllrpdsgevrWNGTPLAEQRDEPHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 89 aveeavselknalnrldevyaayadpDADFdklakeqgqLEAIIQSHDgHNLENQLERAAeaLRLPEwDAKIEKLSGGER 168
Cdd:TIGR01189 93 --------------------------NLHF---------WAAIHGGAQ-RTIEDALAAVG--LTGFE-DLPAAQLSAGQQ 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739061588 169 RRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAITH 217
Cdd:TIGR01189 134 RRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-189 |
2.18e-16 |
|
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: 78.74 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGE---ARPQPGikIGYLPQEPKLNPE 83
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLvkpdsgkilldGQDITKLpmhKRARLG--IGYLPQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 84 HTVREAVeEAVSELknalnrldevyaayadpdadFDKLAKEQGQ-LEAIIQSHDGHNLENQLERAaealrlpewdakiek 162
Cdd:cd03218 90 LTVEENI-LAVLEI--------------------RGLSKKEREEkLEELLEEFHITHLRKSKASS--------------- 133
|
170 180
....*....|....*....|....*..
gi 739061588 163 LSGGERRRVAICRLLLEKPDMLLLDEP 189
Cdd:cd03218 134 LSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
11-217 |
2.33e-16 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 78.39 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 11 VGKIVPPKR---HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------------ARPQPGIKIGY 73
Cdd:cd03258 7 VSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSvlvdgtdltllsgkELRKARRRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 74 LPQEPKLNPEHTVREAVeeavselknalnrldevyaAYAdpdadfdklakeqgqLEaiiqsHDGHNLENQLERAAEALRL 153
Cdd:cd03258 87 IFQHFNLLSSRTVFENV-------------------ALP---------------LE-----IAGVPKAEIEERVLELLEL 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739061588 154 ----PEWDAKIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDYEG-TVVAITH 217
Cdd:cd03258 128 vgleDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPEttqSILALLRDINRELGlTIVLITH 199
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
319-521 |
2.59e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.86 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 319 LGDKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGD-----------TVK 387
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 388 LASVDQFRDSMDDSKTV------WEEVSGGQDIMR-------IGNFEIPSRA--YVGRFNFKGVDQGKRVGELSGGERGR 452
Cdd:PRK10619 81 VADKNQLRLLRTRLTMVfqhfnlWSHMTVLENVMEapiqvlgLSKQEARERAvkYLAKVGIDERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 453 LHLAKLLQVGGNMLLLDEPTNDLDV----ETLRALENaLLEFPGCAMVISHDRWFLDRIATHIIdYQDEGKVE 521
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPelvgEVLRIMQQ-LAEEGKTMVVVTHEMGFARHVSSHVI-FLHQGKIE 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
321-477 |
2.63e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.06 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTV-----------KLA 389
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 390 SVDQfRDSMDDSKTVWEEVSggqdimrIGNFeiPSRAYVGRFnfkGVDQGKRVGE-----------------LSGGERGR 452
Cdd:PRK10575 89 YLPQ-QLPAAEGMTVRELVA-------IGRY--PWHGALGRF---GAADREKVEEaislvglkplahrlvdsLSGGERQR 155
|
170 180
....*....|....*....|....*
gi 739061588 453 LHLAKLLQVGGNMLLLDEPTNDLDV 477
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
18-207 |
3.07e-16 |
|
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: 78.10 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIKI-GY-LPQEPKlnpehtvreaveeavs 95
Cdd:TIGR03864 13 ARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQ------ISVaGHdLRRAPR---------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 96 elkNALNRLDEVYAAyadPDADFDkLAKEQGqleaiIQSH-DGHNLENQ--LERAAEAL-RL---PEWDAKIEKLSGGER 168
Cdd:TIGR03864 71 ---AALARLGVVFQQ---PTLDLD-LSVRQN-----LRYHaALHGLSRAeaRARIAELLaRLglaERADDKVRELNGGHR 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 739061588 169 RRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD 207
Cdd:TIGR03864 139 RRVEIARALLHRPALLLLDEPTVGLDPASRAAITAHVRA 177
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-203 |
3.12e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.26 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE----ARPQPG------IKIGYLPQEPKLNPEHTVREav 90
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlGVPVPArarlarARIGVVPQFDNLDLEFTVRE-- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 91 eeavselkNALnrldeVYAAYadpdadFDKLAKEqgqLEAIIQSHdghnLE-NQLERAAealrlpewDAKIEKLSGGERR 169
Cdd:PRK13536 134 --------NLL-----VFGRY------FGMSTRE---IEAVIPSL----LEfARLESKA--------DARVSDLSGGMKR 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 739061588 170 RVAICRLLLEKPDMLLLDEPTNHLD--AESVAWlER 203
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDphARHLIW-ER 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
324-519 |
3.54e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.04 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLT-KSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGqeqpdsgtlvlgdtvklasvdqfrdsmddsk 402
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 403 tVWEEVSGGQDIMRIGN-FEIPSRAYVGRFNFKGV-----DQgkrvgELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:cd03223 50 -LWPWGSGRIGMPEGEDlLFLPQRPYLPLGTLREQliypwDD-----VLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 739061588 477 VETLRALENALLEFpGCAMV-ISHdRWFLDRIATHIIDYQDEGK 519
Cdd:cd03223 124 EESEDRLYQLLKEL-GITVIsVGH-RPSLWKFHDRVLDLDGEGG 165
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-257 |
3.63e-16 |
|
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: 78.10 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID----TDIEGEARPQPGIKIGYLPQEpklnpeh 84
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllrpdsgeilVDgqdiTGLSEKELYELRRRIGMLFQG------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 tvreaveeavselkNALnrldevyaayadpdadFDKL------A---KEQGQL-EAIIQshdghnlenqlERAAEALRLP 154
Cdd:COG1127 91 --------------GAL----------------FDSLtvfenvAfplREHTDLsEAEIR-----------ELVLEKLELV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 155 EWDAKIEK----LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD----YEGTVVAITHDRYFLDNVA 226
Cdd:COG1127 130 GLPGAADKmpseLSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIA 209
|
250 260 270
....*....|....*....|....*....|.
gi 739061588 227 GWILELDRGEgIPWEGNYSSWLEQKDARLEQ 257
Cdd:COG1127 210 DRVAVLADGK-IIAEGTPEELLASDDPWVRQ 239
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
22-241 |
4.36e-16 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 77.41 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA--------RPQPGIK--IGYLPQEPKLNPEHTVREAVE 91
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAtvaghdvvREPREVRrrIGIVFQDLSVDDELTGWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 92 eavselknalnrldevyaayadpdadfdklakeqgqLEAIIQSHDGHNLEnqlERAAEALRLPE-WDAK---IEKLSGGE 167
Cdd:cd03265 96 ------------------------------------IHARLYGVPGAERR---ERIDELLDFVGlLEAAdrlVKTYSGGM 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 168 RRRVAICRLLLEKPDMLLLDEPTNHLDAESVA--W--LERFLHDYEGTVVAITHDRYFLDNVAGWILELDRG----EGIP 239
Cdd:cd03265 137 RRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGriiaEGTP 216
|
..
gi 739061588 240 WE 241
Cdd:cd03265 217 EE 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-197 |
4.49e-16 |
|
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: 77.16 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA----------RPQPGIKIGYLPQEPKLNPEHTVRE 88
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdRKAARQSLGYCPQFDALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 89 AVEeavselknalnrldevyaayadpdadfdklakeqgqLEAIIQSHDGHNLENQLERAAEALRLPE-WDAKIEKLSGGE 167
Cdd:cd03263 95 HLR------------------------------------FYARLKGLPKSEIKEEVELLLRVLGLTDkANKRARTLSGGM 138
|
170 180 190
....*....|....*....|....*....|
gi 739061588 168 RRRVAICRLLLEKPDMLLLDEPTNHLDAES 197
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-203 |
4.86e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.08 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR----PQPG------IKIGYLPQEPKLNPEHTVREav 90
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgePVPSrarharQRVGVVPQFDNLDPDFTVRE-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 91 eeavselkNALnrldeVYAAYADPDAdfdklakeqGQLEAIIQSHdghnLE-NQLERAAealrlpewDAKIEKLSGGERR 169
Cdd:PRK13537 100 --------NLL-----VFGRYFGLSA---------AAARALVPPL----LEfAKLENKA--------DAKVGELSGGMKR 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 739061588 170 RVAICRLLLEKPDMLLLDEPTNHLD--AESVAWlER 203
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDpqARHLMW-ER 180
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-477 |
4.87e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI---DT-DIE--GEARPQPGIK------IGYLPQEPKLNPEHTVREA 89
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIytrDAgSILylGKEVTFNGPKssqeagIGIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 90 VEEAvSELKNALNRLD--EVYAayadpdaDFDKLAKEQGQleaiiqSHDGHNLenqleraaealrlpewdakIEKLSGGE 167
Cdd:PRK10762 100 IFLG-REFVNRFGRIDwkKMYA-------EADKLLARLNL------RFSSDKL-------------------VGELSIGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 168 RRRVAICRLLLEKPDMLLLDEPTNHL-DAESVAWLE--RFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPwegny 244
Cdd:PRK10762 147 QQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRviRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIA----- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 245 sswlEQKDARLEQEAATEAArhksiqkelewirqnpKGRqakgkarlaRFEELnsvdYqkrnetselfippgPRL----G 320
Cdd:PRK10762 222 ----EREVADLTEDSLIEMM----------------VGR---------KLEDQ----Y--------------PRLdkapG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSyGdrvlIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISG---------------------QEQPDSGT 379
Cdd:PRK10762 255 EVRLKVDNLSGP-G----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGalprtsgyvtldghevvtrspQDGLANGI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 380 -----------LVLGDTVK----LASVDQFrdsmddSKTvWEEVSGGQDIMRIGNFeipsrayVGRFNFKGVDQGKRVGE 444
Cdd:PRK10762 330 vyisedrkrdgLVLGMSVKenmsLTALRYF------SRA-GGSLKHADEQQAVSDF-------IRLFNIKTPSMEQAIGL 395
|
490 500 510
....*....|....*....|....*....|...
gi 739061588 445 LSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDV 477
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-205 |
5.31e-16 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 76.51 E-value: 5.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD--IEGE----ARPQPG---IKIGYLPQEPKLNPEHTVRE 88
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEilinGRPLDKnfqRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 89 AVeeavselknalnrldevyaayadpdadfdklakeqgqleaiiqshdghnlenqleraaealrlpEWDAKIEKLSGGER 168
Cdd:cd03232 99 AL----------------------------------------------------------------RFSALLRGLSVEQR 114
|
170 180 190
....*....|....*....|....*....|....*..
gi 739061588 169 RRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFL 205
Cdd:cd03232 115 KRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
324-508 |
5.78e-16 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 77.38 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLiDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQfRD------ 396
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDITNLPPEK-RDisyvpq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 397 --SMDDSKTVWEEVSGGQDIMRIGNFEIPSRAY-VGRfnFKGVDQ--GKRVGELSGGERGRLHLAKLLQVGGNMLLLDEP 471
Cdd:cd03299 79 nyALFPHMTVYKNIAYGLKKRKVDKKEIERKVLeIAE--MLGIDHllNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 739061588 472 TNDLDVET----LRALENALLEFPGCAMVISHD----RWFLDRIA 508
Cdd:cd03299 157 FSALDVRTkeklREELKKIRKEFGVTVLHVTHDfeeaWALADKVA 201
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-239 |
6.18e-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: 77.77 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEG---EARPQPGIKIGYlpQEPKLNPEHT 85
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFyrptsgrilfdGRDITGlppHRIARLGIARTF--QNPRLFPELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 86 VREAVEEAvselknALNRLDEVYAAYAdpdADFDKLAKEQGQLEaiiqshdghnlenqlERAAEALRL----PEWDAKIE 161
Cdd:COG0411 96 VLENVLVA------AHARLGRGLLAAL---LRLPRARREEREAR---------------ERAEELLERvglaDRADEPAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLLLDEPT---NHLDAESVAWLERFLHDYEG-TVVAITHDRYFLDNVAGWILELDRG-- 235
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGrv 231
|
....*.
gi 739061588 236 --EGIP 239
Cdd:COG0411 232 iaEGTP 237
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-477 |
7.07e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 7.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE----ARPQ----------PGIKIGYlpQEPKLNPEHTVR 87
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSilidGQEMrfasttaalaAGVAIIY--QELHLVPEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 88 EAVeeAVSELKNALNRLDEvyaayadpdadfdKLAKEQGQLeaiiqshdghnlenQLERAAEALrlpEWDAKIEKLSGGE 167
Cdd:PRK11288 98 ENL--YLGQLPHKGGIVNR-------------RLLNYEARE--------------QLEHLGVDI---DPDTPLKYLSIGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 168 RRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVA-ITH--DRYFLDNVAGWILeldrgegipweg 242
Cdd:PRK11288 146 RQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELraEGRVILyVSHrmEEIFALCDAITVF------------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 243 nysswleqKDARLeqeaateAARHKSIQK-ELEWIRQNPKGRqakgkarlarfeELNSV-DYQKRNetselfippgprLG 320
Cdd:PRK11288 214 --------KDGRY-------VATFDDMAQvDRDQLVQAMVGR------------EIGDIyGYRPRP------------LG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTksyGDRvLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASV-DQFRDSM 398
Cdd:PRK11288 255 EVRLRLDGLK---GPG-LREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKPIDIRSPrDAIRAGI 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 399 ----DDSK--------TVWEE--VSGGQDIMRIGNF------EIPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKL 458
Cdd:PRK11288 331 mlcpEDRKaegiipvhSVADNinISARRHHLRAGCLinnrweAENADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRW 410
|
490
....*....|....*....
gi 739061588 459 LQVGGNMLLLDEPTNDLDV 477
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDV 429
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
289-523 |
8.67e-16 |
|
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: 80.18 E-value: 8.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 289 ARLArFEELNSV--DYQKRNETSELfipPGPRlGDkvLEINNLTKSY--GDRVLIDDLSFSIPKGAIVGIIGPNGAGKST 364
Cdd:COG4618 301 ARQA-YRRLNELlaAVPAEPERMPL---PRPK-GR--LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKST 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 365 LFRMISGQEQPDSGTLVLGDtvklASVDQfrdsmddsktvWEEVSGG-------QDIM--------RIGNFEIPSRAYV- 428
Cdd:COG4618 374 LARLLVGVWPPTAGSVRLDG----ADLSQ-----------WDREELGrhigylpQDVElfdgtiaeNIARFGDADPEKVv 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 429 ------------GRFNfKGVDqgKRVGE----LSGGERGRLHLAKLLQvgGN--MLLLDEPTNDLDVETLRALENALLEF 490
Cdd:COG4618 439 aaaklagvhemiLRLP-DGYD--TRIGEggarLSGGQRQRIGLARALY--GDprLVVLDEPNSNLDDEGEAALAAAIRAL 513
|
250 260 270
....*....|....*....|....*....|....*....
gi 739061588 491 ---PGCAMVISHDRWFL---DRIAthIIdyqDEGKVEFF 523
Cdd:COG4618 514 karGATVVVITHRPSLLaavDKLL--VL---RDGRVQAF 547
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-217 |
9.52e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 74.77 E-value: 9.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIKIGYLPQEPkLNPEHtvreaveeavselkn 99
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE------ILVDGKEVSF-ASPRD--------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 100 alnrldevyaayadpdadfdklAKEQGqLEAIIQshdghnlenqleraaealrlpewdakiekLSGGERRRVAICRLLLE 179
Cdd:cd03216 72 ----------------------ARRAG-IAMVYQ-----------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 739061588 180 KPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITH 217
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIFISH 140
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-190 |
1.02e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 76.56 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 7 SMLRV-------GKIvppkrHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEG---EARP 65
Cdd:COG0410 2 PMLEVenlhagyGGI-----HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLlpprsgsirfdGEDITGlppHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 66 QPGikIGYLPQEPKLNPEHTVRE---AVEEAVSELKNALNRLDEVYAAyadpdadFDKLAKEQGQleaiiqshdghnlen 142
Cdd:COG0410 77 RLG--IGYVPEGRRIFPSLTVEEnllLGAYARRDRAEVRADLERVYEL-------FPRLKERRRQ--------------- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 739061588 143 qleRAAEalrlpewdakiekLSGGERRRVAICRLLLEKPDMLLLDEPT 190
Cdd:COG0410 133 ---RAGT-------------LSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
316-524 |
1.03e-15 |
|
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: 76.42 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 316 GPRLGDKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL-VLGdtvKLASVDQF 394
Cdd:cd03220 15 GGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtVRG---RVSSLLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 395 RDSMDdsktvwEEVSGGQDIMRIGNF------EIPSR-AYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLL 467
Cdd:cd03220 92 GGGFN------PELTGRENIYLNGRLlglsrkEIDEKiDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 468 LDEPTNDLDVETLRALENALLEF-PGCAMVI--SHDRWFLDRIATHIIdYQDEGKVEFFE 524
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELlKQGKTVIlvSHDPSSIKRLCDRAL-VLEKGKIRFDG 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-218 |
1.06e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 78.58 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID----TDIEGEARpqpgiKIGYLPQEPKLNPE 83
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGledptsgeilIGgrdvTDLPPKDR-----NIAMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 84 HTVREAVEEAvseLKNAlnrldevyaayadpdadfdKLAKEQgqleaiiqshdghnLENQLERAAEALRLPEW-DAKIEK 162
Cdd:COG3839 90 MTVYENIAFP---LKLR-------------------KVPKAE--------------IDRRVREAAELLGLEDLlDRKPKQ 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739061588 163 LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDA--------EsvawLERFLHDYEGTVVAITHD 218
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDAklrvemraE----IKRLHRRLGTTTIYVTHD 193
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
21-217 |
1.11e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 76.17 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR-------PQPGIKIGYLPQEPKLNPEHTVREAVeea 93
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldIAARNRIGYLPEERGLYPKMKVIDQL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 94 vselknalnrldeVYAAyadpdadfdklakeqgQLEAIIQSHDGHNLENQLERaaeaLRLPEW-DAKIEKLSGGERRRVA 172
Cdd:cd03269 92 -------------VYLA----------------QLKGLKKEEARRRIDEWLER----LELSEYaNKRVEELSKGNQQKVQ 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 739061588 173 ICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG---TVVAITH 217
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTH 186
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-231 |
1.15e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.03 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIGYLPQEPK----------------- 79
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKLNRAQRkafrrdiqmvfqdsisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 80 LNPEHTVREAVEEAVSELKNalnrLDEvyaayadpdadfdklakeqgqleaiiqshdghnlENQLERAAEALRLPEWDAK 159
Cdd:PRK10419 102 VNPRKTVREIIREPLRHLLS----LDK----------------------------------AERLARASEMLRAVDLDDS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 160 I-----EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD----RYFLDNVA 226
Cdd:PRK10419 144 VldkrpPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDlrlvERFCQRVM 223
|
....*....
gi 739061588 227 ----GWILE 231
Cdd:PRK10419 224 vmdnGQIVE 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-236 |
1.26e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 76.16 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 3 QYVYSMLRVGKIVP---PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD---------IEGEARPQPGIK 70
Cdd:cd03234 1 QRVLPWWDVGLKAKnwnKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggttsgqilFNGQPRKPDQFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 71 --IGYLPQEPKLNPEHTVREAVEEAvselknALNRLdevyaAYADPDADFDKLAkEQGQLEAIIQSHDGHNLenqleraa 148
Cdd:cd03234 81 kcVAYVRQDDILLPGLTVRETLTYT------AILRL-----PRKSSDAIRKKRV-EDVLLRDLALTRIGGNL-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 149 ealrlpewdakIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAIT-H----DRY- 220
Cdd:cd03234 141 -----------VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLarRNRIVILTiHqprsDLFr 209
|
250
....*....|....*.
gi 739061588 221 FLDNvagwILELDRGE 236
Cdd:cd03234 210 LFDR----ILLLSSGE 221
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
18-189 |
1.33e-15 |
|
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: 76.54 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKST-------LLRIMAGI----DTDI-----EGEARpqpgIKIGYLPQEPKLN 81
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTsfymivgLVRPDAGKilidGQDIthlpmHERAR----LGIGYLPQEASIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 PEHTVREAVeEAVSELKNALNRldevyaayadpdadfdklaKEQGQ-LEAIIQshdghnlENQLERAAEALRLpewdaki 160
Cdd:TIGR04406 89 RKLTVEENI-MAVLEIRKDLDR-------------------AEREErLEALLE-------EFQISHLRDNKAM------- 134
|
170 180
....*....|....*....|....*....
gi 739061588 161 eKLSGGERRRVAICRLLLEKPDMLLLDEP 189
Cdd:TIGR04406 135 -SLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-511 |
1.46e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 76.69 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTvKLASVDQFR----- 395
Cdd:COG4674 8 GPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT-DLTGLDEHEiarlg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 -------DSMDDSKTVWEevsggqdimrigNFEIPSRAYVG-----RFNFKGVD----------------QGKRVGELSG 447
Cdd:COG4674 87 igrkfqkPTVFEELTVFE------------NLELALKGDRGvfaslFARLTAEErdrieevletigltdkADRLAGLLSH 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739061588 448 GERGRLHLAKLLQVGGNMLLLDEPTNDL-DVETLR--ALENALLEfpGCA-MVISHDRWFLDRIATHI 511
Cdd:COG4674 155 GQKQWLEIGMLLAQDPKLLLLDEPVAGMtDAETERtaELLKSLAG--KHSvVVVEHDMEFVRQIARKV 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-217 |
1.53e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--------IDTDIEGEARPQPGIKIGYLPQEPKLNPEHTVREAV 90
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGllppaagtIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 91 EeavselknalnrldeVYAAYadpdadfdklakeQGQLEAIIqshdghnlenqlERAAEALRLPE-WDAKIEKLSGGERR 169
Cdd:PRK13539 95 E---------------FWAAF-------------LGGEELDI------------AAALEAVGLAPlAHLPFGYLSAGQKR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 739061588 170 RVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAITH 217
Cdd:PRK13539 135 RVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHlaqGGIVIAATH 185
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-224 |
1.54e-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: 74.66 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRImagidtdIEGEARPQPGikigylpqEPKLNPEHTvrEAVEEAVSELKN 99
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQL-------LTGDLKPQQG--------EITLDGVPV--SDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 100 ALNRLDEVYAAyadpdadfdklakeqgqleaiiqshdghNLENQLERaaealrlpewdakieKLSGGERRRVAICRLLLE 179
Cdd:cd03247 79 VLNQRPYLFDT----------------------------TLRNNLGR---------------RFSGGERQRLALARILLQ 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 180 KPDMLLLDEPTNHLDAES-VAWLERFLHDYEG-TVVAITH--------DR-YFLDN 224
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDkTLIWITHhltgiehmDKiLFLEN 171
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-217 |
1.62e-15 |
|
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: 74.56 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR-----------PQPGIKIGYLPQEPKLNPEhTV 86
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRldgadisqwdpNELGDHVGYLPQDDELFSG-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 87 REAVeeavselknalnrldevyaayadpdadfdklakeqgqleaiiqshdghnlenqleraaealrlpewdakiekLSGG 166
Cdd:cd03246 93 AENI------------------------------------------------------------------------LSGG 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739061588 167 ERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD---YEGTVVAITH 217
Cdd:cd03246 101 QRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAlkaAGATRIVIAH 154
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
326-500 |
1.72e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.31 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 326 INNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQfRDSMDdsKTVW 405
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ-KLYLD--TTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 406 EEVSggqDIMRIgnfeipsrayvgRFNFKGVDQG---KRVG----------ELSGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:PRK09544 84 LTVN---RFLRL------------RPGTKKEDILpalKRVQaghlidapmqKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190
....*....|....*....|....*....|..
gi 739061588 473 NDLDVE---TLRALENALLEFPGCA-MVISHD 500
Cdd:PRK09544 149 QGVDVNgqvALYDLIDQLRRELDCAvLMVSHD 180
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
323-472 |
1.86e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 75.79 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLgdtvklasvdqfrdsmddsk 402
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 403 tvweevsGGQDIMRIGNFEIPSR--AYV------------------GRFNFKGVDQGKRV-------------------G 443
Cdd:COG0410 63 -------DGEDITGLPPHRIARLgiGYVpegrrifpsltveenlllGAYARRDRAEVRADlervyelfprlkerrrqraG 135
|
170 180
....*....|....*....|....*....
gi 739061588 444 ELSGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:COG0410 136 TLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
321-500 |
2.63e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 76.31 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSY--GDRVLiDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL-VLGDTVKLASVDQFRDS 397
Cdd:PRK13647 2 DNIIEVEDLHFRYkdGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 398 M-------DD---SKTVWEEVSGGQDIMRIGNFEIPSRA-----YVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVG 462
Cdd:PRK13647 81 VglvfqdpDDqvfSSTVWDDVAFGPVNMGLDKDEVERRVeealkAVRMWDFR----DKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 739061588 463 GNMLLLDEPTNDLD---VETLRALENALLEFPGCAMVISHD 500
Cdd:PRK13647 157 PDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-218 |
2.87e-15 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 74.98 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIKIGylpqepklnpehtvreavEEAVSE 96
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGR------IYIG------------------GRDVTD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 97 LKNALNRLDEVYAAYA-DPDAD-FDKLA---KEQGQLEAIIqshdghnlENQLERAAEALRLPEW-DAKIEKLSGGERRR 170
Cdd:cd03301 67 LPPKDRDIAMVFQNYAlYPHMTvYDNIAfglKLRKVPKDEI--------DERVREVAELLQIEHLlDRKPKQLSGGQRQR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739061588 171 VAICRLLLEKPDMLLLDEPTNHLDA----ESVAWLERFLHDYEGTVVAITHD 218
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDAklrvQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-197 |
3.56e-15 |
|
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: 78.32 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---ID-TDIegeaR--PQPGIK--IGYLPQEpkln 81
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfrfydvtSGrilIDgQDI----RdvTQASLRaaIGIVPQD---- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 pehTVreaveeavseLKNalnrlDEVYA--AYADPDADfdklakeqgqleaiiqshdghnlENQLERAAEA-------LR 152
Cdd:COG5265 441 ---TV----------LFN-----DTIAYniAYGRPDAS-----------------------EEEVEAAARAaqihdfiES 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 739061588 153 LPE-WDAKI-E---KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAES 197
Cdd:COG5265 480 LPDgYDTRVgErglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-218 |
3.58e-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: 77.07 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 31 PGAKI-GVLGLNGAGKSTLLRIMAGIDTDIEGE--------ARPQPGI-------KIGYLPQEPKLNPEHTVREAVEEAV 94
Cdd:TIGR02142 21 PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEivlngrtlFDSRKGIflppekrRIGYVFQEARLFPHLSVRGNLRYGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 95 SELKNALNRldevyaayadpdADFDKLAkeqgQLEAIiqshdGHNLEnqleraaealRLPEwdakieKLSGGERRRVAIC 174
Cdd:TIGR02142 101 KRARPSERR------------ISFERVI----ELLGI-----GHLLG----------RLPG------RLSGGEKQRVAIG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 739061588 175 RLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD 218
Cdd:TIGR02142 144 RALLSSPRLLLMDEPLAALDdprkYEILPYLERLHAEFGIPILYVSHS 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-235 |
3.72e-15 |
|
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: 74.78 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRImagidtdIEGEARPQPGiKIGYLPQEPKLN----PEHTV---REAVEEAV 94
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKC-------IYGNYLPDSG-SILVRHDGGWVDlaqaSPREIlalRRRTIGYV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 95 SELKNALNR---LDEVyaayADPdadfdklAKEQGQLEAIiqshdghnlenQLERAAEALR---LPE--WDAKIEKLSGG 166
Cdd:COG4778 99 SQFLRVIPRvsaLDVV----AEP-------LLERGVDREE-----------ARARARELLArlnLPErlWDLPPATFSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739061588 167 ERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGT-VVAITHDRYFLDNVAGWILELDRG 235
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkaRGTaIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-219 |
3.79e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.05 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE------------ARPQpgiKIGYLPQEPKLNPEHT 85
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHirfhgtdvsrlhARDR---KVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 86 VREAVEEAVSelknALNRLDEVYAAYADpdadfdklAKEQGQLEAIiqshdghnlenQLERAAEalRLPEwdakieKLSG 165
Cdd:PRK10851 91 VFDNIAFGLT----VLPRRERPNAAAIK--------AKVTQLLEMV-----------QLAHLAD--RYPA------QLSG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 166 GERRRVAICRLLLEKPDMLLLDEPTNHLDA----ESVAWLeRFLH-DYEGTVVAITHDR 219
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWL-RQLHeELKFTSVFVTHDQ 197
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
324-489 |
4.70e-15 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 74.57 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGD-RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTVKLASVDQFRDSM--- 398
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSiLIDGQDIREVTLDSLRRAIgvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 399 -------DDskTVW------------EEVSGGQDIMRIGNFeipsrayVGRFNFkGVDqgKRVGE----LSGGERGRLHL 455
Cdd:cd03253 81 pqdtvlfND--TIGynirygrpdatdEEVIEAAKAAQIHDK-------IMRFPD-GYD--TIVGErglkLSGGEKQRVAI 148
|
170 180 190
....*....|....*....|....*....|....
gi 739061588 456 AKLLQVGGNMLLLDEPTNDLDVETLRALENALLE 489
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRD 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-266 |
5.32e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 74.67 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGIDTDIEGEARPQPGI----KIGYLPQEPKLNPE 83
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprsgtlniAGNHFDFSKTPSDKAIRelrrNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 84 HTVREAVEEAVSELKnalnrldevyaayadpdadfdKLAKEQGQLEAiiqshdghnlENQLERaaeaLRLPEW-DAKIEK 162
Cdd:PRK11124 97 LTVQQNLIEAPCRVL---------------------GLSKDQALARA----------EKLLER----LRLKPYaDRFPLH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 163 LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGT---VVAITHDRYFLDNVAGWILELDRGEGIp 239
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgitQVIVTHEVEVARKTASRVVYMENGHIV- 220
|
250 260
....*....|....*....|....*..
gi 739061588 240 wegnysswlEQKDARLEQEAATEAARH 266
Cdd:PRK11124 221 ---------EQGDASCFTQPQTEAFKN 238
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-236 |
5.95e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.22 E-value: 5.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA--RPQPGIKIGYlpqepklnpeHTVREAVEEAVSe 96
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVliRGEPITKENI----------REVRKFVGLVFQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 97 lknalNRLDEVYAAYADPDADFDklakeqgqleAIIQSHDGHNLENQLERAAEALRLPEWDAKI-EKLSGGERRRVAICR 175
Cdd:PRK13652 86 -----NPDDQIFSPTVEQDIAFG----------PINLGLDEETVAHRVSSALHMLGLEELRDRVpHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 176 LLLEKPDMLLLDEPTNHLDAESVAWLERFLHD----YEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDlpetYGMTVIFSTHQLDLVPEMADYIYVMDKGR 215
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-251 |
6.22e-15 |
|
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: 75.18 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDI---EGEARPQPGIKIGYLPQepklNPEH 84
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLlkptsgtvtidGRDItakKKKKLKDLRKKVGLVFQ----FPEH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 TVreaVEEAVselknalnrLDEVyaAYAdPdadfdklaKEQGQLEAIIQshdghnlenqlERAAEALR---LPE--WDAK 159
Cdd:TIGR04521 94 QL---FEETV---------YKDI--AFG-P--------KNLGLSEEEAE-----------ERVKEALElvgLDEeyLERS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 160 IEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAES-VAWLERF--LHDYEG-TVVAITHDryfLDNVAGW---ILEL 232
Cdd:TIGR04521 140 PFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGrKEILDLFkrLHKEKGlTVILVTHS---MEDVAEYadrVIVM 216
|
250 260
....*....|....*....|....
gi 739061588 233 DRG----EGIPWE-GNYSSWLEQK 251
Cdd:TIGR04521 217 HKGkivlDGTPREvFSDVDELEKI 240
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
317-487 |
7.29e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.52 E-value: 7.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 317 PRLGDKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQfR 395
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLdGQDITHVPAEN-R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 D------------SMddskTVWEEVSGGQDIMRIGNFEIPSR-----AYVGRFNFKgvdqGKRVGELSGGERGRLHLAKL 458
Cdd:PRK09452 87 HvntvfqsyalfpHM----TVFENVAFGLRMQKTPAAEITPRvmealRMVQLEEFA----QRKPHQLSGGQQQRVAIARA 158
|
170 180
....*....|....*....|....*....
gi 739061588 459 LQVGGNMLLLDEPTNDLDVETLRALENAL 487
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNEL 187
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-228 |
7.69e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.77 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdtdiegearpqpgikigYLPQEPKLnpehTV--REAVEEAVSEL 97
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI-----------------YLPQRGRV----KVmgREVNAENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 98 KNALNRL-----DEVYAAYADPDADFDKLAKEQGQLEAiiqshdghnlenqLERAAEALRLPE-WDAKiEK----LSGGE 167
Cdd:PRK13647 78 RSKVGLVfqdpdDQVFSSTVWDDVAFGPVNMGLDKDEV-------------ERRVEEALKAVRmWDFR-DKppyhLSYGQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 168 RRRVAICRLLLEKPDMLLLDEPTNHLD----AESVAWLERfLHDYEGTVVAITHDryfLDNVAGW 228
Cdd:PRK13647 144 KKRVAIAGVLAMDPDVIVLDEPMAYLDprgqETLMEILDR-LHNQGKTVIVATHD---VDLAAEW 204
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-226 |
7.83e-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: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI--------------DTDI----EGEARPQPGIKIGYLPQEPK-- 79
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlpppgitsgeilfdGEDLlklsEKELRKIRGREIQMIFQDPMts 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 80 LNPEHTVREAVEEAvselknalnrldevyaayadpdadfdklakeqgqleaiIQSHDGHNLENQLERAAEALR---LPEW 156
Cdd:COG0444 99 LNPVMTVGDQIAEP--------------------------------------LRIHGGLSKAEARERAIELLErvgLPDP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 157 DAKIEK----LSGGERRRVAICRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD----RYFLDN 224
Cdd:COG0444 141 ERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqAQILNLLKDLQRELGLAILFITHDlgvvAEIADR 220
|
..
gi 739061588 225 VA 226
Cdd:COG0444 221 VA 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-218 |
7.89e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 74.71 E-value: 7.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------ARPQPGIKIGYlpQEPKLNPEHTVREAV 90
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEllagtaplAEAREDTRLMF--QDARLLPWKKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 91 EEAVSE--LKNALNRLDEVYAAyadpdadfdklakeqgqleaiiqshdghnlenqlERAAEalrlpeWDAKiekLSGGER 168
Cdd:PRK11247 103 GLGLKGqwRDAALQALAAVGLA----------------------------------DRANE------WPAA---LSGGQK 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739061588 169 RRVAICRLLLEKPDMLLLDEPTNHLDA----ESVAWLERFLHDYEGTVVAITHD 218
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGALDAltriEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-218 |
8.68e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 74.38 E-value: 8.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAgidtdieGEARPQPGiKIGY-------------------LPQEP 78
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLT-------GELTPSSG-EVRLngrplaawspwelarrravLPQHS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 79 KLNPEHTVREAVeeavselknALNRldevyAAYADPDADFDKLAKEqgQLEAIiqshDGHNLENQLERAaealrlpewda 158
Cdd:COG4559 85 SLAFPFTVEEVV---------ALGR-----APHGSSAAQDRQIVRE--ALALV----GLAHLAGRSYQT----------- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 159 kiekLSGGERRRVAICRLLL-------EKPDMLLLDEPTNHLD-AESVAWLE--RFLHDYEGTVVAITHD 218
Cdd:COG4559 134 ----LSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDlAHQHAVLRlaRQLARRGGGVVAVLHD 199
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-508 |
9.24e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.20 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKS----TLLRIMAGIDTDIEGEA---------------------RPQPGIKIGYLPQ 76
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKmllrrrsrqvielseqsaaqmRHVRGADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 77 EP--KLNPEHTVREAVEEAVselknalnRLDEvyaayadpdadfdKLAKEQGQLEAiiqshdghnlenqlERAAEALRLP 154
Cdd:PRK10261 112 EPmtSLNPVFTVGEQIAESI--------RLHQ-------------GASREEAMVEA--------------KRMLDQVRIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 155 EWDAKIEK----LSGGERRRVAICRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHDRYFLDNVA 226
Cdd:PRK10261 157 EAQTILSRyphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMGVIFITHDMGVVAEIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 227 GWILELDRGEGIpwegnysswleqKDARLEQeaATEAARHKSIQKELEWIrqnPKGRQAKGKARLARFEELNSVDYQKRN 306
Cdd:PRK10261 237 DRVLVMYQGEAV------------ETGSVEQ--IFHAPQHPYTRALLAAV---PQLGAMKGLDYPRRFPLISLEHPAKQE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 307 ETSE--LFIPpgprlGDKVLEINNLTKSYG------DRV-----LIDDLSFSIPKGAIVGIIGPNGAGKST----LFRMI 369
Cdd:PRK10261 300 PPIEqdTVVD-----GEPILQVRNLVTRFPlrsgllNRVtrevhAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 370 SGQEqpdsGTLVLG----DTV---KLASVDQ-----FRD---SMDDSKTVweevsgGQDIMRignfeiPSRAYvgrfnfk 434
Cdd:PRK10261 375 ESQG----GEIIFNgqriDTLspgKLQALRRdiqfiFQDpyaSLDPRQTV------GDSIME------PLRVH------- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 435 GVDQGK-----------RVG-----------ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALL---- 488
Cdd:PRK10261 432 GLLPGKaaaarvawlleRVGllpehawryphEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLdlqr 511
|
570 580
....*....|....*....|
gi 739061588 489 EFPGCAMVISHDRWFLDRIA 508
Cdd:PRK10261 512 DFGIAYLFISHDMAVVERIS 531
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-236 |
1.01e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.03 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------------ARPqpgikIGYLPQEPKLNPEH 84
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQimldgvdlshvppyQRP-----INMMFQSYALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 TVREAVEEAVSElknalnrldevyaayadpdadfDKLAKEQgqleaiIQShdghnlenqleRAAEALRLPEWDA----KI 160
Cdd:PRK11607 107 TVEQNIAFGLKQ----------------------DKLPKAE------IAS-----------RVNEMLGLVHMQEfakrKP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 161 EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDA--------ESVAWLERFlhdyEGTVVAITHDRYFLDNVAGWILEL 232
Cdd:PRK11607 148 HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdrmqlEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIM 223
|
....
gi 739061588 233 DRGE 236
Cdd:PRK11607 224 NRGK 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-217 |
1.07e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 72.91 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPGikigylpqepklnPEHTVREAVEEAVselk 98
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-------------PLDFQRDSIARGL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 99 nalnrldeVYAAYADpdadfdKLAKEQGQLEAIIQSHDGHNLENQLERAAEA-LRLPEwDAKIEKLSGGERRRVAICRLL 177
Cdd:cd03231 76 --------LYLGHAP------GIKTTLSVLENLRFWHADHSDEQVEEALARVgLNGFE-DRPVAQLSAGQQRRVALARLL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739061588 178 LEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAITH 217
Cdd:cd03231 141 LSGRPLWILDEPTTALDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-251 |
1.26e-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: 73.42 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---ID-TDIEGEARPQPGIKIGYLPQEPKLNPEhTVREA 89
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGrilIDgHDVRDYTLASLRRQIGLVSQDVFLFND-TVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 90 VeeavselknalnrldevyaAYADPDADfdklakeqgqleaiiqshdghnlENQLERAAEA-------LRLPE-WDAKIE 161
Cdd:cd03251 96 I-------------------AYGRPGAT-----------------------REEVEEAARAanahefiMELPEgYDTVIG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 162 ----KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYegTVVAITHDRYFLDNvAGWILELD 233
Cdd:cd03251 134 ergvKLSGGQRQRIAIARALLKDPPILILDEATSALDTESerlvQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLE 210
|
250
....*....|....*...
gi 739061588 234 RGEgIPWEGNYSSWLEQK 251
Cdd:cd03251 211 DGK-IVERGTHEELLAQG 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-218 |
1.37e-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: 73.43 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEArpqpgikigYLPQEPKLN-PEHtvreaveeavselK 98
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI---------LLDGKDITNlPPH-------------K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 99 NALNRLDEVYAAYadPDAD-FDKLA---KEQGQLEAIIQshdghnlenqlERAAEALRLPEWDA----KIEKLSGGERRR 170
Cdd:cd03300 72 RPVNTVFQNYALF--PHLTvFENIAfglRLKKLPKAEIK-----------ERVAEALDLVQLEGyanrKPSQLSGGQQQR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739061588 171 VAICRLLLEKPDMLLLDEPTNHLDAESVAWLE---RFLHDYEG-TVVAITHD 218
Cdd:cd03300 139 VAIARALVNEPKVLLLDEPLGALDLKLRKDMQlelKRLQKELGiTFVFVTHD 190
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-236 |
1.45e-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: 73.27 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMagidtdiEGEARPQPGIKIgyLPQEPKLNPEHTVREAVEEAVSE 96
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL-------ENFYQPQGGQVL--LDGKPISQYEHKYLHSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 97 LKNALNRLDEVYAAYADPDADFDKLakeqgqLEAIIQSHDGHNL-ENQLERAAEAlrlpewDAKIEKLSGGERRRVAICR 175
Cdd:cd03248 96 EPVLFARSLQDNIAYGLQSCSFECV------KEAAQKAHAHSFIsELASGYDTEV------GEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 176 LLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHdRYFLDNVAGWILELDRGE 236
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH-RLSTVERADQILVLDGGR 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
325-482 |
1.46e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 75.22 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 325 EINNLTKSY----GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTlVLGDTVKLASVD-----QFR 395
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGR-VLVDGQDLTALSekelrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 DSMD---------DSKTVWEEVSGGQDIMRIGNFEIPSR-----AYVGRfnfkgVDQGKRV-GELSGGERGRLHLAKLLQ 460
Cdd:PRK11153 82 RQIGmifqhfnllSSRTVFDNVALPLELAGTPKAEIKARvtellELVGL-----SDKADRYpAQLSGGQKQRVAIARALA 156
|
170 180
....*....|....*....|..
gi 739061588 461 VGGNMLLLDEPTNDLDVETLRA 482
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRS 178
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-500 |
1.50e-14 |
|
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: 76.26 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKS----TLLRIMAGIDTDIEGEAR---------PQP------GIKIGYLPQEP- 78
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILfdgqdllglSERelrrirGNRIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 79 -KLNPEHTVreavEEAVSElknalnrldevyaayadpdadfdklakeqgqleaIIQSHDGHNLENQLERAAEALR---LP 154
Cdd:COG4172 103 tSLNPLHTI----GKQIAE----------------------------------VLRLHRGLSGAAARARALELLErvgIP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 155 EWDAKIEK----LSGGERRRVAICRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD----RYFL 222
Cdd:COG4172 145 DPERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqAQILDLLKDLQRELGMALLLITHDlgvvRRFA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 223 DNVA----GWILEldrgegipwegnysswleqkdarleqEAATE----AARHKSIQKELEWIrqnPKGRQakgkarlarf 294
Cdd:COG4172 225 DRVAvmrqGEIVE--------------------------QGPTAelfaAPQHPYTRKLLAAE---PRGDP---------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 295 eelnsvdyqkrnetselfiPPGPRLGDKVLEINNLTKSY-----------GDRVLIDDLSFSIPKGAIVGIIGPNGAGKS 363
Cdd:COG4172 266 -------------------RPVPPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKS 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 364 TLFRMISGQeQPDSGTLVLGDTvKLASVDQ-------------FRD---SMDDSKTVWEEVSGGQDIMRIGNFEIPSRAY 427
Cdd:COG4172 327 TLGLALLRL-IPSEGEIRFDGQ-DLDGLSRralrplrrrmqvvFQDpfgSLSPRMTVGQIIAEGLRVHGPGLSAAERRAR 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 428 VgrfnfkgVDQGKRVG-----------ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDV-------ETLRALENALle 489
Cdd:COG4172 405 V-------AEALEEVGldpaarhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVsvqaqilDLLRDLQREH-- 475
|
570
....*....|..
gi 739061588 490 fpGCAMV-ISHD 500
Cdd:COG4172 476 --GLAYLfISHD 485
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
324-384 |
1.62e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.58 E-value: 1.62e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 324 LEINNLTKSYG-----DRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGD 384
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG 67
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-241 |
1.73e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.90 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdtdiegeARPQPG-IKIGYLPqepkLNpehtvreavEEAVSE 96
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL-------LLPEAGtITVGGMV----LS---------EETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 97 LKNalnrldEVYAAYADPDADFdklakeqgqLEAIIQSHDGHNLENQ-------LERAAEALRL----PEWDAKIEKLSG 165
Cdd:PRK13635 79 VRR------QVGMVFQNPDNQF---------VGATVQDDVAFGLENIgvpreemVERVDQALRQvgmeDFLNREPHRLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 166 GERRRVAICRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHDYEG-TVVAITHDryfLDNVAGW--ILELDRG---- 235
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPrgrREVLETVRQLKEQKGiTVLSITHD---LDEAAQAdrVIVMNKGeile 220
|
....*.
gi 739061588 236 EGIPWE 241
Cdd:PRK13635 221 EGTPEE 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
324-499 |
2.14e-14 |
|
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: 75.91 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYG--DRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDT----VKLAS------- 390
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHdladYTLASlrrqval 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 391 VDQFRDSMDDskTVWEEVSGGqDIMRIGNFEIPS---RAYVGRF---NFKGVDQ--GKRVGELSGGERGRLHLAKLLQVG 462
Cdd:TIGR02203 411 VSQDVVLFND--TIANNIAYG-RTEQADRAEIERalaAAYAQDFvdkLPLGLDTpiGENGVLLSGGQRQRLAIARALLKD 487
|
170 180 190
....*....|....*....|....*....|....*....
gi 739061588 463 GNMLLLDEPTNDLDVETLRALENALLEF-PG-CAMVISH 499
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLmQGrTTLVIAH 526
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-218 |
2.22e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.28 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA--RPQP---------GIKIGYLPQEPKLNPEHT 85
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIllDAQPleswsskafARKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 86 VREAVEEAVSELKNALNRLDevyaayadpdadfdklAKEQGQLEAIIQSHDGHNLENQLeraaealrlpewdakIEKLSG 165
Cdd:PRK10575 102 VRELVAIGRYPWHGALGRFG----------------AADREKVEEAISLVGLKPLAHRL---------------VDSLSG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 166 GERRRVAICRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD 218
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHRLSQERGLTVIAVLHD 207
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
323-476 |
2.78e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 72.44 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQFRDSMDDS 401
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 402 --------KTVWEEVSGGQDIMRIGNFEIPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTN 473
Cdd:PRK10247 87 aqtptlfgDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
...
gi 739061588 474 DLD 476
Cdd:PRK10247 167 ALD 169
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
323-498 |
2.96e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 73.30 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSY-GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTVKLASVDQFRDSM-- 398
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSvLIRGEPITKENIREVRKFVgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 399 -----DD---SKTVWEEVSGGQDIMRIGNFEIPSRAYVGRFNFKGVDQGKRV-GELSGGERGRLHLAKLLQVGGNMLLLD 469
Cdd:PRK13652 83 vfqnpDDqifSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVpHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190
....*....|....*....|....*....|..
gi 739061588 470 EPTNDLD---VETLRALENALLEFPGCAMVIS 498
Cdd:PRK13652 163 EPTAGLDpqgVKELIDFLNDLPETYGMTVIFS 194
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-252 |
3.05e-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: 72.26 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID-TDIEGEARPQPGIKIGYLPQEPKLNPEhT 85
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfydpqkgqilIDgIDIRDISRKSLRSMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 86 VREAVeeavselknALNRLDEvyaayadPDADFDKLAKEQGQLEAIIQSHDGhnLENQLERAAEalrlpewdakieKLSG 165
Cdd:cd03254 93 IMENI---------RLGRPNA-------TDEEVIEAAKEAGAHDFIMKLPNG--YDTVLGENGG------------NLSQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 166 GERRRVAICRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYegTVVAITHDRYFLDNvAGWILELDRGEgIPWE 241
Cdd:cd03254 143 GERQLLAIARAMLRDPKILILDEATSNIDTETekliQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGK-IIEE 218
|
250
....*....|.
gi 739061588 242 GNYSSWLEQKD 252
Cdd:cd03254 219 GTHDELLAKKG 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
328-521 |
3.21e-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: 73.99 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 328 NLTKSYGDRVLidDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVkLASVDQFRDSMDDSKT---V 404
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRT-LFDSRKGIFLPPEKRRigyV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 405 WEEVSGGQDIMRIGNFEI---PSRAYVGRFNFKGVDQ--------GKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTN 473
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRYgmkRARPSERRISFERVIEllgighllGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739061588 474 DLDV----ETLRALENALLEFPGCAMVISHDRWFLDRIATHIIDYQDeGKVE 521
Cdd:TIGR02142 161 ALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED-GRVA 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
20-236 |
4.10e-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: 71.95 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT------DIEGEARPQPGI-------KIGYLPQEPKLNPEHTV 86
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiTVDGEDLTDSKKdinklrrKVGMVFQQFNLFPHLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 87 REAVEEAVSELKnalnrldevyaayadpdadfdKLAKEqgqlEAIiqshdghnlenqlERAAEALR---LPE-WDAKIEK 162
Cdd:COG1126 95 LENVTLAPIKVK---------------------KMSKA----EAE-------------ERAMELLErvgLADkADAYPAQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 163 LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD--YEG-TVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDlaKEGmTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-236 |
5.86e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 72.15 E-value: 5.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdtdiegeARPQPGiKIGYLPQE-PKLNPEH--TVREAVEEAVSEL 97
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL-------EKPAQG-TVSFRGQDlYQLDRKQrrAFRRDVQLVFQDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 98 KNALNRLDEVYAAYADPDADFDKLAKEQgqleaiiqshdghnlenQLERAAEALRLPEWDAKI-----EKLSGGERRRVA 172
Cdd:TIGR02769 98 PSAVNPRMTVRQIIGEPLRHLTSLDESE-----------------QKARIAELLDMVGLRSEDadklpRQLSGGQLQRIN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739061588 173 ICRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDmvlqAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
324-484 |
5.97e-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: 71.56 E-value: 5.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGD-RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTVKLASVDQFRDSMD-- 399
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEiFIDGEDIREQDPVELRRKIGyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 400 -------DSKTVWEEVSGGQDIMRIGNFEIPSRAY-------VGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNM 465
Cdd:cd03295 81 iqqiglfPHMTVEENIALVPKLLKWPKEKIRERADellalvgLDPAEFA----DRYPHELSGGQQQRVGVARALAADPPL 156
|
170
....*....|....*....
gi 739061588 466 LLLDEPTNDLDVETLRALE 484
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQ 175
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-258 |
6.45e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.39 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEArpqpgikigylpqepkLNPEHTVREAVEEAVSELKNa 100
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV----------------IFNGQPMSKLSSAAKAELRN- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 101 lNRLDEVYAaYADPDADFDKLakEQGQLEAIIqshDGHNLENQLERAAEALRLPEWDAKIE----KLSGGERRRVAICRL 176
Cdd:PRK11629 87 -QKLGFIYQ-FHHLLPDFTAL--ENVAMPLLI---GKKKPAEINSRALEMLAAVGLEHRANhrpsELSGGERQRVAIARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 177 LLEKPDMLLLDEPTNHLD---AESVAWLERFLHDYEGTV-VAITHDryfldnvagwiLELdrgegipwEGNYSSWLEQKD 252
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTAfLVVTHD-----------LQL--------AKRMSRQLEMRD 220
|
....*.
gi 739061588 253 ARLEQE 258
Cdd:PRK11629 221 GRLTAE 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
324-488 |
6.71e-14 |
|
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: 74.32 E-value: 6.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSY-GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDtVKLASVDQ--------- 393
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG-VPVSSLDQdevrrrvsv 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 -------FRDSMDDSKTVWEEVSGGQDIM----RIGnFEIPSRAYVGRFNFKGVDQGKRvgeLSGGERGRLHLAKLLQVG 462
Cdd:TIGR02868 414 caqdahlFDTTVRENLRLARPDATDEELWaaleRVG-LADWLRALPDGLDTVLGEGGAR---LSGGERQRLALARALLAD 489
|
170 180
....*....|....*....|....*.
gi 739061588 463 GNMLLLDEPTNDLDVETLRALENALL 488
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLEDLL 515
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-218 |
6.82e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.41 E-value: 6.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdTDIEGEA----RPQPGIKI-------GYLPQ--EPKLN------- 81
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEIllngRPLSDWSAaelarhrAYLSQqqSPPFAmpvfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 ----PEHTVREAVEEAVSELKNALNrLDevyaayadpdadfDKLAKEQGQleaiiqshdghnlenqleraaealrlpewd 157
Cdd:COG4138 91 alhqPAGASSEAVEQLLAQLAEALG-LE-------------DKLSRPLTQ------------------------------ 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739061588 158 akiekLSGGERRRVAICRLLLE-----KPD--MLLLDEPTNHLD-AESVA---WLERFlHDYEGTVVAITHD 218
Cdd:COG4138 127 -----LSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPMNSLDvAQQAAldrLLREL-CQQGITVVMSSHD 192
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
324-476 |
8.14e-14 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 70.60 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLidDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLG--DTVKLASVDQFRDSMDDS 401
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 402 KTVWEEVSGGQDimrIGNFEIPS-----------RAYVGRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLLDE 470
Cdd:cd03298 79 NNLFAHLTVEQN---VGLGLSPGlkltaedrqaiEVALARVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
....*.
gi 739061588 471 PTNDLD 476
Cdd:cd03298 155 PFAALD 160
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-477 |
8.23e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.71 E-value: 8.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI------DTDI--EGEARPQPGIK------IGYLPQEPKLNPEHTVR 87
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwDGEIywSGSPLKASNIRdteragIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 88 EAVEEAvSELKNALNRLDevYAAyadpdadfdklakeqgqleaiiQSHDGHNLENQLERAAEALRLPewdakIEKLSGGE 167
Cdd:TIGR02633 97 ENIFLG-NEITLPGGRMA--YNA----------------------MYLRAKNLLRELQLDADNVTRP-----VGDYGGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 168 RRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAG---WILELDRGEGIpwegny 244
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvcdTICVIRDGQHV------ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 245 sswleqkdarleqeaATEAARHKSIQKelewIRQNPKGRqakgkarlarfeelnsvdyqkrnETSELFiPPGPR-LGDKV 323
Cdd:TIGR02633 221 ---------------ATKDMSTMSEDD----IITMMVGR-----------------------EITSLY-PHEPHeIGDVI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGD---RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISG-------------QEQPDSGT-------- 379
Cdd:TIGR02633 258 LEARNLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvfinGKPVDIRNpaqairag 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 380 ----------------LVLGDTVKLASVDQF--RDSMDDSKTvweevsggQDIMRIGnfeipsrayVGRFNFKGVDQGKR 441
Cdd:TIGR02633 338 iamvpedrkrhgivpiLGVGKNITLSVLKSFcfKMRIDAAAE--------LQIIGSA---------IQRLKVKTASPFLP 400
|
490 500 510
....*....|....*....|....*....|....*.
gi 739061588 442 VGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDV 477
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
324-532 |
8.58e-14 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 71.14 E-value: 8.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEqpdsGTLVLGDTVKLASVDQFRDSMDD--- 400
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHP----SYEVTSGTILFKGQDLLELEPDErar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 401 -----SKTVWEEVSG------------------GQDIMRIGNFE------IPSRAYVGRFNFKGVDQGkrvgeLSGGERG 451
Cdd:TIGR01978 77 aglflAFQYPEEIPGvsnleflrsalnarrsarGEEPLDLLDFEkllkekLALLDMDEEFLNRSVNEG-----FSGGEKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 452 RLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEF--PGCAM-VISHDRWFLDRIATHIIDYQDEGKVeFFEGNFT 528
Cdd:TIGR01978 152 RNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrePDRSFlIITHYQRLLNYIKPDYVHVLLDGRI-VKSGDVE 230
|
....
gi 739061588 529 EYEE 532
Cdd:TIGR01978 231 LAKE 234
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-217 |
8.63e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.22 E-value: 8.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 24 NISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIG-----------YLPQEPKLNPEHTVREAVee 92
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ-GEPIRrqrdeyhqdllYLGHQPGIKTELTALENL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 93 avselkNALNRLdevyAAYADPDADFDKLAKEqgqleaiiqshdghNLENQLeraaealrlpewDAKIEKLSGGERRRVA 172
Cdd:PRK13538 96 ------RFYQRL----HGPGDDEALWEALAQV--------------GLAGFE------------DVPVRQLSAGQQRRVA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 739061588 173 ICRLLLEKPDMLLLDEPTNHLDAESVAWLERFL--H-DYEGTVVAITH 217
Cdd:PRK13538 140 LARLWLTRAPLWILDEPFTAIDKQGVARLEALLaqHaEQGGMVILTTH 187
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-252 |
8.82e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.09 E-value: 8.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAgidtdiegeaR---PQPG-IKIGYLPqepkLN--PEHTVREA---V 90
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT----------RawdPQQGeILLNGQP----IAdySEAALRQAisvV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 91 EEAV----SELKNALnrldevyaAYADPDADFDKLAK--EQGQLEAIIQSHDGhnLENQLeraAEALRlpewdakieKLS 164
Cdd:PRK11160 420 SQRVhlfsATLRDNL--------LLAAPNASDEALIEvlQQVGLEKLLEDDKG--LNAWL---GEGGR---------QLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 165 GGERRRVAICRLLLEKPDMLLLDEPTNHLDAESvawlER------FLHDYEGTVVAITHDRYFLDNVAGWILeLDRGEGI 238
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAET----ERqilellAEHAQNKTVLMITHRLTGLEQFDRICV-MDNGQII 552
|
250
....*....|....
gi 739061588 239 PwEGNYSSWLEQKD 252
Cdd:PRK11160 553 E-QGTHQELLAQQG 565
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
325-489 |
9.65e-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: 70.72 E-value: 9.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 325 EINNLTKSY-GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGD----TVKLASVDQ-----F 394
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirDISRKSLRSmigvvL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 395 RDSMDDSKTVWEEVSGGQDIMRIGNFEIPSRAyVGRFNF-----KGVDQ--GKRVGELSGGERGRLHLAKLLQVGGNMLL 467
Cdd:cd03254 84 QDTFLFSGTIMENIRLGRPNATDEEVIEAAKE-AGAHDFimklpNGYDTvlGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180
....*....|....*....|..
gi 739061588 468 LDEPTNDLDVETLRALENALLE 489
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEK 184
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
324-520 |
9.78e-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: 70.72 E-value: 9.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGD--RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDT----VKLAS------- 390
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdYTLASlrrqigl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 391 VDQfrDSMDDSKTVWEEVSGG------QDIMR----------IGNFEipsrayvgrfnfKGVDQ--GKRVGELSGGERGR 452
Cdd:cd03251 81 VSQ--DVFLFNDTVAENIAYGrpgatrEEVEEaaraanahefIMELP------------EGYDTviGERGVKLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739061588 453 LHLAKLLQVGGNMLLLDEPTNDLDVETLRALENAL--LEFPGCAMVISHdrwfldRIAT----HIIDYQDEGKV 520
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALerLMKNRTTFVIAH------RLSTienaDRIVVLEDGKI 214
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
327-520 |
1.03e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.56 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 327 NNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTV-KLASVDQFRD-------- 396
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIqHYASKEVARRigllaqna 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 397 SMDDSKTVWEEVSGGqdimRIGNFEIPSR-------AYVGRFNFKGVDQ--GKRVGELSGGERGRLHLAKLLQVGGNMLL 467
Cdd:PRK10253 91 TTPGDITVQELVARG----RYPHQPLFTRwrkedeeAVTKAMQATGITHlaDQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 468 LDEPTNDLDVE---TLRALENALLEFPGCAM-VISHDRWFLDRIATHIIDYQDeGKV 520
Cdd:PRK10253 167 LDEPTTWLDIShqiDLLELLSELNREKGYTLaAVLHDLNQACRYASHLIALRE-GKI 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
323-489 |
1.10e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.04 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYgdRVLI-----------------------DDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT 379
Cdd:COG4586 1 IIEVENLSKTY--RVYEkepglkgalkglfrreyreveavDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 380 L-VLGdtvklasVDQFRDSMDDSKTVweevsG---GQ------DIMRIGNFE-------IPSRAY-------VGRFNFKG 435
Cdd:COG4586 79 VrVLG-------YVPFKRRKEFARRI-----GvvfGQrsqlwwDLPAIDSFRllkaiyrIPDAEYkkrldelVELLDLGE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739061588 436 -VDQgkRVGELSGGERGR-------LHLAKLlqvggnmLLLDEPTNDLDVETLRALENALLE 489
Cdd:COG4586 147 lLDT--PVRQLSLGQRMRcelaaalLHRPKI-------LFLDEPTIGLDVVSKEAIREFLKE 199
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
323-500 |
1.20e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.26 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGD-RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVK-----LASVDQ-- 393
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIKydkksLLEVRKtv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 ---FRDSMDD--SKTVWEEVSGGQDIMRIGNFEIPSRAyvgrfnfkgVDQGKRVG----------ELSGGERGRLHLAKL 458
Cdd:PRK13639 81 givFQNPDDQlfAPTVEEDVAFGPLNLGLSKEEVEKRV---------KEALKAVGmegfenkpphHLSGGQKKRVAIAGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 739061588 459 LQVGGNMLLLDEPTNDLDVETLRALENALLEF--PGCAMVIS-HD 500
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGITIIIStHD 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
324-549 |
1.27e-13 |
|
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: 73.30 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQ--PDSGTL--------------------- 380
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 381 ---VLGDTVKLASVD-------QFRDSMD-------------DSKTVWEEVsggqdIMRIGNFEIPSRAYVGRFN--FKG 435
Cdd:TIGR03269 81 pcpVCGGTLEPEEVDfwnlsdkLRRRIRKriaimlqrtfalyGDDTVLDNV-----LEALEEIGYEGKEAVGRAVdlIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 436 VDQGKRVG----ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEF---PGCAMVI-SHDRWFLDRI 507
Cdd:TIGR03269 156 VQLSHRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkaSGISMVLtSHWPEVIEDL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 739061588 508 ATHIIDYQD-----EGK----VEFFEGNFTEYEEYKKRTLGNDAIQPRRMK 549
Cdd:TIGR03269 236 SDKAIWLENgeikeEGTpdevVAVFMEGVSEVEKECEVEVGEPIIKVRNVS 286
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
324-475 |
1.31e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.41 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSY-GDRVLiDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVdqfRDSMDD- 400
Cdd:PRK11288 5 LSFDGIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMRFAST---TAALAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 401 ------------SKTVWEEVSGGQDIMRIGNFEIPSRAYVGRFNFKG----VDQGKRVGELSGGERGRLHLAKLLQVGGN 464
Cdd:PRK11288 81 vaiiyqelhlvpEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHlgvdIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170
....*....|.
gi 739061588 465 MLLLDEPTNDL 475
Cdd:PRK11288 161 VIAFDEPTSSL 171
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
324-500 |
1.46e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.64 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLtkSYGDRVLidDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGqEQPDSGTLVLGDT----VKLASVDQFRD--- 396
Cdd:COG4138 1 LQLNDV--AVAGRLG--PISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRplsdWSAAELARHRAyls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 397 -------SMDdsktVWEEVS-GGQDIMRIGNFEIPSRAYVGRFNFKgvDQ-GKRVGELSGGERGRLHLAK-LLQV----- 461
Cdd:COG4138 76 qqqsppfAMP----VFQYLAlHQPAGASSEAVEQLLAQLAEALGLE--DKlSRPLTQLSGGEWQRVRLAAvLLQVwptin 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739061588 462 -GGNMLLLDEPTNDLDVETLRALENALLEF--PGCAMVIS-HD 500
Cdd:COG4138 150 pEGQLLLLDEPMNSLDVAQQAALDRLLRELcqQGITVVMSsHD 192
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
324-520 |
1.59e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.55 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLAS---------VDQF 394
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 395 RD---------SMDDSKTVWEEVSGGQDIMR---IGNFEIPSRAYVGRFNFKGVDQG--KRvgeLSGGERGRLHLAKLLQ 460
Cdd:PRK11264 84 RQhvgfvfqnfNLFPHRTVLENIIEGPVIVKgepKEEATARARELLAKVGLAGKETSypRR---LSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 461 VGGNMLLLDEPTNDLDVE-------TLRAL--ENAllefpgcAMVI-SHDRWFLDRIATHIIdYQDEGKV 520
Cdd:PRK11264 161 MRPEVILFDEPTSALDPElvgevlnTIRQLaqEKR-------TMVIvTHEMSFARDVADRAI-FMDQGRI 222
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
320-508 |
1.68e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 71.69 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 320 GDKVLEINNLTKSY---------GDRVL--IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLG--DTV 386
Cdd:COG4608 4 AEPLLEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 387 KLASVDQ----------FRD---SMDDSKTVWEEVSGGQDIMRIGnfeiPSRAYVGRfnfkgVDQG-KRVG--------- 443
Cdd:COG4608 84 GLSGRELrplrrrmqmvFQDpyaSLNPRMTVGDIIAEPLRIHGLA----SKAERRER-----VAELlELVGlrpehadry 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 444 --ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDV----------ETLRAlenallEFpGCAMV-ISHD----RWFLDR 506
Cdd:COG4608 155 phEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVsiqaqvlnllEDLQD------EL-GLTYLfISHDlsvvRHISDR 227
|
..
gi 739061588 507 IA 508
Cdd:COG4608 228 VA 229
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
326-498 |
1.92e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.68 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 326 INNLTKSYGD-RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL-VLGDTVKLASVDQFRDSMDDSKT 403
Cdd:PRK15056 9 VNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsILGQPTRQALQKNLVAYVPQSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 404 V-WEEVSGGQDIMRIGNF------EIPSR----------AYVGRFNFKGvdqgKRVGELSGGERGRLHLAKLLQVGGNML 466
Cdd:PRK15056 89 VdWSFPVLVEDVVMMGRYghmgwlRRAKKrdrqivtaalARVDMVEFRH----RQIGELSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190
....*....|....*....|....*....|....
gi 739061588 467 LLDEPTNDLDVETLRALENALLEF--PGCAMVIS 498
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRELrdEGKTMLVS 198
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-234 |
2.00e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.43 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI--------------DTDIEG---EARpqpgiKIGYLPQEPKLN 81
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlspafsasgevllnGRRLTAlpaEQR-----RIGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 PEHTVREAVeeavselknalnrldevyaAYADPDAdfdkLAKEQGQlEAIIQShdghnLEnQLERAAEALRLPEwdakie 161
Cdd:COG4136 89 PHLSVGENL-------------------AFALPPT----IGRAQRR-ARVEQA-----LE-EAGLAGFADRDPA------ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERF----LHDYEGTVVAITHDRyflDNV--AGWILELDR 234
Cdd:COG4136 133 TLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDE---EDApaAGRVLDLGN 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-500 |
2.55e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.43 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKS-TLLRIMAGIDT--------DI-----------EGEARPQPGIKIGYLPQEP 78
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvypsgDIrfhgesllhasEQTLRGVRGNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 79 --KLNPEHTVREAVEEAVSelknaLNRldevyaayadpdadfdKLAKEQGQLEAIiqshdghnleNQLERAA---EALRL 153
Cdd:PRK15134 102 mvSLNPLHTLEKQLYEVLS-----LHR----------------GMRREAARGEIL----------NCLDRVGirqAAKRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 154 PEWDakiEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG----TVVAITHD----RYFLDNV 225
Cdd:PRK15134 151 TDYP---HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNlsivRKLADRV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 226 AgwileldrgegipwegnysswLEQKDARLEQEAATE---AARHKSIQKELEwirQNPKGRQ---AKGKARLARFEELnS 299
Cdd:PRK15134 228 A---------------------VMQNGRCVEQNRAATlfsAPTHPYTQKLLN---SEPSGDPvplPEPASPLLDVEQL-Q 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 300 VDYQKRNETselfippgprlgdkvleinnLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKST----LFRMISGQEQP 375
Cdd:PRK15134 283 VAFPIRKGI--------------------LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 376 --DSGTLVLGDTVKLASVDQ-----FRD---SMDDSKTVWEEVSGGqdiMRIGNFEIPSRAYVGR----FNFKGVDQGKR 441
Cdd:PRK15134 343 wfDGQPLHNLNRRQLLPVRHriqvvFQDpnsSLNPRLNVLQIIEEG---LRVHQPTLSAAQREQQviavMEEVGLDPETR 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 442 ---VGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDvETLRA----LENALLEFPGCAMV-ISHD 500
Cdd:PRK15134 420 hryPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQAqilaLLKSLQQKHQLAYLfISHD 485
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
339-500 |
3.14e-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: 69.42 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQ---FRD-SMDDSKTVWEEVSGGQD 413
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQITEPGPDRmvvFQNySLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 414 IMRiGNFEIPSRAYVGRFNFKGVD----QGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLE 489
Cdd:TIGR01184 81 RVL-PDLSKSERRAIVEEHIALVGlteaADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170
....*....|....*.
gi 739061588 490 F-----PGCAMViSHD 500
Cdd:TIGR01184 160 IweehrVTVLMV-THD 174
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-241 |
3.38e-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 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: 69.77 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGIDTDIEG---EARPqpgiKIGYLPQepklN 81
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLnglllptsgkvtvDGLDTLDEEnlwEIRK----KVGMVFQ----N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 PEHT-VREAVEEAVselknalnrldevyaAYAdpdadfdklakeqgqleaiiqshdghnLENQ-------LERAAEALRL 153
Cdd:TIGR04520 86 PDNQfVGATVEDDV---------------AFG---------------------------LENLgvpreemRKRVDEALKL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 154 PEWDAKIEK----LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAES---VAWLERFLHDYEG-TVVAITHDryfLDNV 225
Cdd:TIGR04520 124 VGMEDFRDRephlLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGrkeVLETIRKLNKEEGiTVISITHD---MEEA 200
|
250 260
....*....|....*....|..
gi 739061588 226 --AGWILELDRG----EGIPWE 241
Cdd:TIGR04520 201 vlADRVIVMNKGkivaEGTPRE 222
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-229 |
3.86e-13 |
|
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: 69.32 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 31 PGAKIGVLGLNGAGKSTLLRIMAGidtdiegEARPQPGikigylpqepKLNPEHTVREAVEE-AVSELKNALNRL--DEV 107
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAG-------KLKPNLG----------KFDDPPDWDEILDEfRGSELQNYFTKLleGDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 108 YAA----YAD--PDA------DFDKLAKEQGQLEAIIQSHDghnLENQLERaaealrlpewdaKIEKLSGGERRRVAICR 175
Cdd:cd03236 88 KVIvkpqYVDliPKAvkgkvgELLKKKDERGKLDELVDQLE---LRHVLDR------------NIDQLSGGELQRVAIAA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 176 LLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDYEGTVVAITHDRYFLDNVAGWI 229
Cdd:cd03236 153 ALARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
230-305 |
4.06e-13 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 64.90 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 230 LELDRGEGIPWEGNYSSWLEQKDARLEQEAATEAARHKSIQKELEWIRQNP----KGRQAKGKA-RLARFEELNSVDYQK 304
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRakasKAKQAQSRIkALEKMERIEKPERDK 80
|
.
gi 739061588 305 R 305
Cdd:pfam12848 81 P 81
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-472 |
4.15e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.08 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-----------IDTDI-EGEARPQPGIKIGYLPQ--EPKLNPE 83
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarkiqqgrvevLGGDMaDARHRRAVCPRIAYMPQglGKNLYPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 84 HTVREAVeeavselknalnrldevyaayadpdaDFdklakeQGQLEaiiqshdGHNLENQLERAAEALR----LPEWDAK 159
Cdd:NF033858 93 LSVFENL--------------------------DF------FGRLF-------GQDAAERRRRIDELLRatglAPFADRP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 160 IEKLSGGERRRVAICRLLLEKPDMLLLDEPT---------------NHLDAE----SV----AWLE---RFLHdyegtVV 213
Cdd:NF033858 134 AGKLSGGMKQKLGLCCALIHDPDLLILDEPTtgvdplsrrqfweliDRIRAErpgmSVlvatAYMEeaeRFDW-----LV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 214 AithdryfLDnvAGWILeldrGEGIPwegnysswleqkdARLEQEAAT---EAArhksiqkeleWIRQNPKGRQAKGKAr 290
Cdd:NF033858 209 A-------MD--AGRVL----ATGTP-------------AELLARTGAdtlEAA----------FIALLPEEKRRGHQP- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 291 larfeelnsvdyqkrnetseLFIPPGPRLGDK--VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRM 368
Cdd:NF033858 252 --------------------VVIPPRPADDDDepAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKM 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 369 ISGQEQPDSGT-LVLGDTVKlasvdqfRDSMDDSKTV---------WEEVSGGQDIM------RIGNFEIPSR--AYVGR 430
Cdd:NF033858 312 LTGLLPASEGEaWLFGQPVD-------AGDIATRRRVgymsqafslYGELTVRQNLElharlfHLPAAEIAARvaEMLER 384
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 739061588 431 FNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:NF033858 385 FDLADV-ADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
320-378 |
4.26e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.79 E-value: 4.26e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 320 GDKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSG 378
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHG 62
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-64 |
4.29e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.95 E-value: 4.29e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR 64
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
321-520 |
4.53e-13 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 68.65 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSY---GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTV---------- 386
Cdd:cd03248 9 KGIVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdGKPIsqyehkylhs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 387 KLASVDQ----FRDSMDDS------KTVWEEVSGGQDIMRIGNF--EIPSRAYVgrfnfkgvDQGKRVGELSGGERGRLH 454
Cdd:cd03248 89 KVSLVGQepvlFARSLQDNiayglqSCSFECVKEAAQKAHAHSFisELASGYDT--------EVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739061588 455 LAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEFPG--CAMVISHdrwfldRIAT----HIIDYQDEGKV 520
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH------RLSTveraDQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
336-483 |
4.64e-13 |
|
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: 69.05 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 336 RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTlVLGDTVKLASVDQ----------FRDSMDDSKTVW 405
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGR-VLVDGHDLALADPawlrrqvgvvLQENVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 406 EEVSGGQDIMRIGNFEIPSRaYVGRFNF-----KGVDQ--GKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVE 478
Cdd:cd03252 94 DNIALADPGMSMERVIEAAK-LAGAHDFiselpEGYDTivGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
....*
gi 739061588 479 TLRAL 483
Cdd:cd03252 173 SEHAI 177
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
321-522 |
4.77e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.76 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLT-KSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQ------ 393
Cdd:COG4178 360 DGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQrpylpl 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 -----------FRDSMDDsktvwEEVsggQDIMRIGNFEipsrAYVGRFnfkgvDQGKRVG-ELSGGERGRLHLAKLLQV 461
Cdd:COG4178 440 gtlreallypaTAEAFSD-----AEL---REALEAVGLG----HLAERL-----DEEADWDqVLSLGEQQRLAFARLLLH 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 462 GGNMLLLDEPTNDLDVETLRALENALL-EFPGCAMV-ISHdRWFLDRIATHIIDYQDEGKVEF 522
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLReELPGTTVIsVGH-RSTLAAFHDRVLELTGDGSWQL 564
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
324-520 |
5.41e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.89 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDtvklASVDqFRDSMDDSKT 403
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAG----HQFD-FSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 404 ---------------VWEEVSGGQDIMrignfEIPSRAyVGRFNFKGVDQGKRVGE--------------LSGGERGRLH 454
Cdd:COG4161 78 rllrqkvgmvfqqynLWPHLTVMENLI-----EAPCKV-LGLSKEQAREKAMKLLArlrltdkadrfplhLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 455 LAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEFPGCAM---VISHDRWFLDRIATHIIdYQDEGKV 520
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVV-YMEKGRI 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
319-500 |
5.71e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 69.27 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 319 LGDKVLEINNLTKSYGD--RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTV---------- 386
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 387 -KLASVDQFRDSMDDSKTVWEEVSGGqdimrIGNFEIPSRAYVGRfnfkgVDQG-KRVG----------ELSGGERGRLH 454
Cdd:PRK13635 81 rQVGMVFQNPDNQFVGATVQDDVAFG-----LENIGVPREEMVER-----VDQAlRQVGmedflnrephRLSGGQKQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 455 LAKLLQVGGNMLLLDEPTNDLD-------VETLRALENAllefpGCAMVIS--HD 500
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDprgrrevLETVRQLKEQ-----KGITVLSitHD 200
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
328-476 |
7.71e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.06 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 328 NLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTvklasvdqfrdSMDD---SK-- 402
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-----------RMNDvppAErg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 403 --------------TVWEEVSGGQDIMRIGNFEIPSRayvgrfnfkgVDQGKRV-----------GELSGGERGRLHLAK 457
Cdd:PRK11000 77 vgmvfqsyalyphlSVAENMSFGLKLAGAKKEEINQR----------VNQVAEVlqlahlldrkpKALSGGQRQRVAIGR 146
|
170
....*....|....*....
gi 739061588 458 LLQVGGNMLLLDEPTNDLD 476
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLD 165
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
342-500 |
9.80e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.04 E-value: 9.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 342 LSFSIPKGAIVGIIGPNGAGKSTLFRMISGQeQPDSGTLVLGDTV----KLASVDQFRD----------SMDdsktVWEE 407
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPleawSAAELARHRAylsqqqtppfAMP----VFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 408 VSGGQ-DIMRIGNFEIPSRAYVGRFNFKgvDQ-GKRVGELSGGERGRLHLAK-LLQV------GGNMLLLDEPTNDLDVE 478
Cdd:PRK03695 90 LTLHQpDKTRTEAVASALNEVAEALGLD--DKlGRSVNQLSGGEWQRVRLAAvVLQVwpdinpAGQLLLLDEPMNSLDVA 167
|
170 180
....*....|....*....|....*
gi 739061588 479 TLRALENALLEFP--GCAMVIS-HD 500
Cdd:PRK03695 168 QQAALDRLLSELCqqGIAVVMSsHD 192
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
321-476 |
1.01e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.67 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSYGD--RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISG----QEQPDSGTLVLGDTV-------- 386
Cdd:PRK13640 3 DNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpDDNPNSKITVDGITLtaktvwdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 387 --KLASVDQFRDSMDDSKTVWEEVSGG--------QDIMRIGNFEIpsrAYVGRFNFkgvdQGKRVGELSGGERGRLHLA 456
Cdd:PRK13640 83 reKVGIVFQNPDNQFVGATVGDDVAFGlenravprPEMIKIVRDVL---ADVGMLDY----IDSEPANLSGGQKQRVAIA 155
|
170 180
....*....|....*....|
gi 739061588 457 KLLQVGGNMLLLDEPTNDLD 476
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLD 175
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
324-513 |
1.10e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 70.62 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDR--VLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTvKLASVD--QFRDSMd 399
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ-PIADYSeaALRQAI- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 400 dskTVweeVSGGQDI--------MRIGNFEIPSRAYVGRFNFKG----VDQGKR----VGE----LSGGERGRLHLAKLL 459
Cdd:PRK11160 417 ---SV---VSQRVHLfsatlrdnLLLAAPNASDEALIEVLQQVGleklLEDDKGlnawLGEggrqLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 460 QVGGNMLLLDEPTNDLDVETLRALENALLEFpgCA----MVISHDRWFL---DRIatHIID 513
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAEH--AQnktvLMITHRLTGLeqfDRI--CVMD 547
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
324-476 |
1.12e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 68.35 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYG----DRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQ---FR 395
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdGVPVTGPGADRgvvFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 DsmdDS----KTVWEEVSGGQDIMRIGNFEIPSRA--YVGRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLLD 469
Cdd:COG4525 84 K---DAllpwLNVLDNVAFGLRLRGVPKAERRARAeeLLALVGLADFAR-RRIWQLSGGMRQRVGIARALAADPRFLLMD 159
|
....*..
gi 739061588 470 EPTNDLD 476
Cdd:COG4525 160 EPFGALD 166
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
325-529 |
1.33e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 70.38 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 325 EINNLTKSY-GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTlVLGD-----TVKLASVDQ----- 393
Cdd:PRK13657 336 EFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGR-ILIDgtdirTVTRASLRRniavv 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 FRDSMDDSKTVweevsggQDIMRIG-----NFEI---PSRAYVGRF---NFKGVDQ--GKRVGELSGGERGRLHLAKLLQ 460
Cdd:PRK13657 415 FQDAGLFNRSI-------EDNIRVGrpdatDEEMraaAERAQAHDFierKPDGYDTvvGERGRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 461 VGGNMLLLDEPTNDLDVETLRALENALlefpGCAM------VISHdRWFLDRIATHIIdYQDEGK-VEffEGNFTE 529
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAAL----DELMkgrttfIIAH-RLSTVRNADRIL-VFDNGRvVE--SGSFDE 555
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-217 |
1.36e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.88 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDtdiegearpqpgikigylpqepKLNPEHTVREAVeeavseL 97
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMN----------------------DLNPEVTITGSI------V 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 98 KNALNrldeVYAayadPDADFDKLAKEQGQL------------EAIIQS------HDGHNLENQLERAAEALRLpeWDAK 159
Cdd:PRK14239 69 YNGHN----IYS----PRTDTVDLRKEIGMVfqqpnpfpmsiyENVVYGlrlkgiKDKQVLDEAVEKSLKGASI--WDEV 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 160 IEKL-------SGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFL----HDYegTVVAITH 217
Cdd:PRK14239 139 KDRLhdsalglSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLlglkDDY--TMLLVTR 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-490 |
1.53e-12 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 66.30 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 320 GDKVLEINNLTKsyGDRVliDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQFRDS- 397
Cdd:cd03215 1 GEPVLEVRGLSV--KGAV--RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVTRRSPRDAIRAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 398 ----MDDSKTvwEEVSGGQDIMRigNFEIPSRayvgrfnfkgvdqgkrvgeLSGGERGRLHLAKLLQVGGNMLLLDEPTN 473
Cdd:cd03215 77 iayvPEDRKR--EGLVLDLSVAE--NIALSSL-------------------LSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170
....*....|....*..
gi 739061588 474 DLDVETLRALENALLEF 490
Cdd:cd03215 134 GVDVGAKAEIYRLIREL 150
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
324-500 |
1.77e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.42 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQFRDSMDDSK 402
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdGKPVEGPGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 403 TVWEEVSGGQDI-MRIGNFEIPSRAYVGRFNFKGVD----QGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDV 477
Cdd:PRK11248 82 LPWRNVQDNVAFgLQLAGVEKMQRLEIAHQMLKKVGlegaEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180
....*....|....*....|....*..
gi 739061588 478 ETLRALENALL----EFPGCAMVISHD 500
Cdd:PRK11248 162 FTREQMQTLLLklwqETGKQVLLITHD 188
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
288-488 |
1.94e-12 |
|
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: 69.77 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 288 KARLArFEELNSV-----DYQKRNETSELFIPpgprLGDkvLEINNLTKSYG-DRVLIDDLSFSIPKGAIVGIIGPNGAG 361
Cdd:TIGR01193 440 AARVA-NNRLNEVylvdsEFINKKKRTELNNL----NGD--IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSG 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 362 KSTLFRMISGQEQPDSGTLVLGDTvKLASVDQ----------------FRDSMDDS-------KTVWEEVSGGQDIMRI- 417
Cdd:TIGR01193 513 KSTLAKLLVGFFQARSGEILLNGF-SLKDIDRhtlrqfinylpqepyiFSGSILENlllgakeNVSQDEIWAACEIAEIk 591
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 418 GNFEIPSRAYVGRFNFKGvdqgkrvGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALL 488
Cdd:TIGR01193 592 DDIENMPLGYQTELSEEG-------SSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLL 655
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-490 |
2.01e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 67.25 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRM------------ISGQEQPDSGTLVLGDTVKLAS 390
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 391 VDQFRDSMDD---SKTVWEEVSGGQDIMRIGNF--EIPSRAYVGRFNFKGVDQGKR-----VGELSGGERGRLHLAKLLQ 460
Cdd:PRK14247 83 RVQMVFQIPNpipNLSIFENVALGLKLNRLVKSkkELQERVRWALEKAQLWDEVKDrldapAGKLSGGQQQRLCIARALA 162
|
170 180 190
....*....|....*....|....*....|
gi 739061588 461 VGGNMLLLDEPTNDLDVETLRALENALLEF 490
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLEL 192
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
323-483 |
2.18e-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: 66.04 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTK------SYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQ--EQPDSGTLVLgdtvklasvdqf 394
Cdd:cd03213 3 TLSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLI------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 395 rDSMDDSKTVWEEVSG--GQDIMRIGNFEIpsRAYVgRF--NFKGvdqgkrvgeLSGGERGRLHLAKLLQVGGNMLLLDE 470
Cdd:cd03213 71 -NGRPLDKRSFRKIIGyvPQDDILHPTLTV--RETL-MFaaKLRG---------LSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180
....*....|....*....|
gi 739061588 471 PTNDLD-------VETLRAL 483
Cdd:cd03213 138 PTSGLDsssalqvMSLLRRL 157
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-236 |
2.31e-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: 66.74 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEA---------------RPQpgikIGYLPQEPKL 80
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladpawlRRQ----VGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 81 NpEHTVREAVeeavselknalnrldevyaAYADPDADFDKL---AKEQGQLEAIIQSHDGHNlenQL--ERAAealrlpe 155
Cdd:cd03252 88 F-NRSIRDNI-------------------ALADPGMSMERVieaAKLAGAHDFISELPEGYD---TIvgEQGA------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 156 wdakieKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG--TVVAITHdRYFLDNVAGWILELD 233
Cdd:cd03252 138 ------GLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAH-RLSTVKNADRIIVME 210
|
...
gi 739061588 234 RGE 236
Cdd:cd03252 211 KGR 213
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-217 |
2.52e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 68.36 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 37 VLGLNGAGKSTLLRIMAGIDTDIEGEAR--------PQPGI-------KIGYLPQEPKLNPEHTVReaveeavSELKNAL 101
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVlngrvlfdAEKGIclppekrRIGYVFQDARLFPHYKVR-------GNLRYGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 102 NRLDevyaayadpDADFDKLAkeqgQLEAIiqshdGHNLEnqleraaealRLPEwdakieKLSGGERRRVAICRLLLEKP 181
Cdd:PRK11144 102 AKSM---------VAQFDKIV----ALLGI-----EPLLD----------RYPG------SLSGGEKQRVAIGRALLTAP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 739061588 182 DMLLLDEPTNHLDA----ESVAWLERFLHDYEGTVVAITH 217
Cdd:PRK11144 148 ELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSH 187
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
324-520 |
2.84e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.58 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLG----DTVKLASVDQFRDSMD 399
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAgnhfDFSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 400 DSKTV------WEEVSGGQDI----MRI---GNFEIPSRA-----------YVGRFNFkgvdqgkrvgELSGGERGRLHL 455
Cdd:PRK11124 83 NVGMVfqqynlWPHLTVQQNLieapCRVlglSKDQALARAekllerlrlkpYADRFPL----------HLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739061588 456 AKLLQVGGNMLLLDEPTNDLDVETLRALENALLEFPGCAM---VISHDRWFLDRIATHIIdYQDEGKV 520
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVEVARKTASRVV-YMENGHI 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
323-507 |
3.12e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.38 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGD-RVLID---DLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTV----------- 386
Cdd:PRK11629 5 LLQCDNLCKRYQEgSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFnGQPMsklssaakael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 387 ---KLASVDQFRDSMDDSkTVWEEVSGGQDIMRIGNFEIPSRAyvgRFNFKGVDQGKRV----GELSGGERGRLHLAKLL 459
Cdd:PRK11629 85 rnqKLGFIYQFHHLLPDF-TALENVAMPLLIGKKKPAEINSRA---LEMLAAVGLEHRAnhrpSELSGGERQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739061588 460 QVGGNMLLLDEPTNDLDVETLRALENALLEF---PGCA-MVISHDRWFLDRI 507
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELnrlQGTAfLVVTHDLQLAKRM 212
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
8-218 |
3.15e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.16 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 8 MLRVGKIVPPKRH--ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGidtDIEGEARPQpGIKIgylPQEPKLNPEHT 85
Cdd:PRK13547 1 MLTADHLHVARRHraILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG---DLTGGGAPR-GARV---TGDVTLNGEPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 86 vreaveEAVSELKnaLNRLDEVYAAYADPDADF--DKL--------AKEQGQLeaiiQSHDGHNLENQLERA-AEALrlp 154
Cdd:PRK13547 74 ------AAIDAPR--LARLRAVLPQAAQPAFAFsaREIvllgryphARRAGAL----THRDGEIAWQALALAgATAL--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 155 ewDAK-IEKLSGGERRRVAICRLLLE---------KPDMLLLDEPTNHLD-------AESVAWLERflhDYEGTVVAITH 217
Cdd:PRK13547 139 --VGRdVTTLSGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVH 213
|
.
gi 739061588 218 D 218
Cdd:PRK13547 214 D 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-257 |
3.43e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.92 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGearpqpgiKIGYLPQEPKLNPEHTVREAVEEAvSELKNA 100
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEG--------SIVVNGQTINLVRDKDGQLKVADK-NQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 101 LNRLDEVYAAYADpdadFDKLAKEQGQLEAIIQSHdGHNLENQLERAAEALRLPEWDAKIE-----KLSGGERRRVAICR 175
Cdd:PRK10619 91 RTRLTMVFQHFNL----WSHMTVLENVMEAPIQVL-GLSKQEARERAVKYLAKVGIDERAQgkypvHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 176 LLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHDRYFLDNVAGWILELDRGEgIPWEGNYSSWLEQ-K 251
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaeEGkTMVVVTHEMGFARHVSSHVIFLHQGK-IEEEGAPEQLFGNpQ 244
|
....*.
gi 739061588 252 DARLEQ 257
Cdd:PRK10619 245 SPRLQQ 250
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
335-483 |
3.46e-12 |
|
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: 66.14 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 335 DRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPD---SGTLVLG------DTVK--LASVDQFrDSMDDSKT 403
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNgqprkpDQFQkcVAYVRQD-DILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 404 VWEEV-----SGGQDIMRigNFEIPSRAYVGRFNFKGVDQ--GKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:cd03234 98 VRETLtytaiLRLPRKSS--DAIRKKRVEDVLLRDLALTRigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170
....*....|....
gi 739061588 477 -------VETLRAL 483
Cdd:cd03234 176 sftalnlVSTLSQL 189
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
8-194 |
3.48e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.14 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 8 MLRVGKIVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------------ARPqpgikIGY 73
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSltlngqdhtttppsRRP-----VSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 74 LPQEPKLNPEHTVREAVeeavselknALN-----RLDevyaayadpdadfdklAKEQGQLEAIIQSHdghNLENQLERaa 148
Cdd:PRK10771 76 LFQENNLFSHLTVAQNI---------GLGlnpglKLN----------------AAQREKLHAIARQM---GIEDLLAR-- 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 739061588 149 ealrLPEwdakieKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLD 194
Cdd:PRK10771 126 ----LPG------QLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-218 |
3.65e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.96 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARpqpgikigYLPQepklnPEHTVREaveEAVSELKnA 100
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVS--------LVGQ-----PLHQMDE---EARAKLR-A 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 101 LNrLDEVYAAYA-DPDADfdklAKEQGQLEAIIQshdGHNLENQLERAAEAL-------RLPEWDAKiekLSGGERRRVA 172
Cdd:PRK10584 88 KH-VGFVFQSFMlIPTLN----ALENVELPALLR---GESSRQSRNGAKALLeqlglgkRLDHLPAQ---LSGGEQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 739061588 173 ICRLLLEKPDMLLLDEPTNHLDAESVAWLERFL----HDYEGTVVAITHD 218
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-236 |
3.79e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.13 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIKIGylpqEPKLNPehtvreaVEEAvselKN 99
Cdd:PRK11000 17 VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD------LFIG----EKRMND-------VPPA----ER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 100 ALNRLDEVYAAY-----ADPDADFDKLAKEQgqlEAIIQShdghnlenQLERAAEALRLPEW-DAKIEKLSGGERRRVAI 173
Cdd:PRK11000 76 GVGMVFQSYALYphlsvAENMSFGLKLAGAK---KEEINQ--------RVNQVAEVLQLAHLlDRKPKALSGGQRQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 174 CRLLLEKPDMLLLDEPTNHLDAE-------SVAWLERFLhdyEGTVVAITHDRYFLDNVAGWILELDRGE 236
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAAlrvqmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
323-383 |
3.91e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.00 E-value: 3.91e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL-VLG 383
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLG 62
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
21-243 |
3.95e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 66.27 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIgylpqepkLNPEHTVREAVEEA------- 93
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVD-GLKV--------NDPKVDERLIRQEAgmvfqqf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 94 -----VSELKNALNRLDEVYAAyadPDADFDKLAKEqgqleaiiqshdghnLENQLERAAEALRLPEwdakieKLSGGER 168
Cdd:PRK09493 87 ylfphLTALENVMFGPLRVRGA---SKEEAEKQARE---------------LLAKVGLAERAHHYPS------ELSGGQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 169 RRVAICRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDyEG-TVVAITHDRYFLDNVAGWILELDRGeGIPWEGN 243
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPElrhEVLKVMQDLAE-EGmTMVIVTHEIGFAEKVASRLIFIDKG-RIAEDGD 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
321-529 |
3.97e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.80 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSYGDRV-LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDT---------VKL-- 388
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglMKLre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 389 --ASVDQFRDSMDDSKTVWEEVSGGQDIMRIGNFEIPSRayVGRFNFK-GVD--QGKRVGELSGGERGRLHLAKLLQVGG 463
Cdd:PRK13636 83 svGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKR--VDNALKRtGIEhlKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 464 NMLLLDEPTNDLD---VETLRALENALLEFPGCAMVishdrwfldrIATHIID----------YQDEGKVeFFEGNFTE 529
Cdd:PRK13636 161 KVLVLDEPTAGLDpmgVSEIMKLLVEMQKELGLTII----------IATHDIDivplycdnvfVMKEGRV-ILQGNPKE 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-216 |
4.06e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEG---EARPQPGIkiGYLPQEPKLnpeh 84
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvprdagniiidDEDISLlplHARARRGI--GYLPQEASI---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 tvreaveeavselknaLNRLdevyaayadpdADFDKLAkeqgqleAIIQSHDGHNLENQLERAAEALRlpEW------DA 158
Cdd:PRK10895 90 ----------------FRRL-----------SVYDNLM-------AVLQIRDDLSAEQREDRANELME--EFhiehlrDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 159 KIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDYeGTVVAIT 216
Cdd:PRK10895 134 MGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIiehLRDS-GLGVLIT 193
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
321-508 |
5.33e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 66.68 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSYG---DRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTV---------- 386
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQiIIDGDLLteenvwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 387 KLASVDQFRDSMDDSKTVWEEVSGGQDIMRIGNFEIPSR-----AYVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQV 461
Cdd:PRK13650 82 KIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERvnealELVGMQDFK----EREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 739061588 462 GGNMLLLDEPTNDLD----VETLRALENALLEFPGCAMVISHDrwfLDRIA 508
Cdd:PRK13650 158 RPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-195 |
6.87e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.15 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLL-----RIMAGIDTD----IEGEARPQPGIKI--GYLPQEPKLNPEHT 85
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKGSgsvlLNGMPIDAKEMRAisAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 86 VREAVeeavseLKNALNRLDEvyaayadpdadfdKLAKEQGQL--EAIIQshdghnlENQLERAAEALRLPEWDAKieKL 163
Cdd:TIGR00955 116 VREHL------MFQAHLRMPR-------------RVTKKEKRErvDEVLQ-------ALGLRKCANTRIGVPGRVK--GL 167
|
170 180 190
....*....|....*....|....*....|..
gi 739061588 164 SGGERRRVAICRLLLEKPDMLLLDEPTNHLDA 195
Cdd:TIGR00955 168 SGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-197 |
7.05e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.98 E-value: 7.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-------IDTDIEGEARPQPGI--KIGYLPQEPKLNPEHTVRE 88
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriqgnnfTGTILANNRKPTKQIlkRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 89 A-VEEAVSELKNALNRLDEVYAAyadpdadfdklakeqgqlEAIIQSHDGHNLENQLERaaealrlpewDAKIEKLSGGE 167
Cdd:PLN03211 160 TlVFCSLLRLPKSLTKQEKILVA------------------ESVISELGLTKCENTIIG----------NSFIRGISGGE 211
|
170 180 190
....*....|....*....|....*....|
gi 739061588 168 RRRVAICRLLLEKPDMLLLDEPTNHLDAES 197
Cdd:PLN03211 212 RKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
323-476 |
7.52e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.30 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDT-VKL----ASVDQFRDS 397
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdISLlplhARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 398 MDDSKTVWEEVSGGQDIMRIgnFEIpsrayvgRFNFKGVDQGKRVGE-----------------LSGGERGRLHLAKLLQ 460
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAV--LQI-------RDDLSAEQREDRANElmeefhiehlrdsmgqsLSGGERRRVEIARALA 153
|
170
....*....|....*.
gi 739061588 461 VGGNMLLLDEPTNDLD 476
Cdd:PRK10895 154 ANPKFILLDEPFAGVD 169
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
324-522 |
8.27e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 66.22 E-value: 8.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYG-----DRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGD------TVKLAS-- 390
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkKVKLSDir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 391 -----VDQFRDSMDDSKTVWEEVSGGQDIMRIGNFEIPSRAYVGrFNFKGVD----QGKRVGELSGGERGRLHLAKLLQV 461
Cdd:PRK13637 83 kkvglVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRA-MNIVGLDyedyKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 462 GGNMLLLDEPTNDLDV----ETLRALENALLEFPGCAMVISHDRWFLDRIATHIIdYQDEGKVEF 522
Cdd:PRK13637 162 EPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSHSMEDVAKLADRII-VMNKGKCEL 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
322-499 |
9.63e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 9.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 322 KVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGD------TVKLA-----S 390
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynklDHKLAaqlgiG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 391 VDQFRDSMDDSKTVWEEVSGGQDIMR-------IGNFEIPSRAYV--GRFNFKgVDQGKRVGELSGGERGRLHLAKLLQV 461
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMmlLRVGLK-VDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 739061588 462 GGNMLLLDEPTNDL---DVETLRALENALLEfPGCAMV-ISH 499
Cdd:PRK09700 163 DAKVIIMDEPTSSLtnkEVDYLFLIMNQLRK-EGTAIVyISH 203
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-217 |
9.63e-12 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 64.87 E-value: 9.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKST----LLR---------IMAGIDT-DIEGEARPQpgiKIGYLPQEPKLNp 82
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTvvslLERfydptsgeiLLDGVDIrDLNLRWLRS---QIGLVSQEPVLF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 83 EHTVREAVeeavselknalnrldevyaAYADPDA---DFDKLAKEQGQLEAIIQSHDGHNLENQlERAAealrlpewdak 159
Cdd:cd03249 90 DGTIAENI-------------------RYGKPDAtdeEVEEAAKKANIHDFIMSLPDGYDTLVG-ERGS----------- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 160 ieKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY-EG-TVVAITH 217
Cdd:cd03249 139 --QLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAmKGrTTIVIAH 196
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-228 |
1.05e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.88 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIKIGYLPQEPKLNPEHTVREAVEEAVS-----E 96
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGT------IEWIFKDEKNKKKTKEKEKVLEKLVIQktrfkK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 97 LKNALN---RLDEVY--AAYadpdadfdklakeqgQL-EAIIQShD--------GHNLENQLERAAEALR---LPEwdAK 159
Cdd:PRK13651 97 IKKIKEirrRVGVVFqfAEY---------------QLfEQTIEK-DiifgpvsmGVSKEEAKKRAAKYIElvgLDE--SY 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 160 IEK----LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVA-WLERF--LHDYEGTVVAITHDryfLDNVAGW 228
Cdd:PRK13651 159 LQRspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKeILEIFdnLNKQGKTIILVTHD---LDNVLEW 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
333-516 |
1.06e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.91 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 333 YGDRVLIDdLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTV---------------KLASVDQFRDS 397
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkeikpvrkKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 398 MDDSKTVWEEVSGGQDIMRIGNFEIPSRAyVGRFNFKGVDQ---GKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTND 474
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNFGIPKEKAEKIA-AEKLEMVGLADefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 739061588 475 LD----VETLRALEnALLEFPGCAMVISHdrwFLDRIAthiiDYQD 516
Cdd:PRK13643 175 LDpkarIEMMQLFE-SIHQSGQTVVLVTH---LMDDVA----DYAD 212
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
3-217 |
1.09e-11 |
|
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: 67.47 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 3 QYVYSMLRVGKI--VPPKRHILKNiSLSF-FP-GAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-ARPQPGiKIGYLPQE 77
Cdd:TIGR00954 446 EYQDNGIKFENIplVTPNGDVLIE-SLSFeVPsGNNLLICGPNGCGKSSLFRILGELWPVYGGRlTKPAKG-KLFYVPQR 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 78 PKLNpEHTVREAVeeavselknalnrldevyaAYADPDADFDKLAKEQGQLEAIIQSHDghnLENQLERAAEALRLPEWd 157
Cdd:TIGR00954 524 PYMT-LGTLRDQI-------------------IYPDSSEDMKRRGLSDKDLEQILDNVQ---LTHILEREGGWSAVQDW- 579
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 158 akIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITH 217
Cdd:TIGR00954 580 --MDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
321-476 |
1.12e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.40 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSYGD--RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQFRDS 397
Cdd:PRK13632 5 SVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 398 MD------DSK----TVWEEVSGGQDIMRIGNFEIPSRAYvgrfnfkgvDQGKRVG----------ELSGGERGRLHLAK 457
Cdd:PRK13632 85 IGiifqnpDNQfigaTVEDDIAFGLENKKVPPKKMKDIID---------DLAKKVGmedyldkepqNLSGGQKQRVAIAS 155
|
170
....*....|....*....
gi 739061588 458 LLQVGGNMLLLDEPTNDLD 476
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLD 174
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-88 |
1.35e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 64.48 E-value: 1.35e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT----DIEGEARPQPGIKIGYlpqepKLNPEHTVRE 88
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpdsgTVTVRGRVSSLLGLGG-----GFNPELTGRE 103
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
18-223 |
1.59e-11 |
|
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: 64.59 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGID----------------TDIEGEARPQPGIKIGY-LPQE-PK 79
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPsyevtsgtilfkgqdlLELEPDERARAGLFLAFqYPEEiPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 80 LNPEHTVREAVEeAVSELKNalnrLDEVyaayadPDADFDKLAKEQGQLEAIIqshdghnlENQLERAAEalrlpewdak 159
Cdd:TIGR01978 92 VSNLEFLRSALN-ARRSARG----EEPL------DLLDFEKLLKEKLALLDMD--------EEFLNRSVN---------- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 160 iEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAITHDRYFLD 223
Cdd:TIGR01978 143 -EGFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLN 208
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-477 |
1.62e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.49 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 1 MAQYVYSMLRVGKIVPPKRhILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI------DTDIEGEARP--------- 65
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyEGEIIFEGEElqasnirdt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 66 -QPGIKIGYlpQEPKLNPEHTVREAVEEAVSELKNALNRLDEVYAayadpdadfdklakeqgqleaiiqshdghnlenql 144
Cdd:PRK13549 80 eRAGIAIIH--QELALVKELSVLENIFLGNEITPGGIMDYDAMYL----------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 145 eRAAEALRLPEWD----AKIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVA---ITH 217
Cdd:PRK13549 123 -RAQKLLAQLKLDinpaTPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIAciyISH 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 218 DryfLDNV---AGWILELDRGEGIpwegnysswleqkdarleqeaATEAARHKSIQKelewIRQNPKGRqakgkarlarf 294
Cdd:PRK13549 202 K---LNEVkaiSDTICVIRDGRHI---------------------GTRPAAGMTEDD----IITMMVGR----------- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 295 eelnsvdyqkrnETSELFiPPGPR-LGDKVLEINNLT---KSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMIS 370
Cdd:PRK13549 243 ------------ELTALY-PREPHtIGEVILEVRNLTawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLF 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 371 G----------------------QEQPDSG---------------TLVLGDTVKLASVDQF--RDSMDDSKTVweevsgg 411
Cdd:PRK13549 310 GaypgrwegeifidgkpvkirnpQQAIAQGiamvpedrkrdgivpVMGVGKNITLAALDRFtgGSRIDDAAEL------- 382
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 412 QDImrignfeipsRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDV 477
Cdd:PRK13549 383 KTI----------LESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-236 |
1.64e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.03 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdtdiegeARPQPGikiGYLPQEPKLNPEHTVREAVEEAVSELKNA 100
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL-------LRPQKG---AVLWQGKPLDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 101 LNRldEVYaaYADPDADFDKLAKEQGQLEAIIQshdghnlenqlERAAEALRLPewDAK------IEKLSGGERRRVAIC 174
Cdd:PRK13638 86 PEQ--QIF--YTDIDSDIAFSLRNLGVPEAEIT-----------RRVDEALTLV--DAQhfrhqpIQCLSHGQKKRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 175 RLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHdyEGTVVAI-THDRYFLDNVAGWILELDRGE 236
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDpagrTQMIAIIRRIVA--QGNHVIIsSHDIDLIYEISDAVYVLRQGQ 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
324-522 |
1.88e-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: 63.67 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSY---GDRVLiDDLSFSIPKGAIVGIIGPNGAGKST----LFRMIsgqeQPDSGTLVLgDTVKLASVD--QF 394
Cdd:cd03244 3 IEFKNVSLRYrpnLPPVL-KNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILI-DGVDISKIGlhDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 395 RDSMD-----------------------DSKTVW---EEVSggqdimrignfeipSRAYVGRFNFKGVDQGKRVGE-LSG 447
Cdd:cd03244 77 RSRISiipqdpvlfsgtirsnldpfgeySDEELWqalERVG--------------LKEFVESLPGGLDTVVEEGGEnLSV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 448 GERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENAL-LEFPGCAMV-ISHdrwfldRIAThIIDYQ-----DEGKV 520
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIrEAFKDCTVLtIAH------RLDT-IIDSDrilvlDKGRV 215
|
...
gi 739061588 521 -EF 522
Cdd:cd03244 216 vEF 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-238 |
2.16e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.48 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdTDIEGEARPQPGIKI-GYLPQEPKLNPEHTVREAveEAVSELK 98
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRL-LELNEEARVEGEVRLfGRNIYSPDVDPIEVRREV--GMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 99 NALNRLdEVYAAYAdPDADFDKLAKEQGQLEAIIqshdghnlENQLERAAEalrlpeWDA-------KIEKLSGGERRRV 171
Cdd:PRK14267 95 NPFPHL-TIYDNVA-IGVKLNGLVKSKKELDERV--------EWALKKAAL------WDEvkdrlndYPSNLSGGQRQRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 172 AICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHDRYFLDNVAGWILELDRGEGI 238
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
328-484 |
2.25e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 64.73 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 328 NLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLA-SVDQFRDSMDDSKTVwe 406
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGrSIFNYRDVLEFRRRV-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 407 evsgGQDIMRIGNFEIP--------SRAY--VGRFNFKGVDQGK--RVG--------------ELSGGERGRLHLAKLLQ 460
Cdd:PRK14271 104 ----GMLFQRPNPFPMSimdnvlagVRAHklVPRKEFRGVAQARltEVGlwdavkdrlsdspfRLSGGQQQLLCLARTLA 179
|
170 180
....*....|....*....|....
gi 739061588 461 VGGNMLLLDEPTNDLDVETLRALE 484
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIE 203
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
323-516 |
2.29e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLgdtvklasvdqFRDSMDDSK 402
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILF-----------ERQSIKKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 403 TVWEevsggQDIMRIG-------NFEIPSRAYVGrFNFK----GVDQGKRV-----------GELSGGERGRLHLAKLLQ 460
Cdd:PRK13540 70 CTYQ-----KQLCFVGhrsginpYLTLRENCLYD-IHFSpgavGITELCRLfslehlidypcGLLSSGQKRQVALLRLWM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 461 VGGNMLLLDEPTNDLDVETLRALENALLEFP---GCAMVISHDRWFLDRiathiIDYQD 516
Cdd:PRK13540 144 SKAKLWLLDEPLVALDELSLLTIITKIQEHRakgGAVLLTSHQDLPLNK-----ADYEE 197
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
21-235 |
2.32e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.00 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT---------DIEGEA----RPQPGI------KIGYLPQEPKLN 81
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtirvgDITIDTarslSQQKGLirqlrqHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 PEHTVREAVEEAVSELKnalnrldevyaayADPDADFDKLAKEQgqleaiiqshdghnlenqleRAAEALRLPEwDAKIE 161
Cdd:PRK11264 98 PHRTVLENIIEGPVIVK-------------GEPKEEATARAREL--------------------LAKVGLAGKE-TSYPR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLE---RFLHDYEGTVVAITHDRYFLDNVAGWILELDRG 235
Cdd:PRK11264 144 RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLntiRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-227 |
2.71e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.13 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 24 NISLSffPGAKIGVLGLNGAGKS-TLLRIMA-----GIdtdIEGEARPQpGIKIGYLPQepklnpehtvreaveeavsel 97
Cdd:PRK09473 36 NFSLR--AGETLGIVGESGSGKSqTAFALMGllaanGR---IGGSATFN-GREILNLPE--------------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 98 kNALNRL--DEVYAAYADPDADFDKLAKEQGQLEAIIQSHDGHNLENQLE---RAAEALRLPEWDAKI----EKLSGGER 168
Cdd:PRK09473 89 -KELNKLraEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEesvRMLDAVKMPEARKRMkmypHEFSGGMR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 169 RRVAICRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHDryfLDNVAG 227
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD---LGVVAG 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-236 |
2.94e-11 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 62.87 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLriMAgidtdIEGEARPQPGI-----KIGYLPQEPKLNPEhTVREAV----- 90
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLL--SA-----LLGELEKLSGSvsvpgSIAYVSQEPWIQNG-TIRENIlfgkp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 91 --EEavselknalnRLDEVYAAYAdPDADFDKLAkeqgqleaiiqshDGHNLEnqleraaealrlpewdakI-EK---LS 164
Cdd:cd03250 92 fdEE----------RYEKVIKACA-LEPDLEILP-------------DGDLTE------------------IgEKginLS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 165 GGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWL-ER----FLHDyEGTVVAITHDRYFLDNVAgWILELDRGE 236
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENcilgLLLN-NKTRILVTHQLQLLPHAD-QIVVLDNGR 204
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-242 |
3.00e-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: 62.90 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 26 SLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIGYLP----------QEPKLNPEHTVREAVEEAVS 95
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN-GVDVTAAPpadrpvsmlfQENNLFAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 96 -ELKnaLNrldevyaayadpdadfdklAKEQGQLEAIIQshdghnlenQLERAAEALRLPEwdakieKLSGGERRRVAIC 174
Cdd:cd03298 97 pGLK--LT-------------------AEDRQAIEVALA---------RVGLAGLEKRLPG------ELSGGERQRVALA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739061588 175 RLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEgIPWEG 242
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR-IAAQG 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
323-487 |
3.20e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.88 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFR----MISGQEQPDSGTLVLGDTVKLAS-------- 390
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRTVQREGrlardirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 391 --------VDQFrdSMDDSKTVWEEVSGG--------QDIMRIGNFEIPSRAY-----VGRFNFKgvdqGKRVGELSGGE 449
Cdd:PRK09984 84 srantgyiFQQF--NLVNRLSVLENVLIGalgstpfwRTCFSWFTREQKQRALqaltrVGMVHFA----HQRVSTLSGGQ 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 739061588 450 RGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENAL 487
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTL 195
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-218 |
3.34e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.95 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID-TDIEGEARPQPGIKIGYLPQEPKLN--PEHT 85
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGslppdsgsilIDgKDVTKLPEYKRAKYIGRVFQDPMMGtaPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 86 vreaVEE--AVSELKNALNRLdevyaayadpdadfdKLAKEQGQLEAIIQ--SHDGHNLENQLeraaealrlpewDAKIE 161
Cdd:COG1101 99 ----IEEnlALAYRRGKRRGL---------------RRGLTKKRRELFREllATLGLGLENRL------------DTKVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739061588 162 KLSGGERRRVAicrLL---LEKPDMLLLDEPTNHLD---AESVAWL-ERFLHDYEGTVVAITHD 218
Cdd:COG1101 148 LLSGGQRQALS---LLmatLTKPKLLLLDEHTAALDpktAALVLELtEKIVEENNLTTLMVTHN 208
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-239 |
3.50e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.85 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 8 MLRVGKI---VPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTL-------LR------IMAGIDTdieGEARPQPGIK- 70
Cdd:PRK13644 1 MIRLENVsysYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLalhlnglLRpqkgkvLVSGIDT---GDFSKLQGIRk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 71 -IGYLPQepklNPE-HTVREAVEEAVSelknalnrldevyaayadpdadfdkLAKEQGQLEAIiqshdghNLENQLERAA 148
Cdd:PRK13644 78 lVGIVFQ----NPEtQFVGRTVEEDLA-------------------------FGPENLCLPPI-------EIRKRVDRAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 149 EALRLPEWDAKIEK-LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAES-VAWLERF--LHDYEGTVVAITHDRYFLdN 224
Cdd:PRK13644 122 AEIGLEKYRHRSPKtLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIkkLHEKGKTIVYITHNLEEL-H 200
|
250
....*....|....*....
gi 739061588 225 VAGWILELDRG----EGIP 239
Cdd:PRK13644 201 DADRIIVMDRGkivlEGEP 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
324-512 |
3.80e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.55 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQE--QPDSGTLVL-GDTVKLASVDQ------- 393
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLdGEDILELSPDEraragif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 --FRDSMddsktvweEVSGgqdiMRIGNF-----------EIPSRAYVGRFNFK----GVDQG--KR---VGeLSGGERG 451
Cdd:COG0396 81 laFQYPV--------EIPG----VSVSNFlrtalnarrgeELSAREFLKLLKEKmkelGLDEDflDRyvnEG-FSGGEKK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 452 RLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEF--PGCAM-VISHDRWFLDRIA---THII 512
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrsPDRGIlIITHYQRILDYIKpdfVHVL 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-218 |
3.99e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.94 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIGYlPQEPKLNPEHTVREAVEeavselknal 101
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIK-GEPIKY-DKKSLLEVRKTVGIVFQ---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 102 NRLDEVYAAYADPDADFD----KLAKEQgqleaiiqshdghnLENQLERAAEALRLPEWDAKI-EKLSGGERRRVAICRL 176
Cdd:PRK13639 86 NPDDQLFAPTVEEDVAFGplnlGLSKEE--------------VEKRVKEALKAVGMEGFENKPpHHLSGGQKKRVAIAGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 739061588 177 LLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EG-TVVAITHD 218
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGiTIIISTHD 196
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-195 |
4.11e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 63.73 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI------DTDIEGEARPQPGIKIGYLPQEPKLNPEHTVREAVEE 92
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFlapssgEITLDGVPVTGPGADRGVVFQKDALLPWLNVLDNVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 93 AvseLKnalnrldevyaayadpdadFDKLAKEQgqleaiiqshdghnlenQLERAAEALRLPEW----DAKIEKLSGGER 168
Cdd:COG4525 100 G---LR-------------------LRGVPKAE-----------------RRARAEELLALVGLadfaRRRIWQLSGGMR 140
|
170 180
....*....|....*....|....*..
gi 739061588 169 RRVAICRLLLEKPDMLLLDEPTNHLDA 195
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
314-489 |
4.51e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.10 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 314 PPGPRLGDKVLEINNLTKSYGDR-----VLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTV-- 386
Cdd:PRK13631 12 VPNPLSDDIILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYig 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 387 ------------------------KLAS-VDQFRDSMDDSKTVWEEVSGGQDIMRIGNFEIPSRA--YVGRFNFKGVDQG 439
Cdd:PRK13631 92 dkknnhelitnpyskkiknfkelrRRVSmVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAkfYLNKMGLDDSYLE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 739061588 440 KRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALLE 489
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-218 |
4.90e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.52 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdTDIEGEARPQPGIkigylpqepklnpehtvrEAVEEAVSELKNA 100
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRV------------------EFFNQNIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 101 LNRLD-EVYAAYADPD----ADFDKLAKEQgqleAIIQSHDGHNLENQLERAAEALRLpeWDA---KIEK----LSGGER 168
Cdd:PRK14258 83 LNRLRrQVSMVHPKPNlfpmSVYDNVAYGV----KIVGWRPKLEIDDIVESALKDADL--WDEikhKIHKsaldLSGGQQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 739061588 169 RRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY----EGTVVAITHD 218
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHN 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
331-508 |
5.39e-11 |
|
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: 63.43 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 331 KSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTVKLASVDQFRD------SMD---- 399
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKvLIDGQDIAAMSRKELRElrrkkiSMVfqsf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 400 ---DSKTVWEEVSGGQDIMRIGNFEIPSRA-----YVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEP 471
Cdd:cd03294 112 allPHRTVLENVAFGLEVQGVPRAEREERAaealeLVGLEGWE----HKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 739061588 472 TNDLDVETLRALENALL----EFPGCAMVISHDrwfL-------DRIA 508
Cdd:cd03294 188 FSALDPLIRREMQDELLrlqaELQKTIVFITHD---LdealrlgDRIA 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-477 |
6.33e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 1 MAQYVYSMLRVGKIVPPKrHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI------DTDIEGEARP--------Q 66
Cdd:PRK09700 1 MATPYISMAGIGKSFGPV-HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIheptkgTITINNINYNkldhklaaQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 67 PGIKIGYlpQEPKLNPEHTVREAVeeavselknALNRLdEVYAAYADPDADFDKLAkeqgqleaiiqshdghnlenqlER 146
Cdd:PRK09700 80 LGIGIIY--QELSVIDELTVLENL---------YIGRH-LTKKVCGVNIIDWREMR----------------------VR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 147 AAEAL-RLP---EWDAKIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGT-VVAITH-- 217
Cdd:PRK09700 126 AAMMLlRVGlkvDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLrkEGTaIVYISHkl 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 218 -------DRYfldnvagwileldrgeGIPWEGNYSSWLEQKDARLEQeaateaarhksiqkelewIRQNPKGRQAKGKar 290
Cdd:PRK09700 206 aeirricDRY----------------TVMKDGSSVCSGMVSDVSNDD------------------IVRLMVGRELQNR-- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 291 larfeelnsvdYQKRNETSelfippGPRLGDKVLEINNLTKSygDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMIS 370
Cdd:PRK09700 250 -----------FNAMKENV------SNLAHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLF 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 371 GQEQPDSGTLVL-GDTVKLAS-VDQFRDSM---DDSKtvweevsggQDIMRIGNFEIPSRAYVGRF----NFKG------ 435
Cdd:PRK09700 311 GVDKRAGGEIRLnGKDISPRSpLDAVKKGMayiTESR---------RDNGFFPNFSIAQNMAISRSlkdgGYKGamglfh 381
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 436 ---------------------VDQGkrVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDV 477
Cdd:PRK09700 382 evdeqrtaenqrellalkchsVNQN--ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-223 |
7.86e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.90 E-value: 7.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGidtdiegEARPQPGIKIGYLPQEPkLNPEHTVREAV--EEAVS 95
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-------ALKGTPVAGCVDVPDNQ-FGREASLIDAIgrKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 96 ELKNALNRldevyAAYADPdadfdklakeqgqleaiiqshdghnlenqleraaealrlPEWDAKIEKLSGGERRRVAICR 175
Cdd:COG2401 114 DAVELLNA-----VGLSDA---------------------------------------VLWLRRFKELSTGQKFRFRLAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739061588 176 LLLEKPDMLLLDEPTNHLD---AESVAW-LERFLHDYEGTVVAITHDRYFLD 223
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDrqtAKRVARnLQKLARRAGITLVVATHHYDVID 201
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-236 |
8.01e-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: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKST----LLRIMAG------IDT-DIEGEARPQPGIKIGYLPQEPKLNpEHTVREA 89
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVELssgsilIDGvDISKIGLHDLRSRISIIPQDPVLF-SGTIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 90 V----EEAVSELKNALnrldevyaayadpdadfdklakEQGQLEAIIQSHDGHNlenqleraaealrlpewDAKIEK--- 162
Cdd:cd03244 98 LdpfgEYSDEELWQAL----------------------ERVGLKEFVESLPGGL-----------------DTVVEEgge 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 163 -LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITH--------DRyfldnvagwILE 231
Cdd:cd03244 139 nLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAHrldtiidsDR---------ILV 209
|
....*
gi 739061588 232 LDRGE 236
Cdd:cd03244 210 LDKGR 214
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
21-218 |
8.66e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 62.41 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE----------------ARpqpgiKIGYLPQEPKLNPEH 84
Cdd:COG4604 16 VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEvlvdgldvattpsrelAK-----RLAILRQENHINSRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 TVREAVEeavselknalnrldevyaayadpdadFDKLAKEQGQL----EAIIqshdghnlenqlERAAEALRLPEW-DAK 159
Cdd:COG4604 91 TVRELVA--------------------------FGRFPYSKGRLtaedREII------------DEAIAYLDLEDLaDRY 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 160 IEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLD-AESVAW---LERFLHDYEGTVVAITHD 218
Cdd:COG4604 133 LDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmKHSVQMmklLRRLADELGKTVVIVLHD 195
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
22-236 |
8.76e-11 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 62.71 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVL-GLNGAGKSTLLRIMAGIDTDIEGEARPQPGIKIgyLPQEPKLNPEHTV-------REAVEEA 93
Cdd:COG3950 14 FEDLEIDFDNPPRLTVLvGENGSGKTTLLEAIALALSGLLSRLDDVKFRKL--LIRNGEFGDSAKLilyygtsRLLLDGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 94 VSELKNALNRLDEVYAAYA---DPDADFDKLAKEQGQLEAIIQSHDGHNLENQLERAAEALR--LPEWDA---------- 158
Cdd:COG3950 92 LKKLERLKEEYFSRLDGYDsllDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVREALNklLPDFKDiridrdpgrl 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 159 ----------KIEKLSGGERRRVAIC-----RLLLEKPDM---------LLLDEPTNHLdaeSVAWLERFLHDYEGT--- 211
Cdd:COG3950 172 vildkngeelPLNQLSDGERSLLALVgdlarRLAELNPALenplegegiVLIDEIDLHL---HPKWQRRILPDLRKIfpn 248
|
250 260
....*....|....*....|....*...
gi 739061588 212 --VVAITHDRYFLDNV-AGWILELDRGE 236
Cdd:COG3950 249 iqFIVTTHSPLILSSLeDEEVIVLERDE 276
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-225 |
1.05e-10 |
|
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: 61.39 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGID----------------TDIEGEARPQPGIKIGYlpQEPkln 81
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyevtegeilfkgediTDLPPEERARLGIFLAF--QYP--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 pehtvreaveEAVSELKNAlNRLDEVyaayadpdadfdklakeqgqleaiiqshdghnleNqleraaealrlpewdakiE 161
Cdd:cd03217 87 ----------PEIPGVKNA-DFLRYV----------------------------------N------------------E 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDYEGTVVAITHDRYFLDNV 225
Cdd:cd03217 104 GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVinkLREEGKSVLIITHYQRLLDYI 170
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-236 |
1.09e-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: 61.27 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 9 LRVGKIVPPkrhILKNISLSFFPGAKIGVLGLNGAGKSTL----LRIMAGIDTDIEGEARPQPGI-------KIGYLPQE 77
Cdd:cd03369 14 VRYAPDLPP---VLKNVSFKVKAGEKIGIVGRTGAGKSTLilalFRFLEAEEGKIEIDGIDISTIpledlrsSLTIIPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 78 PKLnpehtvreaveeAVSELKNALNRLDEvyaaYADpdadfdklakeqgqleaiiqshdghnlenqlERAAEALRLPEWD 157
Cdd:cd03369 91 PTL------------FSGTIRSNLDPFDE----YSD-------------------------------EEIYGALRVSEGG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 158 akiEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHD--YEGTVVAITHDryfLDNVAGW--ILELD 233
Cdd:cd03369 124 ---LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREefTNSTILTIAHR---LRTIIDYdkILVMD 197
|
...
gi 739061588 234 RGE 236
Cdd:cd03369 198 AGE 200
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
21-194 |
1.15e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.43 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIGYLPQEPK----------LNPEHTVREAV 90
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-GQDITHVPAENRhvntvfqsyaLFPHMTVFENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 91 eeavselknalnrldevyaAYAdpdadfdklAKEQGQLEAIIQshdghnlenqlERAAEALRLPEWDA----KIEKLSGG 166
Cdd:PRK09452 108 -------------------AFG---------LRMQKTPAAEIT-----------PRVMEALRMVQLEEfaqrKPHQLSGG 148
|
170 180
....*....|....*....|....*...
gi 739061588 167 ERRRVAICRLLLEKPDMLLLDEPTNHLD 194
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-218 |
1.23e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.42 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEArpqpgikigylpqepKLNPEHTVREaveeavselkNAL 101
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV---------------KIDGELLTAE----------NVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 102 NRLDEVYAAYADPDADFDKLAKEQGQleAIIQSHDGHNLENQLERAAEAL-RLPEWDAKIE---KLSGGERRRVAICRLL 177
Cdd:PRK13642 78 NLRRKIGMVFQNPDNQFVGATVEDDV--AFGMENQGIPREEMIKRVDEALlAVNMLDFKTRepaRLSGGQKQRVAVAGII 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 739061588 178 LEKPDMLLLDEPTNHLDAESVAWLERFLHD----YEGTVVAITHD 218
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEikekYQLTVLSITHD 200
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-235 |
1.33e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.43 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDtdiegeaRPQPGiKIGYLPQEpklnpehtvreaveeaVSELK 98
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIE-------RPSAG-KIWFSGHD----------------ITRLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 99 NA----LNRldEVYAAYADPDADFDKLAKEQGQLEAIIQSHDGHNLENQLERAAEALRLPEWDAKIE-KLSGGERRRVAI 173
Cdd:PRK10908 71 NRevpfLRR--QIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPiQLSGGEQQRVGI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 174 CRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG---TVVAITHDRYFLDNVAGWILELDRG 235
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-241 |
1.45e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.08 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgikIGYLPQEPKLNPEHTVREaveeavselknal 101
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGE--------IFYNNQAITDDNFEKLRK------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 102 nrldEVYAAYADPDADFdklakeqgqLEAIIQSHDGHNLENQL-------ERAAEALR----LPEWDAKIEKLSGGERRR 170
Cdd:PRK13648 84 ----HIGIVFQNPDNQF---------VGSIVKYDVAFGLENHAvpydemhRRVSEALKqvdmLERADYEPNALSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 171 VAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLH----DYEGTVVAITHDryfLDNVAG--WILELDRG----EGIPW 240
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRkvksEHNITIISITHD---LSEAMEadHVIVMNKGtvykEGTPT 227
|
.
gi 739061588 241 E 241
Cdd:PRK13648 228 E 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
324-501 |
1.53e-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: 64.16 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSY--GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTL----FRMIS--GQEQPDSgtlVLGDTVKLAS----- 390
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLSteGEIQIDG---VSWNSVTLQTwrkaf 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 391 --VDQ--------FRDSMDDSKTvWEEvsggQDIMRIGNfEIPSRAYV----GRFNFKGVDQGKRvgeLSGGERGRLHLA 456
Cdd:TIGR01271 1295 gvIPQkvfifsgtFRKNLDPYEQ-WSD----EEIWKVAE-EVGLKSVIeqfpDKLDFVLVDGGYV---LSNGHKQLMCLA 1365
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 739061588 457 KLLQVGGNMLLLDEPTNDLDVETLRALENALLE-FPGCAMVISHDR 501
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQsFSNCTVILSEHR 1411
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
17-218 |
1.82e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 61.64 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDT------DIEGEARPQPGIKIGYLPQEPKLNPEHTVREAV 90
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 91 EEAVselknalnrldevyaayadpdadfdKLAkeqgqleaiiqshdGHNLENQLERAAEALR---LPEWDAK-IEKLSGG 166
Cdd:PRK11248 92 AFGL-------------------------QLA--------------GVEKMQRLEIAHQMLKkvgLEGAEKRyIWQLSGG 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 167 ERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFL----HDYEGTVVAITHD 218
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHD 188
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-217 |
1.82e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.59 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----DTDIEGEAR------PQPGI-------KIGYLPQEPk 79
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILldgediYDPDVdvvelrrRVGMVFQKP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 80 lNP-EHTVREAVeeavselknalnrldevyaAYAdpdadfdklAKEQG-----QLEAIIqshdghnlENQLERAAealrL 153
Cdd:COG1117 102 -NPfPKSIYDNV-------------------AYG---------LRLHGiksksELDEIV--------EESLRKAA----L 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 154 peWD---AKIEK----LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLH----DYegTVVAITH 217
Cdd:COG1117 141 --WDevkDRLKKsalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILelkkDY--TIVIVTH 211
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-217 |
1.83e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 64.10 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 15 VPPKR-HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD--IEGEARPQPGIKI--------GYLPQEPKLNPE 83
Cdd:PLN03140 888 VTEDRlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKqetfarisGYCEQNDIHSPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 84 HTVREAVeeavselknalnrldeVYAAyadpdadFDKLAKEQGQLEAII---QSHDGHNLENqLERAAEALrlpewdAKI 160
Cdd:PLN03140 968 VTVRESL----------------IYSA-------FLRLPKEVSKEEKMMfvdEVMELVELDN-LKDAIVGL------PGV 1017
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 161 EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLH---DYEGTVVAITH 217
Cdd:PLN03140 1018 TGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRntvDTGRTVVCTIH 1077
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
321-476 |
1.84e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 61.69 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSY-GDRVL-IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDtvKLASVDQFRDSM 398
Cdd:PRK13648 5 NSIIVFKNVSFQYqSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN--QAITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 399 DD-------------SKTVWEEVSGGqdimrIGNFEIPSRAYVGRFN--FKGVDQGKRVGE----LSGGERGRLHLAKLL 459
Cdd:PRK13648 83 KHigivfqnpdnqfvGSIVKYDVAFG-----LENHAVPYDEMHRRVSeaLKQVDMLERADYepnaLSGGQKQRVAIAGVL 157
|
170
....*....|....*..
gi 739061588 460 QVGGNMLLLDEPTNDLD 476
Cdd:PRK13648 158 ALNPSVIILDEATSMLD 174
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-217 |
2.00e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.97 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 13 KIVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD--IEGEARPQPGIK--------IGYLPQEPKLNP 82
Cdd:TIGR00956 770 KIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgvITGGDRLVNGRPldssfqrsIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 83 EHTVREAVEeavselknalnrldevYAAYADPDADFDKLAKEQgQLEAIIQShdghnLEnqLERAAEAL-RLPEwdakiE 161
Cdd:TIGR00956 850 TSTVRESLR----------------FSAYLRQPKSVSKSEKME-YVEEVIKL-----LE--MESYADAVvGVPG-----E 900
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLL-LDEPTNHLDAESvAW----LERFLHDYEGTVVAITH 217
Cdd:TIGR00956 901 GLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT-AWsickLMRKLADHGQAILCTIH 960
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
323-488 |
2.26e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 63.88 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYG--DRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVD-------- 392
Cdd:TIGR01257 1937 ILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISdvhqnmgy 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 393 --QFrDSMDDSKT------VWEEVSG--GQDIMRIGNFEIPS---RAYVGRFnfkgvdqgkrVGELSGGERGRLHLAKLL 459
Cdd:TIGR01257 2017 cpQF-DAIDDLLTgrehlyLYARLRGvpAEEIEKVANWSIQSlglSLYADRL----------AGTYSGGNKRKLSTAIAL 2085
|
170 180
....*....|....*....|....*....
gi 739061588 460 QVGGNMLLLDEPTNDLDVETLRALENALL 488
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-190 |
2.32e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.11 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR----------PQPGIK--IGYLPQEPK---LNPE 83
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvrirsPRDAIRagIAYVPEDRKgegLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 84 HTVREaveeavselkN-ALNRLDEVYAAYadpdadFDKLAKEQGQLEAIIQSHDghnlenqleraaeaLRLPEWDAKIEK 162
Cdd:COG1129 345 LSIRE----------NiTLASLDRLSRGG------LLDRRRERALAEEYIKRLR--------------IKTPSPEQPVGN 394
|
170 180
....*....|....*....|....*...
gi 739061588 163 LSGGERRRVAICRLLLEKPDMLLLDEPT 190
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
339-522 |
2.58e-10 |
|
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: 59.64 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMI---SGQEQPDSGTLVLGDTvKLASVDQFRDSMDdsktvweevsggqdiM 415
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGlyaSGKARLISFLPKFSRN-KLIFIDQLQFLID---------------V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 416 RIGNFEIpsrayvgrfnfkgvdqGKRVGELSGGERGRLHLAKLLQVG--GNMLLLDEPTNDLDVETLRALENALLEFPGC 493
Cdd:cd03238 75 GLGYLTL----------------GQKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLLEVIKGLIDL 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 739061588 494 A---MVISHDRWFLDRiATHIIDY-----QDEGKVEF 522
Cdd:cd03238 139 GntvILIEHNLDVLSS-ADWIIDFgpgsgKSGGKVVF 174
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-217 |
2.65e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.20 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE----ARPQPGI-------KIGYLPQEPKLNpEHT 85
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQvlldGVPLVQYdhhylhrQVALVGQEPVLF-SGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 86 VREAVeeavselknalnrldeVYAAYADPDADFDKLAKEQGQLEAIIQSHDGHNlenqleraaealrlPEWDAKIEKLSG 165
Cdd:TIGR00958 571 VRENI----------------AYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYD--------------TEVGEKGSQLSG 620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 739061588 166 GERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITH 217
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
20-218 |
2.76e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 62.02 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------ID-TDIEG-------EARPqpgiKIGYLPQEPKLN 81
Cdd:COG1135 19 TALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLlerptsgsvlVDgVDLTAlserelrAARR----KIGMIFQHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 PEHTVREAVeeavselknalnrldevyaAYAdpdadfdklakeqgqLEaiiqsHDGHNLENQLERAAEALRLPEWDAKIE 161
Cdd:COG1135 95 SSRTVAENV-------------------ALP---------------LE-----IAGVPKAEIRKRVAELLELVGLSDKAD 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 162 K----LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDYEG-TVVAITHD 218
Cdd:COG1135 136 AypsqLSGGQKQRVGIARALANNPKVLLCDEATSALDPEttrSILDLLKDINRELGlTIVLITHE 200
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-218 |
2.80e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.64 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEAR-----PQP---------GIKIGylpQEPKLNPEHTVR 87
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvPFKrrkefarriGVVFG---QRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 88 EAVEeavselknaLNRldevyAAYADPDADFDKlakeqgqleaiiqshdghnlenQLERAAEALRL-PEWDAKIEKLSGG 166
Cdd:COG4586 115 DSFR---------LLK-----AIYRIPDAEYKK----------------------RLDELVELLDLgELLDTPVRQLSLG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 167 ERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EG-TVVAITHD 218
Cdd:COG4586 159 QRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnreRGtTILLTSHD 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-490 |
2.97e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.01 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDtVKLASVDQFRDSMDDSK- 402
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGE-VRLFGRNIYSPDVDPIEv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 403 -----------------TVWEEVSGGQDIMRI--GNFEIPSRAyvgRFNFKGVDQGKRV--------GELSGGERGRLHL 455
Cdd:PRK14267 84 rrevgmvfqypnpfphlTIYDNVAIGVKLNGLvkSKKELDERV---EWALKKAALWDEVkdrlndypSNLSGGQRQRLVI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 739061588 456 AKLLQVGGNMLLLDEPTNDLDVETLRALENALLEF 490
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL 195
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-226 |
3.39e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.90 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI------DTDIEGEarpqpgikigylpqepklnpehtvrEAVEE 92
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLleaesgQIIIDGD-------------------------LLTEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 93 AVSELKnalnrlDEVYAAYADPDADFdklakeqgqLEAIIQSHDGHNLENQ-------LERAAEALRLPEW----DAKIE 161
Cdd:PRK13650 75 NVWDIR------HKIGMVFQNPDNQF---------VGATVEDDVAFGLENKgipheemKERVNEALELVGMqdfkEREPA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHDryfLDNVA 226
Cdd:PRK13650 140 RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGrlelIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-218 |
3.57e-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: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 2 AQYVYSMLRVGKivpPKRHILK---------NISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDI-- 59
Cdd:cd03294 14 PQKAFKLLAKGK---SKEEILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLieptsgkvlidGQDIaa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 60 --EGEARPQPGIKIGYLPQEPKLNPEHTVREAVeeavselknalnrldevyaAYAdpdadfdklakeqgqLEaiIQshdG 137
Cdd:cd03294 91 msRKELRELRRKKISMVFQSFALLPHRTVLENV-------------------AFG---------------LE--VQ---G 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 138 HNLENQLERAAEALR---LPEW-DAKIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYE 209
Cdd:cd03294 132 VPRAEREERAAEALElvgLEGWeHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQ 211
|
....*....
gi 739061588 210 GTVVAITHD 218
Cdd:cd03294 212 KTIVFITHD 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
322-384 |
4.00e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.39 E-value: 4.00e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 322 KVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGD 384
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG 66
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
323-485 |
4.45e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.43 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSY---GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLgDTV------------K 387
Cdd:TIGR00958 478 LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-DGVplvqydhhylhrQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 388 LASVDQ----FRDSMDDS------KTVWEEV------SGGQDImrIGNFEipsrayvgrfnfKGVDQ--GKRVGELSGGE 449
Cdd:TIGR00958 557 VALVGQepvlFSGSVRENiaygltDTPDEEImaaakaANAHDF--IMEFP------------NGYDTevGEKGSQLSGGQ 622
|
170 180 190
....*....|....*....|....*....|....*.
gi 739061588 450 RGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALEN 485
Cdd:TIGR00958 623 KQRIAIARALVRKPRVLILDEATSALDAECEQLLQE 658
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
323-499 |
5.12e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQeQPdSGT-----LVLGDTVKLASVdqfRDS 397
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YP-HGTyegeiIFEGEELQASNI---RDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 398 -------------MDDSKTVWEEVSGGQDIMRIG--NF-EIPSRAY--VGRFNFkGVDQGKRVGELSGGERGRLHLAKLL 459
Cdd:PRK13549 80 eragiaiihqelaLVKELSVLENIFLGNEITPGGimDYdAMYLRAQklLAQLKL-DINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739061588 460 QVGGNMLLLDEPTNDLDVETLRALENAL--LEFPGCAMV-ISH 499
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIrdLKAHGIACIyISH 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
323-499 |
5.69e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSY-GDRVLiDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLV-LGDTVKLASVdqfRDSmdd 400
Cdd:PRK10762 4 LLQLKGIDKAFpGVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGP---KSS--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 401 sktvwEEVSGG---QDIMRIGNFEIPSRAYVGR---FNFKGVDQGK--------------------RVGELSGGERGRLH 454
Cdd:PRK10762 77 -----QEAGIGiihQELNLIPQLTIAENIFLGRefvNRFGRIDWKKmyaeadkllarlnlrfssdkLVGELSIGEQQMVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 739061588 455 LAKLLQVGGNMLLLDEPTNDL-DVETlRALENAL--LEFPGCAMV-ISH 499
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALtDTET-ESLFRVIreLKSQGRGIVyISH 199
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
321-509 |
5.86e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.49 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSY---GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTV---------- 386
Cdd:PRK13642 2 NKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLtaenvwnlrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 387 KLASVDQFRDSMDDSKTVWEEVSGGQDIMRIGNFEIPSRAYVGRFNFKGVD-QGKRVGELSGGERGRLHLAKLLQVGGNM 465
Cdd:PRK13642 82 KIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDfKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 739061588 466 LLLDEPTNDLD----VETLRALENALLEFPGCAMVISHDrwfLDRIAT 509
Cdd:PRK13642 162 IILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD---LDEAAS 206
|
|
| 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 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----DTDIEGEArpqpgikigYLP-QEPKLNPEHTVREAVEeAV 94
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEV---------YLDgQDIFKMDVIELRRRVQ-MV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 95 SELKNALNRLDEVYAAYADPDadFDKLAKEQGQLEaiiqshdghnlenqlERAAEALRLPE-WD-------AKIEKLSGG 166
Cdd:PRK14247 88 FQIPNPIPNLSIFENVALGLK--LNRLVKSKKELQ---------------ERVRWALEKAQlWDevkdrldAPAGKLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 167 ERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHDRYFLDNVAGWILELDRGEGIPW 240
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELkkDMTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-218 |
6.55e-10 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 59.62 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 10 RVGKIVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-------ARPQPGI----KIGYLPQEP 78
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEifidgedIREQDPVelrrKIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 79 KLNPEHTVREAVEeAVSELknalnrldevyaayadpdadfdklakeQGQLEAIIQshdghnlenqlERAAEALRLPEWDA 158
Cdd:cd03295 85 GLFPHMTVEENIA-LVPKL---------------------------LKWPKEKIR-----------ERADELLALVGLDP 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 159 KI------EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDA-------ESVAWLERFLHDyegTVVAITHD 218
Cdd:cd03295 126 AEfadrypHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPitrdqlqEEFKRLQQELGK---TIVFVTHD 195
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-218 |
7.91e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 25 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdTDIEGEAR---------PQPGIKI--GYLPQE--PKLN---------- 81
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQfagqpleawSAAELARhrAYLSQQqtPPFAmpvfqyltlh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 -PEHTVREAVEEAVSELKNALNrLDevyaayadpdadfDKLAKEQGQLeaiiqshdghnlenqleraaealrlpewdaki 160
Cdd:PRK03695 94 qPDKTRTEAVASALNEVAEALG-LD-------------DKLGRSVNQL-------------------------------- 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739061588 161 eklSGGERRRVAICRLLLE-----KPD--MLLLDEPTNHLDAESVAWLERFLHDYE---GTVVAITHD 218
Cdd:PRK03695 128 ---SGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-218 |
9.78e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 61.28 E-value: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARpQPGIKIGYLPQE--PKLNPEHT----VREAVEEAV 94
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYR-VAGQDVATLDADalAQLRREHFgfifQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 95 SELKNAlnrldEVYAAYADpdadfdkLAKEQgqleaiiqshdghnlenQLERAAEALRLPEWDAKIE----KLSGGERRR 170
Cdd:PRK10535 102 TAAQNV-----EVPAVYAG-------LERKQ-----------------RLLRAQELLQRLGLEDRVEyqpsQLSGGQQQR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 739061588 171 VAICRLLLEKPDMLLLDEPTNHLDAES---VAWLERFLHDYEGTVVAITHD 218
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
324-386 |
1.10e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 60.24 E-value: 1.10e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739061588 324 LEINNLTKSY-GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTV 386
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV 67
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
320-511 |
1.15e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.29 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 320 GDKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQ-EQPDSGTLVLGDTVKLASvDQFR-DS 397
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSKIKVDGKVLYFGK-DIFQiDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 398 MDDSK---TVWEEVSGGQDIMRIGNFEIPSRAY----------VGRFNFKGVDQGKRV--------GELSGGERGRLHLA 456
Cdd:PRK14246 86 IKLRKevgMVFQQPNPFPHLSIYDNIAYPLKSHgikekreikkIVEECLRKVGLWKEVydrlnspaSQLSGGQQQRLTIA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 457 KLLQVGGNMLLLDEPTNDLDVETLRALENALLEFPG--CAMVISHDRWFLDRIATHI 511
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV 222
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
329-517 |
1.19e-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: 57.58 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 329 LTKSYGD-RVLIDDLSFSipKGAIVGIIGPNGAGKSTLFRMISGQEQPdsgtlvlgdtvklasvdqfrdsmDDSKTVWEE 407
Cdd:cd03222 6 CVKRYGVfFLLVELGVVK--EGEVIGIVGPNGTGKTTAVKILAGQLIP-----------------------NGDNDEWDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 408 VSGGQDIMRIgnfeipsrayvgrfnfkgvdqgkrvgELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVE----TLRAL 483
Cdd:cd03222 61 ITPVYKPQYI--------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAI 114
|
170 180 190
....*....|....*....|....*....|....
gi 739061588 484 ENALLEFPGCAMVISHDRWFLDRIATHIIDYQDE 517
Cdd:cd03222 115 RRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
324-517 |
1.25e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.80 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSY--GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTV---KLAS------- 390
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdGHDLrdyTLASlrnqval 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 391 VDQ----FRDSMDDSKT-VWEEVSGGQDIMRIGNFeipsrAYVGRFnFKGVDQG--KRVGE----LSGGERGRLHLAKLL 459
Cdd:PRK11176 422 VSQnvhlFNDTIANNIAyARTEQYSREQIEEAARM-----AYAMDF-INKMDNGldTVIGEngvlLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 460 QVGGNMLLLDEPTNDLDVETLRALENALLEFPG--CAMVISHdrwfldRIAThiIDYQDE 517
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH------RLST--IEKADE 547
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-246 |
1.26e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.63 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---------ID----TDIEGEARPQpgiKIGYLPQEPKLnPEHTVR 87
Cdd:PRK11174 365 LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkINgielRELDPESWRK---HLSWVGQNPQL-PHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 88 EAVeeavselknalnrldevyaAYADPDADFDKL--AKEQGQL-EAIIQSHDGHNLENQlERAAealrlpewdakieKLS 164
Cdd:PRK11174 441 DNV-------------------LLGNPDASDEQLqqALENAWVsEFLPLLPQGLDTPIG-DQAA-------------GLS 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 165 GGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHDryfLDNVAGW--ILELDRGEgIPW 240
Cdd:PRK11174 488 VGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQ---LEDLAQWdqIWVMQDGQ-IVQ 563
|
....*.
gi 739061588 241 EGNYSS 246
Cdd:PRK11174 564 QGDYAE 569
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-216 |
1.39e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.20 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQPG------------IKIGYLPQEPKLNpEHTVRE 88
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrSKIGVVSQDPLLF-SNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 89 AVEEAVSELKNaLNRLDEVY-----AAYADPDADFDKLAKEQGQLEAIIQSHDGHNL-----ENQLERAAEALR------ 152
Cdd:PTZ00265 479 NIKYSLYSLKD-LEALSNYYnedgnDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELiemrkNYQTIKDSEVVDvskkvl 557
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 153 -------LPE-WDAKI----EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAIT 216
Cdd:PTZ00265 558 ihdfvsaLPDkYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-241 |
1.55e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.48 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLrimagidTDIEGEARPQPG-IKIGYLPQEPKLNPEHTVREAVEEAVSELKN 99
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLV-------THFNGLIKSKYGtIQVGDIYIGDKKNNHELITNPYSKKIKNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 100 ALNRLDEV-----YAAYAD---PDADFDKLAKEQGQLEAiiqshdgHNLEN-QLERAAeaLRLPEWDAKIEKLSGGERRR 170
Cdd:PRK13631 114 LRRRVSMVfqfpeYQLFKDtieKDIMFGPVALGVKKSEA-------KKLAKfYLNKMG--LDDSYLERSPFGLSGGQKRR 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739061588 171 VAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG---TVVAITHDRYFLDNVAGWILELDRGE----GIPWE 241
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMDKGKilktGTPYE 262
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
324-476 |
1.67e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 60.51 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSY----GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL-VLGDTVklASVDQfrdsm 398
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYrVAGQDV--ATLDA----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 399 DDSKTVWEE--------------VSGGQdimrigNFEIP--------------SRAYVGRFNFkgvdqGKRV----GELS 446
Cdd:PRK10535 78 DALAQLRREhfgfifqryhllshLTAAQ------NVEVPavyaglerkqrllrAQELLQRLGL-----EDRVeyqpSQLS 146
|
170 180 190
....*....|....*....|....*....|
gi 739061588 447 GGERGRLHLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:PRK10535 147 GGQQQRVSIARALMNGGQVILADEPTGALD 176
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
336-500 |
1.86e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 336 RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGqEQPDS----GTLVLGDTV----KLASVDQFRdsMDDSKTVWEE 407
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprGARVTGDVTlngePLAAIDAPR--LARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 408 VS------GGQDIMRIGNF--------------EIPSRAyVGRFNFKGVDqGKRVGELSGGERGRLHLAKLL-------- 459
Cdd:PRK13547 91 AAqpafafSAREIVLLGRYpharragalthrdgEIAWQA-LALAGATALV-GRDVTTLSGGELARVQFARVLaqlwpphd 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 739061588 460 -QVGGNMLLLDEPTNDLD-------VETLRALENallEFPGCAMVISHD 500
Cdd:PRK13547 169 aAQPPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVHD 214
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
324-520 |
1.96e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.54 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSY---------GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDT--VKLASVD 392
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 393 Q----------FRDS---MDDSKTVWEEVSggqDIMR-IGNFEIPSRAYVGRFNFKGVD-----QGKRVGELSGGERGRL 453
Cdd:PRK10419 84 RkafrrdiqmvFQDSisaVNPRKTVREIIR---EPLRhLLSLDKAERLARASEMLRAVDlddsvLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 454 HLAKLLQVGGNMLLLDEPTNDLDV----ETLRALENALLEFPGCAMVISHDRWFLDRIATHIIdYQDEGKV 520
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVM-VMDNGQI 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-216 |
2.12e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.49 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 7 SMLRVGKIVPPKRH--ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdtdIEGEARPQPGIKI-GYLPQ-EPKLNP 82
Cdd:PRK09984 3 TIIRVEKLAKTFNQhqALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGSHIELlGRTVQrEGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 83 EHTVREAVEEAVSELKNALNRLDE-----VYAAYADP--DADFDKLAKEQGQ--LEAIIQ---SHDGHNlenqleraaea 150
Cdd:PRK09984 80 DIRKSRANTGYIFQQFNLVNRLSVlenvlIGALGSTPfwRTCFSWFTREQKQraLQALTRvgmVHFAHQ----------- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 151 lrlpewdaKIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAIT 216
Cdd:PRK09984 149 --------RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqnDGITVVVT 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
344-511 |
2.22e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.18 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 344 FSIP---KGAIVGIIGPNGAGKSTLFRMISGQEQPDsgtlvLGDTVKLASVDQ----FRDSmdDSKTVWEEVSGG----- 411
Cdd:COG1245 91 YGLPvpkKGKVTGILGPNGIGKSTALKILSGELKPN-----LGDYDEEPSWDEvlkrFRGT--ELQDYFKKLANGeikva 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 412 ---QDIMRIGNF------EIPSRA--------YVGRFNFKGV-DQgkRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTN 473
Cdd:COG1245 164 hkpQYVDLIPKVfkgtvrELLEKVdergkldeLAEKLGLENIlDR--DISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 739061588 474 DLDV-ETLRA--LENALLEFPGCAMVISHDRWFLDRIATHI 511
Cdd:COG1245 242 YLDIyQRLNVarLIRELAEEGKYVLVVEHDLAILDYLADYV 282
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
341-476 |
2.30e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.49 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 341 DLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTV---------------KLASVDQFRDSMDDSKTVW 405
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkplrkKVGIVFQFPEHQLFEETVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 406 EEVSGGQdiMRIGNFEIPSRAyvgrfnfKGVDQGKRVG-----------ELSGGERGRLHLAKLLQVGGNMLLLDEPTND 474
Cdd:PRK13634 105 KDICFGP--MNFGVSEEDAKQ-------KAREMIELVGlpeellarspfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
..
gi 739061588 475 LD 476
Cdd:PRK13634 176 LD 177
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-195 |
2.41e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 59.09 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 11 VGKIVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIKIG-----YLpqEPK------ 79
Cdd:PRK11650 9 VRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE------IWIGgrvvnEL--EPAdrdiam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 80 ------LNPEHTVREAVEEAvseLKNAlnrldevyaayadpdadfdKLAKEQgqleaiiqshdghnLENQLERAAEALRL 153
Cdd:PRK11650 81 vfqnyaLYPHMSVRENMAYG---LKIR-------------------GMPKAE--------------IEERVAEAARILEL 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739061588 154 -PEWDAKIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDA 195
Cdd:PRK11650 125 ePLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
321-367 |
2.66e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 58.12 E-value: 2.66e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 739061588 321 DKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFR 367
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLR 55
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-218 |
3.19e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 58.08 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQepklNPEH 84
Cdd:PRK13632 19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLlkpqsgeikidGITISKENLKEIRKKIGIIFQ----NPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 T-VREAVEEAVS-ELKNALNRLDEVyaayadpDADFDKLAKEQGqleaiiqshdghnLENQLERAAEalrlpewdakieK 162
Cdd:PRK13632 95 QfIGATVEDDIAfGLENKKVPPKKM-------KDIIDDLAKKVG-------------MEDYLDKEPQ------------N 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 163 LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG----TVVAITHD 218
Cdd:PRK13632 143 LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrkkTLISITHD 202
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-236 |
3.40e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 58.27 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdtdiegearpqpgikigYLPQEpklNPEHTVreAVEEAVSEL 97
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL-----------------LLPDD---NPNSKI--TVDGITLTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 98 KNALNRLDEVYAAYADPDADFdklakeqgqLEAIIQSHDGHNLENQ----------LERAAEALRLPEW-DAKIEKLSGG 166
Cdd:PRK13640 77 KTVWDIREKVGIVFQNPDNQF---------VGATVGDDVAFGLENRavprpemikiVRDVLADVGMLDYiDSEPANLSGG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 167 ERRRVAICRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHDryfLD--NVAGWILELDRGE 236
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGkeqiLKLIRKLKKKNNLTVISITHD---IDeaNMADQVLVLDDGK 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
320-520 |
3.52e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.10 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 320 GDKVLEinNLTKSYGDRV-----LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQF 394
Cdd:PRK13645 5 KDIILD--NVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 395 RDSMDDSK----------------TVWEEVSGG--------QDIMRignfEIPS--------RAYVGRFNFkgvdqgkrv 442
Cdd:PRK13645 83 KEVKRLRKeiglvfqfpeyqlfqeTIEKDIAFGpvnlgenkQEAYK----KVPEllklvqlpEDYVKRSPF--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 443 gELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETLRALENALL----EFPGCAMVISHDRWFLDRIATHIIdYQDEG 518
Cdd:PRK13645 150 -ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFErlnkEYKKRIIMVTHNMDQVLRIADEVI-VMHEG 227
|
..
gi 739061588 519 KV 520
Cdd:PRK13645 228 KV 229
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
324-516 |
3.67e-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: 56.71 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRV-----LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVklASVDQ----- 393
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQepwiq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 ---------FRDSMDDS--KTVWEEVSGGQDImrignfEIpsrayvgrfnFKGVDQgKRVGE----LSGGERGRLHLAKL 458
Cdd:cd03250 79 ngtirenilFGKPFDEEryEKVIKACALEPDL------EI----------LPDGDL-TEIGEkginLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739061588 459 LQVGGNMLLLDEPTNDLDVETLRAL-ENAL---LEFPGCAMVISHDRWFLDRiATHIIDYQD 516
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIfENCIlglLLNNKTRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
343-489 |
4.40e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 56.90 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 343 SFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQFRDSMDDSK-------TVWEEVSGG--- 411
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDHTTTPPSRRPVSMLFQEnnlfshlTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 412 ------------QDI---MRIGNfeipsraYVGRFNfkgvdqgkrvGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:PRK10771 99 glklnaaqreklHAIarqMGIED-------LLARLP----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170
....*....|...
gi 739061588 477 vetlRALENALLE 489
Cdd:PRK10771 162 ----PALRQEMLT 170
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-270 |
5.78e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.44 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARpqpgikigylpqepklnpehtVREAVEEAVS 95
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVT---------------------VGDIVVSSTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 96 ELKNALNRLDEVYAAYADPDAdfdKLAKEQGQLEAIIQSHD-GHNLENQLERAAEALRL-----PEWDAKIEKLSGGERR 169
Cdd:PRK13643 75 KQKEIKPVRKKVGVVFQFPES---QLFEETVLKDVAFGPQNfGIPKEKAEKIAAEKLEMvgladEFWEKSPFELSGGQMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 170 RVAICRLLLEKPDMLLLDEPTNHLDAES-VAWLERF--LHDYEGTVVAITHdryFLDNV---AGWILELDRGEGIPWeGN 243
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDPKArIEMMQLFesIHQSGQTVVLVTH---LMDDVadyADYVYLLEKGHIISC-GT 227
|
250 260
....*....|....*....|....*..
gi 739061588 244 YSSWLEQKDARLEQEAATEAARHKSIQ 270
Cdd:PRK13643 228 PSDVFQEVDFLKAHELGVPKATHFADQ 254
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-223 |
5.86e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 57.00 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGID----------------TDIEGEARPQPGIKIGYlpQEPKLNPEH 84
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyevtsgsilldgediLELSPDERARAGIFLAF--QYPVEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 85 TVREAveeavseLKNALN--RLDEVYAAyadpdaDFDKLAKEqgqleaiiqshdghnlenqlerAAEALRLPEWDAKI-- 160
Cdd:COG0396 93 SVSNF-------LRTALNarRGEELSAR------EFLKLLKE----------------------KMKELGLDEDFLDRyv 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 161 -EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAES---VAWLERFLHDYEGTVVAITHDRYFLD 223
Cdd:COG0396 138 nEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDAlriVAEGVNKLRSPDRGILIITHYQRILD 204
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
323-472 |
6.77e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.43 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLG--DTVKLASVDQFRDSMD- 399
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkDITDWQTAKIMREAVAi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 400 --------DSKTVWEEVSGG----------QDIMRIgnFEIPSRAYVGRFnfkgvdqgKRVGELSGGERGRLHLAKLLQV 461
Cdd:PRK11614 85 vpegrrvfSRMTVEENLAMGgffaerdqfqERIKWV--YELFPRLHERRI--------QRAGTMSGGEQQMLAIGRALMS 154
|
170
....*....|.
gi 739061588 462 GGNMLLLDEPT 472
Cdd:PRK11614 155 QPRLLLLDEPS 165
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
317-520 |
6.93e-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: 55.88 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 317 PRLGDkvLEINNLTKSYGDRV--LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLgDTVKLASVD-- 392
Cdd:cd03369 2 PEHGE--IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTIPle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 393 QFRDSMddskTVWEevsggQD-IMRIGNFeipsRAYVGRFNFKGVDQ---GKRVGE----LSGGERGRLHLAKLLQVGGN 464
Cdd:cd03369 79 DLRSSL----TIIP-----QDpTLFSGTI----RSNLDPFDEYSDEEiygALRVSEgglnLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 465 MLLLDEPTNDLDVETLRALENALLE-FPGCAMV-ISHdrwfldRIAThIIDYQ-----DEGKV 520
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREeFTNSTILtIAH------RLRT-IIDYDkilvmDAGEV 201
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
321-484 |
7.31e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 56.71 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFR-------MISGQeQPDSGTLVLGDTVKLASVDQ 393
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGF-RVEGKVTFHGKNLYAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 ----------FRDSMDDSKTVWEEVSGGQdimRIGNFEIPSRAYVGRFNFKGV------DQGKRVG-ELSGGERGRLHLA 456
Cdd:PRK14243 87 vevrrrigmvFQKPNPFPKSIYDNIAYGA---RINGYKGDMDELVERSLRQAAlwdevkDKLKQSGlSLSGGQQQRLCIA 163
|
170 180
....*....|....*....|....*....
gi 739061588 457 KLLQVGGNMLLLDEPTNDLD-VETLRALE 484
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDpISTLRIEE 192
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
346-512 |
7.87e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 346 IPK-GAIVGIIGPNGAGKSTLFRMISGQEQPDsgtlvLGDTVKLAS----VDQFRDSmdDSKTVWEEVSGG--------Q 412
Cdd:PRK13409 95 IPKeGKVTGILGPNGIGKTTAVKILSGELIPN-----LGDYEEEPSwdevLKRFRGT--ELQNYFKKLYNGeikvvhkpQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 413 DIMRI------------------GNFeipsRAYVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTND 474
Cdd:PRK13409 168 YVDLIpkvfkgkvrellkkvderGKL----DEVVERLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739061588 475 LDV-ETLRAlENALLEF-PGCA-MVISHDRWFLDRIA--THII 512
Cdd:PRK13409 243 LDIrQRLNV-ARLIRELaEGKYvLVVEHDLAVLDYLAdnVHIA 284
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
337-522 |
8.24e-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: 58.22 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 337 VLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQ--------FRD------SMDDSK 402
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQrpymtlgtLRDqiiypdSSEDMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 403 ----------TVWEEVSGGQDIMRIGNFEIPSrayvgrfNFKGVdqgkrvgeLSGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:TIGR00954 546 rrglsdkdleQILDNVQLTHILEREGGWSAVQ-------DWMDV--------LSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 739061588 473 NDLDVETLRALENALLEFPGCAMVISHdRWFLDRIATHIIDYQDEGKVEF 522
Cdd:TIGR00954 611 SAVSVDVEGYMYRLCREFGITLFSVSH-RKSLWKYHEYLLYMDGRGGYQF 659
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
341-476 |
9.49e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.68 E-value: 9.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 341 DLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTV---------------KLASVDQFRDSMDDSKTVW 405
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirkKVGLVFQFPESQLFEETVL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739061588 406 EEVSGGQDIMRIGNFEIPSRAYvGRFNFKGVDQ---GKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:PRK13649 105 KDVAFGPQNFGVSQEEAEALAR-EKLALVGISEslfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
324-512 |
9.85e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 55.69 E-value: 9.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLtKSYGDRVLIDdlsFSIPkgaIVGIIGPNGAGKSTLF-------------RMISGQEQPDsgtlVLGDTVKLAS 390
Cdd:cd03240 4 LSIRNI-RSFHERSEIE---FFSP---LTLIVGQNGAGKTTIIealkyaltgelppNSKGGAHDPK----LIREGEVRAQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 391 VD-QFRDSMDDSKTVWEEVsggqDIMRignfeipSRAYV--GRFNFKGVDQgkrVGELSGGERG------RLHLAKLLQV 461
Cdd:cd03240 73 VKlAFENANGKKYTITRSL----AILE-------NVIFChqGESNWPLLDM---RGRCSGGEKVlasliiRLALAETFGS 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 462 GGNMLLLDEPTNDLDVETLR-----ALENALLEFPGCAMVISHDRWFLDRiATHII 512
Cdd:cd03240 139 NCGILALDEPTTNLDEENIEeslaeIIEERKSQKNFQLIVITHDEELVDA-ADHIY 193
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
320-550 |
1.07e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 56.63 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 320 GDKVLEINNLTKSYGD------RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLG--DTVKLASV 391
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDglDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 392 DQFR----------DSMDDSKTVWEEVSGGQDIMRIGNFEIPSRayvgrfnfkgVDQG-KRVGE----------LSGGER 450
Cdd:PRK13633 81 WDIRnkagmvfqnpDNQIVATIVEEDVAFGPENLGIPPEEIRER----------VDESlKKVGMyeyrrhaphlLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 451 GRLHLAKLLQVGGNMLLLDEPTNDLD----VETLRALENALLEFPGCAMVISHdrwFLDRI--ATHIIdYQDEGKVeFFE 524
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH---YMEEAveADRII-VMDSGKV-VME 225
|
250 260 270
....*....|....*....|....*....|
gi 739061588 525 GN----FTEYEEYKKrtLGNDAIQPRRMKY 550
Cdd:PRK13633 226 GTpkeiFKEVEMMKK--IGLDVPQVTELAY 253
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
324-489 |
1.10e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.93 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLT-KSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQeQPDSGTLvLGDTVKLASVDqfrdsmddsK 402
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSL-KINGIELRELD---------P 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 403 TVW-EEVSG-GQ----------DIMRIGNFEIP--------SRAYVGRF---NFKGVDQ--GKRVGELSGGERGRLHLAK 457
Cdd:PRK11174 419 ESWrKHLSWvGQnpqlphgtlrDNVLLGNPDASdeqlqqalENAWVSEFlplLPQGLDTpiGDQAAGLSVGQAQRLALAR 498
|
170 180 190
....*....|....*....|....*....|..
gi 739061588 458 LLQVGGNMLLLDEPTNDLDVETLRALENALLE 489
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLDAHSEQLVMQALNA 530
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-199 |
1.90e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.89 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---ID-TDIEGEARPQPGIKIGYLPQEPKL---N 81
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGrilIDgTDIRTVTRASLRRNIAVVFQDAGLfnrS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 PEHTVREAVEEAVSElknalnrldEVYAAyADPDADFDKLAKEQGQLEAIIQshdghnlenqlERAaealrlpewdakiE 161
Cdd:PRK13657 425 IEDNIRVGRPDATDE---------EMRAA-AERAQAHDFIERKPDGYDTVVG-----------ERG-------------R 470
|
170 180 190
....*....|....*....|....*....|....*...
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVA 199
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVETEA 508
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
324-512 |
1.94e-08 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 54.97 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTkSYGDRVLIDdlsFS-IPKGAIVGIIGPNGAGKSTLFrmisgqeqpDSGTLVL-GDTVKLASVDQFRDSMdds 401
Cdd:cd03279 6 LELKNFG-PFREEQVID---FTgLDNNGLFLICGPTGAGKSTIL---------DAITYALyGKTPRYGRQENLRSVF--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 402 ktvweevSGGQDIMRIG-NFEIPSRAY-VGRfnFKGVD-----------QGK-------RVGELSGGERGR------LHL 455
Cdd:cd03279 70 -------APGEDTAEVSfTFQLGGKKYrVER--SRGLDydqftrivllpQGEfdrflarPVSTLSGGETFLaslslaLAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739061588 456 AKLLQVGGNM----LLLDEPTNDLDVETLRALENALLEFPG---CAMVISHDRWFLDRIATHII 512
Cdd:cd03279 141 SEVLQNRGGArleaLFIDEGFGTLDPEALEAVATALELIRTenrMVGVISHVEELKERIPQRLE 204
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
332-487 |
2.30e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 56.75 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 332 SY-GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGD----TVKLAS-------VDQ----FR 395
Cdd:COG5265 366 GYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirDVTQASlraaigiVPQdtvlFN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 DSM---------DDSKtvwEEVSGGQDIMRIGNF--EIPsrayvgrfnfKGVDqgKRVGE----LSGGERGRLHLAKLLQ 460
Cdd:COG5265 446 DTIayniaygrpDASE---EEVEAAARAAQIHDFieSLP----------DGYD--TRVGErglkLSGGEKQRVAIARTLL 510
|
170 180
....*....|....*....|....*..
gi 739061588 461 VGGNMLLLDEPTNDLDVETLRALENAL 487
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAAL 537
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
321-384 |
2.58e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.18 E-value: 2.58e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 321 DKVLEINNLTKSYGDRV---------LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGD 384
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD 74
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
321-535 |
2.59e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.17 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 321 DKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMIS--GQEQPD---SGTLVLG---------DTV 386
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNghniysprtDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 387 KL----ASVdqFRDSMDDSKTVWEEVSGGQDIMRIGNFEIPSRAyVGRfNFKGVDQGKRVGE--------LSGGERGRLH 454
Cdd:PRK14239 83 DLrkeiGMV--FQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEA-VEK-SLKGASIWDEVKDrlhdsalgLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 455 LAKLLQVGGNMLLLDEPTNDLDVETLRALENALLEFPG--CAMVISHDRWFLDRIAThiidyqdegKVEFF-EGNFTEYE 531
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQQASRISD---------RTGFFlDGDLIEYN 229
|
....
gi 739061588 532 EYKK 535
Cdd:PRK14239 230 DTKQ 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-226 |
2.72e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 55.24 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIKIGYLPQEPKLNPEHTVREAVEEAVSELKN 99
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGR------ILFDGKPIDYSRKGLMKLRESVGMVFQDPDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 100 ALnrldevYAAYADPDADFD----KLAKEQGQleaiiqshdgHNLENQLERAAEAlrlPEWDAKIEKLSGGERRRVAICR 175
Cdd:PRK13636 94 QL------FSASVYQDVSFGavnlKLPEDEVR----------KRVDNALKRTGIE---HLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 176 LLLEKPDMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHDryfLDNVA 226
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD---IDIVP 206
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-526 |
3.08e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.04 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTV--------KLASVDQFR 395
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEffnqniyeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 396 D--SMDDSK------TVWEEVSGGQDIM----RIGNFEIPSRAYVGRFNFKGVDQG--KRVGELSGGERGRLHLAKLLQV 461
Cdd:PRK14258 88 RqvSMVHPKpnlfpmSVYDNVAYGVKIVgwrpKLEIDDIVESALKDADLWDEIKHKihKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 462 GGNMLLLDEPTNDLD------VETLraLENALLEFPGCAMVISHDRWFLDRIAthiiDYqdegkVEFFEGN 526
Cdd:PRK14258 168 KPKVLLMDEPCFGLDpiasmkVESL--IQSLRLRSELTMVIVSHNLHQVSRLS----DF-----TAFFKGN 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
317-477 |
3.17e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 317 PRLGDKVLEINNLT---KSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTL----F-----RMISGQ-----EQPDSGT 379
Cdd:NF040905 251 PKIGEVVFEVKNWTvyhPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELamsvFgrsygRNISGTvfkdgKEVDVST 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 380 --------------------LVLGDTVK----LASVDQF--RDSMDDSktvwEEVSGGQDimrignfeipsraYVGRFNF 433
Cdd:NF040905 331 vsdaidaglayvtedrkgygLNLIDDIKrnitLANLGKVsrRGVIDEN----EEIKVAEE-------------YRKKMNI 393
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 739061588 434 K--GVDQGkrVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDV 477
Cdd:NF040905 394 KtpSVFQK--VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-218 |
3.33e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.99 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE-----------ARPQPGIKIGYLPQEPKLNPEHTV 86
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHvwldgehiqhyASKEVARRIGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 87 REAVeeavselknALNRLDEvyaayadpDADFDKLAKEQgqleaiiqshdghnlENQLERAAEALRLPEW-DAKIEKLSG 165
Cdd:PRK10253 99 QELV---------ARGRYPH--------QPLFTRWRKED---------------EEAVTKAMQATGITHLaDQSVDTLSG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 166 GERRRVAICRLLLEKPDMLLLDEPTNHLD-AESVAWLERF--LHDYEG-TVVAITHD 218
Cdd:PRK10253 147 GQRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQIDLLELLseLNREKGyTLAAVLHD 203
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
21-195 |
3.65e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.50 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTD------IEGEARPQPGIK---IGYLPQEPKLNPEHTVREAVE 91
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPtegqifIDGEDVTHRSIQqrdICMVFQSYALFPHMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 92 EAVselknalnrldevyaayadpdadfdklaKEQGQLEAIIQshdghnlenqlERAAEALRLPEW----DAKIEKLSGGE 167
Cdd:PRK11432 101 YGL----------------------------KMLGVPKEERK-----------QRVKEALELVDLagfeDRYVDQISGGQ 141
|
170 180
....*....|....*....|....*...
gi 739061588 168 RRRVAICRLLLEKPDMLLLDEPTNHLDA 195
Cdd:PRK11432 142 QQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
323-385 |
3.68e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 3.68e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDT 385
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN 73
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-194 |
4.75e-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: 56.07 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRImagidtdIEGEARPQPG-IK----IGYLPQEPKLNPeHTVREAVEEAVS 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMM-------IMGELEPSEGkIKhsgrISFSPQTSWIMP-GTIKDNIIFGLS 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 96 elknalnrldevYAAYadpdadfdklakeqgQLEAIIQSHdghNLENQLERAAEALRLPEWDAKIeKLSGGERRRVAICR 175
Cdd:TIGR01271 513 ------------YDEY---------------RYTSVIKAC---QLEEDIALFPEKDKTVLGEGGI-TLSGGQRARISLAR 561
|
170
....*....|....*....
gi 739061588 176 LLLEKPDMLLLDEPTNHLD 194
Cdd:TIGR01271 562 AVYKDADLYLLDSPFTHLD 580
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
324-513 |
4.77e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.88 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSY-GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLgDTVKLAS------------ 390
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL-DGRPLSSlshsvlrqgvam 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 391 VDQfrDSMDDSKTVWEEVSGGQDIMRIGNFEIPSRAYVGRFnFKGVDQG--KRVGE----LSGGERGRLHLAKLLQVGGN 464
Cdd:PRK10790 420 VQQ--DPVVLADTFLANVTLGRDISEEQVWQALETVQLAEL-ARSLPDGlyTPLGEqgnnLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 739061588 465 MLLLDEPTNDLDVETLRALENALLEFPGCA--MVISHdrwfldRIAThIID 513
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTtlVVIAH------RLST-IVE 540
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
346-511 |
4.93e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.29 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 346 IPK-GAIVGIIGPNGAGKSTLFRMISGQEQPDSG------------------------TLVLGDTVKLASVDQFRDSMdd 400
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildefrgselqnyfTKLLEGDVKVIVKPQYVDLI-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 401 SKTVWEEVsgGQDIMRI---GNFEIpsraYVGRFNFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDV 477
Cdd:cd03236 100 PKAVKGKV--GELLKKKderGKLDE----LVDQLELRHVLD-RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 739061588 478 E---TLRALENALLEFPGCAMVISHDRWFLDRIATHI 511
Cdd:cd03236 173 KqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-240 |
5.91e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.90 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI----DTDIEGEArpqpgiKIGYLPQEPKLNPEHTVREAVEeAV 94
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiyDSKIKVDG------KVLYFGKDIFQIDAIKLRKEVG-MV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 95 SELKNALNRLdEVYAAYADPDADFDklAKEQGQLEAIIQshdghnlenqleraaEALR-LPEW-------DAKIEKLSGG 166
Cdd:PRK14246 96 FQQPNPFPHL-SIYDNIAYPLKSHG--IKEKREIKKIVE---------------ECLRkVGLWkevydrlNSPASQLSGG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 167 ERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHDRYFLDNVAGWILELDRGEGIPW 240
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVADYVAFLYNGELVEW 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-241 |
5.98e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 54.32 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdtdiegearpqpgikigYLPQEPKLNPEHTvreaveeAVSELKNAL 101
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL-----------------LIPSEGKVYVDGL-------DTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 102 NRLDEVYAAYADPDadfdklakeqGQLEAIIQSHD----GHNL----ENQLERAAEAL-RLPEWDAKIEK---LSGGERR 169
Cdd:PRK13633 82 DIRNKAGMVFQNPD----------NQIVATIVEEDvafgPENLgippEEIRERVDESLkKVGMYEYRRHAphlLSGGQKQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 170 RVAICRLLLEKPDMLLLDEPTNHLDA----ESVAWLERFLHDYEGTVVAITHdryFLDNV--AGWILELDRG----EGIP 239
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPsgrrEVVNTIKELNKKYGITIILITH---YMEEAveADRIIVMDSGkvvmEGTP 228
|
..
gi 739061588 240 WE 241
Cdd:PRK13633 229 KE 230
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
321-371 |
6.10e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 6.10e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 739061588 321 DKVLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISG 371
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
143-253 |
6.38e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.41 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 143 QLERAAEALRLPEWDAKIEK------------LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESvawlERFLH---- 206
Cdd:PRK11176 449 QIEEAARMAYAMDFINKMDNgldtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTES----ERAIQaald 524
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 739061588 207 --DYEGTVVAITHDRYFLDNvAGWILELDRGEgIPWEGNYSSWLEQKDA 253
Cdd:PRK11176 525 elQKNRTSLVIAHRLSTIEK-ADEILVVEDGE-IVERGTHAELLAQNGV 571
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
324-501 |
6.44e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.09 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSY--GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLF----RMIS--GQEQPDSgtlVLGDTVKLAS----- 390
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLNteGDIQIDG---VSWNSVPLQKwrkaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 391 --VDQ--------FRDSMDDSKTvWEEvsggQDIMRIGNfEIPSRAYV----GRFNFKGVDQGKrvgELSGGERGRLHLA 456
Cdd:cd03289 80 gvIPQkvfifsgtFRKNLDPYGK-WSD----EEIWKVAE-EVGLKSVIeqfpGQLDFVLVDGGC---VLSHGHKQLMCLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 739061588 457 KLLQVGGNMLLLDEPTNDLDVETLRALENALLE-FPGCAMVISHDR 501
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQaFADCTVILSEHR 196
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
339-478 |
6.48e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.06 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL-VLGDTV--------------KLASVDQFRDSMDDSKT 403
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItIAGYHItpetgnknlkklrkKVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 404 VWEEVSGGQdiMRIGNFEIPSRAyvgrfnfKGVDQGKRVG-----------ELSGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:PRK13641 103 VLKDVEFGP--KNFGFSEDEAKE-------KALKWLKKVGlsedliskspfELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
....*.
gi 739061588 473 NDLDVE 478
Cdd:PRK13641 174 AGLDPE 179
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-219 |
7.62e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 55.69 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIdTDIEGEarpqpgIKI-GYLPQEPKLNPEHTVREAVEEAVSEL 97
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGE------IQIdGVSWNSVTLQTWRKAFGVIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 98 KNALNRLDEVYAAYAdpDADFDKLAKEQGqLEAIIQSHDGhNLENQLERAAEAlrlpewdakiekLSGGERRRVAICRLL 177
Cdd:TIGR01271 1305 SGTFRKNLDPYEQWS--DEEIWKVAEEVG-LKSVIEQFPD-KLDFVLVDGGYV------------LSNGHKQLMCLARSI 1368
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739061588 178 LEKPDMLLLDEPTNHLDAESVAWLERFL-HDYEGTVVAITHDR 219
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLkQSFSNCTVILSEHR 1411
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-219 |
7.94e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.18 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIGYLPQEpklnpehTVREAVEEAVSelKNA 100
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFE-GEDISTLKPE-------IYRQQVSYCAQ--TPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 101 LNRlDEVYAAYADPDadfdKLAKEQGQLEAIIQSHDGHNL-ENQLERaaealrlpewdaKIEKLSGGERRRVAICRLLLE 179
Cdd:PRK10247 92 LFG-DTVYDNLIFPW----QIRNQQPDPAIFLDDLERFALpDTILTK------------NIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 739061588 180 KPDMLLLDEPTNHLDAESVAWLERFLHDY----EGTVVAITHDR 219
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYvreqNIAVLWVTHDK 198
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-226 |
8.04e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 54.35 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 24 NISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIGYLP---------------QEP--KLNPEHTV 86
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD-GQDITGLSgrelrplrrrmqmvfQDPyaSLNPRMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 87 REAVEEAVselknalnrldevyaayadpdadfdklaKEQGQLEAiiqshdghnlENQLERAAEALRL----PEWdakIEK 162
Cdd:COG4608 115 GDIIAEPL----------------------------RIHGLASK----------AERRERVAELLELvglrPEH---ADR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 163 ----LSGGERRRVAICRLLLEKPDMLLLDEPTNHLD----AESVAWLERfLHDYEG-TVVAITHD----RYFLDNVA 226
Cdd:COG4608 154 ypheFSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQVLNLLED-LQDELGlTYLFISHDlsvvRHISDRVA 229
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
320-542 |
9.85e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 55.30 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 320 GDKVLEINNLTkSYGDRVLiDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL--------------VLGDT 385
Cdd:TIGR01271 425 GDDGLFFSNFS-LYVTPVL-KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIkhsgrisfspqtswIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 386 VKL-----ASVDQFRdsmddSKTVWEEVSGGQDIMRIGNfeiPSRAYVGRfnfKGVdqgkrvgELSGGERGRLHLAKLLQ 460
Cdd:TIGR01271 503 IKDniifgLSYDEYR-----YTSVIKACQLEEDIALFPE---KDKTVLGE---GGI-------TLSGGQRARISLARAVY 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 461 VGGNMLLLDEPTNDLDVETlralENALLEFPGCAMVISHDRWFLDRIATHI-----IDYQDEGkVEFFEGNFTEYE---- 531
Cdd:TIGR01271 565 KDADLYLLDSPFTHLDVVT----EKEIFESCLCKLMSNKTRILVTSKLEHLkkadkILLLHEG-VCYFYGTFSELQakrp 639
|
250
....*....|.
gi 739061588 532 EYKKRTLGNDA 542
Cdd:TIGR01271 640 DFSSLLLGLEA 650
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
348-509 |
1.16e-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: 51.22 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 348 KGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRdsmddsktvweevsggqdimrignfeipsray 427
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQ-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 428 vgrfnFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVET---------LRALENALLEFPGCAMVIS 498
Cdd:smart00382 49 -----LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTT 123
|
170
....*....|.
gi 739061588 499 HDRWFLDRIAT 509
Cdd:smart00382 124 NDEKDLGPALL 134
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-194 |
1.19e-07 |
|
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: 54.75 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-----------DTDIEGEARPQPGIKIGYLPQEPKLNpehtvr 87
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFfqarsgeillnGFSLKDIDRHTLRQFINYLPQEPYIF------ 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 88 eaveeAVSELKNALNRldevyaayadpdadfdklAKEQGQLEAIIQshdghnlenqleraaeALRLPEWDAKIEK----- 162
Cdd:TIGR01193 561 -----SGSILENLLLG------------------AKENVSQDEIWA----------------ACEIAEIKDDIENmplgy 601
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 739061588 163 ----------LSGGERRRVAICRLLLEKPDMLLLDEPTNHLD 194
Cdd:TIGR01193 602 qtelseegssISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
323-506 |
1.27e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.57 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSY-GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLG--DTVKLASVDQ------ 393
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghDITRLKNREVpflrrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 ----FRDS---MDdsKTVWEEVSGGQDIMRIGNFEIPSRAYVGRFNFKGVDQGKRVG-ELSGGERGRLHLAKLLQVGGNM 465
Cdd:PRK10908 81 igmiFQDHhllMD--RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPiQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 739061588 466 LLLDEPTNDLDVETLRALENALLEFPGCAMVI---SHDRWFLDR 506
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVlmaTHDIGLISR 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
323-499 |
1.44e-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: 54.06 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISG---QEQPDSGTLVLGDTVKLASVdqfRDS-- 397
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvypHGTWDGEIYWSGSPLKASNI---RDTer 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 398 -----------MDDSKTVWEEVSGGQDIMRIGNF----EIPSRAY--VGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQ 460
Cdd:TIGR02633 78 agiviihqeltLVPELSVAENIFLGNEITLPGGRmaynAMYLRAKnlLRELQLDADNVTRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 739061588 461 VGGNMLLLDEPTNDLDVETLRALENAL--LEFPGCAMV-ISH 499
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIrdLKAHGVACVyISH 199
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-220 |
1.46e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.16 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 31 PGAKIGVLGLNGAGKSTLLRIMAG--------IDTDIEGEARPQPGIKIGYLPQEPKLNPEhtvreaveeaVSELKNaLN 102
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGllhvesgqIQIDGKTATRGDRSRFMAYLGHLPGLKAD----------LSTLEN-LH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 103 RLDEVYAAYADpdadfdklaKEQGQLEAIIqSHDGHNlenqleraaealrlpewDAKIEKLSGGERRRVAICRLLLEKPD 182
Cdd:PRK13543 105 FLCGLHGRRAK---------QMPGSALAIV-GLAGYE-----------------DTLVRQLSAGQKKRLALARLWLSPAP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 739061588 183 MLLLDEPTNHLDAESVAWLERFLHDY---EGTVVAITHDRY 220
Cdd:PRK13543 158 LWLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTHGAY 198
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-217 |
1.48e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.10 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgIKIGylpqepklnpEHTVreaveeaVS 95
Cdd:PRK13634 17 PFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGT------VTIG----------ERVI-------TA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 96 ELKNAlnrldevyaayadpdaDFDKLAKEQG--------QL-EAIIQ-------SHDGHNLENQLERAAEALRLPEWDAK 159
Cdd:PRK13634 74 GKKNK----------------KLKPLRKKVGivfqfpehQLfEETVEkdicfgpMNFGVSEEDAKQKAREMIELVGLPEE 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739061588 160 I-EK----LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDA----ESVAWLERfLHDYEG-TVVAITH 217
Cdd:PRK13634 138 LlARspfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPkgrkEMMEMFYK-LHKEKGlTTVLVTH 204
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
339-380 |
1.80e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.74 E-value: 1.80e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 739061588 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL 380
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
161-217 |
2.32e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 2.32e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 161 EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY----EGTVVAITH 217
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdkaDKTIITIAH 1417
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-241 |
2.58e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 52.32 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 4 YVYSmlrvgKIVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEArpqpgIKIGYlpqepklnpe 83
Cdd:PRK13645 14 YTYA-----KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-----IVGDY---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 84 htvreAVEEAVSELKNALNRLDEVYAAYADPDADF--DKLAKEQgqleAIIQSHDGHNLENQLERAAEALRL---PEWDA 158
Cdd:PRK13645 74 -----AIPANLKKIKEVKRLRKEIGLVFQFPEYQLfqETIEKDI----AFGPVNLGENKQEAYKKVPELLKLvqlPEDYV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 159 KIE--KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHDRYFLDNVAGWILEL 232
Cdd:PRK13645 145 KRSpfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
250
....*....|...
gi 739061588 233 DRGE----GIPWE 241
Cdd:PRK13645 225 HEGKvisiGSPFE 237
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
323-485 |
2.68e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 52.30 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRV-LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-----GDTVKLASVD---- 392
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtGDFSKLQGIRklvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 393 ---QFRDSMDDSKTVWEEVSGGQDIMRIGNFEIPSR-----AYVGRFNFKgvdqGKRVGELSGGERGRLHLAKLLQVGGN 464
Cdd:PRK13644 81 ivfQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRvdralAEIGLEKYR----HRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180
....*....|....*....|..
gi 739061588 465 MLLLDEPTNDLDVETLRA-LEN 485
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAvLER 178
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-198 |
3.06e-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: 51.11 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 17 PKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI---DTDIEG----------EARPQPGIKIGYLPQEPKLNPE 83
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGdihyngipykEFAEKYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 84 HTVREAVEEAvselknalnrldevyaayadpdadfdklAKEQGqleaiiqshdghnlenqleraaealrlpewDAKIEKL 163
Cdd:cd03233 98 LTVRETLDFA----------------------------LRCKG------------------------------NEFVRGI 119
|
170 180 190
....*....|....*....|....*....|....*
gi 739061588 164 SGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESV 198
Cdd:cd03233 120 SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
163-238 |
3.16e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.14 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 163 LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG---TVVAITHDryfLDNVAGW---ILELDRGE 236
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHN---MDDVAEYaddVLVLEHGK 222
|
..
gi 739061588 237 GI 238
Cdd:PRK13641 223 LI 224
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
342-396 |
3.44e-07 |
|
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: 52.88 E-value: 3.44e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 342 LSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQFRD 396
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLdGQPVTADNREAYRQ 406
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
324-485 |
3.67e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.01 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRV-----LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL--VLGDTVKLASVDQFRD 396
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 397 SMDD---SKTVWEEVSGGQDI-MRIGN---------FE--IPSRAYVGRFNFkGVDQG----------KRVG-------- 443
Cdd:PRK13651 83 VLEKlviQKTRFKKIKKIKEIrRRVGVvfqfaeyqlFEqtIEKDIIFGPVSM-GVSKEeakkraakyiELVGldesylqr 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 739061588 444 ---ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD----VETLRALEN 485
Cdd:PRK13651 162 spfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDN 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
323-476 |
3.76e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.93 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL-------------VLGDTVKLA 389
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldyskrgLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 390 SVdqFRDSmdDSKTVWEEVSggQDI-MRIGNFEIPSRAYVGRFN--FKGVD-QGKR---VGELSGGERGRLHLAKLLQVG 462
Cdd:PRK13638 81 TV--FQDP--EQQIFYTDID--SDIaFSLRNLGVPEAEITRRVDeaLTLVDaQHFRhqpIQCLSHGQKKRVAIAGALVLQ 154
|
170
....*....|....
gi 739061588 463 GNMLLLDEPTNDLD 476
Cdd:PRK13638 155 ARYLLLDEPTAGLD 168
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
323-499 |
4.11e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.00 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL-VLGDTVKLASVDQFRDSMDDS 401
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqIDGKTATRGDRSRFMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 402 KTVWEEVSGGQDIMRIGNF------EIPSRAY--VGrfnFKGVDQgKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTN 473
Cdd:PRK13543 91 PGLKADLSTLENLHFLCGLhgrrakQMPGSALaiVG---LAGYED-TLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180
....*....|....*....|....*....
gi 739061588 474 DLDVETLRALENAL---LEFPGCAMVISH 499
Cdd:PRK13543 167 NLDLEGITLVNRMIsahLRGGGAALVTTH 195
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-236 |
4.95e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 51.59 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 16 PPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLR-------------IMAGID-TDIE---GEARPQPGIKIGYlpqep 78
Cdd:PRK13637 17 PFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQhlngllkptsgkiIIDGVDiTDKKvklSDIRKKVGLVFQY----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 79 klnPEHTV-REAVEEAVSELKNALNRLDEvyaayadpdadfdklakeqgqleaiiqshdghNLENQLERAAEALRLPEWD 157
Cdd:PRK13637 92 ---PEYQLfEETIEKDIAFGPINLGLSEE--------------------------------EIENRVKRAMNIVGLDYED 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 158 AKIE---KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDA---ESVAWLERFLHD-YEGTVVAITHDRYFLDNVAGWIL 230
Cdd:PRK13637 137 YKDKspfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrDEILNKIKELHKeYNMTIILVSHSMEDVAKLADRII 216
|
....*.
gi 739061588 231 ELDRGE 236
Cdd:PRK13637 217 VMNKGK 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
325-487 |
6.08e-07 |
|
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: 50.62 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 325 EINNLTKSYGDR--VLI-DDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQFRDSM-- 398
Cdd:cd03249 2 EFKNVSFRYPSRpdVPIlKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRDLNLRWLRSQIgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 399 -------------------DDSKTVWEEVsggqdimrignfEIPSRAYVGRFNFKGVDQ-----GKRVGELSGGERGRLH 454
Cdd:cd03249 82 vsqepvlfdgtiaenirygKPDATDEEVE------------EAAKKANIHDFIMSLPDGydtlvGERGSQLSGGQKQRIA 149
|
170 180 190
....*....|....*....|....*....|...
gi 739061588 455 LAKLLQVGGNMLLLDEPTNDLDVETLRALENAL 487
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEAL 182
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
163-226 |
6.36e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 51.28 E-value: 6.36e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 163 LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERF---LHDYEGTVVAITHdryFLDNVA 226
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLfkkLHQSGMTIVLVTH---LMDDVA 209
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-194 |
6.54e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.50 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------ARPQPGI------KIGYLPQEP--KLNPEHT 85
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGElyyqgqdlLKADPEAqkllrqKIQIVFQNPygSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 86 VREAVEEAVselknALNrldevyaayadpdadfDKLAKEQgqleaiiqshdghnlenQLERAAEALRL----PE-WDAKI 160
Cdd:PRK11308 111 VGQILEEPL-----LIN----------------TSLSAAE-----------------RREKALAMMAKvglrPEhYDRYP 152
|
170 180 190
....*....|....*....|....*....|....
gi 739061588 161 EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLD 194
Cdd:PRK11308 153 HMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-218 |
6.93e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.94 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFfPGAKI-GVLGLNGAGKSTLLRIMAGIDTDIEGeARPQPgiKIGYLPQE---PKLNPEHTVReaveeavsel 97
Cdd:PRK14243 26 VKNVWLDI-PKNQItAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEG--KVTFHGKNlyaPDVDPVEVRR---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 98 knalnRLDEVYA-AYADPDADFDKLAkeqgqLEAIIQSHDGhNLENQLERAAEALRLpeWDAKIEKL-------SGGERR 169
Cdd:PRK14243 92 -----RIGMVFQkPNPFPKSIYDNIA-----YGARINGYKG-DMDELVERSLRQAAL--WDEVKDKLkqsglslSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 739061588 170 RVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDY--EGTVVAITHD 218
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTHN 209
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
324-500 |
8.55e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 49.62 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLtKSYGDRVLIDdlsfsIPKGaIVGIIGPNGAGKSTLFR-------------------MISGQEQPDSGTLVL-- 382
Cdd:COG0419 5 LRLENF-RSYRDTETID-----FDDG-LNLIVGPNGAGKSTILEairyalygkarsrsklrsdLINVGSEEASVELEFeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 383 -----------GDTVKLAS---------------VDQFRDSMDDSKTVWEEVSggQDIMRIGNFEIPSRAYVGRFN-FKG 435
Cdd:COG0419 78 ggkryrierrqGEFAEFLEakpserkealkrllgLEIYEELKERLKELEEALE--SALEELAELQKLKQEILAQLSgLDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 436 VDQgkrvgeLSGGERGRLHLAKLLQvggnmLLLDepTNDLDVETLRALENALLEfpgcAMVISHD 500
Cdd:COG0419 156 IET------LSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
162-214 |
8.59e-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: 51.64 E-value: 8.59e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVA 214
Cdd:TIGR02203 469 LLSGGQRQRLAIARALLKDAPILILDEATSALDNESerlvQAALERLMQGRTTLVIA 525
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-219 |
8.79e-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: 50.62 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGIDTDIEGEarpqpGIKIGYLPqepkLNPEHTVREAVEEAVSEL 97
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAflrLLNTEGDIQID-----GVSWNSVP----LQKWRKAFGVIPQKVFIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 98 KNALNRLDEVYAAYAdpDADFDKLAKEQGqLEAIIQSHDGHnLENQLERAAEAlrlpewdakiekLSGGERRRVAICRLL 177
Cdd:cd03289 90 SGTFRKNLDPYGKWS--DEEIWKVAEEVG-LKSVIEQFPGQ-LDFVLVDGGCV------------LSHGHKQLMCLARSV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739061588 178 LEKPDMLLLDEPTNHLDAESVAWLERFL-HDYEGTVVAITHDR 219
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLkQAFADCTVILSEHR 196
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
290-476 |
1.54e-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: 51.48 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 290 RLARF---EELNSVDYQKRNetselfIPPGprlGDKVLEINNLTKSY--GDRVLIDDLSFSIPKGAIVGIIGPNGAGKST 364
Cdd:TIGR00957 609 RLRIFlshEELEPDSIERRT------IKPG---EGNSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 365 LFRMISGQEQPDSGTLVLGDTVklASVDQfrDSMDDSKTVWEEVSGG--------QDIMR----IGNFEI-PS--RAYVG 429
Cdd:TIGR00957 680 LLSALLAEMDKVEGHVHMKGSV--AYVPQ--QAWIQNDSLRENILFGkalnekyyQQVLEacalLPDLEIlPSgdRTEIG 755
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 739061588 430 RfnfKGVDqgkrvgeLSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD 476
Cdd:TIGR00957 756 E---KGVN-------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
320-500 |
2.51e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 320 GDKVLEINNLTKSY--------GDRVL--IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKL 388
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 389 ASVDQFRD--------------SMDDSKTVW----------------EEVSGGQDIMRignfeipsrayvgrfnfkgvdq 438
Cdd:PRK11308 82 ADPEAQKLlrqkiqivfqnpygSLNPRKKVGqileepllintslsaaERREKALAMMA---------------------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 439 gkRVG---E--------LSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVeTLRALENALL-----EFpGCAMV-ISHD 500
Cdd:PRK11308 140 --KVGlrpEhydryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQAQVLNLMmdlqqEL-GLSYVfISHD 214
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-223 |
2.70e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.87 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-----------------IdTDIEGEARPQPGIKIGYlpQEPklnpe 83
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykilegdilfkgesI-LDLEPEERAHLGIFLAF--QYP----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 84 htvreaVE-EAVSelknalnrldevyaayadpDADFDKLA-----KEQGQLEAiiqshdgHNLENqLERAAEALRLPEWD 157
Cdd:CHL00131 94 ------IEiPGVS-------------------NADFLRLAynskrKFQGLPEL-------DPLEF-LEIINEKLKLVGMD 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 158 AKI------EKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAE---SVAWLERFLHDYEGTVVAITHDRYFLD 223
Cdd:CHL00131 141 PSFlsrnvnEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSENSIILITHYQRLLD 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-218 |
2.73e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 49.32 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGeARPQPGIKIGylpqepklnpehtvreavEEAVSELK 98
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLG------------------GRSIFNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 99 NALNRLDEVYAAYADPDAdfdklaKEQGQLEAIIQSHDGHNLENQLE-RAAEALRLPE---WDAKIEKLS-------GGE 167
Cdd:PRK14271 95 DVLEFRRRVGMLFQRPNP------FPMSIMDNVLAGVRAHKLVPRKEfRGVAQARLTEvglWDAVKDRLSdspfrlsGGQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 739061588 168 RRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG--TVVAITHD 218
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
326-516 |
3.03e-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: 50.40 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 326 INNLTKSY--GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASVDQFRDSMD---D 400
Cdd:TIGR01257 931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGmcpQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 401 SKTVWEEVSGGQDIMRIGNFEIPSRAYvGRFNFKGV--DQG---KRVGE---LSGGERGRLHLAKLLQVGGNMLLLDEPT 472
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGRSWEE-AQLEMEAMleDTGlhhKRNEEaqdLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 739061588 473 NDLDVETLRALENALLEFPGCAMVIshdrwfldrIATHIIDYQD 516
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRSGRTII---------MSTHHMDEAD 1124
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
324-479 |
3.16e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.35 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAG--KSTLFRMISGqeqPDSGTLVLGDTVKLASVDQFRDSMDDS 401
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 402 KTV----WEEVSGGQDIMRIGNFEIPSRA--------YVGRFNFKGVdQGKRVGELSGGERGRLHLAKLLQVGGNMLLLD 469
Cdd:NF000106 91 RPVr*grRESFSGRENLYMIGR*LDLSRKdararadeLLERFSLTEA-AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170
....*....|
gi 739061588 470 EPTNDLDVET 479
Cdd:NF000106 170 EPTTGLDPRT 179
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-236 |
3.49e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.59 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEArpqpgikigYLPQEPklnpehtVREAVEEAVSELKNAL 101
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI---------LLDGKP-------VTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 102 nrLDEVYAayadpdadFDKLAKEQGQleaiiqSHDGHNLENQLER--AAEALRLPEWDAKIEKLSGGERRRVAICRLLLE 179
Cdd:PRK10522 403 --FTDFHL--------FDQLLGPEGK------PANPALVEKWLERlkMAHKLELEDGRISNLKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 180 KPDMLLLDEPTNHLDAEsvawLERF--------LHDYEGTVVAITHDRYFLDNvAGWILELDRGE 236
Cdd:PRK10522 467 ERDILLLDEWAADQDPH----FRREfyqvllplLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQ 526
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
19-218 |
3.71e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.38 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 19 RHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGidtdiegEARPQPGiKIGYLPQEPKLNPEHTVREAveeavsELK 98
Cdd:PRK11701 19 RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA-------RLAPDAG-EVHYRMRDGQLRDLYALSEA------ERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 99 nALNRLDEVYAaYADPdADFDKLAKEQG-----QLEAIIQSHDGhnleNQLERAAEALRLPEWDA-KIEKL----SGGER 168
Cdd:PRK11701 85 -RLLRTEWGFV-HQHP-RDGLRMQVSAGgnigeRLMAVGARHYG----DIRATAGDWLERVEIDAaRIDDLpttfSGGMQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 169 RRVAICRLLLEKPDMLLLDEPTNHLDAeSVA-----WLERFLHDYEGTVVAITHD 218
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDV-SVQarlldLLRGLVRELGLAVVIVTHD 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
163-235 |
3.81e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 48.10 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 163 LSGGERRRVAICRLLLEKPDMLLLDEP--------TNHLDAESVAwleRFLHDYEGTVVAITHDRYFLDNvAGWILELDR 234
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPfsaldihlSDHLMQEGIL---KFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKD 216
|
.
gi 739061588 235 G 235
Cdd:cd03290 217 G 217
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
336-513 |
4.52e-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: 46.97 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 336 RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISgqeqpdsgtLVLGdtvklasvdqfrdsMDDSKTVWEEVSGGQDIm 415
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------LALG--------------GAQSATRRRSGVKAGCI- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 416 rignfeipsRAYVG-RFNFkgvdqgkRVGELSGGERGRLHLAKLLQ----VGGNMLLLDEPTNDLDVETLRALENALLEF 490
Cdd:cd03227 64 ---------VAAVSaELIF-------TRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEH 127
|
170 180
....*....|....*....|....*.
gi 739061588 491 --PGC-AMVISHDRWFLDRiATHIID 513
Cdd:cd03227 128 lvKGAqVIVITHLPELAEL-ADKLIH 152
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-194 |
6.26e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 47.93 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIGVLGLNGAGKSTLLRImagidtdIEGEARPQPGI-----KIGYLPQEPKLNPeHTVREAVEEAVS 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLML-------ILGELEPSEGKikhsgRISFSSQFSWIMP-GTIKENIIFGVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 96 elknalnrldevYAAYadpdadfdklakeqgQLEAIIQSHdghNLENQLERAAEALRLPEWDAKIeKLSGGERRRVAICR 175
Cdd:cd03291 124 ------------YDEY---------------RYKSVVKAC---QLEEDITKFPEKDNTVLGEGGI-TLSGGQRARISLAR 172
|
170
....*....|....*....
gi 739061588 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 ... |
160-223 |
7.18e-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: 7.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739061588 160 IEKLSGGERR------RVAICRLLLEKPDMLLLDEPTNHLDAESVAW-LERFLHDYEGT----VVAITHDRYFLD 223
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQknfqLIVITHDEELVD 187
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
328-499 |
7.52e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 328 NLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGT-LVLGDTVKLASvdqfrdsmddSKTVWE 406
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSiLFQGKEIDFKS----------SKEALE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 407 E-VSG-GQDIMRIGNFEIPSRAYVGRFNFKG--VDQGK--------------------RVGELSGGERGRLHLAKLLQVG 462
Cdd:PRK10982 73 NgISMvHQELNLVLQRSVMDNMWLGRYPTKGmfVDQDKmyrdtkaifdeldididpraKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 739061588 463 GNMLLLDEPTNDL---DVETLRALENALLEfPGCAMV-ISH 499
Cdd:PRK10982 153 AKIVIMDEPTSSLtekEVNHLFTIIRKLKE-RGCGIVyISH 192
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
162-226 |
7.95e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.41 E-value: 7.95e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAE----SVAWLERFLHDYEGTVVAITHDRYFLDNVA 226
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLS 139
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
35-218 |
8.24e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.93 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 35 IGVLGLNGAGKSTLLRimaGIDTDIEGEARPQPGIKIGYLPQEPKLN-----------------PEHTVREAVEEAVSEL 97
Cdd:COG0419 26 NLIVGPNGAGKSTILE---AIRYALYGKARSRSKLRSDLINVGSEEAsvelefehggkryrierRQGEFAEFLEAKPSER 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 98 KNALNRL--DEVYAAYADpdadfdKLAKEQGQLEAIIQShdghnLENQLERAAEALRLPEWDAKIEKLSGGERRRVAICR 175
Cdd:COG0419 103 KEALKRLlgLEIYEELKE------RLKELEEALESALEE-----LAELQKLKQEILAQLSGLDPIETLSGGERLRLALAD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739061588 176 LLlekpdMLLLDepTNHLDAESvawLERFLHDYEGTVVaITHD 218
Cdd:COG0419 172 LL-----SLILD--FGSLDEER---LERLLDALEELAI-ITHV 203
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
20-217 |
8.54e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 47.87 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 20 HILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE------------------ARPQpgikIGYLPQEPKLN 81
Cdd:PRK11153 19 HALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRvlvdgqdltalsekelrkARRQ----IGMIFQHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 82 PEHTVREAVEEAVsELKNAlnrldevyaayadPDADFDKlakeqgqleaiiqshdghnlenqleRAAEALRLPEWDAKIE 161
Cdd:PRK11153 95 SSRTVFDNVALPL-ELAGT-------------PKAEIKA-------------------------RVTELLELVGLSDKAD 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739061588 162 K----LSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAE---SV-AWLERFLHDYEGTVVAITH 217
Cdd:PRK11153 136 RypaqLSGGQKQRVAIARALASNPKVLLCDEATSALDPAttrSIlELLKDINRELGLTIVLITH 199
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
139-223 |
8.90e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.83 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 139 NLENQLERAAEALRLPEWDAKIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWL---------ERFLHDYE 209
Cdd:smart00382 37 DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleelrllLLLKSEKN 116
|
90
....*....|....
gi 739061588 210 GTVVAITHDRYFLD 223
Cdd:smart00382 117 LTVILTTNDEKDLG 130
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
324-523 |
9.11e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.95 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 324 LEINnLTKSYGDRVLidDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLasvdqfrdsmDDSKT 403
Cdd:PRK11144 2 LELN-FKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF----------DAEKG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 404 VW---EEvsggqdiMRIGnfeipsraYV-------------G--RFNFKGVDQG---------------KRV-GELSGGE 449
Cdd:PRK11144 69 IClppEK-------RRIG--------YVfqdarlfphykvrGnlRYGMAKSMVAqfdkivallgiepllDRYpGSLSGGE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 450 RGRLHLAKLLQVGGNMLLLDEPTNDLDV----ETLRALENALLEFPGCAMVISHDrwfLD---RIATHIIdYQDEGKVEF 522
Cdd:PRK11144 134 KQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHS---LDeilRLADRVV-VLEQGKVKA 209
|
.
gi 739061588 523 F 523
Cdd:PRK11144 210 F 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-477 |
9.26e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgikIGYLPQEPKLnpeHTVREAVEEAVSELKNAL 101
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGS--------ILFQGKEIDF---KSSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 102 NRLDEVYAayadpdadFDKLAKEQGQLEAIIQSHDghnlenQLERAAEALrLPEWD------AKIEKLSGGERRRVAICR 175
Cdd:PRK10982 83 NLVLQRSV--------MDNMWLGRYPTKGMFVDQD------KMYRDTKAI-FDELDididprAKVATLSVSQMQMIEIAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 176 LLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEgtvvaithdryfldnvagwilelDRGEGIPwegnYSSWLEQKDARL 255
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLK-----------------------ERGCGIV----YISHKMEEIFQL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 256 EQEAateaarhkSIQKELEWIRQNP-KGRQAKGKARLARFEELNSVDYQKRNETSELfippgprlgdkVLEINNLTKSyg 334
Cdd:PRK10982 201 CDEI--------TILRDGQWIATQPlAGLTMDKIIAMMVGRSLTQRFPDKENKPGEV-----------ILEVRNLTSL-- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 335 DRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVK-----------LASVDQFRDS----- 397
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLhGKKINnhnaneainhgFALVTEERRStgiya 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 398 ------------MDDSKTVWEEVSGGQ---------DIMRIgnfEIPSrayvgrfnfkgvdQGKRVGELSGGERGRLHLA 456
Cdd:PRK10982 340 yldigfnslisnIRNYKNKVGLLDNSRmksdtqwviDSMRV---KTPG-------------HRTQIGSLSGGNQQKVIIG 403
|
490 500
....*....|....*....|.
gi 739061588 457 KLLQVGGNMLLLDEPTNDLDV 477
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDV 424
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
339-520 |
9.94e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.47 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTV---------------KLASVDQFRDSMDDSKT 403
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyirpvrkRIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 404 VWEEVSGGQDIMRIGNFEIPSRAY--VGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLD----V 477
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVKNYAHrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqskR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 739061588 478 ETLRALENALLEFPGCAMVISHDrwfLDRIAThiidYQDEGKV 520
Cdd:PRK13646 183 QVMRLLKSLQTDENKTIILVSHD---MNEVAR----YADEVIV 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
322-395 |
1.52e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 1.52e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739061588 322 KVLEINNLTKSYGDRVL-IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVL-GDTVKLASVDQFR 395
Cdd:PRK10522 321 QTLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPVTAEQPEDYR 396
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
162-226 |
1.54e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.08 E-value: 1.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 162 KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAES----VAWLERFLHDYEGTVVAITHDryfLDNVA 226
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSkrqvMRLLKSLQTDENKTIILVSHD---MNEVA 210
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
338-484 |
1.71e-05 |
|
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: 45.72 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 338 LIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPD---SGTLVLGDTVKLASVDQFR-----DSMDDSK----TVW 405
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPgeiiyVSEEDVHfptlTVR 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 406 EEVSggqdimrignFEIPSRayvGRFNFKGVdqgkrvgelSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVETlrALE 484
Cdd:cd03233 102 ETLD----------FALRCK---GNEFVRGI---------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSST--ALE 156
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
323-380 |
2.14e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 2.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 739061588 323 VLEINNLTKSYGDRVLIDdLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL 380
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI 57
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
336-522 |
2.18e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.47 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 336 RVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTlVLGDTvKLASVDQFRDSMDdsKTVW--------EE 407
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR-VWAER-SIAYVPQQAWIMN--ATVRgnilffdeED 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 408 VSGGQDIMRIGNFEIPSRAYVG----RFNFKGVDqgkrvgeLSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVET-LRA 482
Cdd:PTZ00243 749 AARLADAVRVSQLEADLAQLGGgletEIGEKGVN-------LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERV 821
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 739061588 483 LENALL-EFPGCAMVISHDRWFLDRIATHIIDYQDeGKVEF 522
Cdd:PTZ00243 822 VEECFLgALAGKTRVLATHQVHVVPRADYVVALGD-GRVEF 861
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-199 |
2.37e-05 |
|
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: 45.12 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE--------ARPQPG----IKIGYLPQEPK---LNPEHTV 86
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEitldgkpvTRRSPRdairAGIAYVPEDRKregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 87 REAVeeavselknALNRLdevyaayadpdadfdklakeqgqleaiiqshdghnlenqleraaealrlpewdakiekLSGG 166
Cdd:cd03215 96 AENI---------ALSSL----------------------------------------------------------LSGG 108
|
170 180 190
....*....|....*....|....*....|...
gi 739061588 167 ERRRVAICRLLLEKPDMLLLDEPTNHLDAESVA 199
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
342-499 |
2.53e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 342 LSFSIPKGAIVGIIGPNGAGKST----LFRMISGQEQ------------------------PDSGTLVLGdTVKLaSVDQ 393
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSmlnaLFRIVELEKGrimiddcdvakfgltdlrrvlsiiPQSPVLFSG-TVRF-NIDP 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 394 FRDSMDdsKTVWE--EVSGGQDIMRIGNFEIPSRAYVGRFNFkgvdqgkrvgelSGGERGRLHLAKLLQVGGNMLLLDEP 471
Cdd:PLN03232 1333 FSEHND--ADLWEalERAHIKDVIDRNPFGLDAEVSEGGENF------------SVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190
....*....|....*....|....*....|
gi 739061588 472 TNDLDVETLRALENALL-EFPGCAM-VISH 499
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIReEFKSCTMlVIAH 1428
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
22-197 |
3.11e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEarpqpgikIGYlpqepklnpehtvreaveeavselKNA- 100
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGN--------IYY------------------------KNCn 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 101 LNRLDEVYAAYADPDADfdkLAKEQGQLEAIIQSHDGHNLENQLERAAEALRLPEW-DAKIEKLSGGERRRVAICRLLLE 179
Cdd:PRK13541 64 INNIAKPYCTYIGHNLG---LKLEMTVFENLKFWSEIYNSAETLYAAIHYFKLHDLlDEKCYSLSSGMQKIVAIARLIAC 140
|
170
....*....|....*...
gi 739061588 180 KPDMLLLDEPTNHLDAES 197
Cdd:PRK13541 141 QSDLWLLDEVETNLSKEN 158
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
323-371 |
3.53e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 3.53e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISG 371
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-194 |
5.14e-05 |
|
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: 45.97 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 14 IVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI-DTDIEGEA----------RPQPGI--KIGYLPQEPK- 79
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVfingkpvdirNPAQAIraGIAMVPEDRKr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 80 --LNPEHTVREAVEEAVSELKNALNRLDEvyaayadpdadfdklAKEQGQLEAIIQshdghnlenQLERAAEALRLPewd 157
Cdd:TIGR02633 348 hgIVPILGVGKNITLSVLKSFCFKMRIDA---------------AAELQIIGSAIQ---------RLKVKTASPFLP--- 400
|
170 180 190
....*....|....*....|....*....|....*..
gi 739061588 158 akIEKLSGGERRRVAICRLLLEKPDMLLLDEPTNHLD 194
Cdd:TIGR02633 401 --IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-218 |
5.19e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.50 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 24 NISLSFFPGAKIGVLGLNGAGKS-TLLRIMAGID--------------TDI----EGEARPQPGIKIGYLPQEP--KLNP 82
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgrvmaeklefngQDLqrisEKERRNLVGAEVAMIFQDPmtSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 83 EHTVREAVEEAvselknalnrldevyaayadpdadfdklakeqgqleaiIQSHDGHNLENQLERAAEALRL---PEWDAK 159
Cdd:PRK11022 105 CYTVGFQIMEA--------------------------------------IKVHQGGNKKTRRQRAIDLLNQvgiPDPASR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739061588 160 IE----KLSGGERRRVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEG----TVVAITHD 218
Cdd:PRK11022 147 LDvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkenmALVLITHD 213
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
339-380 |
6.31e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 6.31e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 739061588 339 IDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTL 380
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
322-363 |
1.03e-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: 43.61 E-value: 1.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 739061588 322 KVLEINNLtKSYGDRVLIDdlsfsIPKGaIVGIIGPNGAGKS 363
Cdd:cd03278 2 KKLELKGF-KSFADKTTIP-----FPPG-LTAIVGPNGSGKS 36
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
444-518 |
1.29e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 43.76 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 444 ELSGGERGRLHLAKLLQ---VGGNMLLLDEPTNDL---DVETLRALENALLEFPGCAMVISHDrwfLD--RIATHIIDYQ 515
Cdd:cd03271 169 TLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLhfhDVKKLLEVLQRLVDKGNTVVVIEHN---LDviKCADWIIDLG 245
|
...
gi 739061588 516 DEG 518
Cdd:cd03271 246 PEG 248
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
323-539 |
1.62e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.63 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQE--QPDSGTLVL--GDTVKLASVDQFRDSM 398
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFkgKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 399 DDSKTVWEEVSGGQDIMRIGNFEIPSRAYVG-----RFNFKGVDQGK---------------RVGeLSGGERGRLHLAKL 458
Cdd:PRK09580 81 FMAFQYPVEIPGVSNQFFLQTALNAVRSYRGqepldRFDFQDLMEEKiallkmpedlltrsvNVG-FSGGEKKRNDILQM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 459 LQVGGNMLLLDEPTNDLDVETLRALE---NALLEFPGCAMVISHDRWFLDRIATHIIDYQDEGKVeFFEGNFTEYEEYKK 535
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRI-VKSGDFTLVKQLEE 238
|
....
gi 739061588 536 RTLG 539
Cdd:PRK09580 239 QGYG 242
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-190 |
1.70e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 43.33 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 18 KRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGidtdiegEARPQPGiKIGYLPQE-PKLNPEHTVREAVEeAVSE 96
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-------DPRATSG-RIVFDGKDiTDWQTAKIMREAVA-IVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 97 LKNALNRLD-EVYAAYADPDADfdklaKEQGQlEAIIQSHD--GHNLENQLERAAealrlpewdakieKLSGGERRRVAI 173
Cdd:PRK11614 88 GRRVFSRMTvEENLAMGGFFAE-----RDQFQ-ERIKWVYElfPRLHERRIQRAG-------------TMSGGEQQMLAI 148
|
170
....*....|....*..
gi 739061588 174 CRLLLEKPDMLLLDEPT 190
Cdd:PRK11614 149 GRALMSQPRLLLLDEPS 165
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-218 |
1.90e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 43.33 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFfPGAKIGVL-GLNGAGKSTLLRIMAGIDTDIEGEAR--PQPGIK------IGYLPQEPKLNPEHTVreAVEE 92
Cdd:PRK15056 23 LRDASFTV-PGGSIAALvGVNGSGKSTLFKALMGFVRLASGKISilGQPTRQalqknlVAYVPQSEEVDWSFPV--LVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 93 AVselknalnrldeVYAAYAdpdadfdklakEQGQLEaIIQSHDGHNLENQLERAAealRLPEWDAKIEKLSGGERRRVA 172
Cdd:PRK15056 100 VV------------MMGRYG-----------HMGWLR-RAKKRDRQIVTAALARVD---MVEFRHRQIGELSGGQKKRVF 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 739061588 173 ICRLLLEKPDMLLLDEPTNHLDAESVAW---LERFLHDYEGTVVAITHD 218
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARiisLLRELRDEGKTMLVSTHN 201
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
21-170 |
2.69e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 21 ILKNISLSFFPGAKIgVLGLNGAGKSTLLR-IMAGIDTDIEGEA----RPQPGIKIGYLPQEPKLNPEHTVREAVEEAVS 95
Cdd:COG4717 13 KFRDRTIEFSPGLNV-IYGPNEAGKSTLLAfIRAMLLERLEKEAdelfKPQGRKPELNLKELKELEEELKEAEEKEEEYA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 96 ELKNALN----RLDEVYAAYADPDADFDKLAKEQGQLEAIIQSHDghnLENQLERAAEalRLPEWDAKIEKLSGGERRR 170
Cdd:COG4717 92 ELQEELEeleeELEELEAELEELREELEKLEKLLQLLPLYQELEA---LEAELAELPE--RLEELEERLEELRELEEEL 165
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
163-238 |
5.11e-04 |
|
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: 41.15 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 163 LSGGERRRVAICRLLLE--KPDMLLLDEPTNHLDAESvawLERFLHDYEG------TVVAITHDRYFLDNvAGWILELDR 234
Cdd:cd03238 88 LSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQD---INQLLEVIKGlidlgnTVILIEHNLDVLSS-ADWIIDFGP 163
|
....
gi 739061588 235 GEGI 238
Cdd:cd03238 164 GSGK 167
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-218 |
7.14e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 42.33 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGEARPQpGIKIGYLpQEPKLNPEHTVREAVEEAVSELKNAL 101
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID-GVDIAKI-SDAELREVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 102 NRLDEVyaAYADPDADFDKLAKEQGQLEAIIQShdghNLENQleraaeALRLPEwdakieKLSGGERRRVAICRLLLEKP 181
Cdd:PRK10070 122 TVLDNT--AFGMELAGINAEERREKALDALRQV----GLENY------AHSYPD------ELSGGMRQRVGLARALAINP 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 739061588 182 DMLLLDEPTNHLD----AESVAWLERFLHDYEGTVVAITHD 218
Cdd:PRK10070 184 DILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
163-241 |
7.30e-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: 42.69 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 163 LSGGERRRVAICRLLLEK---PDMLLLDEPTNHLDAESVAWLERFLH---DYEGTVVAITHDryfLD--NVAGWILEL-- 232
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQrlvDKGNTVVVIEHN---LDviKTADYIIDLgp 906
|
90
....*....|....*..
gi 739061588 233 ---DRG-----EGIPWE 241
Cdd:TIGR00630 907 eggDGGgtvvaSGTPEE 923
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
160-223 |
1.13e-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: 1.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 160 IEKLSGGERR---RVAICRLLLEKPDMLLLDEPTNHLDAESVAWLERFL---HDYEGTVVAITHDRYFLD 223
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLkelSRNGAQLILTTHSPLLLD 303
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
316-392 |
1.21e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 316 GPRLGD-KVLEINNLTKSYGDRVLID---DLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTLVLGDTVKLASV 391
Cdd:PTZ00265 374 GKKLKDiKKIQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDI 453
|
.
gi 739061588 392 D 392
Cdd:PTZ00265 454 N 454
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
445-518 |
1.45e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 445 LSGGERGRLHLAKLLQ---VGGNMLLLDEPTNDL---DVETLRALENALLEFPGCAMVISHDrwfLDRI--ATHIIDYQD 516
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLhfdDIKKLLEVLQRLVDKGNTVVVIEHN---LDVIktADYIIDLGP 906
|
..
gi 739061588 517 EG 518
Cdd:TIGR00630 907 EG 908
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
351-507 |
1.48e-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: 40.84 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 351 IVGIIGPNGAGKSTLFRMISgqeqpdsgtlVLGDTVKLASVDQFRDSMDDSKTVWEEVSGGQDIMRIGNFEIP-----SR 425
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALR----------FLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISefledGV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 426 AYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTND--LDVETLRALENALLEFPGCAMVISHDRWF 503
Cdd:pfam13304 71 RYRYGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRlgLDVEERIELSLSELSDLISGLLLLSIISP 150
|
....
gi 739061588 504 LDRI 507
Cdd:pfam13304 151 LSFL 154
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-63 |
1.73e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.03 E-value: 1.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGI------DTDIEGEA 63
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtmpnkgTVDIKGSA 87
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
22-225 |
1.77e-03 |
|
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: 40.76 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 22 LKNISLSFFPGakIGVL-GLNGAGKSTLLRIMAGIdtdIEGEARPQPGIKIGYLPQEPKLnPEHTVREAVEEAVSELKNA 100
Cdd:COG3593 14 IKDLSIELSDD--LTVLvGENNSGKSSILEALRLL---LGPSSSRKFDEEDFYLGDDPDL-PEIEIELTFGSLLSRLLRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 101 L---NRLDEVYAAYADPDADFDKLAKEqgqLEAIIQSHDGHNLEN-QLERAAEALRLPEWDAK------------IEKLS 164
Cdd:COG3593 88 LlkeEDKEELEEALEELNEELKEALKA---LNELLSEYLKELLDGlDLELELSLDELEDLLKSlslriedgkelpLDRLG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739061588 165 GGERRRV--AICRLLLE-----KPDMLLLDEPTNHLDAESVAWLERFLHDYEGT---VVAITHDRYFLDNV 225
Cdd:COG3593 165 SGFQRLIllALLSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKpnqVIITTHSPHLLSEV 235
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
334-479 |
1.98e-03 |
|
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: 39.53 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 334 GDRVLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEqpDSGTL---VLGDTVKL--------ASVDQFrDSMDDSK 402
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK--TAGVItgeILINGRPLdknfqrstGYVEQQ-DVHSPNL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739061588 403 TVWEEVsggqdimrignfeipsrayvgRF--NFKGvdqgkrvgeLSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVET 479
Cdd:cd03232 95 TVREAL---------------------RFsaLLRG---------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
445-513 |
2.16e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 2.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739061588 445 LSGGERGRLHLAKLL---QVGGNMLLLDEPTNDL---DVETL-RALeNALLEFPGCAMVISHDrwfLDRIAT--HIID 513
Cdd:COG0178 827 LSGGEAQRVKLASELskrSTGKTLYILDEPTTGLhfhDIRKLlEVL-HRLVDKGNTVVVIEHN---LDVIKTadWIID 900
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
322-370 |
3.26e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (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: 213242 [Multi-domain] Cd Length: 247 Bit Score: 39.48 E-value: 3.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 739061588 322 KVLEINNLtKSYGDRVLIDDL-SFSipkgaivGIIGPNGAGKSTLFRMIS 370
Cdd:cd03275 2 KRLELENF-KSYKGRHVIGPFdRFT-------CIIGPNGSGKSNLMDAIS 43
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
160-237 |
3.39e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 160 IEKLSGGERR------RVAICRLLLEKPDMLLLDEPTNHLDAESVAWL----ERFLHDYEG--TVVAITHDRYFLdNVAG 227
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLkdiiEYSLKDSSDipQVIMISHHRELL-SVAD 877
|
90
....*....|
gi 739061588 228 WILELDRGEG 237
Cdd:PRK01156 878 VAYEVKKSSG 887
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-62 |
4.12e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 4.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 739061588 22 LKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDTDIEGE 62
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
323-508 |
4.35e-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: 39.67 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 323 VLEINNLTKSYGD----RVLIDDLSFSIPKGAIVGIIGPNGAGKS----TLFRMISGQEQPDSGTLVLGDtvklasvdqf 394
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDG---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 395 RDSMDDSKTVWEEVSGG------QD-------IMRIGN--FEI----------PSRAYVgrfnfkgVDQGKRVG------ 443
Cdd:COG4172 76 QDLLGLSERELRRIRGNriamifQEpmtslnpLHTIGKqiAEVlrlhrglsgaAARARA-------LELLERVGipdper 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 444 -------ELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDVeTLRA--LEnaLL-----EFpGCAMV-ISHD----RWFL 504
Cdd:COG4172 149 rldayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQAqiLD--LLkdlqrEL-GMALLlITHDlgvvRRFA 224
|
....
gi 739061588 505 DRIA 508
Cdd:COG4172 225 DRVA 228
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
331-363 |
4.57e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 4.57e-03
10 20 30
....*....|....*....|....*....|...
gi 739061588 331 KSYGDRVLIDdlsfsIPKGaIVGIIGPNGAGKS 363
Cdd:TIGR02168 11 KSFADPTTIN-----FDKG-ITGIVGPNGCGKS 37
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
439-513 |
4.77e-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: 40.00 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739061588 439 GKRVGELSGGERGRLHLAKllQVG----GNMLLLDEPT-------NDLDVET---LRALENALLefpgcamVISHDRWFL 504
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLAT--QIGsgltGVLYVLDEPSiglhqrdNRRLINTlkrLRDLGNTLI-------VVEHDEDTI 553
|
....*....
gi 739061588 505 dRIATHIID 513
Cdd:TIGR00630 554 -RAADYVID 561
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
324-370 |
6.04e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.83 E-value: 6.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 739061588 324 LEINNLtKSYGDRvlidDLSFSIPKGAIVgIIGPNGAGKSTLFRMIS 370
Cdd:COG3950 6 LTIENF-RGFEDL----EIDFDNPPRLTV-LVGENGSGKTTLLEAIA 46
|
|
| |
