|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-639 |
0e+00 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 745.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQELPRADE 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 RIVFDVVAEGLAEVGKLLAEYHHLSLNIHTD---DDLARLSRVQQELEARDGWRLQQLVDSTLSRLQLPADKTLAELSGG 157
Cdd:PRK11147 81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDpseKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 158 WRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLIDWNGDYAS 237
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 238 FLVHKEQQLAAEEAANALFDKRLAQEEVWIRQGIKARRTRNEGRVRALKEMRRERAERRERQGKASFQLESADKSGKQVI 317
Cdd:PRK11147 241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRSGKIVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 318 VVEHVSFAHPGGQpLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEVAYFDQLRHQLEPEQT 397
Cdd:PRK11147 321 EMENVNYQIDGKQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 398 VIDNISEGREFITIDGQNRHVLSYLGDFLFSPQRARTPVKALSGGERARLLLAKLFSKPANLLVLDEPTNDLDVETLELL 477
Cdd:PRK11147 400 VMDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 478 EEVLLGFQGTVLMVSHDRAFLDNVVTSTLVFEGEGKVREFVGGYQDWLRQGGTPRLLGVSESKSGKAElntalapaaepa 557
Cdd:PRK11147 480 EELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQQQAQYLALKQPAVKKKEEA------------ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 558 PAAAAPSEAPAKKKLSYKLQRELEALPGQIDAVEAELAGVQETIAQQDFYLRPQDEQRETLARLDALQQELDALLERWAE 637
Cdd:PRK11147 548 AAPKAETVKRSSKKLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLADLADAEQELEVAFERWEE 627
|
..
gi 15598215 638 LE 639
Cdd:PRK11147 628 LE 629
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-527 |
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: 597.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 6 FTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQELPRADERIVFD 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 86 VVAEGLAEVGKLLAEYHHLSLNI-HTDDDLARLSRVQQELEARDGWRLQQLVDSTLSRLQLPA---DKTLAELSGGWRRR 161
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLaEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEedlDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 162 VLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLIDWNGDYASFLVH 241
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 242 KEQQLAAEEAANALFDKRLAQEEVWIRQ-GIKARR-TRNEGRVRALKEMRRERAERRErqGKASFQLESADKSGKQVIVV 319
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARKaKQAQSRIKALEKLEREEPPRRD--KTVEIRFPPPERLGKKVLEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 320 EHVSFAHpGGQPLVRDFSMVLQRGDRIGLLGANgtgkttllklllgDLQPTSGKIEVGTKLEVAYFDQLRHQLEPEQTVI 399
Cdd:COG0488 319 EGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNgagkstllkllagELEPDSGTVKLGETVKIGYFDQHQEELDPDKTVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 400 DNISEGREfitiDGQNRHVLSYLGDFLFSPQRARTPVKALSGGERARLLLAKLFSKPANLLVLDEPTNDLDVETLELLEE 479
Cdd:COG0488 398 DELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEE 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15598215 480 VLLGFQGTVLMVSHDRAFLDNVVTSTLVFEgEGKVREFVGGYQDWLRQ 527
Cdd:COG0488 474 ALDDFPGTVLLVSHDRYFLDRVATRILEFE-DGGVREYPGGYDDYLEK 520
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
29-524 |
5.75e-118 |
|
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: 362.72 E-value: 5.75e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 29 GERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQELPRADERIVFDVVAEGLAEVGKLLAEYHHLSLNI 108
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEISAKY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 109 HTDDD-----LARLSRVQQELEARDGWRLQQLVDSTLSRLQLPA-DKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTN 182
Cdd:TIGR03719 111 AEPDAdfdklAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 183 HLDIGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLIDWNGDYASFLVHKEQQLAAEEAANALFDKRLAQ 262
Cdd:TIGR03719 191 HLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLEQEEKEESARQKTLKR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 263 EEVWIRQGIKARRTRNEGRVRALKEMRRERAERRErqGKASFQLESADKSGKQVIVVEHVSFAHpGGQPLVRDFSMVLQR 342
Cdd:TIGR03719 271 ELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRN--ETAEIYIPPGPRLGDKVIEAENLTKAF-GDKLLIDDLSFKLPP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 343 GDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEVAYFDQLRHQLEPEQTVIDNISEGREFITIDgqNRHVLS-- 420
Cdd:TIGR03719 348 GGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKLG--KREIPSra 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 421 YLGDFLFSPQRARTPVKALSGGERARLLLAKLFSKPANLLVLDEPTNDLDVETLELLEEVLLGFQGTVLMVSHDRAFLDN 500
Cdd:TIGR03719 426 YVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDR 505
|
490 500
....*....|....*....|....
gi 15598215 501 VVTSTLVFEGEGKVREFVGGYQDW 524
Cdd:TIGR03719 506 IATHILAFEGDSHVEWFEGNFSEY 529
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-523 |
1.72e-112 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 348.65 E-value: 1.72e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 34 VIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQELPRADERIVFDVVAEGLAEVGKLLAEYHHLSLNIHTDDD 113
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRFNEIYAAYAEPDA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 114 -----LARLSRVQQELEARDGWRLqqlvDSTLSR----LQLPA-DKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNH 183
Cdd:PRK11819 118 dfdalAAEQGELQEIIDAADAWDL----DSQLEIamdaLRCPPwDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 184 LDIGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLIDWNGDYASFLVHKEQQLAAEEAANALFDKRLAQE 263
Cdd:PRK11819 194 LDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAKRLAQEEKQEAARQKALKRE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 264 EVWIRQGIKARRTRNEGRVRALKEMRRERAERRErqGKASFQLESADKSGKQVIVVEHVSFAHpGGQPLVRDFSMVLQRG 343
Cdd:PRK11819 274 LEWVRQSPKARQAKSKARLARYEELLSEEYQKRN--ETNEIFIPPGPRLGDKVIEAENLSKSF-GDRLLIDDLSFSLPPG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 344 DRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEVAYFDQLRHQLEPEQTVIDNISEGREFITIDgqNRHVLS--Y 421
Cdd:PRK11819 351 GIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKVG--NREIPSraY 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 422 LGDFLFSPQRARTPVKALSGGERARLLLAKLFSKPANLLVLDEPTNDLDVETLELLEEVLLGFQGTVLMVSHDRAFLDNV 501
Cdd:PRK11819 429 VGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRI 508
|
490 500
....*....|....*....|..
gi 15598215 502 VTSTLVFEGEGKVREFVGGYQD 523
Cdd:PRK11819 509 ATHILAFEGDSQVEWFEGNFQE 530
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-529 |
3.46e-65 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 223.23 E-value: 3.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 13 FGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQELPRADERIVFDVVAEGLA 92
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVIMGHT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 93 EVGKLLAEYHHL-SLNIHTDDDLARLSrvqqELEAR----DGWRLQQLVDSTLSRLQLPADK---TLAELSGGWRRRVLL 164
Cdd:PRK15064 91 ELWEVKQERDRIyALPEMSEEDGMKVA----DLEVKfaemDGYTAEARAGELLLGVGIPEEQhygLMSEVAPGWKLRVLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 165 AQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLIDWNGDYASFLVH--- 241
Cdd:PRK15064 167 AQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAatq 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 242 -KEQQLAaeeaanalfDKRLAQEEVWIRQGIKARRTRNEGRVRALKEMRRERAERRERQGKAS------FQLESADKSGK 314
Cdd:PRK15064 247 aRERLLA---------DNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLEEVKPSsrqnpfIRFEQDKKLHR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 315 QVIVVEHVSFAHPGGqPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEVAYFDQ-LRHQLE 393
Cdd:PRK15064 318 NALEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdHAYDFE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 394 PEQTVIDNISEGREfitiDGQNRHVL-SYLGDFLFSPQRARTPVKALSGGERARLLLAKLFSKPANLLVLDEPTNDLDVE 472
Cdd:PRK15064 397 NDLTLFDWMSQWRQ----EGDDEQAVrGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598215 473 TLELLEEVLLGFQGTVLMVSHDRAFLDNVVTSTLVFEGEGkVREFVGGYQDWLRQGG 529
Cdd:PRK15064 473 SIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDG-VVDFSGTYEEYLRSQG 528
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-627 |
3.15e-58 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 206.94 E-value: 3.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 6 FTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQELPrADERIVFD 85
Cdd:PRK10636 4 FSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETP-ALPQPALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 86 VVAEGLAEVGKLLAEYHHLslNIHTDDDLarLSRVQQELEARDGWRLQQLVDSTLSRL---QLPADKTLAELSGGWRRRV 162
Cdd:PRK10636 83 YVIDGDREYRQLEAQLHDA--NERNDGHA--IATIHGKLDAIDAWTIRSRAASLLHGLgfsNEQLERPVSDFSGGWRMRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 163 LLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLIDWNGDYASFLVHK 242
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 243 EQQLAAEEAANALFDKRLAQEEVWI-RQGIKARRTRN-EGRVRALKEMRRERAERRERQGKASFQleSADKSGKQVIVVE 320
Cdd:PRK10636 239 ATRLAQQQAMYESQQERVAHLQSYIdRFRAKATKAKQaQSRIKMLERMELIAPAHVDNPFHFSFR--APESLPNPLLKME 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 321 HVSfAHPGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEVAYFDQlrHQLE---PEQT 397
Cdd:PRK10636 317 KVS-AGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ--HQLEflrADES 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 398 VIDNISEgrefITIDGQNRHVLSYLGDFLFSPQRARTPVKALSGGERARLLLAKLFSKPANLLVLDEPTNDLDVETLELL 477
Cdd:PRK10636 394 PLQHLAR----LAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 478 EEVLLGFQGTVLMVSHDRAFLDNvVTSTLVFEGEGKVREFVG---GYQDWL--------RQGGTPRLLGVSESKSGK--- 543
Cdd:PRK10636 470 TEALIDFEGALVVVSHDRHLLRS-TTDDLYLVHDGKVEPFDGdleDYQQWLsdvqkqenQTDEAPKENNANSAQARKdqk 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 544 ---AELNTalapaaepapaaaapseapakkkLSYKLQRELEALPGQIDAVEAELAGVQETIAQQDFYlrpqDEQRETlAR 620
Cdd:PRK10636 549 rreAELRT-----------------------QTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELY----DQSRKA-EL 600
|
....*..
gi 15598215 621 LDALQQE 627
Cdd:PRK10636 601 TACLQQQ 607
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-239 |
9.37e-55 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 194.90 E-value: 9.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQELPRAD-E 80
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDpD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 RIVFDVVAEGLAEvgkllaeyhhlslnihtdddlarlsrvQQELEARdgwrlqqlvdSTLSRLQLP---ADKTLAELSGG 157
Cdd:COG0488 394 KTVLDELRDGAPG---------------------------GTEQEVR----------GYLGRFLFSgddAFKPVGVLSGG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 158 WRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLIDWNGDYAS 237
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDD 516
|
..
gi 15598215 238 FL 239
Cdd:COG0488 517 YL 518
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-227 |
1.10e-49 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 169.55 E-value: 1.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQelpraderiv 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 84 fdvvaeglaevgkllaeyhhlslnihtdddlarlsrvqqeleardgwrlqqlvdstlsrlqlpadktlaeLSGGWRRRVL 163
Cdd:cd03221 71 ----------------------------------------------------------------------LSGGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598215 164 LAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGH 227
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
10-526 |
1.74e-49 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 183.91 E-value: 1.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 10 SLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKgeQQADDGevwrAPA-LKIGELPQELPrADERIVFDVVA 88
Cdd:PLN03073 184 SISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDG----IPKnCQILHVEQEVV-GDDTTALQCVL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 89 EGLAEVGKLLAEYHHL------------------SLNIHTDDDLA--RLSRVQQELEARDGWRLQQLVDSTLSRLQLPAD 148
Cdd:PLN03073 257 NTDIERTQLLEEEAQLvaqqrelefetetgkgkgANKDGVDKDAVsqRLEEIYKRLELIDAYTAEARAASILAGLSFTPE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 149 ---KTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDR 225
Cdd:PLN03073 337 mqvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 226 GHLIDWNGDYASFLVHKEQQLAAEEAANALFDKRLAQEEVWI---RQGIKaRRTRNEGRVRALKEMRRERAERRERQGKA 302
Cdd:PLN03073 417 QKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIdkfRYNAK-RASLVQSRIKALDRLGHVDAVVNDPDYKF 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 303 SFQLESaDKSGKQVIVVEHVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEV 382
Cdd:PLN03073 496 EFPTPD-DRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRM 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 383 AYFDQlRHQLEPEQTVIDNISEGREFITIDGQNrhVLSYLGDFLFSPQRARTPVKALSGGERARLLLAKL-FSKPaNLLV 461
Cdd:PLN03073 575 AVFSQ-HHVDGLDLSSNPLLYMMRCFPGVPEQK--LRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKItFKKP-HILL 650
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598215 462 LDEPTNDLDVETLELLEEVLLGFQGTVLMVSHDRAFLDNVVTSTLVFEgEGKVREFVGGYQDWLR 526
Cdd:PLN03073 651 LDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVS-EGKVTPFHGTFHDYKK 714
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-228 |
2.56e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 141.77 E-value: 2.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV------WRAPALKIGELPQE 74
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgkpPRRARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 75 LpRADERI---VFDVVAEGLaevgkllaeYHHLSLnihtdddLARLSRVQQELeardgwrlqqlVDSTLSRLQLP--ADK 149
Cdd:COG1121 84 A-EVDWDFpitVRDVVLMGR---------YGRRGL-------FRRPSRADREA-----------VDEALERVGLEdlADR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 150 TLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG---AVLFITHDRAFLQSLATRILELDRG 226
Cdd:COG1121 136 PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRG 215
|
..
gi 15598215 227 HL 228
Cdd:COG1121 216 LV 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-229 |
4.05e-36 |
|
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: 135.94 E-value: 4.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW-----------RAPALKIGEL 71
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlaslsrRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 72 PQELPRADERIVFDVVAeglaevgklLAEYHHLSLnihtdddLARLSrvqqeleARDgwrlQQLVDSTLSRLQLP--ADK 149
Cdd:COG1120 81 PQEPPAPFGLTVRELVA---------LGRYPHLGL-------FGRPS-------AED----REAVEEALERTGLEhlADR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 150 TLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIG-AIAWLE--EALLGFNG-AVLFITHDRAFLQSLATRILELDR 225
Cdd:COG1120 134 PVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAhQLEVLEllRRLARERGrTVVMVLHDLNLAARYADRLVLLKD 213
|
....
gi 15598215 226 GHLI 229
Cdd:COG1120 214 GRIV 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-242 |
1.70e-32 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 131.94 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 8 DVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQELPR--ADERIVFD 85
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYdfENDLTLFD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 86 VVAEGLAEvgkllaeyhhlslnihTDDDlarlsrvqqeleardgwrlqQLVDSTLSRLQLPAD---KTLAELSGGWRRRV 162
Cdd:PRK15064 404 WMSQWRQE----------------GDDE--------------------QAVRGTLGRLLFSQDdikKSVKVLSGGEKGRM 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 163 LLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLIDWNGDYASFLVHK 242
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-228 |
1.53e-31 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 120.58 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV-------WRAPAL---KIGELPQ 73
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdiKKEPEEvkrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 74 ELPraderivfdvvaeglaevgkllaEYHHLSlnihtdddlarlsrVQQELEardgwrlqqlvdstlsrlqlpadktlae 153
Cdd:cd03230 81 EPS-----------------------LYENLT--------------VRENLK---------------------------- 95
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598215 154 LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFN---GAVLFITHDRAFLQSLATRILELDRGHL 228
Cdd:cd03230 96 LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-229 |
7.88e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 120.55 E-value: 7.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW--------RAPALK--IGELPQ 73
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvarDPAEVRrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 74 ElPRADERI-VFDVVaeglaevgKLLAEYHHLSlnihtdddlarlsrvQQELEARdgwrlqqlVDSTLSRLQLP--ADKT 150
Cdd:COG1131 81 E-PALYPDLtVRENL--------RFFARLYGLP---------------RKEARER--------IDELLELFGLTdaADRK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 151 LAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG---AVLFITHDRAFLQSLATRILELDRGH 227
Cdd:COG1131 129 VGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
..
gi 15598215 228 LI 229
Cdd:COG1131 209 IV 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-225 |
2.59e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 118.35 E-value: 2.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapaLKIGELPQELPRADERI 82
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVL----WNGEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VFdvvaeglaeVGKLLAEYHHLSL--NIHTdddLARLSRVQQELEArdgwrlqqlVDSTLSRLQLP--ADKTLAELSGGW 158
Cdd:COG4133 78 AY---------LGHADGLKPELTVreNLRF---WAALYGLRADREA---------IDEALEAVGLAglADLPVRQLSAGQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 159 RRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFN---GAVLFITHDRAFLqsLATRILELDR 225
Cdd:COG4133 137 KRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLEL--AAARVLDLGD 204
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
317-512 |
6.39e-30 |
|
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: 114.85 E-value: 6.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHpGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEVAYFDQLrhqlepeq 396
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 397 tvidnisegrefitidgqnrhvlsylgdflfspqrartpvkalSGGERARLLLAKLFSKPANLLVLDEPTNDLDVETLEL 476
Cdd:cd03221 72 -------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598215 477 LEEVLLGFQGTVLMVSHDRAFLDNVVTSTLVFEGEG 512
Cdd:cd03221 109 LEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-229 |
1.05e-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: 117.05 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAF-GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW-----------RAPALKIGEL 71
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdgkditkknlRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 72 PQelpRADERIVFDVVAEglaevgkllaeyhhlslnihtddDLA------RLSRvqQELEARdgwrlqqlVDSTLSRLQL 145
Cdd:COG1122 81 FQ---NPDDQLFAPTVEE-----------------------DVAfgpenlGLPR--EEIRER--------VEEALELVGL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 146 P--ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGA---VLFITHDRAFLQSLATRI 220
Cdd:COG1122 125 EhlADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAELADRV 204
|
....*....
gi 15598215 221 LELDRGHLI 229
Cdd:COG1122 205 IVLDDGRIV 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-227 |
1.52e-29 |
|
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: 116.03 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 5 KFTDVSLAFGT--TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRApalkigelpqelpraDERI 82
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD---------------GKDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VFDVVAEGLAEVGKLLAEYHHLSLNIHTDDDLA----RLSRVQQELEARDGWRLQQLvdstlsRLQLPADKTLAELSGGW 158
Cdd:cd03225 66 TKLSLKELRRKVGLVFQNPDDQFFGPTVEEEVAfgleNLGLPEEEIEERVEEALELV------GLEGLRDRSPFTLSGGQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598215 159 RRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGA---VLFITHDRAFLQSLATRILELDRGH 227
Cdd:cd03225 140 KQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-228 |
2.13e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 115.68 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW---------RAPAL--KIGELP 72
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsamPPPEWrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 73 QELPRADERivfdvVAEGLAEVgkllAEYHHLSLNIHTDDDLarlsrvqqeleardgwrlqqlvdstLSRLQLPA---DK 149
Cdd:COG4619 81 QEPALWGGT-----VRDNLPFP----FQLRERKFDRERALEL-------------------------LERLGLPPdilDK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 150 TLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF----NGAVLFITHDRAFLQSLATRILELDR 225
Cdd:COG4619 127 PVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEA 206
|
...
gi 15598215 226 GHL 228
Cdd:COG4619 207 GRL 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-232 |
2.77e-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: 115.32 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 5 KFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPA------LKIGELPQ--ELP 76
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerKRIGYVPQrrSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 77 RaDERI-VFDVVAEGLaevgkllaeYHHLSLnihtdddLARLSRVQQELeardgwrlqqlVDSTLSRLQLP--ADKTLAE 153
Cdd:cd03235 81 R-DFPIsVRDVVLMGL---------YGHKGL-------FRRLSKADKAK-----------VDEALERVGLSelADRQIGE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 154 LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG---AVLFITHDRAFLQSLATRILELDRgHLID 230
Cdd:cd03235 133 LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNR-TVVA 211
|
..
gi 15598215 231 WN 232
Cdd:cd03235 212 SG 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-229 |
6.80e-29 |
|
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: 115.57 E-value: 6.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQ-QADDGEV---------WRAPALK--I 68
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVrlfgerrggEDVWELRkrI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 69 G----ELPQELPRaDERiVFDVVAEGL-AEVGkLLAEYhhlslnihTDDDLARlsrVQQELEArdgWRLQQLvdstlsrl 143
Cdd:COG1119 81 GlvspALQLRFPR-DET-VLDVVLSGFfDSIG-LYREP--------TDEQRER---ARELLEL---LGLAHL-------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 144 qlpADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL--LGFNG--AVLFITHDRAFLQSLATR 219
Cdd:COG1119 136 ---ADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLdkLAAEGapTLVLVTHHVEEIPPGITH 212
|
250
....*....|
gi 15598215 220 ILELDRGHLI 229
Cdd:COG1119 213 VLLLKDGRVV 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-229 |
2.22e-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: 113.80 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapaLKIGELPQELPR-ADER 81
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSI-----LIDGEDVRKEPReARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 IVFDVVAEGLaevgkllaeYHHLSL--NIHTdddLARLSRVQQEleardgwRLQQLVDSTLSRLQL--PADKTLAELSGG 157
Cdd:COG4555 76 IGVLPDERGL---------YDRLTVreNIRY---FAELYGLFDE-------ELKKRIEELIELLGLeeFLDRRVGELSTG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598215 158 WRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF---NGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:COG4555 137 MKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-466 |
5.89e-28 |
|
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: 118.08 E-value: 5.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MT-LLKFTDVSLAF--GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFK----------VVKGEQQADDGEVWRAPAL- 66
Cdd:COG1123 1 MTpLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALalmgllphggRISGEVLLDGRDLLELSEAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 67 ---KIGELPQELPRA-DERIVFDVVAEGLAevgkllaeyhhlslnihtdddLARLSRvqQELEARDGWRLQQLvdstlsR 142
Cdd:COG1123 81 rgrRIGMVFQDPMTQlNPVTVGDQIAEALE---------------------NLGLSR--AEARARVLELLEAV------G 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 143 LQLPADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD----IGAIAWLEEALLGFNGAVLFITHDRAFLQSLAT 218
Cdd:COG1123 132 LERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIAD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 219 RILELDRGHLIdWNGDYASFLVHkeqqlaaeeaanalfDKRLAQEEVWIRQGIKARRTRNEGRVralkemrreraerrer 298
Cdd:COG1123 212 RVVVMDDGRIV-EDGPPEEILAA---------------PQALAAVPRLGAARGRAAPAAAAAEP---------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 299 qgkasfqlesadksgkqVIVVEHVSFAHP----GGQPLVRDFSMVLQRGDRIGLLGANgtgkttllklllgdLQPTSGKI 374
Cdd:COG1123 260 -----------------LLEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESgsgkstlarlllglLRPTSGSI 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 375 EV-GTKLEVAYFDQLR--------------HQLEPEQTVIDNISEG-REFITIDGQNRH--VLSYLGDFLFSPQRARTPV 436
Cdd:COG1123 323 LFdGKDLTKLSRRSLRelrrrvqmvfqdpySSLNPRMTVGDIIAEPlRLHGLLSRAERRerVAELLERVGLPPDLADRYP 402
|
490 500 510
....*....|....*....|....*....|.
gi 15598215 437 KALSGGERARLLLAK-LFSKPAnLLVLDEPT 466
Cdd:COG1123 403 HELSGGQRQRVAIARaLALEPK-LLILDEPT 432
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-221 |
1.11e-27 |
|
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: 117.73 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQELPRAD-ERI 82
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDpNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VFDVVAEGLaevgkllaeyHHLSLNIHTDDDLARLSRVQqeLEARDgwrlQQlvdstlsrlqlpadKTLAELSGGWRRRV 162
Cdd:TIGR03719 403 VWEEISGGL----------DIIKLGKREIPSRAYVGRFN--FKGSD----QQ--------------KKVGQLSGGERNRV 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598215 163 LLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRIL 221
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHIL 511
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-229 |
1.23e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 109.83 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 8 DVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkigelpqelpraderivFDvv 87
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL----------------------LD-- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 88 aeglaevGKLLAEYHHLslnihtddDLAR-LSRVQQELEArdgWRLQQLvdstlsrlqlpADKTLAELSGGWRRRVLLAQ 166
Cdd:cd03214 60 -------GKDLASLSPK--------ELARkIAYVPQALEL---LGLAHL-----------ADRPFNELSGGERQRVLLAR 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598215 167 ALVAEPDLLLLDEPTNHLDIG-AIAWLEeaLL-----GFNGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:cd03214 111 ALAQEPPILLLDEPTSHLDIAhQIELLE--LLrrlarERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-227 |
3.15e-26 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 105.02 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 5 KFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRapalkigelpqelpraderivf 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 85 dvvaeglaevgkllaeyhhlslnihtdDDLARLSRVQQELEARDGWRLQqlvdstlsrlqlpadktlaeLSGGWRRRVLL 164
Cdd:cd00267 59 ---------------------------DGKDIAKLPLEELRRRIGYVPQ--------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 165 AQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG---AVLFITHDRAFLQSLATRILELDRGH 227
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-239 |
6.85e-26 |
|
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: 106.60 E-value: 6.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW----RAPALKIGELpQELPRa 78
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvdgqDITGLSEKEL-YELRR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 79 deRI--------------VFDVVAeglaevgkllaeyhhLSLNIHTDddlarLSrvqqELEARDgwrlqqLVDSTLSRLQ 144
Cdd:COG1127 83 --RIgmlfqggalfdsltVFENVA---------------FPLREHTD-----LS----EAEIRE------LVLEKLELVG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 145 LP--ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD-IGA------IAWLEEALlgfNGAVLFITHDRAFLQS 215
Cdd:COG1127 131 LPgaADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpITSavidelIRELRDEL---GLTSVVVTHDLDSAFA 207
|
250 260
....*....|....*....|....
gi 15598215 216 LATRILELDRGHLIdWNGDYASFL 239
Cdd:COG1127 208 IADRVAVLADGKII-AEGTPEELL 230
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-221 |
9.00e-26 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 111.75 E-value: 9.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQElpRA---DE 80
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQS--RDaldPN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 RIVFDVVAEGL--AEVGKllaeyhhlslnihtdddlarlsrvqQELEAR-----------DgwrlQQlvdstlsrlqlpa 147
Cdd:PRK11819 403 KTVWEEISGGLdiIKVGN-------------------------REIPSRayvgrfnfkggD----QQ------------- 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598215 148 dKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRIL 221
Cdd:PRK11819 441 -KKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHIL 513
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-229 |
4.41e-25 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 103.74 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAF----GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRA--PALKIGELPQELP 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgkDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 77 RADERIVFdvvAEGLA------EVGKLLAEyhhlSLNIHTDDDLARLSRVQQELEARdgwrlqqlvdstlsrlQLPADKT 150
Cdd:cd03257 81 RKEIQMVF---QDPMSslnprmTIGEQIAE----PLRIHGKLSKKEARKEAVLLLLV----------------GVGLPEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 151 LA-----ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIgAIAWLEEALL-----GFNGAVLFITHDRAFLQSLATRI 220
Cdd:cd03257 138 VLnryphELSGGQRQRVAIARALALNPKLLIADEPTSALDV-SVQAQILDLLkklqeELGLTLLFITHDLGVVAKIADRV 216
|
....*....
gi 15598215 221 LELDRGHLI 229
Cdd:cd03257 217 AVMYAGKIV 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-233 |
9.63e-25 |
|
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: 102.97 E-value: 9.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 6 FTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW----RAPALKIGELpQELPRadeR 81
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgeDISGLSEAEL-YRLRR---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 I--------------VFDVVAEGLAEvgkllaeyhhlslniHTdddlaRLSRvqqeleardgWRLQQLVDSTLSRLQLPA 147
Cdd:cd03261 79 MgmlfqsgalfdsltVFENVAFPLRE---------------HT-----RLSE----------EEIREIVLEKLEAVGLRG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 148 DKTL--AELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD-IGA------IAWLEEALlgfNGAVLFITHDRAFLQSLAT 218
Cdd:cd03261 129 AEDLypAELSGGMKKRVALARALALDPELLLYDEPTAGLDpIASgviddlIRSLKKEL---GLTSIMVTHDLDTAFAIAD 205
|
250
....*....|....*
gi 15598215 219 RILELDRGHLIdWNG 233
Cdd:cd03261 206 RIAVLYDGKIV-AEG 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-229 |
1.48e-24 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 101.83 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRApalkiGELPQELPRADERI- 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID-----GRDVTGVPPERRNIg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 -VFDVvaeglaevgklLAEYHHLSL--NIHTDDDLARLSRvqQELEARDGWRLQQLvdstlsRLQLPADKTLAELSGGWR 159
Cdd:cd03259 76 mVFQD-----------YALFPHLTVaeNIAFGLKLRGVPK--AEIRARVRELLELV------GLEGLLNRYPHELSGGQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598215 160 RRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGA----VLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:cd03259 137 QRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRElgitTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-229 |
1.56e-24 |
|
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: 102.52 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV-------WRAPALKIGEL----- 71
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgediTGLPPHEIARLgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 72 ---PQELPRADeriVFDVVaeglaevgkLLAEYHHLSLNIHtdddLARLSRVQQELEARdgwrlqqlVDSTLSRLQLP-- 146
Cdd:cd03219 81 fqiPRLFPELT---VLENV---------MVAAQARTGSGLL----LARARREEREARER--------AEELLERVGLAdl 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 147 ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPT---NHLDIGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILEL 223
Cdd:cd03219 137 ADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVL 216
|
....*.
gi 15598215 224 DRGHLI 229
Cdd:cd03219 217 DQGRVI 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-223 |
1.87e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.16 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 12 AFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQ--ELPRADERIVFDVVAE 89
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsEVPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 90 GLaevgkllaeYHHLSLnihtdddLARLSRvqqelEARdgwrlqQLVDSTLSRLQLP--ADKTLAELSGGWRRRVLLAQA 167
Cdd:NF040873 81 GR---------WARRGL-------WRRLTR-----DDR------AAVDDALERVGLAdlAGRQLGELSGGQRQRALLAQG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598215 168 LVAEPDLLLLDEPTNHLDIGAIAWLEEAL---LGFNGAVLFITHDRAfLQSLATRILEL 223
Cdd:NF040873 134 LAQEADLLLLDEPTTGLDAESRERIIALLaeeHARGATVVVVTHDLE-LVRRADPCVLL 191
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-230 |
1.89e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 102.05 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGT-TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW------------RAPAL--KI 68
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrlkrrEIPYLrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 69 GELPQE---LPradERIVFDVVAEGLAEVGKLLAEYHhlslnihtdddlarlSRVQQELEardgwrlqqLVDstLSRLql 145
Cdd:COG2884 82 GVVFQDfrlLP---DRTVYENVALPLRVTGKSRKEIR---------------RRVREVLD---------LVG--LSDK-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 146 pADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFN--G-AVLFITHDRAFLQSLATRILE 222
Cdd:COG2884 131 -AKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINrrGtTVLIATHDLELVDRMPKRVLE 209
|
....*...
gi 15598215 223 LDRGHLID 230
Cdd:COG2884 210 LEDGRLVR 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-221 |
2.05e-24 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 101.78 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGT----TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV------WRAPALKIGELPQ 73
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 74 E---LPRadeRIVFDVVAEGLAEVGKLLAEyhhlslnihtdddlaRLSRVQQELEardgwrlqqLVDstlsrLQLPADKT 150
Cdd:cd03293 81 QdalLPW---LTVLDNVALGLELQGVPKAE---------------ARERAEELLE---------LVG-----LSGFENAY 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598215 151 LAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLG----FNGAVLFITHD--RAFLqsLATRIL 221
Cdd:cd03293 129 PHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwreTGKTVLLVTHDidEAVF--LADRVV 203
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-221 |
2.99e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 102.48 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAF----GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW------RAPALKIGE 70
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvTGPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 71 LPQE---LPRadeRIVFDVVAEGLAEVGKLLAEyhhlslnihtdddlaRLSRVQQELEardgwrlqqLVDstLSRLqlpA 147
Cdd:COG1116 85 VFQEpalLPW---LTVLDNVALGLELRGVPKAE---------------RRERARELLE---------LVG--LAGF---E 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 148 DKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDigAI------AWLEEALLGFNGAVLFITHDR--AFLqsLATR 219
Cdd:COG1116 133 DAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALD--ALtrerlqDELLRLWQETGKTVLFVTHDVdeAVF--LADR 208
|
..
gi 15598215 220 IL 221
Cdd:COG1116 209 VV 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-229 |
6.06e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 101.27 E-value: 6.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW-------RAPALKIGEL-- 71
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrditGLPPHRIARLgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 72 ------PQELPRADeriVFDVVaeglaevgkLLAEYHHLSLNIHtdDDLARLSRVQQELEArdgwrLQQLVDSTLSRLQL 145
Cdd:COG0411 82 artfqnPRLFPELT---VLENV---------LVAAHARLGRGLL--AALLRLPRARREERE-----ARERAEELLERVGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 146 P--ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPT---NHLDIGAIAWLEEALLGFNG-AVLFITHDRAFLQSLATR 219
Cdd:COG0411 143 AdrADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADR 222
|
250
....*....|
gi 15598215 220 ILELDRGHLI 229
Cdd:COG0411 223 IVVLDFGRVI 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-230 |
8.42e-24 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 99.60 E-value: 8.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalkigelpqelpRADERIV 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI----------------TFDGKSY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 84 FDVvAEGLAEVGKLLaEYHHLSLNIHTDDDLARLSRVQQELEARdgwrlqqlVDSTLSRLQLP--ADKTLAELSGGWRRR 161
Cdd:cd03268 65 QKN-IEALRRIGALI-EAPGFYPNLTARENLRLLARLLGIRKKR--------IDEVLDVVGLKdsAKKKVKGFSLGMKQR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598215 162 VLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLG---FNGAVLFITHDRAFLQSLATRILELDRGHLID 230
Cdd:cd03268 135 LGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSlrdQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-230 |
5.65e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.99 E-value: 5.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPL---------LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV-WRAPALkiGE 70
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLsgkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVsWRGEPL--AK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 71 LPQELPRADERIVFDVVAEGLA------EVGKLLAE--YHHLSLnihtdDDLARLSRVQQELEARDgwrlqqLVDSTLSR 142
Cdd:PRK10419 79 LNRAQRKAFRRDIQMVFQDSISavnprkTVREIIREplRHLLSL-----DKAERLARASEMLRAVD------LDDSVLDK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 143 LQlpadktlAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDI----GAIAWLEEALLGFNGAVLFITHDRAFLQSLAT 218
Cdd:PRK10419 148 RP-------PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQ 220
|
250
....*....|..
gi 15598215 219 RILELDRGHLID 230
Cdd:PRK10419 221 RVMVMDNGQIVE 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-229 |
1.51e-22 |
|
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: 97.18 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGT----TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW-----------RAPALK 67
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgrpvtrrrrKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 68 IGELPQElPRA--DER-IVFDVVAEGLAevgkllaeyHHlslniHTDDDLARLSRVqqeleardgwrlqqlvdstLSRLQ 144
Cdd:COG1124 81 VQMVFQD-PYAslHPRhTVDRILAEPLR---------IH-----GLPDREERIAEL-------------------LEQVG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 145 LPA---DKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIG----AIAWLEEALLGFNGAVLFITHDRAFLQSLA 217
Cdd:COG1124 127 LPPsflDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSvqaeILNLLKDLREERGLTYLFVSHDLAVVAHLC 206
|
250
....*....|..
gi 15598215 218 TRILELDRGHLI 229
Cdd:COG1124 207 DRVAVMQNGRIV 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-229 |
1.60e-22 |
|
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: 101.52 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAF-----GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV-------WRAPALKIG 69
Cdd:COG1123 259 PLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdlTKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 70 ELPQEL------------PRadeRIVFDVVAEGLAevgkllaeyhhlslnIHTDDDlarlsrvQQELEARdgwrlqqlVD 137
Cdd:COG1123 339 ELRRRVqmvfqdpysslnPR---MTVGDIIAEPLR---------------LHGLLS-------RAERRER--------VA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 138 STLSRLQLP---ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLG----FNGAVLFITHDR 210
Cdd:COG1123 386 ELLERVGLPpdlADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlqreLGLTYLFISHDL 465
|
250
....*....|....*....
gi 15598215 211 AFLQSLATRILELDRGHLI 229
Cdd:COG1123 466 AVVRYIADRVAVMYDGRIV 484
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-229 |
2.85e-22 |
|
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: 101.00 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAF--GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkIGELP-QELPRADE 80
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT------LGGVDlRDLDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 RivfDVVAeglaevgkLLAEYHHL---SL--NIH------TDDDLAR-LSRVQqeleardgwrLQQLVDSTLSRLQLPAD 148
Cdd:COG4987 408 R---RRIA--------VVPQRPHLfdtTLreNLRlarpdaTDEELWAaLERVG----------LGDWLAALPDGLDTWLG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 149 KTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF--NGAVLFITHDRAFLQsLATRILELDRG 226
Cdd:COG4987 467 EGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAGLE-RMDRILVLEDG 545
|
...
gi 15598215 227 HLI 229
Cdd:COG4987 546 RIV 548
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-182 |
5.54e-22 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 92.71 E-value: 5.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW-----------RAPALKIGELPQELPRADERIVFDVV 87
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 88 AEGLaevgkLLAEYHHLSLNIHTDDDLARLSRVqqELEARdgwrlqqlvdstlsrlqlPADKTLAELSGGWRRRVLLAQA 167
Cdd:pfam00005 81 RLGL-----LLKGLSKREKDARAEEALEKLGLG--DLADR------------------PVGERPGTLSGGQRQRVAIARA 135
|
170
....*....|....*
gi 15598215 168 LVAEPDLLLLDEPTN 182
Cdd:pfam00005 136 LLTKPKLLLLDEPTA 150
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-229 |
6.43e-22 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 94.18 E-value: 6.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVcVIGRNGTGKSSLFKVVKGEQQADDGEVWR--APALK--------IGELPQ 73
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIdgQDVLKqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 74 ElPRADERI-VFDVVaeglaevgkllaeyhhlslnihtdDDLARLSRVQQEleardgwRLQQLVDSTLSRLQLP--ADKT 150
Cdd:cd03264 80 E-FGVYPNFtVREFL------------------------DYIAWLKGIPSK-------EVKARVDEVLELVNLGdrAKKK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 151 LAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL--LGFNGAVLFITHDRAFLQSLATRILELDRGHL 228
Cdd:cd03264 128 IGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLseLGEDRIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
.
gi 15598215 229 I 229
Cdd:cd03264 208 V 208
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-245 |
3.52e-21 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 97.93 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQ---ELPRAD 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQhqlEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 80 ErivfdvvaeglaevgkllAEYHHlslnihtdddLARLSRVQQELEARD-----GWRLQQLVDSTlsrlqlpadktlAEL 154
Cdd:PRK10636 392 E------------------SPLQH----------LARLAPQELEQKLRDylggfGFQGDKVTEET------------RRF 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 155 SGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLIDWNG- 233
Cdd:PRK10636 432 SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGd 511
|
250
....*....|....
gi 15598215 234 --DYASFLVHKEQQ 245
Cdd:PRK10636 512 leDYQQWLSDVQKQ 525
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-229 |
6.21e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 91.88 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAF--GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwRAPALKIGEL-PQELPR--- 77
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV-LLDGTDIRQLdPADLRRnig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 78 ---ADERIVFDVVAEGLAevgkllaeyhhLSLNIHTDDDLARLSRVQQeleardgwrLQQLVDSTLSRLQLPADKTLAEL 154
Cdd:cd03245 82 yvpQDVTLFYGTLRDNIT-----------LGAPLADDERILRAAELAG---------VTDFVNKHPNGLDLQIGERGRGL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598215 155 SGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG--AVLFITHDRAFLQsLATRILELDRGHLI 229
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-242 |
7.74e-21 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 96.75 E-value: 7.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAF-GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV--------------WRApalKI 68
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdldpasWRR---QI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 69 GELPQelpraDERIVFDVVAEGLAeVGKLLAeyhhlslnihTDDDLAR-LSRVQqeleardgwrLQQLVDstlsrlQLPA 147
Cdd:COG4988 414 AWVPQ-----NPYLFAGTIRENLR-LGRPDA----------SDEELEAaLEAAG----------LDEFVA------ALPD 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 148 --DKTLAE----LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF--NGAVLFITHDRAFLQsLATR 219
Cdd:COG4988 462 glDTPLGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLA-QADR 540
|
250 260
....*....|....*....|...
gi 15598215 220 ILELDRGHLIDwNGDYASFLVHK 242
Cdd:COG4988 541 ILVLDDGRIVE-QGTHEELLAKN 562
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
4-229 |
1.28e-20 |
|
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: 91.80 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV-----------WRAPALKIGELP 72
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVdlagvdlhglsRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 73 QELPRADERIVFDVVAeglaevgklLAEYHHLSL-NIHTDDDLArlsrvqqeleardgwrlqqLVDSTLSRLQLP--ADK 149
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVA---------LGRIPHRSLwAGDSPHDAA-------------------VVDRALARTELShlADR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 150 TLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGA----IAWLEEaLLGFNGAVLFITHDRAFLQSLATRILELDR 225
Cdd:TIGR03873 134 DMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAqletLALVRE-LAATGVTVVAALHDLNLAASYCDHVVVLDG 212
|
....
gi 15598215 226 GHLI 229
Cdd:TIGR03873 213 GRVV 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-186 |
2.36e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.75 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW-----------RAPALKIG 69
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddvealsaRAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 70 ELPQelpraDERIVFDVVAEGLAEVGKllaeYHHLS-LNIHTDDDLARlsrVQQELEARDGWRLqqlvdstlsrlqlpAD 148
Cdd:PRK09536 81 SVPQ-----DTSLSFEFDVRQVVEMGR----TPHRSrFDTWTETDRAA---VERAMERTGVAQF--------------AD 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598215 149 KTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDI 186
Cdd:PRK09536 135 RPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-229 |
2.96e-20 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 90.09 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRApalkiGELPQELPRADERIV 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG-----GEDATDVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 84 FdvvaeglaeVGKLLAEYHHLSLNihtdDDLARLSRVQQELEARDGWRLQQLVDSTLSRLQLP--ADKTLAELSGGWRRR 161
Cdd:cd03296 78 F---------VFQHYALFRHMTVF----DNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDwlADRYPAQLSGGQRQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598215 162 VLLAQALVAEPDLLLLDEPTNHLDIGA----IAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVrkelRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-226 |
4.11e-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: 4.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAF------GTT-PLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapaLKIGELPQE 74
Cdd:COG4778 3 TLLEVENLSKTFtlhlqgGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL----VRHDGGWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 75 LPRADERIVF-----------------------DVVAEGLAEVGkllaeyhhlslnihTDDDLARLsrvqqelEARDgwr 131
Cdd:COG4778 79 LAQASPREILalrrrtigyvsqflrviprvsalDVVAEPLLERG--------------VDREEARA-------RARE--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 132 lqqlvdsTLSRLQLPadKTLAEL-----SGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIG----AIAWLEEALLgfNG- 201
Cdd:COG4778 135 -------LLARLNLP--ERLWDLppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAAnravVVELIEEAKA--RGt 203
|
250 260
....*....|....*....|....*
gi 15598215 202 AVLFITHDRAFLQSLATRILELDRG 226
Cdd:COG4778 204 AIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-230 |
9.68e-20 |
|
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: 89.48 E-value: 9.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 17 PLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV-WRAPALKigELPQELPRADERIVFDVVAEGLAEV- 94
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsFRGQDLY--QLDRKQRRAFRRDVQLVFQDSPSAVn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 95 -----GKLLAE--YHHLSLnihtdDDLARLSRVQQELEARDgwrlqqLVDSTLSRLQlpadktlAELSGGWRRRVLLAQA 167
Cdd:TIGR02769 103 prmtvRQIIGEplRHLTSL-----DESEQKARIAELLDMVG------LRSEDADKLP-------RQLSGGQLQRINIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598215 168 LVAEPDLLLLDEPTNHLDI----GAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLID 230
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-229 |
1.02e-19 |
|
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: 88.54 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 17 PLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRApalkiGELPQElpradERIVFdvvaegLAEVGK 96
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA-----GLVPWK-----RRKKF------LRRIGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 97 LLAEYHHLSLNIHTDDDLARLSRVQQELEARDGWRLQQLVDstLSRLQLPADKTLAELSGGWRRRVLLAQALVAEPDLLL 176
Cdd:cd03267 99 VFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSE--LLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598215 177 LDEPTNHLDIGAIAWLEEALLGFN----GAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNrergTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-221 |
1.19e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.15 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFG----TTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalKIGELPQELP 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI------TLDGVPVTGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 77 RADERIVF------------DVVAEGLaevgkllaeyhhlslnihtddDLARLSRVQQELEARdgwRLQQLVDstlsrLQ 144
Cdd:COG4525 75 GADRGVVFqkdallpwlnvlDNVAFGL---------------------RLRGVPKAERRARAE---ELLALVG-----LA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 145 LPADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF----NGAVLFITHD--RAFLqsLAT 218
Cdd:COG4525 126 DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwqrtGKGVFLITHSveEALF--LAT 203
|
...
gi 15598215 219 RIL 221
Cdd:COG4525 204 RLV 206
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-230 |
2.26e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.41 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAFGT----TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkIGElpQELPR 77
Cdd:COG1136 3 PLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVL------IDG--QDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 78 ADERivfdvvaeglaEVGKLLAEY-------HHL--SL----NIHTDDDLARLSRvqQELEARdgwrlqqlVDSTLSRLQ 144
Cdd:COG1136 75 LSER-----------ELARLRRRHigfvfqfFNLlpELtaleNVALPLLLAGVSR--KERRER--------ARELLERVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 145 LP--ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD----IGAIAWLEEALLGFNGAVLFITHDRAfLQSLAT 218
Cdd:COG1136 134 LGdrLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgEEVLELLRELNRELGTTIVMVTHDPE-LAARAD 212
|
250
....*....|..
gi 15598215 219 RILELDRGHLID 230
Cdd:COG1136 213 RVIRLRDGRIVS 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-229 |
3.94e-19 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 86.85 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKG-----EQQADDGEVWRAPA--LKIGELPQELP 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKdiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 77 RadeRI-------------VFDVVAEGLAEVGKLLAEyhhlslnihtdddlarlsrvqqELEARdgwrlqqlVDSTLSRL 143
Cdd:cd03260 81 R---RVgmvfqkpnpfpgsIYDNVAYGLRLHGIKLKE----------------------ELDER--------VEEALRKA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 144 QLP---ADKTLA-ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG--AVLFITHDRAFLQSLA 217
Cdd:cd03260 128 ALWdevKDRLHAlGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQQAARVA 207
|
250
....*....|..
gi 15598215 218 TRILELDRGHLI 229
Cdd:cd03260 208 DRTAFLLNGRLV 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-228 |
4.40e-19 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 86.39 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFG----TTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRApalkiGELPQELP--- 76
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD-----GTDISKLSeke 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 77 RADERivfdvvaegLAEVGKLLAEYH---HLSL--NIHTDDDLARLSRVQQELEARDgwrlqqlvdsTLSRLQLP--ADK 149
Cdd:cd03255 76 LAAFR---------RRHIGFVFQSFNllpDLTAleNVELPLLLAGVPKKERRERAEE----------LLERVGLGdrLNH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 150 TLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG----AVLFITHDRaFLQSLATRILELDR 225
Cdd:cd03255 137 YPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeagtTIVVVTHDP-ELAEYADRIIELRD 215
|
...
gi 15598215 226 GHL 228
Cdd:cd03255 216 GKI 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-227 |
5.56e-19 |
|
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: 84.74 E-value: 5.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTT--PLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalKIGELP-QELPRADE 80
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI------LIDGVDlRDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 RivfdvvaeglaevgkllaeyhhlslnihtdddlARLSRVQQeleardgwrlqqlvDSTLsrlqlpADKTLAE--LSGGW 158
Cdd:cd03228 75 R---------------------------------KNIAYVPQ--------------DPFL------FSGTIREniLSGGQ 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598215 159 RRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG--AVLFITHDRAFLQsLATRILELDRGH 227
Cdd:cd03228 102 RQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-223 |
5.98e-19 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 90.42 E-value: 5.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAF-GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV--------------WRAPALKI 68
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladadadsWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 69 GELPQelpraderIVFDVVAEGLAevgkllaeyhhLSLNIHTDDDLARLSRvqqeleaRDGwrLQQLVDSTLSRLQLPAD 148
Cdd:TIGR02857 402 PQHPF--------LFAGTIAENIR-----------LARPDASDAEIREALE-------RAG--LDEFVAALPQGLDTPIG 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598215 149 KTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF--NGAVLFITHDRAfLQSLATRILEL 223
Cdd:TIGR02857 454 EGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLA-LAALADRIVVL 529
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-229 |
6.79e-19 |
|
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: 91.05 E-value: 6.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFG--TTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV--------------WRApalK 67
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqidpasLRR---Q 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 68 IGELPQelpraDERIVFDVVAEglaevgkllaeyhhlslNIH------TDDDL---ARLSRVQQELEAR-DGWRLQqlvd 137
Cdd:COG2274 551 IGVVLQ-----DVFLFSGTIRE-----------------NITlgdpdaTDEEIieaARLAGLHDFIEALpMGYDTV---- 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 138 stlsrlqlpadktLAE----LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG--AVLFITHDRA 211
Cdd:COG2274 605 -------------VGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLS 671
|
250
....*....|....*...
gi 15598215 212 FLQsLATRILELDRGHLI 229
Cdd:COG2274 672 TIR-LADRIIVLDKGRIV 688
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-229 |
1.26e-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: 87.85 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkIGE-----LPqel 75
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL------LDGrdvtgLP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 76 prADER---IVF---------DV---VAEGLaevgkllaeyhhlslnihtddDLARLSRvqQELEARdgwrlqqlVDSTL 140
Cdd:COG3842 74 --PEKRnvgMVFqdyalfphlTVaenVAFGL---------------------RMRGVPK--AEIRAR--------VAELL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 141 SRLQLP--ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD----------IGAIawLEEallgFNGAVLFITH 208
Cdd:COG3842 121 ELVGLEglADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklreemreeLRRL--QRE----LGITFIYVTH 194
|
250 260
....*....|....*....|...
gi 15598215 209 DR--AFlqSLATRILELDRGHLI 229
Cdd:COG3842 195 DQeeAL--ALADRIAVMNDGRIE 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-209 |
1.32e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.94 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQELpRADE 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKL-YLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 RIVFDVvaeglaevgkllAEYHHLSLNIHTDDDLARLSRVQQeleardgwrlQQLVDSTLSRlqlpadktlaeLSGGWRR 160
Cdd:PRK09544 81 TLPLTV------------NRFLRLRPGTKKEDILPALKRVQA----------GHLIDAPMQK-----------LSGGETQ 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598215 161 RVLLAQALVAEPDLLLLDEPTNHLDI-GAIA---WLEEALLGFNGAVLFITHD 209
Cdd:PRK09544 128 RVLLARALLNRPQLLVLDEPTQGVDVnGQVAlydLIDQLRRELDCAVLMVSHD 180
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-226 |
1.59e-18 |
|
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: 84.61 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkigelpqelprADERIV 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY----------------IGGRDV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 84 FDVVAE--GLAEVGKLLAEYHHLSL--NIHTDDDLARLSRvqQELEARdgwrlqqlVDSTLSRLQLPA--DKTLAELSGG 157
Cdd:cd03301 65 TDLPPKdrDIAMVFQNYALYPHMTVydNIAFGLKLRKVPK--DEIDER--------VREVAELLQIEHllDRKPKQLSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598215 158 WRRRVLLAQALVAEPDLLLLDEPTNHLDigaiAWLEEALLG--------FNGAVLFITHDRAFLQSLATRILELDRG 226
Cdd:cd03301 135 QRQRVALGRAIVREPKVFLMDEPLSNLD----AKLRVQMRAelkrlqqrLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-209 |
1.75e-18 |
|
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: 88.96 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAF-GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapaLKIGELPQELPRADERI 82
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV-----TLDGVPVSSLDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VFDVVAEGLAEVGKLLAEYHHLSLNIHTDDDLAR-LSRVqqeleardgwRLQQLVDSTLSRLQLPADKTLAELSGGWRRR 161
Cdd:TIGR02868 410 RVSVCAQDAHLFDTTVRENLRLARPDATDEELWAaLERV----------GLADWLRALPDGLDTVLGEGGARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598215 162 VLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALL-GFNG-AVLFITHD 209
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLaALSGrTVVLITHH 529
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-227 |
2.48e-18 |
|
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: 83.01 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkigelpqelpraderiv 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 84 FDvvaeglaevgkllaeyhhlslnihtDDDLARLSRVQQELEARDGWRLQQLvdstlsrlQLPADKTLAE-----LSGGW 158
Cdd:cd03229 59 ID-------------------------GEDLTDLEDELPPLRRRIGMVFQDF--------ALFPHLTVLEnialgLSGGQ 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598215 159 RRRVLLAQALVAEPDLLLLDEPTNHLD----IGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGH 227
Cdd:cd03229 106 QQRVALARALAMDPDVLLLDEPTSALDpitrREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-228 |
2.50e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 84.76 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEvwrapaLKIGELPQELPRADERI 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGD------LIVDGLKVNDPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VfdvvaegLAEVGKLLAEYH---HLSL-------NIHTdddlARLSRVQQELEARDgwrlqqlvdsTLSRLQLP--ADKT 150
Cdd:PRK09493 75 I-------RQEAGMVFQQFYlfpHLTAlenvmfgPLRV----RGASKEEAEKQARE----------LLAKVGLAerAHHY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 151 LAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD----------IGAIAwlEEALlgfngAVLFITHDRAFLQSLATRI 220
Cdd:PRK09493 134 PSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDpelrhevlkvMQDLA--EEGM-----TMVIVTHEIGFAEKVASRL 206
|
....*...
gi 15598215 221 LELDRGHL 228
Cdd:PRK09493 207 IFIDKGRI 214
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
571-640 |
3.36e-18 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 79.05 E-value: 3.36e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 571 KLSYKLQRELEALPGQIDAVEAELAGVQETIAQQDFYLRPqDEQRETLARLDALQQELDALLERWAELED 640
Cdd:pfam16326 1 KLSYKEQRELEELEAEIEKLEEEIAELEAQLADPELYSDY-EKLQELSAELEELEAELEELYERWEELEE 69
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-229 |
7.86e-18 |
|
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: 83.01 E-value: 7.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTT----PLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW--------------RAP 64
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllsgkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 65 ALKIGELPQELPRADERIVFDVVAeglaevgkllaeyhhLSLNIHTDDDLARLSRVQQELEardgwrlqqLVDstlsrLQ 144
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVA---------------LPLEIAGVPKAEIEERVLELLE---------LVG-----LE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 145 LPADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG----AVLFITHDRAFLQSLATRI 220
Cdd:cd03258 132 DKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelglTIVLITHEMEVVKRICDRV 211
|
....*....
gi 15598215 221 LELDRGHLI 229
Cdd:cd03258 212 AVMEKGEVV 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-228 |
1.26e-17 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 82.07 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAF-GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW------------RAPAL--KI 68
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngqdvsdlrgrAIPYLrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 69 GELPQELPRADERIVFDVVAEGLAEVGkllaeyhhlslniHTDDDLARlsRVQQELEardgwrlqqLVDstlsrLQLPAD 148
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTG-------------VPPREIRK--RVPAALE---------LVG-----LSHKHR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 149 KTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGA---VLFITHDRAFLQSLATRILELDR 225
Cdd:cd03292 132 ALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAgttVVVATHAKELVDTTRHRVIALER 211
|
...
gi 15598215 226 GHL 228
Cdd:cd03292 212 GKL 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-231 |
2.23e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 82.27 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKV------------VKGEQQADDGEVWRAPALK- 67
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLDGQDIFKMDVIEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 68 ------IGELPQELPRADeriVFDVVAEGLaevgkllaeyhhlslnihtddDLARLSRVQQELEARDGWRLQ--QLVDST 139
Cdd:PRK14247 81 rrrvqmVFQIPNPIPNLS---IFENVALGL---------------------KLNRLVKSKKELQERVRWALEkaQLWDEV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 140 LSRLQLPAdktlAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG--AVLFITHDRAFLQSLA 217
Cdd:PRK14247 137 KDRLDAPA----GKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTHFPQQAARIS 212
|
250
....*....|....
gi 15598215 218 TRILELDRGHLIDW 231
Cdd:PRK14247 213 DYVAFLYKGQIVEW 226
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
4-231 |
3.33e-17 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 81.18 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPAlkigELPQELPRADERI- 82
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGH----DLRRAPRAALARLg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 -VFDVVAEGLaevgkllaeyhHLSL--NIHTDDDLARLSRvqQELEARdgwrlqqlVDSTLSRLQLP--ADKTLAELSGG 157
Cdd:TIGR03864 78 vVFQQPTLDL-----------DLSVrqNLRYHAALHGLSR--AEARAR--------IAELLARLGLAerADDKVRELNGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 158 WRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEE---ALLGFNG-AVLFITH--DRAflqSLATRILELDRGHLIDW 231
Cdd:TIGR03864 137 HRRRVEIARALLHRPALLLLDEPTVGLDPASRAAITAhvrALARDQGlSVLWATHlvDEI---EASDRLVVLHRGRVLAD 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-229 |
3.37e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.46 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV-W------RAPALKIGELPQE-- 74
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlWdgepldPEDRRRIGYLPEErg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 75 LP---RADERIVFdvvaeglaevgklLAEYHHLSLNihtdDDLARLsrvqqelearDGWrlqqlvdstLSRLQLP--ADK 149
Cdd:COG4152 82 LYpkmKVGEQLVY-------------LARLKGLSKA----EAKRRA----------DEW---------LERLGLGdrANK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 150 TLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF--NGA-VLFITHDRAFLQSLATRILELDRG 226
Cdd:COG4152 126 KVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGTtVIFSSHQMELVEELCDRIVIINKG 205
|
...
gi 15598215 227 HLI 229
Cdd:COG4152 206 RKV 208
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-229 |
4.82e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 82.89 E-value: 4.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 8 DVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkIGE--LPQELPRADERI--- 82
Cdd:COG1118 7 NISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIV------LNGrdLFTNLPPRERRVgfv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 -----------VFDVVAEGLaevgkllaeyhhlslnihtdddlarlsRVQQELEARdgwrLQQLVDSTLSRLQLP--ADK 149
Cdd:COG1118 81 fqhyalfphmtVAENIAFGL---------------------------RVRPPSKAE----IRARVEELLELVQLEglADR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 150 TLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDigaiA--------WLEEALLGFNGAVLFITHDR--AFlqSLATR 219
Cdd:COG1118 130 YPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALD----AkvrkelrrWLRRLHDELGGTTVFVTHDQeeAL--ELADR 203
|
250
....*....|
gi 15598215 220 ILELDRGHLI 229
Cdd:COG1118 204 VVVMNQGRIE 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-228 |
5.35e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 80.27 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkIGELPQELPRADERIV 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTII------IDGLKLTDDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 84 fdvvaegLAEVGKLLAEYH---HLSL--NIhtddDLA-----RLSRVQQELEARDgwrlqqlvdsTLSRLQLP--ADKTL 151
Cdd:cd03262 75 -------RQKVGMVFQQFNlfpHLTVleNI----TLApikvkGMSKAEAEERALE----------LLEKVGLAdkADAYP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 152 AELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDigaIAWLEEAL-----LGFNG-AVLFITHDRAFLQSLATRILELDR 225
Cdd:cd03262 134 AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD---PELVGEVLdvmkdLAEEGmTMVVVTHEMGFAREVADRVIFMDD 210
|
...
gi 15598215 226 GHL 228
Cdd:cd03262 211 GRI 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-226 |
5.73e-17 |
|
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: 79.99 E-value: 5.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 18 LLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV-----WRAPAL---KIGELPQELpraDERIVFDVVAE 89
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkPIKAKErrkSIGYVMQDV---DYQLFTDSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 90 GLAEVGKLLaeyhhlslnihtDDDLARLSRVQQELEardgwrLQQLVDstlsrlQLPADktlaeLSGGWRRRVLLAQALV 169
Cdd:cd03226 92 ELLLGLKEL------------DAGNEQAETVLKDLD------LYALKE------RHPLS-----LSGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 170 AEPDLLLLDEPTNHLDIGA---IAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRG 226
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNmerVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-229 |
5.74e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.57 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW----------RAPALKIGE 70
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 71 LPQelpraderivFDvvaeglaevgkllaeyhHLSLNIHTDDDLARLSRVQQeLEARDgwrLQQLVDSTL--SRLQLPAD 148
Cdd:PRK13536 119 VPQ----------FD-----------------NLDLEFTVRENLLVFGRYFG-MSTRE---IEAVIPSLLefARLESKAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 149 KTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEE---ALLGFNGAVLFITHDRAFLQSLATRILELDR 225
Cdd:PRK13536 168 ARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWErlrSLLARGKTILLTTHFMEEAERLCDRLCVLEA 247
|
....
gi 15598215 226 GHLI 229
Cdd:PRK13536 248 GRKI 251
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-229 |
6.30e-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: 80.03 E-value: 6.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 29 GERVCVIGRNGTGKSSLFKVVKGEQQAD------DGEVWRAPALKIgelpqELPRADERIVFdVVAEglaevgklLAEYH 102
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDggtivlNGTVLFDSRKKI-----NLPPQQRKIGL-VFQQ--------YALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 103 HLSLNIHTDDDLARLSRVQQeleardgwrlQQLVDSTLSRLQLP--ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEP 180
Cdd:cd03297 89 HLNVRENLAFGLKRKRNRED----------RISVDELLDLLGLDhlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598215 181 TNHLDIGA----IAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:cd03297 159 FSALDRALrlqlLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-228 |
8.77e-17 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 79.97 E-value: 8.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapaLKIGELPQELPrADER-- 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI-----LLDGKDITNLP-PHKRpv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 -IVFdvvaeglaevgKLLAEYHHLSL--NIHTDDDLARLSRvqQELEARdgwrlqqlVDSTLSRLQLP--ADKTLAELSG 156
Cdd:cd03300 75 nTVF-----------QNYALFPHLTVfeNIAFGLRLKKLPK--AEIKER--------VAEALDLVQLEgyANRKPSQLSG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598215 157 GWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL------LGFngAVLFITHDRAFLQSLATRILELDRGHL 228
Cdd:cd03300 134 GQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELkrlqkeLGI--TFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-186 |
2.82e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.90 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVV-------KGEQQADDGEVW----RAPALKIGE 70
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFarlltpqSGTVFLGDKPISmlssRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 71 LPQELPraderivfdvVAEGLAeVGKLLAeYH---HLSLnihtdddLARLSRvqqeleaRDgwrlQQLVDSTLSRLQLP- 146
Cdd:PRK11231 81 LPQHHL----------TPEGIT-VRELVA-YGrspWLSL-------WGRLSA-------ED----NARVNQAMEQTRINh 130
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598215 147 -ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDI 186
Cdd:PRK11231 131 lADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-233 |
4.76e-16 |
|
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: 77.15 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLldKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalKIGELPQELPRADERIV 83
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV------LINGVDVTAAPPADRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 84 FDVVAEGlaevgKLLAeyhHLSlnIHTDDDLARLSRVQqeLEARDgwrlQQLVDSTLSRLQLPA-DKTLA-ELSGGWRRR 161
Cdd:cd03298 73 SMLFQEN-----NLFA---HLT--VEQNVGLGLSPGLK--LTAED----RQAIEVALARVGLAGlEKRLPgELSGGERQR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 162 VLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG----AVLFITHDRAFLQSLATRILELDRGHlIDWNG 233
Cdd:cd03298 137 VALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAetkmTVLMVTHQPEDAKRLAQRVVFLDNGR-IAAQG 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-228 |
5.78e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 79.73 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkIgelpqelpraDE 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL------I----------GG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 RIVFDVVAE--GLAEVGKLLAEYHHLSL--NIhtdddlA---RLSRV-QQELEARdgwrlqqlVDSTLSRLQLPA--DKT 150
Cdd:COG3839 65 RDVTDLPPKdrNIAMVFQSYALYPHMTVyeNI------AfplKLRKVpKAEIDRR--------VREAAELLGLEDllDRK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 151 LAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD-------IGAIAWLEEALlgfnGA-VLFITHDRAFLQSLATRILE 222
Cdd:COG3839 131 PKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrvemRAEIKRLHRRL----GTtTIYVTHDQVEAMTLADRIAV 206
|
....*.
gi 15598215 223 LDRGHL 228
Cdd:COG3839 207 MNDGRI 212
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-186 |
6.70e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.82 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 7 TDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkigelpqelprADERIVFDV 86
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVL----------------VDGLDVATT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 87 VAEGLAEVGKLLAEYHHLSLNIhTDDDLARLSRV---QQELEARDgwrlQQLVDSTLSRLQLP--ADKTLAELSGGWRRR 161
Cdd:COG4604 69 PSRELAKRLAILRQENHINSRL-TVRELVAFGRFpysKGRLTAED----REIIDEAIAYLDLEdlADRYLDELSGGQRQR 143
|
170 180
....*....|....*....|....*
gi 15598215 162 VLLAQALVAEPDLLLLDEPTNHLDI 186
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-226 |
7.05e-16 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 75.72 E-value: 7.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 14 GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalkigelpqelpRADERIVFDVvaeGLAE 93
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV----------------RLDGADISQW---DPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 94 VGKLLAeYhhlslnihtdddlarlsrVQQELEARDGwrlqqlvdstlsrlqlpadkTLAE--LSGGWRRRVLLAQALVAE 171
Cdd:cd03246 74 LGDHVG-Y------------------LPQDDELFSG--------------------SIAEniLSGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598215 172 PDLLLLDEPTNHLDIGAIAWLEEALLGFNGA---VLFITHDRAFLQSlATRILELDRG 226
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAgatRIVIAHRPETLAS-ADRILVLEDG 171
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-180 |
7.11e-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: 77.20 E-value: 7.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW-------------RApALKIGE 70
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILldgqditklpmhkRA-RLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 71 LPQElpradeRIVFD--VVAEGLAEVgkllaeyhhlsLNIHTDDDLARLSRVQQELEArdgWRLQQLVDSTLSRLqlpad 148
Cdd:cd03218 80 LPQE------ASIFRklTVEENILAV-----------LEIRGLSKKEREEKLEELLEE---FHITHLRKSKASSL----- 134
|
170 180 190
....*....|....*....|....*....|..
gi 15598215 149 ktlaelSGGWRRRVLLAQALVAEPDLLLLDEP 180
Cdd:cd03218 135 ------SGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-226 |
7.84e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 76.55 E-value: 7.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW-------RAPALKIGELPQElp 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldIAARNRIGYLPEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 77 raderivfdvvaEGLAEVGKLLAEYHHLslnihtdddlARLSRVQQELEARDgwrlqqlVDSTLSRLQLP--ADKTLAEL 154
Cdd:cd03269 79 ------------RGLYPKMKVIDQLVYL----------AQLKGLKKEEARRR-------IDEWLERLELSeyANKRVEEL 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598215 155 SGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGA---VLFITHDRAFLQSLATRILELDRG 226
Cdd:cd03269 130 SKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgktVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-229 |
8.90e-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: 76.64 E-value: 8.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 13 FGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRApALKIGELPQELpRADERIVFDVVAegla 92
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVA-GHDVVREPREV-RRRIGIVFQDLS---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 93 eVGKLLAEYHHLSlnIHtdddlARLSRVQqeleardGWRLQQLVDSTLSRLQL--PADKTLAELSGGWRRRVLLAQALVA 170
Cdd:cd03265 84 -VDDELTGWENLY--IH-----ARLYGVP-------GAERRERIDELLDFVGLleAADRLVKTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598215 171 EPDLLLLDEPTNHLDIGAIA--W--LEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-221 |
1.80e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.85 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAFGTTPLldKVS-WQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrAPALKIGELPQELpRADe 80
Cdd:PRK13409 339 TLVEYPDLTKKLGDFSL--EVEgGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYI-KPD- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 rivFDV-VAEGLAEVGKllaeyhhlslNIHTdddlarlSRVQQELeardgwrlqqlvdstLSRLQLPA--DKTLAELSGG 157
Cdd:PRK13409 413 ---YDGtVEDLLRSITD----------DLGS-------SYYKSEI---------------IKPLQLERllDKNVKDLSGG 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598215 158 WRRRVLLAQALVAEPDLLLLDEPTNHLDIgaiawlEEALL----------GFNGAVLFITHDRAFLQSLATRIL 221
Cdd:PRK13409 458 ELQRVAIAACLSRDADLYLLDEPSAHLDV------EQRLAvakairriaeEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-229 |
2.04e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 74.00 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEvwrapalkigelpqelpraderIV 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE----------------------IL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 84 FDvvaeglaevGKllaEYHHLSLNihtDDDLARLSRVQQeleardgwrlqqlvdstlsrlqlpadktlaeLSGGWRRRVL 163
Cdd:cd03216 59 VD---------GK---EVSFASPR---DARRAGIAMVYQ-------------------------------LSVGERQMVE 92
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598215 164 LAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL--LGFNG-AVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIrrLRAQGvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-229 |
2.54e-15 |
|
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: 75.23 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 13 FGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW---------RAPALK-IGELPQelpraderi 82
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYingysirtdRKAARQsLGYCPQ--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 vFDVVAEGL--AEVGKLLAEYHHLSLNIhtdddlarlsrvqqeleardgwrLQQLVDSTLSRLQLP--ADKTLAELSGGW 158
Cdd:cd03263 83 -FDALFDELtvREHLRFYARLKGLPKSE-----------------------IKEEVELLLRVLGLTdkANKRARTLSGGM 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598215 159 RRRVLLAQALVAEPDLLLLDEPTNHLDIGA--IAWleEALLGF--NGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPASrrAIW--DLILEVrkGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-230 |
2.75e-15 |
|
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: 75.55 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAFGTT--PL--LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRApalkiGelpQELPR 77
Cdd:COG4181 7 PIIELRGLTKTVGTGagELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLA-----G---QDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 78 ADErivfDVVAEGLAE-VG------KLLA-----EYHHLSLNIHTDDDlARlSRVQQELEaRDGwrLQQLVDstlsrlQL 145
Cdd:COG4181 79 LDE----DARARLRARhVGfvfqsfQLLPtltalENVMLPLELAGRRD-AR-ARARALLE-RVG--LGHRLD------HY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 146 PAdktlaELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFN---GAVLFI-THDRAfLQSLATRIL 221
Cdd:COG4181 144 PA-----QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNrerGTTLVLvTHDPA-LAARCDRVL 217
|
....*....
gi 15598215 222 ELDRGHLID 230
Cdd:COG4181 218 RLRAGRLVE 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-229 |
4.00e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.58 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV---------WRAPAL--KIGE 70
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrlngrpladWSPAELarRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 71 LPQELPRADERIVFDVVAEGLAevgkllaeyhHLSLNIHTDDDLarlsrVQQELEARDGWRLqqlvdstlsrlqlpADKT 150
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRA----------PHGLSRAEDDAL-----VAAALAQVDLAHL--------------AGRD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 151 LAELSGGWRRRVLLAQALV------AEPDLLLLDEPTNHLDIGAiawlEEALLGF--------NGAVLFITHDRAfLQSL 216
Cdd:PRK13548 132 YPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAH----QHHVLRLarqlaherGLAVIVVLHDLN-LAAR 206
|
250
....*....|....
gi 15598215 217 -ATRILELDRGHLI 229
Cdd:PRK13548 207 yADRIVLLHQGRLV 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-226 |
4.13e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.38 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEvwrapaLKIGE-LPQELPRAD 79
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD------LFIGEkRMNDVPPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 80 ErivfdvvaeGLAEVGKLLAEYHHLSL--NIHTDDDLARLSRVQqeleardgwrLQQLVDSTLSRLQLPA--DKTLAELS 155
Cdd:PRK11000 75 R---------GVGMVFQSYALYPHLSVaeNMSFGLKLAGAKKEE----------INQRVNQVAEVLQLAHllDRKPKALS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598215 156 GGWRRRVLLAQALVAEPDLLLLDEPTNHLDIG-------AIAWLEEALlgfNGAVLFITHDRAFLQSLATRILELDRG 226
Cdd:PRK11000 136 GGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAlrvqmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-209 |
4.67e-15 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 78.75 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDK-VSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQelprader 81
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKnLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQ-------- 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 ivfdvvaeglaevgkllaeyHHLSLNIHTDDDLARLSRV-----QQELEARDGwrlQQLVDSTLsrlqlpADKTLAELSG 156
Cdd:PLN03073 580 --------------------HHVDGLDLSSNPLLYMMRCfpgvpEQKLRAHLG---SFGVTGNL------ALQPMYTLSG 630
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598215 157 GWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHD 209
Cdd:PLN03073 631 GQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHD 683
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-226 |
4.98e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 74.81 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwRAPALKIGElpqelPRADERIVFDVVAeglaeVGKLL 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV-ILEGKQITE-----PGPDRMVVFQNYS-----LLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 99 AEYHHLSLNIhtDDDLARLSRVQQEleardgwrlqQLVDSTLS--RLQLPADKTLAELSGGWRRRVLLAQALVAEPDLLL 176
Cdd:TIGR01184 70 TVRENIALAV--DRVLPDLSKSERR----------AIVEEHIAlvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLL 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 177 LDEPTNHLDIGAIAWLEEALLGF----NGAVLFITH--DRAFLqsLATRILELDRG 226
Cdd:TIGR01184 138 LDEPFGALDALTRGNLQEELMQIweehRVTVLMVTHdvDEALL--LSDRVVMLTNG 191
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-229 |
5.49e-15 |
|
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: 75.03 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAF-GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwRAPALKIGEL-PQELPRadeR 81
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEI-FIDGEDIREQdPVELRR---K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 IVFDVVAEGLaevgkllaeYHHLSL--NIHTdddLARLSRVQQEleardgwRLQQLVDSTLSRLQLP----ADKTLAELS 155
Cdd:cd03295 77 IGYVIQQIGL---------FPHMTVeeNIAL---VPKLLKWPKE-------KIRERADELLALVGLDpaefADRYPHELS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 156 GGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGA----VLFITHD--RAFLqsLATRILELDRGHLI 229
Cdd:cd03295 138 GGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgktIVFVTHDidEAFR--LADRIAIMKNGEIV 215
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-225 |
7.45e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 73.67 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQAD---DGEVW-------RAPALK--IGEL 71
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLlngrrltALPAEQrrIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 72 PQELPRADERIVFDVVAEGLAevgkllaeyhhlslnihtdddlARLSRVQQeleardgwrlQQLVDSTLSRLQLP--ADK 149
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFALP----------------------PTIGRAQR----------RARVEQALEEAGLAgfADR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 150 TLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIA----WLEEALLGFNGAVLFITHDRAFLQSlATRILELDR 225
Cdd:COG4136 130 DPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAqfreFVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-226 |
8.66e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.54 E-value: 8.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGT-TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQE--LPRADE 80
Cdd:COG4178 363 LALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRpyLPLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 RivfDVVAeglaevgkllaeYHHLSLNIhTDDDLAR-LSRVqqeleardgwRLQQLVDstlsRLQLPADKTlAELSGGWR 159
Cdd:COG4178 443 R---EALL------------YPATAEAF-SDAELREaLEAV----------GLGHLAE----RLDEEADWD-QVLSLGEQ 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598215 160 RRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLG--FNGAVLFITHdRAFLQSLATRILELDRG 226
Cdd:COG4178 492 QRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-229 |
9.91e-15 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 77.42 E-value: 9.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGT----TPLLDKVSWQIGRGERVCVIGRNGTGKS----SLFKVVKGEQQADDGEVWRApalkiGelp 72
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFD-----G--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 73 QELPRADER-----------IVFDvvaeglaE----------VGKLLAEyhhlSLNIHTdddlaRLSRVQQELEARDgwr 131
Cdd:COG4172 76 QDLLGLSERelrrirgnriaMIFQ-------EpmtslnplhtIGKQIAE----VLRLHR-----GLSGAAARARALE--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 132 lqqlvdsTLSRLQLPADKTLA-----ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD--IGA-IawLEeaLLG----- 198
Cdd:COG4172 137 -------LLERVGIPDPERRLdayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtVQAqI--LD--LLKdlqre 205
|
250 260 270
....*....|....*....|....*....|.
gi 15598215 199 FNGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:COG4172 206 LGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-227 |
9.96e-15 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 73.62 E-value: 9.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV------------WRAPALKIGEL 71
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIrfdgrditglppHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 72 PQelpradERIVFDV--VAEGLaevgkLLAEYHHLSLNIHTDDD--LARLSRVQQeleardgwRLQQLVdstlsrlqlpa 147
Cdd:cd03224 81 PE------GRRIFPEltVEENL-----LLGAYARRRAKRKARLErvYELFPRLKE--------RRKQLA----------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 148 dktlAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG---AVLFITHDRAFLQSLATRILELD 224
Cdd:cd03224 131 ----GTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDegvTILLVEQNARFALEIADRAYVLE 206
|
...
gi 15598215 225 RGH 227
Cdd:cd03224 207 RGR 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
333-467 |
1.13e-14 |
|
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: 71.53 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 333 VRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVG-----------TKLEVAYFDQLrHQLEPEQTVIDN 401
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598215 402 ISEGREFITIDGQNR-----HVLSYLGDFLFSPQRARTPVKALSGGERARLLLAKLFSKPANLLVLDEPTN 467
Cdd:pfam00005 80 LRLGLLLKGLSKREKdaraeEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-228 |
2.27e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.74 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 9 VSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDG-------EVWRAPA--LKIGELPQELPRAD 79
Cdd:PRK10851 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGhirfhgtDVSRLHArdRKVGFVFQHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 80 ERIVFDVVAEGLaevgkllaeyhhlslnihtdddlarlsRVQQELEARDGWRLQQLVDSTLSRLQLP--ADKTLAELSGG 157
Cdd:PRK10851 88 HMTVFDNIAFGL---------------------------TVLPRRERPNAAAIKAKVTQLLEMVQLAhlADRYPAQLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598215 158 WRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIA----WL----EEalLGFNGavLFITHDRAFLQSLATRILELDRGHL 228
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKelrrWLrqlhEE--LKFTS--VFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-238 |
2.38e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 73.12 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEvwrapaLKIGE----LPQELPRAD 79
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQ------LNIAGhqfdFSQKPSEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 80 ERivfdvvaEGLAEVGKLLAEYH---HLSLnihTDDDLARLSRV--QQELEARDgwRLQQLvdstLSRLQLP--ADKTLA 152
Cdd:COG4161 77 IR-------LLRQKVGMVFQQYNlwpHLTV---MENLIEAPCKVlgLSKEQARE--KAMKL----LARLRLTdkADRFPL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 153 ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL--LGFNGAVLFI-THDRAFLQSLATRILELDRGHLI 229
Cdd:COG4161 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIreLSQTGITQVIvTHEVEFARKVASQVVYMEKGRII 220
|
....*....
gi 15598215 230 DWnGDYASF 238
Cdd:COG4161 221 EQ-GDASHF 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-209 |
4.05e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.81 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalKIGELPQELPRADERI 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI------TLDGKPVEGPGAERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VFDvvAEGLAEVGKLLAeyhhlslNIHTDDDLARLSRVQQELEARdgwRLQQLVDstlsrLQLPADKTLAELSGGWRRRV 162
Cdd:PRK11248 75 VFQ--NEGLLPWRNVQD-------NVAFGLQLAGVEKMQRLEIAH---QMLKKVG-----LEGAEKRYIWQLSGGQRQRV 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598215 163 LLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALL----GFNGAVLFITHD 209
Cdd:PRK11248 138 GIARALAANPQLLLLDEPFGALDAFTREQMQTLLLklwqETGKQVLLITHD 188
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-221 |
4.59e-14 |
|
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: 73.55 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAF----GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKG---EQQADDGEVWrapaLKigelPQEL 75
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEIL----FD----GEDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 76 PRADERIVFDVVAEGLA--------------EVGKLLAEyhhlSLNIHTdddlaRLSRvqQELEARdgwrlqqlVDSTLS 141
Cdd:COG0444 73 LKLSEKELRKIRGREIQmifqdpmtslnpvmTVGDQIAE----PLRIHG-----GLSK--AEARER--------AIELLE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 142 RLQLPADKTLA-----ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD--IGA-IawLEeaLLG-----FNGAVLFITH 208
Cdd:COG0444 134 RVGLPDPERRLdryphELSGGMRQRVMIARALALEPKLLIADEPTTALDvtIQAqI--LN--LLKdlqreLGLAILFITH 209
|
250
....*....|...
gi 15598215 209 DRAFLQSLATRIL 221
Cdd:COG0444 210 DLGVVAEIADRVA 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-230 |
5.97e-14 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 71.24 E-value: 5.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRApALKIGELPQELPRadeRIVFDVVAEGLaevgkll 98
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD-GFDVVKEPAEARR---RLGFVSDSTGL------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 99 aeYHHLSL--NIHTDDDLARLSRvqQELEARdgwrlqqlVDSTLSRLQLPA--DKTLAELSGGWRRRVLLAQALVAEPDL 174
Cdd:cd03266 90 --YDRLTAreNLEYFAGLYGLKG--DELTAR--------LEELADRLGMEEllDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598215 175 LLLDEPTNHLDIGAIAWLEEAL-----LGfnGAVLFITHDRAFLQSLATRILELDRGHLID 230
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIrqlraLG--KCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-180 |
1.20e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.83 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW-------------RApALK 67
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFldgedithlpmhkRA-RLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 68 IGELPQElpradeRIVFdvvaeglaevGKLLAEYhhlslNIHTDDDLARLSRVQQELeardgwRLQQLVDS-TLSRLQlp 146
Cdd:COG1137 80 IGYLPQE------ASIF----------RKLTVED-----NILAVLELRKLSKKEREE------RLEELLEEfGITHLR-- 130
|
170 180 190
....*....|....*....|....*....|....*
gi 15598215 147 adKTLA-ELSGGWRRRVLLAQALVAEPDLLLLDEP 180
Cdd:COG1137 131 --KSKAySLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-185 |
1.24e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 70.79 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapaL---KIGELPQELPRAD 79
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIT----VdgeDLTDSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 80 ERI--VF------------DVVAEGLAEVGKLlaeyhhlslnihtdddlarlSRVQQELEARDgwrlqqlvdsTLSRLQL 145
Cdd:COG1126 77 RKVgmVFqqfnlfphltvlENVTLAPIKVKKM--------------------SKAEAEERAME----------LLERVGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598215 146 P--ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD 185
Cdd:COG1126 127 AdkADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-224 |
1.25e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 69.10 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGT-TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVkgeqqaddGEVWrapalkigelpqelPRADERI 82
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL--------AGLW--------------PWGSGRI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VfdvvaeglaevgkllaeyhhlslnIHTDDDLARLSrvqqeleardgwrlQQ--LVDSTLsRLQL--PADKtlaELSGGW 158
Cdd:cd03223 59 G------------------------MPEGEDLLFLP--------------QRpyLPLGTL-REQLiyPWDD---VLSGGE 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 159 RRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHdRAFLQSLATRILELD 224
Cdd:cd03223 97 QQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-229 |
1.56e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 71.76 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapaLKIGE-LPQELPRADERi 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI-----SLCGEpVPSRARHARQR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 vfdvvaeglaeVGkLLAEYHHLSLNIHTDDDLARLSRVQQELEARDGWRLQQLVDstLSRLQLPADKTLAELSGGWRRRV 162
Cdd:PRK13537 82 -----------VG-VVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLE--FAKLENKADAKVGELSGGMKRRL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 163 LLAQALVAEPDLLLLDEPTNHLDIGAIAWLEE---ALLGFNGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWErlrSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-239 |
1.97e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 70.17 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLldKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW--------RAPAL-KIGELPQE 74
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwngqdltaLPPAErPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 75 lpraderivfdvvaeglaevGKLlaeYHHLS------LNIHtdDDLaRLSRVQQeleardgwrlqQLVDSTLSRLQLP-- 146
Cdd:COG3840 80 --------------------NNL---FPHLTvaqnigLGLR--PGL-KLTAEQR-----------AQVEQALERVGLAgl 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 147 ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIG----AIAWLEEALLGFNGAVLFITHDRAFLQSLATRILE 222
Cdd:COG3840 123 LDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAlrqeMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLL 202
|
250
....*....|....*..
gi 15598215 223 LDRGHlIDWNGDYASFL 239
Cdd:COG3840 203 VADGR-IAADGPTAALL 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
8-223 |
2.44e-13 |
|
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: 68.92 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 8 DVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwRAPALKIGELPQELpraderivfdvv 87
Cdd:TIGR01189 5 NLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV-RWNGTPLAEQRDEP------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 88 AEGLAEVGKLLAEYHHLSL--NIHTdddLARLSRVQQeleaRDGWRLQQLVDSTlSRLQLPAdktlAELSGGWRRRVLLA 165
Cdd:TIGR01189 72 HENILYLGHLPGLKPELSAleNLHF---WAAIHGGAQ----RTIEDALAAVGLT-GFEDLPA----AQLSAGQQRRLALA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598215 166 QALVAEPDLLLLDEPTNHLDIGAIAWLEEAL---LGFNGAVLFITHDRafLQSLATRILEL 223
Cdd:TIGR01189 140 RLWLSRRPLWILDEPTTALDKAGVALLAGLLrahLARGGIVLLTTHQD--LGLVEARELRL 198
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
13-238 |
3.67e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 69.66 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 13 FGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVvkgeqqaddgevwrapaLKIGELPQ--ELPRADERivFDVVA-- 88
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRV-----------------LNLLEMPRsgTLNIAGNH--FDFSKtp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 89 ---EGLA---EVGKLLAEYH---HLSL--N-IHTDDDLARLSRVQQELEArdgwrlqqlvDSTLSRLQLP--ADKTLAEL 154
Cdd:PRK11124 73 sdkAIRElrrNVGMVFQQYNlwpHLTVqqNlIEAPCRVLGLSKDQALARA----------EKLLERLRLKpyADRFPLHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 155 SGGWRRRVLLAQALVAEPDLLLLDEPTNHLD--IGA-IAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLIDw 231
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDpeITAqIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVE- 221
|
....*..
gi 15598215 232 NGDYASF 238
Cdd:PRK11124 222 QGDASCF 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
302-532 |
4.19e-13 |
|
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: 72.11 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 302 ASFQLESADKSGKQVIVVEHVSFAHPG-GQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV-GTK 379
Cdd:COG4987 319 VTEPAEPAPAPGGPSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLgGVD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 380 LEVAYFDQLRHQL-----EP---EQTVIDNISEGREFITiDGQNRHVLS--YLGDFLFS-PQRARTPV----KALSGGER 444
Cdd:COG4987 399 LRDLDEDDLRRRIavvpqRPhlfDTTLRENLRLARPDAT-DEELWAALErvGLGDWLAAlPDGLDTWLgeggRRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 445 ARLLLAKLFSKPANLLVLDEPTN--DLDVETLELLEEVLLGFQGTVLMVSHDRAFLDNVvtSTLVFEGEGKVREfVGGYQ 522
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEglDAATEQALLADLLEALAGRTVLLITHRLAGLERM--DRILVLEDGRIVE-QGTHE 554
|
250
....*....|
gi 15598215 523 DWLRQGGTPR 532
Cdd:COG4987 555 ELLAQNGRYR 564
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-228 |
4.27e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.13 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAF-GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRA----PALKIGELPQeLPR 77
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghdiTRLKNREVPF-LRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 78 aderivfdvvaeglaEVGKLLAEyHHLSLNIHTDDDLArlsrVQQELEARDGWRLQQLVDSTLSRLQL--PADKTLAELS 155
Cdd:PRK10908 80 ---------------QIGMIFQD-HHLLMDRTVYDNVA----IPLIIAGASGDDIRRRVSAALDKVGLldKAKNFPIQLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 156 GGWRRRVLLAQALVAEPDLLLLDEPTNHLD----IGAIAWLEEallgFNG---AVLFITHDRAFLQSLATRILELDRGHL 228
Cdd:PRK10908 140 GGEQQRVGIARAVVNKPAVLLADEPTGNLDdalsEGILRLFEE----FNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-228 |
5.77e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.32 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEvwrapaLKIGELPQELPRADER 81
Cdd:PRK11247 11 TPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE------LLAGTAPLAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 IVFDvvaeglaevgkllaeyhhlslnihtDDDLARLSRVQQE--LEARDGWRLQQLVDSTLSRLQLPADKTLAELSGGWR 159
Cdd:PRK11247 85 LMFQ-------------------------DARLLPWKKVIDNvgLGLKGQWRDAALQALAAVGLADRANEWPAALSGGQK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598215 160 RRVLLAQALVAEPDLLLLDEPTNHLDigAIAWLE-----EALLGFNG-AVLFITHDRAFLQSLATRILELDRGHL 228
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGALD--ALTRIEmqdliESLWQQHGfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-185 |
9.00e-13 |
|
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: 68.36 E-value: 9.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGT-TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW--------------RAPALKI 68
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinklkgkalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 69 GELPQELPRADERIVFDVVAEG-LAEVGKLLAeyhhlslnihtdddLARLSRVQQELEARdgwrlqqlvdSTLSRLQLpA 147
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrLGRRSTWRS--------------LFGLFPKEEKQRAL----------AALERVGL-L 135
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598215 148 DKTLA---ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD 185
Cdd:cd03256 136 DKAYQradQLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-230 |
1.09e-12 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 68.13 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapaLKIGELPQELPRADERIVFdvvaeglaeVGKLL 98
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI-----LLNGKDITNLPPEKRDISY---------VPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 99 AEYHHLSL--NIHTDDDLARLSRVQQELEARDGWRLQQlVDSTLSRlqlpadkTLAELSGGWRRRVLLAQALVAEPDLLL 176
Cdd:cd03299 81 ALFPHMTVykNIAYGLKKRKVDKKEIERKVLEIAEMLG-IDHLLNR-------KPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598215 177 LDEPTNHLDI----GAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLID 230
Cdd:cd03299 153 LDEPFSALDVrtkeKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
7-208 |
1.18e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.21 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 7 TDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalKIGELPQELPRADERIvfdv 86
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI------KLDGGDIDDPDVAEAC---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 87 vaeglaevgkllaeyHHLSlniHTDDDLARLSrVQQELEardGWR-----LQQLVDSTLSRLQLP--ADKTLAELSGGWR 159
Cdd:PRK13539 76 ---------------HYLG---HRNAMKPALT-VAENLE---FWAaflggEELDIAAALEAVGLAplAHLPFGYLSAGQK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598215 160 RRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL---LGFNGAVLFITH 208
Cdd:PRK13539 134 RRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIrahLAQGGIVIAATH 185
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-229 |
1.74e-12 |
|
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: 67.68 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV-------------WRApALKIGE 70
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIlidgqdithlpmhERA-RLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 71 LPQELPraderiVFD--VVAEGLAEVgkllaeyhhlsLNIHTDddlarLSRVQQELEARDgwrlqQLVDSTLSRLQlpaD 148
Cdd:TIGR04406 81 LPQEAS------IFRklTVEENIMAV-----------LEIRKD-----LDRAEREERLEA-----LLEEFQISHLR---D 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 149 KTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD---IGAIAWLEEALLGFNGAVLFITH---------DRAFLQSL 216
Cdd:TIGR04406 131 NKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVGDIKKIIKHLKERGIGVLITDHnvretldicDRAYIISD 210
|
250
....*....|...
gi 15598215 217 ATRILELDRGHLI 229
Cdd:TIGR04406 211 GKVLAEGTPAEIV 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-221 |
2.01e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.20 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAFGTTPLldKV-SWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrAPALKIGELPQEL-PRAD 79
Cdd:COG1245 340 TLVEYPDLTKSYGGFSL--EVeGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYIsPDYD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 80 ERivfdvVAEGLAEVGKllaeyhhlslnihtdDDLARlSRVQQELeardgwrlqqlvdstLSRLQLPA--DKTLAELSGG 157
Cdd:COG1245 416 GT-----VEEFLRSANT---------------DDFGS-SYYKTEI---------------IKPLGLEKllDKNVKDLSGG 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598215 158 WRRRVLLAQALVAEPDLLLLDEPTNHLDIgaiawlEEALL----------GFNGAVLFITHDRAFLQSLATRIL 221
Cdd:COG1245 460 ELQRVAIAACLSRDADLYLLDEPSAHLDV------EQRLAvakairrfaeNRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
321-527 |
2.27e-12 |
|
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: 69.96 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 321 HVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEVAYFDQlRHQLEPEQTVID 400
Cdd:TIGR03719 9 RVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQ-EPQLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 401 NISEG--------REF--IT-----------------------IDGQNRH----VLSYLGDFLFSPQrARTPVKALSGGE 443
Cdd:TIGR03719 88 NVEEGvaeikdalDRFneISakyaepdadfdklaaeqaelqeiIDAADAWdldsQLEIAMDALRCPP-WDADVTKLSGGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 444 RARLLLAKLF-SKPaNLLVLDEPTNDLDVETLELLEEVLLGFQGTVLMVSHDRAFLDNVVTSTLVFE-GEGKVREfvGGY 521
Cdd:TIGR03719 167 RRRVALCRLLlSKP-DMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDrGRGIPWE--GNY 243
|
....*.
gi 15598215 522 QDWLRQ 527
Cdd:TIGR03719 244 SSWLEQ 249
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-180 |
2.68e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.48 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW----RAPAL---------- 66
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILfdgeNIPAMsrsrlytvrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 67 KIGELPQELPRADERIVFDVVAEGLAEVGKLLAEYHHlslnihtdddlarlSRVQQELEARDgwrlqqlvdstlsrLQLP 146
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLH--------------STVMMKLEAVG--------------LRGA 136
|
170 180 190
....*....|....*....|....*....|....
gi 15598215 147 ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEP 180
Cdd:PRK11831 137 AKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-181 |
3.21e-12 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 66.54 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW-------RAPALKIGEL-- 71
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgeditGLPPHRIARLgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 72 ---PQelpradERIVFD--VVAEGLaEVGkllaeyhhlslnihtdddlARLSRVQQELEARDGW------RLQQlvdstl 140
Cdd:COG0410 81 gyvPE------GRRIFPslTVEENL-LLG-------------------AYARRDRAEVRADLERvyelfpRLKE------ 128
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598215 141 sRLQLPAdktlAELSGGWRRRVLLAQALVAEPDLLLLDEPT 181
Cdd:COG0410 129 -RRRQRA----GTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
307-529 |
3.84e-12 |
|
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: 69.02 E-value: 3.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 307 ESADKSGKQVIVVEHVSFAHPGGQPLVRDFSMVLQRGDRIG---------------LLGAngtgkttllklllgdLQPTS 371
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVAlvgpsgagkstllnlLLGF---------------LPPYS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 372 GKIEV-GTKLEVAYFDQLRHQL-----EP---EQTVIDNISEGREFITiDGQNRHVL--SYLGDFLFS-PQRARTPV--- 436
Cdd:COG4988 392 GSILInGVDLSDLDPASWRRQIawvpqNPylfAGTIRENLRLGRPDAS-DEELEAALeaAGLDEFVAAlPDGLDTPLgeg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 437 -KALSGGERARLLLAKLFSKPANLLVLDEPTN--DLDVETLELLEEVLLGFQGTVLMVSHDRAFLDNvVTSTLVFEGeGK 513
Cdd:COG4988 471 gRGLSGGQAQRLALARALLRDAPLLLLDEPTAhlDAETEAEILQALRRLAKGRTVILITHRLALLAQ-ADRILVLDD-GR 548
|
250
....*....|....*.
gi 15598215 514 VREfVGGYQDWLRQGG 529
Cdd:COG4988 549 IVE-QGTHEELLAKNG 563
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-223 |
3.88e-12 |
|
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: 65.59 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 18 LLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalkigeLPQELPRADERivfDVVAEGLAEVGkl 97
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV----------LLNGGPLDFQR---DSIARGLLYLG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 98 laeyhhlslniHTDDDLARLSRVQQ-ELEARDGWRLQqlVDSTLSRLQLPA--DKTLAELSGGWRRRVLLAQALVAEPDL 174
Cdd:cd03231 80 -----------HAPGIKTTLSVLENlRFWHADHSDEQ--VEEALARVGLNGfeDRPVAQLSAGQQRRVALARLLLSGRPL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598215 175 LLLDEPTNHLDIGAIAWLEEAL---LGFNGAVLFITHDRAFLQSLATRILEL 223
Cdd:cd03231 147 WILDEPTTALDKAGVARFAEAMaghCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-501 |
6.96e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 68.29 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKG--EQQADDGEV-----------WRAPALKIGE 70
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 71 lpqELPRADERIV-FDVVAEGLAE-----VGKLLAEYHHLSLNIHTDDD-LARLSRVQQELEARDGWRLQQLVDsTLSRL 143
Cdd:TIGR03269 81 ---PCPVCGGTLEpEEVDFWNLSDklrrrIRKRIAIMLQRTFALYGDDTvLDNVLEALEEIGYEGKEAVGRAVD-LIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 144 QLPADKT-LA-ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF---NGAVLFIThdraflqSLAT 218
Cdd:TIGR03269 157 QLSHRIThIArDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkaSGISMVLT-------SHWP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 219 RILEldrghlidwngdyasflvhkeqqlaaeeaanalfdkRLAQEEVWIRQG-IKARRTRNEGRVRALKEMRRERAERRE 297
Cdd:TIGR03269 230 EVIE------------------------------------DLSDKAIWLENGeIKEEGTPDEVVAVFMEGVSEVEKECEV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 298 RQGKASFQLESADKsgkQVIVVEHvsfahpGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVG 377
Cdd:TIGR03269 274 EVGEPIIKVRNVSK---RYISVDR------GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 378 --------TKLEVA-------YFDQLrHQ---LEPEQTVIDNISE--GREFITIDGQNR--HVLSYLGdflFSPQRARTP 435
Cdd:TIGR03269 345 vgdewvdmTKPGPDgrgrakrYIGIL-HQeydLYPHRTVLDNLTEaiGLELPDELARMKavITLKMVG---FDEEKAEEI 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598215 436 VK----ALSGGERARLLLAKLFSKPANLLVLDEPTND----LDVETLELLEEVLLGFQGTVLMVSHDRAFLDNV 501
Cdd:TIGR03269 421 LDkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTmdpiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDV 494
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-226 |
7.25e-12 |
|
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: 68.89 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 15 TTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW---RAPALKIGELPQELPRADErivFDVVAEgl 91
Cdd:TIGR01257 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATvagKSILTNISDVHQNMGYCPQ---FDAIDD-- 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 92 aevgkLLAEYHHLSLnihtdddLARLSRV-QQELEARDGWRLQQLvdstlsRLQLPADKTLAELSGGWRRRVLLAQALVA 170
Cdd:TIGR01257 2026 -----LLTGREHLYL-------YARLRGVpAEEIEKVANWSIQSL------GLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598215 171 EPDLLLLDEPTNHLDIGAIAWLEEALLGF---NGAVLFITHDRAFLQSLATRILELDRG 226
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIireGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-230 |
7.70e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.19 E-value: 7.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 15 TTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalKIGELPqelprADERIVFDVvaegLAEV 94
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI------TVGGMV-----LSEETVWDV----RRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 95 GKLLAEYHHLSLNIHTDDDLA------RLSRvqQELEARDGWRLQQLvdstlsRLQLPADKTLAELSGGWRRRVLLAQAL 168
Cdd:PRK13635 84 GMVFQNPDNQFVGATVQDDVAfgleniGVPR--EEMVERVDQALRQV------GMEDFLNREPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598215 169 VAEPDLLLLDEPTNHLD-------IGAIAWLEEALlgfNGAVLFITHD---RAFlqslATRILELDRGHLID 230
Cdd:PRK13635 156 ALQPDIIILDEATSMLDprgrrevLETVRQLKEQK---GITVLSITHDldeAAQ----ADRVIVMNKGEILE 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-229 |
8.19e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.72 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalkigelpqeLPRADERI 82
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV--------------HYRMRDGQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VFDVVAEGLAEvgkllaeyhhlslnihtdddLARLSR-----VQQEleARDGWRLQ-----------------------Q 134
Cdd:PRK11701 72 LRDLYALSEAE--------------------RRRLLRtewgfVHQH--PRDGLRMQvsaggnigerlmavgarhygdirA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 135 LVDSTLSRLQLPA---DKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLG----FNGAVLFIT 207
Cdd:PRK11701 130 TAGDWLERVEIDAariDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlvreLGLAVVIVT 209
|
250 260
....*....|....*....|..
gi 15598215 208 HDRAFLQSLATRILELDRGHLI 229
Cdd:PRK11701 210 HDLAVARLLAHRLLVMKQGRVV 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-229 |
1.06e-11 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 63.87 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFG--TTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalKIGELPqelprader 81
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI------TLDGVP--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 ivfdvvaegLAEVGKLLAEYhhlslnihtdddlarLSRVQQELeardgwrlqQLVDSTLSrlqlpaDKTLAELSGGWRRR 161
Cdd:cd03247 66 ---------VSDLEKALSSL---------------ISVLNQRP---------YLFDTTLR------NNLGRRFSGGERQR 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 162 VLLAQALVAEPDLLLLDEPTNHLDigaiAWLEEALLGF------NGAVLFITHDrafLQSL--ATRILELDRGHLI 229
Cdd:cd03247 107 LALARILLQDAPIVLLDEPTVGLD----PITERQLLSLifevlkDKTLIWITHH---LTGIehMDKILFLENGKII 175
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-226 |
1.14e-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: 64.41 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFG-----TTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPalKIGELPQE--LP 76
Cdd:cd03250 1 ISVEDASFTWDsgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEpwIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 77 RAD--ERIVFDvvaeglaevgkllAEYHHlslnihtdddlARLSRVqqeLEA----RDgwrLQQLVDstlsrlqlpADKT 150
Cdd:cd03250 79 NGTirENILFG-------------KPFDE-----------ERYEKV---IKAcalePD---LEILPD---------GDLT 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 151 L-----AELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWL-EEALLGF---NGAVLFITHDRAFLqSLATRIL 221
Cdd:cd03250 120 EigekgINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGLllnNKTRILVTHQLQLL-PHADQIV 198
|
....*
gi 15598215 222 ELDRG 226
Cdd:cd03250 199 VLDNG 203
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
17-224 |
1.42e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.05 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 17 PLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV-WRAPAlkIGELPQELPRAderivfdvvaegLAEVG 95
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlWQGEP--IRRQRDEYHQD------------LLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 96 KLLAEYHHLSlnihTDDDLARLSRVQQELEARDGWR-LQQLvdSTLSRLQLPAdktlAELSGGWRRRVLLAQALVAEPDL 174
Cdd:PRK13538 81 HQPGIKTELT----ALENLRFYQRLHGPGDDEALWEaLAQV--GLAGFEDVPV----RQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598215 175 LLLDEPTNHLDIGAIAWLEEALLGF---NGAVLFITHDRAFLQSLATRILELD 224
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQHaeqGGMVILTTHQDLPVASDKVRKLRLG 203
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-229 |
1.67e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 65.87 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAF----GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW---------RAPAL---- 66
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLvdgvdltalSERELraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 67 -KIGELPQELPRADERIVFDVVAeglaevgkllaeyhhLSLNIhtdddlARLSRvqQELEARdgwrlqqlVDSTLSRLQL 145
Cdd:COG1135 82 rKIGMIFQHFNLLSSRTVAENVA---------------LPLEI------AGVPK--AEIRKR--------VAELLELVGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 146 P--ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD---IGAIAwleeALLG-----FNGAVLFITHDRAFLQS 215
Cdd:COG1135 131 SdkADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTRSIL----DLLKdinreLGLTIVLITHEMDVVRR 206
|
250
....*....|....
gi 15598215 216 LATRILELDRGHLI 229
Cdd:COG1135 207 ICDRVAVLENGRIV 220
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-229 |
3.65e-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: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKG--EQQADDGEVWrapaLK---IGELPqelprA 78
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSIL----LDgedILELS-----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 79 DERivfdvVAEGL-------AEV-GKLLAEYHHLSLNihtdddlarlSRVQQELEARDgwrLQQLVDSTLSRLQLP---A 147
Cdd:COG0396 72 DER-----ARAGIflafqypVEIpGVSVSNFLRTALN----------ARRGEELSARE---FLKLLKEKMKELGLDedfL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 148 DKTLAE-LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEE---ALLGFNGAVLFITHdraflqslATRILEL 223
Cdd:COG0396 134 DRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEgvnKLRSPDRGILIITH--------YQRILDY 205
|
....*....
gi 15598215 224 ---DRGHLI 229
Cdd:COG0396 206 ikpDFVHVL 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-229 |
4.35e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.37 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV-----------WRAPALK-I 68
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllpLHARARRgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 69 GELPQElpraderivfdvvaeglAEVGKLLAEYHHLSLNIHTDDDLARLSRVQQELEARDGWRLQQLVDSTLSrlqlpad 148
Cdd:PRK10895 81 GYLPQE-----------------ASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQ------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 149 ktlaELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD---IGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDR 225
Cdd:PRK10895 137 ----SLSGGERRRVEIARALAANPKFILLDEPFAGVDpisVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQ 212
|
....
gi 15598215 226 GHLI 229
Cdd:PRK10895 213 GHLI 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
4.50e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.05 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAF-GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapaLKIGElpqelprad 79
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV-----LIRGE--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 80 erivfDVVAEGLAEVGKLLAeyhhlsLNIHTDDDLARLSRVQQELE------ARDGWRLQQLVDSTLSRLQLPA--DKTL 151
Cdd:PRK13652 67 -----PITKENIREVRKFVG------LVFQNPDDQIFSPTVEQDIAfgpinlGLDEETVAHRVSSALHMLGLEElrDRVP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 152 AELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGA----IAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGH 227
Cdd:PRK13652 136 HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGvkelIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGR 215
|
..
gi 15598215 228 LI 229
Cdd:PRK13652 216 IV 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-229 |
4.57e-11 |
|
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: 65.48 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADdGEVWRApalkiGELPQELPRADER-------IVF------- 84
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFD-----GQDLDGLSRRALRplrrrmqVVFqdpfgsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 85 -------DVVAEGLAevgkllaeyhhlslnIHTDDdlarLSRVQQEleardgwrlqQLVDSTLSRLQLPADkTLA----E 153
Cdd:COG4172 376 sprmtvgQIIAEGLR---------------VHGPG----LSAAERR----------ARVAEALEEVGLDPA-ARHryphE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 154 LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD--IGA--IAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDvsVQAqiLDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-229 |
5.24e-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: 62.94 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWR----APALKIG-----ELPQElpradERIVFDVVAE 89
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVrgrvSSLLGLGggfnpELTGR-----ENIYLNGRLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 90 GL--AEVGKLLAEYHHLSlnihtdddlarlsrvqqELEArdgwrlqqlvdstlsRLQLPadktLAELSGGWRRRVLLAQA 167
Cdd:cd03220 113 GLsrKEIDEKIDEIIEFS-----------------ELGD---------------FIDLP----VKTYSSGMKARLAFAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 168 LVAEPDLLLLDEPTNHLDIG----AIAWLEEALLGfNGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:cd03220 157 TALEPDILLIDEVLAVGDAAfqekCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
317-496 |
7.17e-11 |
|
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: 65.00 E-value: 7.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV-GTKLEVAYFDQLRHQLE-- 393
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLADADADSWRDQIAwv 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 394 ------PEQTVIDNISEGREFITIDGQNRHV-LSYLGDFLFS-PQRARTPV----KALSGGERARLLLAKLFSKPANLLV 461
Cdd:TIGR02857 402 pqhpflFAGTIAENIRLARPDASDAEIREALeRAGLDEFVAAlPQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598215 462 LDEPTN--DLDVETLELLEEVLLGFQGTVLMVSHDRA 496
Cdd:TIGR02857 482 LDEPTAhlDAETEAEVLEALRALAQGRTVLLVTHRLA 518
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-230 |
9.40e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.61 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFG--TTPL--LDKVSWQIGRGERVCVIGRNGTGKS-SLFKVV-----KGEQQADDGEVWRAPALKIGE 70
Cdd:PRK11022 1 MALLNVDKLSVHFGdeSAPFraVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMglidyPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 71 LP-QELPRADERIVFDVVAEGLA---EVGKLLAEyhhlSLNIHTDDdlARLSRVQQELEArdgwrLQQL-VDSTLSRLql 145
Cdd:PRK11022 81 KErRNLVGAEVAMIFQDPMTSLNpcyTVGFQIME----AIKVHQGG--NKKTRRQRAIDL-----LNQVgIPDPASRL-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 146 paDKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF----NGAVLFITHDRAFLQSLATRIL 221
Cdd:PRK11022 148 --DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqkeNMALVLITHDLALVAEAAHKII 225
|
....*....
gi 15598215 222 ELDRGHLID 230
Cdd:PRK11022 226 VMYAGQVVE 234
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-181 |
9.48e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.15 E-value: 9.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 7 TDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW------------RAPALKIGELPQe 74
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdmadarhrRAVCPRIAYMPQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 75 lpraderivfdvvaeGLaevGKLLaeYHHLSL--NIhtdDDLARL---SRVQQEleardgWRLQQLVDST-----LSRlq 144
Cdd:NF033858 84 ---------------GL---GKNL--YPTLSVfeNL---DFFGRLfgqDAAERR------RRIDELLRATglapfADR-- 132
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598215 145 lPADKtlaeLSGGWRRRVLLAQALVAEPDLLLLDEPT 181
Cdd:NF033858 133 -PAGK----LSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-229 |
1.21e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.18 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV-WRAPALKIGELPQELPRADERIV--------FDVVAE 89
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEKNKKKTKEKEKVLEKLViqktrfkkIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 90 GLAEVGKLL--AEYHHLSLNIHTDDDLARLSRVQQELEARD-GWRLQQLVDSTLSRLQlpadKTLAELSGGWRRRVLLAQ 166
Cdd:PRK13651 103 IRRRVGVVFqfAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKrAAKYIELVGLDESYLQ----RSPFELSGGQKRRVALAG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 167 ALVAEPDLLLLDEPTNHLD-IGAIAWLE--EALLGFNGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDpQGVKEILEifDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-208 |
1.23e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.27 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW------------RAPALKIGE 70
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILldgepvrfrsprDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 71 LPQELPRADERivfdVVAEglaevgkllaeyhhlslNIHTDDDLARLSRVQQELEARdgwRLQQLvdstLSRLQL--PAD 148
Cdd:COG1129 84 IHQELNLVPNL----SVAE-----------------NIFLGREPRRGGLIDWRAMRR---RAREL----LARLGLdiDPD 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598215 149 KTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF--NG-AVLFITH 208
Cdd:COG1129 136 TPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLkaQGvAIIYISH 198
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-237 |
1.25e-10 |
|
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: 64.35 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTT--PLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapaLKIGELPQELPRADE 80
Cdd:TIGR02203 330 DVEFRNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI-----LLDGHDLADYTLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 RIVFDVVAEGLAEVGKLLAEyhhlslNIHTDDdLARLSRVQQELEARDGWrLQQLVDSTLSRLQLPADKTLAELSGGWRR 160
Cdd:TIGR02203 405 RRQVALVSQDVVLFNDTIAN------NIAYGR-TEQADRAEIERALAAAY-AQDFVDKLPLGLDTPIGENGVLLSGGQRQ 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 161 RVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL--LGFNGAVLFITHDRAFLQSlATRILELDRGHLI--------- 229
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALerLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVergthnell 555
|
....*...
gi 15598215 230 DWNGDYAS 237
Cdd:TIGR02203 556 ARNGLYAQ 563
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-186 |
1.41e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.11 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV---------W--RAPALKIGE 70
Cdd:PRK10575 10 TTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqplesWssKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 71 LPQELPRADERIVFDVVAeglaeVGKLlaEYHhlslnihtdddlARLSRVQQElearDGWRLQQLVdsTLSRLQLPADKT 150
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVA-----IGRY--PWH------------GALGRFGAA----DREKVEEAI--SLVGLKPLAHRL 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598215 151 LAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDI 186
Cdd:PRK10575 145 VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-230 |
1.44e-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: 61.00 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKG--EQQADDGEVWrapaLKiGELPQELPrADER 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEIL----FK-GEDITDLP-PEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 ivfdvvaeglAEVGKLLAeyhhlslnihtdddlarlsrvQQELEARDGWRLQQLVDStlsrlqlpadktLAE-LSGGWRR 160
Cdd:cd03217 75 ----------ARLGIFLA---------------------FQYPPEIPGVKNADFLRY------------VNEgFSGGEKK 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 161 RVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEA---LLGFNGAVLFITHDRaflqslatRILEL---DRGHLID 230
Cdd:cd03217 112 RNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVinkLREEGKSVLIITHYQ--------RLLDYikpDRVHVLY 179
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-196 |
1.44e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV---WRAPALKIGELPQELPR 77
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqFSHITRLSFEQLQKLVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 78 AD-ERIVFDVVAEGLAEVGKLLAEyhhLSLNIHTDDDLArlsrvqQELEARDGwrlqqlVDSTLSRlqlpadkTLAELSG 156
Cdd:PRK10938 81 DEwQRNNTDMLSPGEDDTGRTTAE---IIQDEVKDPARC------EQLAQQFG------ITALLDR-------RFKYLST 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598215 157 GWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL 196
Cdd:PRK10938 139 GETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELL 178
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-241 |
1.77e-10 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 63.99 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFG-TTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPA----LKIGELPQE---L 75
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdIDRHTLRQFinyL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 76 PRadERIVFDvvaeglaevGKLLaeyhhlslnihtdDDL---ARLSRVQQELeardgWRLQQLV--DSTLSRLQLPADKT 150
Cdd:TIGR01193 554 PQ--EPYIFS---------GSIL-------------ENLllgAKENVSQDEI-----WAACEIAeiKDDIENMPLGYQTE 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 151 LAE----LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFN-GAVLFITHdRAFLQSLATRILELDR 225
Cdd:TIGR01193 605 LSEegssISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQdKTIIFVAH-RLSVAKQSDKIIVLDH 683
|
250 260
....*....|....*....|....*
gi 15598215 226 G---------HLIDWNGDYASfLVH 241
Cdd:TIGR01193 684 GkiieqgshdELLDRNGFYAS-LIH 707
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-185 |
1.98e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.04 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRApalkiGELPQELPrADE 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-----GQDITHVP-AEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 R---------------IVFDVVAEGLaevgkllaeyhhlslnihtdddlaRLSRV-QQELEAR--DGWRLQQLVDStlsr 142
Cdd:PRK09452 86 RhvntvfqsyalfphmTVFENVAFGL------------------------RMQKTpAAEITPRvmEALRMVQLEEF---- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598215 143 lqlpADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD 185
Cdd:PRK09452 138 ----AQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-228 |
2.77e-10 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 60.95 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGT---TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW-----------RAPALKI 68
Cdd:cd03248 11 IVKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgkpisqyehKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 69 GELPQElPRADERIVFDVVAEGLAEVGklLAEYHHLSLNIHTDDDLarlsrvqQELEarDGWrlqqlvdstlsrlQLPAD 148
Cdd:cd03248 91 SLVGQE-PVLFARSLQDNIAYGLQSCS--FECVKEAAQKAHAHSFI-------SELA--SGY-------------DTEVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 149 KTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF--NGAVLFITHDRAFLQSlATRILELDRG 226
Cdd:cd03248 146 EKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVER-ADQILVLDGG 224
|
..
gi 15598215 227 HL 228
Cdd:cd03248 225 RI 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
154-228 |
2.82e-10 |
|
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: 59.75 E-value: 2.82e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598215 154 LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF---NGAVLFITHDRAFLQSLATRILELDRGHL 228
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-230 |
3.18e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.60 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 16 TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapALKIGELPQ--ELPRADERIvfdvvaeglAE 93
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV----IFNGQPMSKlsSAAKAELRN---------QK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 94 VGkLLAEYHHLSLNIHTDDDLARLSRVQQELEARDGWRLQQLVDSTlsRLQLPADKTLAELSGGWRRRVLLAQALVAEPD 173
Cdd:PRK11629 89 LG-FIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598215 174 LLLLDEPTNHLDIGAIAWLEEALLGFN----GAVLFITHDRAFLQSLaTRILELDRGHLID 230
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-229 |
3.39e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 62.87 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAF-GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalKIGELP-QELPRADER 81
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI------LIDGVDiRDLTLESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 ----IVF-DV------VAEGLAeVGKLLAeyhhlslnihTDDDL---ARLSRVQQELEArdgwrlqqlvdstlsrlqLPA 147
Cdd:COG1132 414 rqigVVPqDTflfsgtIRENIR-YGRPDA----------TDEEVeeaAKAAQAHEFIEA------------------LPD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 148 --DKTLAE----LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF--NGAVLFITHdRaflqsLAT- 218
Cdd:COG1132 465 gyDTVVGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLmkGRTTIVIAH-R-----LSTi 538
|
250
....*....|....*
gi 15598215 219 ----RILELDRGHLI 229
Cdd:COG1132 539 rnadRILVLDDGRIV 553
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-230 |
3.46e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.35 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTT--PLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDgevwrAPALKIGELPQELpraDER 81
Cdd:PRK13640 6 VEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD-----NPNSKITVDGITL---TAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 IVFDVvaegLAEVGKLLAEYHHLSLNIHTDDDLARlsrvqqELEARDGWR--LQQLVDSTLSRLQLP--ADKTLAELSGG 157
Cdd:PRK13640 78 TVWDI----REKVGIVFQNPDNQFVGATVGDDVAF------GLENRAVPRpeMIKIVRDVLADVGMLdyIDSEPANLSGG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598215 158 WRRRVLLAQALVAEPDLLLLDEPTNHLDIGA---IAWLEEALLGFNGAVLF-ITHD--RAflqSLATRILELDRGHLID 230
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGkeqILKLIRKLKKKNNLTVIsITHDidEA---NMADQVLVLDDGKLLA 223
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-186 |
3.61e-10 |
|
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: 60.88 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 26 IGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwRAPALKIGELPQELPRADERIVFDVVAEGLAEVGkllaeyhhls 105
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-EIELDTVSYKPQYIKADYEGTVRDLLSSITKDFY---------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 106 lnihtdddlarlSRVQQELEARDGWRLQQLVDStlsrlQLPadktlaELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD 185
Cdd:cd03237 91 ------------THPYFKTEIAKPLQIEQILDR-----EVP------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
.
gi 15598215 186 I 186
Cdd:cd03237 148 V 148
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-228 |
5.14e-10 |
|
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: 62.46 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 14 GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV---------WRAPALK--IGELPQ--ELprade 80
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqWDREELGrhIGYLPQdvEL----- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 rivFD-VVAEGLAEVGKLlaeyhhlslnihtDDDL----ARLSRVQQeleardgwrlqqLVdstlsrLQLPA--DKTLAE 153
Cdd:COG4618 418 ---FDgTIAENIARFGDA-------------DPEKvvaaAKLAGVHE------------MI------LRLPDgyDTRIGE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 154 ----LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF---NGAVLFITHDRAFLQSlATRILELDRG 226
Cdd:COG4618 464 ggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHRPSLLAA-VDKLLVLRDG 542
|
..
gi 15598215 227 HL 228
Cdd:COG4618 543 RV 544
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
4-229 |
5.92e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 60.24 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAfgttPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADdGEV---------WRAPAL--KIGELP 72
Cdd:COG4138 1 LQLNDVAVA----GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEIllngrplsdWSAAELarHRAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 73 QE-LPRAderivfdvvaeglaevgkLLAEYHHLSLNIHtddDLARLSRVQQELEardgwrlqQLVdstlSRLQLpADK-- 149
Cdd:COG4138 76 QQqSPPF------------------AMPVFQYLALHQP---AGASSEAVEQLLA--------QLA----EALGL-EDKls 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 150 -TLAELSGGWRRRVLLAQALV-------AEPDLLLLDEPTNHLDIGAIA----WLEE-ALLGfnGAVLFITHD--RAFLQ 214
Cdd:COG4138 122 rPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLDVAQQAaldrLLRElCQQG--ITVVMSSHDlnHTLRH 199
|
250
....*....|....*
gi 15598215 215 slATRILELDRGHLI 229
Cdd:COG4138 200 --ADRVWLLKQGKLV 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-209 |
6.10e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.13 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSSLFKVV-------KGEQQADDGEVWRAPALKIGELpqelpRADERIVFDVVAEGL 91
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLtmietptGGELYYQGQDLLKADPEAQKLL-----RQKIQIVFQNPYGSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 92 ---AEVGKLLAEyhhlSLNIHTDDDLA-RLSRVQQELeARDGWRLQQlvdstlsrlqlpADKTLAELSGGWRRRVLLAQA 167
Cdd:PRK11308 106 nprKKVGQILEE----PLLINTSLSAAeRREKALAMM-AKVGLRPEH------------YDRYPHMFSGGQRQRIAIARA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598215 168 LVAEPDLLLLDEPTNHLDIGAIAW-------LEEAllgFNGAVLFITHD 209
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVSVQAQvlnlmmdLQQE---LGLSYVFISHD 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-239 |
6.47e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.15 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAF--GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkIGELP-QELPRAD 79
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL------LNGQPiADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 80 ERIVFDVVAEGLAEVGKLLAEyhHLSLNIHTDDDlARLSRVQQELEardgwrLQQLVDStlsrlQLPADKTLAE----LS 155
Cdd:PRK11160 412 LRQAISVVSQRVHLFSATLRD--NLLLAAPNASD-EALIEVLQQVG------LEKLLED-----DKGLNAWLGEggrqLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 156 GGWRRRVLLAQALVAEPDLLLLDEPTNHLDigaiAWLE----EALLGF--NGAVLFITHDRAFLQSLaTRILELDRGHLI 229
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLD----AETErqilELLAEHaqNKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
250
....*....|
gi 15598215 230 DwNGDYASFL 239
Cdd:PRK11160 553 E-QGTHQELL 561
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-229 |
6.86e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 61.39 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEvwrapalkigelpqelpraderI 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQ----------------------I 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VFDvvAEGLAEVGKLL----------AEYHHLSL--NIHTDDDLARLSRvqQELEARDGWRLqqlvdsTLSRLQLPADKT 150
Cdd:PRK11607 77 MLD--GVDLSHVPPYQrpinmmfqsyALFPHMTVeqNIAFGLKQDKLPK--AEIASRVNEML------GLVHMQEFAKRK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 151 LAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD--------IGAIAWLEEAllgfnGAV-LFITHDRAFLQSLATRIL 221
Cdd:PRK11607 147 PHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILERV-----GVTcVMVTHDQEEAMTMAGRIA 221
|
....*...
gi 15598215 222 ELDRGHLI 229
Cdd:PRK11607 222 IMNRGKFV 229
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-229 |
7.39e-10 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 60.16 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFG-TTPL----LDKVSWQIGRGERVCVIGRNGTGKSS-------LFKVVKGEQQADDGEVWRAPALKIGEL 71
Cdd:TIGR04521 1 IKLKNVSYIYQpGTPFekkaLDDVSLTIEDGEFVAIIGHTGSGKSTliqhlngLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 72 pqelpRADERIVFDvvaeglaevgklLAEYHHLSLNIHtdDDLA----RLSRVQQELEARdgwrlqqlVDSTLSRLQLP- 146
Cdd:TIGR04521 81 -----RKKVGLVFQ------------FPEHQLFEETVY--KDIAfgpkNLGLSEEEAEER--------VKEALELVGLDe 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 147 --ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAiawlEEALLG--------FNGAVLFITHDRAFLQSL 216
Cdd:TIGR04521 134 eyLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKG----RKEILDlfkrlhkeKGLTVILVTHSMEDVAEY 209
|
250
....*....|...
gi 15598215 217 ATRILELDRGHLI 229
Cdd:TIGR04521 210 ADRVIVMHKGKIV 222
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
153-209 |
1.08e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.51 E-value: 1.08e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598215 153 ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIA----WLEEALLGFNGAVLFITHD 209
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAqimtLLNELKREFNTAIIMITHD 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-229 |
1.14e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.72 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 16 TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFK-------------VVKGEQQADDGEVW--RAPALKIGELPqelpraDE 80
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnallipsegkvYVDGLDTSDEENLWdiRNKAGMVFQNP------DN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 RIVFDVVAEGLAevgkllaeYHHLSLNIHtdddlarlsrvQQELEARdgwrlqqlVDSTLSRLQLPADKTLAE--LSGGW 158
Cdd:PRK13633 97 QIVATIVEEDVA--------FGPENLGIP-----------PEEIRER--------VDESLKKVGMYEYRRHAPhlLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598215 159 RRRVLLAQALVAEPDLLLLDEPTNHLD-IG---AIAWLEEALLGFNGAVLFITHdraFLQSL--ATRILELDRGHLI 229
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDpSGrreVVNTIKELNKKYGITIILITH---YMEEAveADRIIVMDSGKVV 223
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
322-527 |
1.27e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.90 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 322 VSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGtgkttllklllgdlqptSGK-----IEVGTKLE------------VAY 384
Cdd:PRK11819 12 VSKVVPPKKQILKDISLSFFPGAKIGVLGLNG-----------------AGKstllrIMAGVDKEfegearpapgikVGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 385 FDQlRHQLEPEQTVIDNISEG--------REF--IT-----------------------IDGQNRHVL-SYL---GDFLF 427
Cdd:PRK11819 75 LPQ-EPQLDPEKTVRENVEEGvaevkaalDRFneIYaayaepdadfdalaaeqgelqeiIDAADAWDLdSQLeiaMDALR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 428 SPQrARTPVKALSGGERARLLLAKLF-SKPaNLLVLDEPTNDLDVETLELLEEVLLGFQGTVLMVSHDRAFLDNVVTSTL 506
Cdd:PRK11819 154 CPP-WDAKVTKLSGGERRRVALCRLLlEKP-DMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWIL 231
|
250 260
....*....|....*....|..
gi 15598215 507 -VFEGEGKVREfvGGYQDWLRQ 527
Cdd:PRK11819 232 eLDRGRGIPWE--GNYSSWLEQ 251
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-229 |
1.35e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.23 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW-----------RAPALKIGE 70
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWldgehiqhyasKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 71 LPQELPRADERIVFDVVAEGlaevgkllaEYHHLSLnihtdddlarLSRVQQELEARDGWRLQQLVDSTLsrlqlpADKT 150
Cdd:PRK10253 86 LAQNATTPGDITVQELVARG---------RYPHQPL----------FTRWRKEDEEAVTKAMQATGITHL------ADQS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 151 LAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFN-------GAVLfitHDRAFLQSLATRILEL 223
Cdd:PRK10253 141 VDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNrekgytlAAVL---HDLNQACRYASHLIAL 217
|
....*.
gi 15598215 224 DRGHLI 229
Cdd:PRK10253 218 REGKIV 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-229 |
1.36e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 59.46 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGT-TPL----LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAP---ALKIGELPQEL 75
Cdd:PRK13641 3 IKFENVDYIYSPgTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhiTPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 76 PRADERIVFDVVAEGLAEvGKLLAEYHHLSLNIHTDDDLARLSRVQqeleardgWrlqqlvdstLSRLQLP---ADKTLA 152
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLFE-NTVLKDVEFGPKNFGFSEDEAKEKALK--------W---------LKKVGLSedlISKSPF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 153 ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGA---VLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:PRK13641 145 ELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
317-466 |
1.37e-09 |
|
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: 57.39 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGG-QPLVRDFSMVLQRGDRIGLLGANGtgkttllklllgdlqptSGKievgTKLevayFDQLRHQLEPE 395
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSG-----------------SGK----STL----LKLLLRLYDPT 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 396 QtvidniseGRefITIDGQN---------RHVLSYLG--DFLFSpqrarTPVKA--LSGGERARLLLAKLFSKPANLLVL 462
Cdd:cd03228 56 S--------GE--ILIDGVDlrdldleslRKNIAYVPqdPFLFS-----GTIREniLSGGQRQRIAIARALLRDPPILIL 120
|
....
gi 15598215 463 DEPT 466
Cdd:cd03228 121 DEAT 124
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-229 |
1.61e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.94 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRapalkigelpqelpraDERIVFdvvaegLAEVGkll 98
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV----------------NGRVSA------LLELG--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 99 AEYH-HLSL--NIHTdddLARL---SRvqQELEArdgwRLQQLVD-STLSR-LQLPAdKTlaeLSGGWRRRVLLAQALVA 170
Cdd:COG1134 97 AGFHpELTGreNIYL---NGRLlglSR--KEIDE----KFDEIVEfAELGDfIDQPV-KT---YSSGMRARLAFAVATAV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 171 EPDLLLLDEptnHLDIG-------AIAWLEEaLLGFNGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:COG1134 164 DPDILLVDE---VLAVGdaafqkkCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-230 |
1.65e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAF----GTTPLLDKVSWQIGRGERVCVIGRNGTGKS----SLFKVVK--GEQQADDGEVWRAPALKIGELP 72
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEqaGGLVQCDKMLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 73 -------QELPRADERIVFDVVAEGLAEV---GKLLAEyhhlSLNIHTDddlarLSRVQQELEARdgwrlqqlvdSTLSR 142
Cdd:PRK10261 92 eqsaaqmRHVRGADMAMIFQEPMTSLNPVftvGEQIAE----SIRLHQG-----ASREEAMVEAK----------RMLDQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 143 LQLPADKTLA-----ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWL--------EEALLGfngaVLFITHD 209
Cdd:PRK10261 153 VRIPEAQTILsryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQIlqlikvlqKEMSMG----VIFITHD 228
|
250 260
....*....|....*....|.
gi 15598215 210 RAFLQSLATRILELDRGHLID 230
Cdd:PRK10261 229 MGVVAEIADRVLVMYQGEAVE 249
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-226 |
1.68e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 58.83 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRApalkiGELPQELPRADERI- 82
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVN-----GQTINLVRDKDGQLk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VFDVVAEGLAEVgKLLAEYHHLSLNIHT-------DDDLARLSRVQQELEARDGWRLQQLVDSTLSRLQLPADktlaeLS 155
Cdd:PRK10619 81 VADKNQLRLLRT-RLTMVFQHFNLWSHMtvlenvmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVH-----LS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598215 156 GGWRRRVLLAQALVAEPDLLLLDEPTNHLD---IGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRG 226
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
19-185 |
1.77e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.44 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSW-----------QIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQELPraderivfdvv 87
Cdd:PRK10771 4 LTDITWlyhhlpmrfdlTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 88 aeglaeVGKLLAE---YHHLSL--NIH--TDDDLaRLSRVQQELEARdgwRLQQL-VDSTLSRLqlPAdktlaELSGGWR 159
Cdd:PRK10771 73 ------VSMLFQEnnlFSHLTVaqNIGlgLNPGL-KLNAAQREKLHA---IARQMgIEDLLARL--PG-----QLSGGQR 135
|
170 180
....*....|....*....|....*.
gi 15598215 160 RRVLLAQALVAEPDLLLLDEPTNHLD 185
Cdd:PRK10771 136 QRVALARCLVREQPILLLDEPFSALD 161
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-239 |
2.06e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.48 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW----------RAPALKIGELPQELPRADE-----RIV 83
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiyigdkkNNHELITNPYSKKIKNFKElrrrvSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 84 FDvvaeglaevgklLAEYHHLSLNIHTDDDLARLSRVQQELEARdgwrlqQLVDSTLSRLQLPA---DKTLAELSGGWRR 160
Cdd:PRK13631 122 FQ------------FPEYQLFKDTIEKDIMFGPVALGVKKSEAK------KLAKFYLNKMGLDDsylERSPFGLSGGQKR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 161 RVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALL---GFNGAVLFITHDRAFLQSLATRILELDRGHLIDWNGDYAS 237
Cdd:PRK13631 184 RVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILdakANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
..
gi 15598215 238 FL 239
Cdd:PRK13631 264 FT 265
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-229 |
2.10e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 58.91 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalkigelpqelpraderIV--FDVVAEG--LAEV 94
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI---------------------IIdgVDITDKKvkLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 95 GK---LLAEYHHLSLNIHT-DDDLA----RLSRVQQELEARdgwrlqqlVDSTLSRLQLP----ADKTLAELSGGWRRRV 162
Cdd:PRK13637 82 RKkvgLVFQYPEYQLFEETiEKDIAfgpiNLGLSEEEIENR--------VKRAMNIVGLDyedyKDKSPFELSGGQKRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598215 163 LLAQALVAEPDLLLLDEPTNHLD-------IGAIAWLEEAllgFNGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDpkgrdeiLNKIKELHKE---YNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
8-229 |
2.73e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 59.35 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 8 DVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkI-GE--LPQELPRADERIVF 84
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF------IdGEdvTHRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 85 dvvaeglaevgKLLAEYHHLSLNIHTDDDLARLSRVQQELEARDGWRLQqLVDstlsrLQLPADKTLAELSGGWRRRVLL 164
Cdd:PRK11432 85 -----------QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALE-LVD-----LAGFEDRYVDQISGGQQQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598215 165 AQALVAEPDLLLLDEPTNHLDIG-------AIAWLEEAllgFNGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDANlrrsmreKIRELQQQ---FNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-186 |
2.94e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.31 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAfgTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPalKIGELPQE---LPRA-D 79
Cdd:TIGR01271 429 LFFSNFSLY--VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RISFSPQTswiMPGTiK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 80 ERIVFDVVAEglaevgkllaEYHHLSL--NIHTDDDLARLSRvqqeleardgwrlqqlvdstlsrlqlpADKT-LAE--- 153
Cdd:TIGR01271 505 DNIIFGLSYD----------EYRYTSVikACQLEEDIALFPE---------------------------KDKTvLGEggi 547
|
170 180 190
....*....|....*....|....*....|....
gi 15598215 154 -LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDI 186
Cdd:TIGR01271 548 tLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-226 |
2.98e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.08 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwRAPALKIGELP-QELPRADE 80
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI-LLRGQHIEGLPgHQIARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 RIVFD--------VVAEGLaevgkLLAEYHHLSLNIhtdddLARLSRV----QQELEARDgwRLQQLVDsTLSRLQLpAD 148
Cdd:PRK11300 83 VRTFQhvrlfremTVIENL-----LVAQHQQLKTGL-----FSGLLKTpafrRAESEALD--RAATWLE-RVGLLEH-AN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 149 KTLAELSGGWRRRVLLAQALVAEPDLLLLDEP--------TNHLDiGAIAWLEEAllgFNGAVLFITHDRAFLQSLATRI 220
Cdd:PRK11300 149 RQAGNLAYGQQRRLEIARCMVTQPEILMLDEPaaglnpkeTKELD-ELIAELRNE---HNVTVLLIEHDMKLVMGISDRI 224
|
....*.
gi 15598215 221 LELDRG 226
Cdd:PRK11300 225 YVVNQG 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
317-466 |
3.16e-09 |
|
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: 56.55 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPG-GQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEVAYFDQLRHQLepe 395
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLI--- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598215 396 qTVIDnisegrefitidgQNRHvlsylgdfLFSPQRARTPVKALSGGERARLLLAKLFSKPANLLVLDEPT 466
Cdd:cd03247 78 -SVLN-------------QRPY--------LFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPT 126
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-230 |
3.48e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.43 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 9 VSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapaLKIGE--LPQELPRADERivfdv 86
Cdd:TIGR03269 290 ISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVN----VRVGDewVDMTKPGPDGR----- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 87 vaeGLAE--VGKLLAEYhhlSLNIHTD--DDLARLSRVQ--QELEARDGWRLQQLVDSTLSRLQLPADKTLAELSGGWRR 160
Cdd:TIGR03269 361 ---GRAKryIGILHQEY---DLYPHRTvlDNLTEAIGLElpDELARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERH 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598215 161 RVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLG----FNGAVLFITHDRAFLQSLATRILELDRGHLID 230
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKareeMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
15-226 |
3.77e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.20 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 15 TTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGE------------VWRAPAlKIGELPQElprADERI 82
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQiiidgdllteenVWDIRH-KIGMVFQN---PDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VF----DVVAEGLAEVGKLLAEYhhlslnihtdddlarLSRVQQELEardgwrlqqLVDstlsrLQLPADKTLAELSGGW 158
Cdd:PRK13650 95 VGatveDDVAFGLENKGIPHEEM---------------KERVNEALE---------LVG-----MQDFKEREPARLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598215 159 RRRVLLAQALVAEPDLLLLDEPTNHLD-------IGAIAWLEEAllgFNGAVLFITHDRAFLqSLATRILELDRG 226
Cdd:PRK13650 146 KQRVAIAGAVAMRPKIIILDEATSMLDpegrlelIKTIKGIRDD---YQMTVISITHDLDEV-ALSDRVLVMKNG 216
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-186 |
4.38e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.97 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 14 GTTPLLDkVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGE--VWRAPALKigELPQEL----PRADE-RIVFDV 86
Cdd:PRK15056 19 GHTALRD-ASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKisILGQPTRQ--ALQKNLvayvPQSEEvDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 87 VAEGLAEVGKllaeYHHLSLnihtdddlarLSRVQqeleARDgwrlQQLVDSTLSRLQLPA--DKTLAELSGGWRRRVLL 164
Cdd:PRK15056 96 LVEDVVMMGR----YGHMGW----------LRRAK----KRD----RQIVTAALARVDMVEfrHRQIGELSGGQKKRVFL 153
|
170 180
....*....|....*....|..
gi 15598215 165 AQALVAEPDLLLLDEPTNHLDI 186
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDV 175
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-223 |
4.40e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.17 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGevwrapalkigelpqelpradeRI 82
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESG----------------------QI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VFDVVAEGLAEVGKLLAEYHHLSlniHTDDDLARLSRVQQeLEARDGWRLQQLVDSTLSRLQLP--ADKTLAELSGGWRR 160
Cdd:PRK13543 69 QIDGKTATRGDRSRFMAYLGHLP---GLKADLSTLENLHF-LCGLHGRRAKQMPGSALAIVGLAgyEDTLVRQLSAGQKK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 161 RVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL---LGFNGAVLFITHDRAFLQSLATRILEL 223
Cdd:PRK13543 145 RLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMIsahLRGGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-208 |
4.82e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.27 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW--------RAP----ALKI 68
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILidgkpvriRSPrdaiALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 69 GELPQE--LpraderivFDV--VAE----GLAEVGKLLAeyhhlslnihtddDLARLSRVQQELEARDGwrlqqlvdstl 140
Cdd:COG3845 83 GMVHQHfmL--------VPNltVAEnivlGLEPTKGGRL-------------DRKAARARIRELSERYG----------- 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598215 141 srLQLPADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIawleEALLGF------NG-AVLFITH 208
Cdd:COG3845 131 --LDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEA----DELFEIlrrlaaEGkSIIFITH 199
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-209 |
4.93e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 58.20 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW----RAPALKIGELpQELpRADERIVF---------- 84
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqDITGLSGREL-RPL-RRRMQMVFqdpyaslnpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 85 ----DVVAEGLAevgkllaeyhhlslnIHTDDDlarlsrvQQELEARdgwrlqqlVDSTLSRLQLP---ADKTLAELSGG 157
Cdd:COG4608 112 mtvgDIIAEPLR---------------IHGLAS-------KAERRER--------VAELLELVGLRpehADRYPHEFSGG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598215 158 WRRRVLLAQALVAEPDLLLLDEPTNHLD--IGA--IAWLEE--ALLGFngAVLFITHD 209
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDvsIQAqvLNLLEDlqDELGL--TYLFISHD 217
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-229 |
5.07e-09 |
|
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: 56.41 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKG--EQQADDGEVW--------RAPALKIGELP 72
Cdd:cd03213 9 LTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLingrpldkRSFRKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 73 QElpraderivfdvvaeglaevgkllaEYHHLSLNIHtdddlarlsrvqqelEArdgwrlqqlvdstlsrLQLPADktLA 152
Cdd:cd03213 89 QD-------------------------DILHPTLTVR---------------ET----------------LMFAAK--LR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 153 ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL--LGFNG-AVLFITHD-RAFLQSLATRILELDRGHL 228
Cdd:cd03213 111 GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLrrLADTGrTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
.
gi 15598215 229 I 229
Cdd:cd03213 191 I 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
8-185 |
5.19e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 8 DVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGE-------------QQADDGE-VWRAPAlKIGELPQ 73
Cdd:PRK10938 265 NGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysndltlfgRRRGSGEtIWDIKK-HIGYVSS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 74 ELpRADERI---VFDVVAEGLAEvgkllaeyhhlSLNIHtdddlarlsrvQQELEardgwRLQQLVDSTLSRLQLP---A 147
Cdd:PRK10938 344 SL-HLDYRVstsVRNVILSGFFD-----------SIGIY-----------QAVSD-----RQQKLAQQWLDILGIDkrtA 395
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598215 148 DKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD 185
Cdd:PRK10938 396 DAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-228 |
5.37e-09 |
|
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: 58.20 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 21 KVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQAD------DGEVWRAPALKIgELPQELPRADerIVFdvvaeglaEV 94
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDegeivlNGRTLFDSRKGI-FLPPEKRRIG--YVF--------QE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 95 GKLlaeYHHLSL--NIhtdddLARLSRVQQELEARDGWRLQQL--VDSTLSRLqlPADktlaeLSGGWRRRVLLAQALVA 170
Cdd:TIGR02142 84 ARL---FPHLSVrgNL-----RYGMKRARPSERRISFERVIELlgIGHLLGRL--PGR-----LSGGEKQRVAIGRALLS 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598215 171 EPDLLLLDEPTNHLDIGA----IAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHL 228
Cdd:TIGR02142 149 SPRLLLMDEPLAALDDPRkyeiLPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-185 |
5.76e-09 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 56.90 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 18 LLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADD---GEVW-----RAPAL---KIGELPQelpraderivFDV 86
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILfngqpRKPDQfqkCVAYVRQ----------DDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 87 VAEGLAeVGKLLAEYHHLSLNIHTDDdlarlsRVQQELEARDgwRLQQLVDSTLsrlqlpADKTLAELSGGWRRRVLLAQ 166
Cdd:cd03234 92 LLPGLT-VRETLTYTAILRLPRKSSD------AIRKKRVEDV--LLRDLALTRI------GGNLVKGISGGERRRVSIAV 156
|
170
....*....|....*....
gi 15598215 167 ALVAEPDLLLLDEPTNHLD 185
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLD 175
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
316-510 |
6.19e-09 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 57.02 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 316 VIVVEHVSFAHpGGQPLVRDFSMVLQRGDRIGLLGANgtgkttllklllgdLQPTSGKIEV-GTKLE-----VAYFDQlR 389
Cdd:COG1121 6 AIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNgagkstllkailglLPPTSGTVRLfGKPPRrarrrIGYVPQ-R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 390 HQLEPEQ--TVIDNISEGRefitidgqnrhvLSYLGDFLFSPQR-----------------ARTPVKALSGGERARLLLA 450
Cdd:COG1121 84 AEVDWDFpiTVRDVVLMGR------------YGRRGLFRRPSRAdreavdealervgledlADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598215 451 KLFSKPANLLVLDEPTN--DLDVETLelleevllgF---------QG-TVLMVSHD----RAFLDNVV--TSTLVFEG 510
Cdd:COG1121 152 RALAQDPDLLLLDEPFAgvDAATEEA---------LyellrelrrEGkTILVVTHDlgavREYFDRVLllNRGLVAHG 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-245 |
7.96e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSS----LFKVVKGEqqaddGEVW-RAPALKIGELPQELP-RADERIVF-------- 84
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWfDGQPLHNLNRRQLLPvRHRIQVVFqdpnssln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 85 ------DVVAEGLaevgkllaEYHHLSLNIHtdddlarlSRVQQELEArdgwrLQQLVDSTLSRLQLPAdktlaELSGGW 158
Cdd:PRK15134 377 prlnvlQIIEEGL--------RVHQPTLSAA--------QREQQVIAV-----MEEVGLDPETRHRYPA-----EFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 159 RRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG----AVLFITHDRAFLQSLATRILELDRGHLIDwNGD 234
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQkhqlAYLFISHDLHVVRALCHQVIVLRQGEVVE-QGD 509
|
250
....*....|.
gi 15598215 235 YASFLVHKEQQ 245
Cdd:PRK15134 510 CERVFAAPQQE 520
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
147-228 |
8.02e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 147 ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGA---IAWLEEALLGFNGAVLFITHDRAFLQSLATRILEL 223
Cdd:PRK15439 397 AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSArndIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVM 476
|
....*
gi 15598215 224 DRGHL 228
Cdd:PRK15439 477 HQGEI 481
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-210 |
8.10e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 56.26 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPAlKIGELPQELPR----- 77
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE-DISTLKPEIYRqqvsy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 78 -ADERIVF-DVVAEGLA---EVGKLLAEYHHLSlnihtdDDLARLsrvqqeleardgwrlqQLVDSTLsrlqlpaDKTLA 152
Cdd:PRK10247 86 cAQTPTLFgDTVYDNLIfpwQIRNQQPDPAIFL------DDLERF----------------ALPDTIL-------TKNIA 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598215 153 ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG----AVLFITHDR 210
Cdd:PRK10247 137 ELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVReqniAVLWVTHDK 198
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-236 |
8.43e-09 |
|
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: 56.73 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 18 LLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGevwrapalkigelpqelpradeRIVFDVVAEGLA----- 92
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENG----------------------RVLVDGHDLALAdpawl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 93 --EVGKLLAEYHHLSLNIHTDDDLARLSRVQQELEArdgwrLQQLVDSTLSRLQLPA--DKTLAE----LSGGWRRRVLL 164
Cdd:cd03252 75 rrQVGVVLQENVLFNRSIRDNIALADPGMSMERVIE-----AAKLAGAHDFISELPEgyDTIVGEqgagLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 165 AQALVAEPDLLLLDEPTNHLDI---GAIAWLEEALLGfNGAVLFITHDRAFLQSlATRILELDRG---------HLIDWN 232
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYeseHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGriveqgshdELLAEN 227
|
....
gi 15598215 233 GDYA 236
Cdd:cd03252 228 GLYA 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
318-513 |
8.68e-09 |
|
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: 55.94 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 318 VVEHVSFAHPGG-QPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV-GTKLEVAYFDQLRHQL--- 392
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLTKLSLKELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 393 --EPEQ-----TVIDNISEGREFITIDGQ--NRHVLSYLGDFLFSPQRARtPVKALSGGERARLLLAKLFSKPANLLVLD 463
Cdd:cd03225 81 fqNPDDqffgpTVEEEVAFGLENLGLPEEeiEERVEEALELVGLEGLRDR-SPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598215 464 EPTN--DLDVETLELLEEVLLGFQG-TVLMVSHDRAFLDNVVTSTLVFEgEGK 513
Cdd:cd03225 160 EPTAglDPAGRRELLELLKKLKAEGkTIIIVTHDLDLLLELADRVIVLE-DGK 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
16-229 |
9.20e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.05 E-value: 9.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 16 TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwRAPALKIGELPQELPRA---------DERI---- 82
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV-KVMGREVNAENEKWVRSkvglvfqdpDDQVfsst 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VFDVVAEGLAEVGKLLAEYhhlslnihtdddlarLSRVQQELEARDGWRLqqlvdstlsrlqlpADKTLAELSGGWRRRV 162
Cdd:PRK13647 97 VWDDVAFGPVNMGLDKDEV---------------ERRVEEALKAVRMWDF--------------RDKPPYHLSYGQKKRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 163 LLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGA---VLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgktVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
101-230 |
9.77e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.77 E-value: 9.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 101 YHHLSL--NIHTDDDLARLSRVQQELEARDGWRLQQ--LVDSTLSRLQlpaDKTlAELSGGWRRRVLLAQALVAEPDLLL 176
Cdd:PRK14267 97 FPHLTIydNVAIGVKLNGLVKSKKELDERVEWALKKaaLWDEVKDRLN---DYP-SNLSGGQRQRLVIARALAMKPKILL 172
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 177 LDEPTNHLDIGAIAWLEEALLGFNG--AVLFITHDRAFLQSLATRILELDRGHLID 230
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-229 |
9.79e-09 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 56.88 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 7 TDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW---------RAPAL------KIGEL 71
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLidgqdiaamSRKELrelrrkKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 72 PQELPRADERIVFDVVAEGLaevgkllaEYHHLSLNIhtdddlaRLSRVQQELEARD--GWrlqqlvdstlsrlqlpADK 149
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGL--------EVQGVPRAE-------REERAAEALELVGleGW----------------EHK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 150 TLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG----AVLFITHDRAFLQSLATRILELDR 225
Cdd:cd03294 157 YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAelqkTIVFITHDLDEALRLGDRIAIMKD 236
|
....
gi 15598215 226 GHLI 229
Cdd:cd03294 237 GRLV 240
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-243 |
9.93e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.71 E-value: 9.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKgeQQAD-DGEVWRAPALKIGELPQELPRADe 80
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN--RMNDlNPEVTITGSIVYNGHNIYSPRTD- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 rivfdvVAEGLAEVGKLLAEYHHLSLNIHTD----------DDLARLSR-VQQELEARDGWrlqqlvDSTLSRLQlpaDK 149
Cdd:PRK14239 81 ------TVDLRKEIGMVFQQPNPFPMSIYENvvyglrlkgiKDKQVLDEaVEKSLKGASIW------DEVKDRLH---DS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 150 TLAeLSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHDRAFLQslATRILE-----LD 224
Cdd:PRK14239 146 ALG-LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQ--ASRISDrtgffLD 222
|
250 260
....*....|....*....|.
gi 15598215 225 rGHLIDWNGDYASFL--VHKE 243
Cdd:PRK14239 223 -GDLIEYNDTKQMFMnpKHKE 242
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-229 |
1.09e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 57.50 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 5 KFTDVSLAF----GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW--------------RAPAL 66
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLvdgqdltalsekelRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 67 KIGELPQELPRADERIVFDVVAeglaevgkllaeyhhLSLnihtddDLARLSRvqQELEARdgwrlqqlVDSTLSRLQLP 146
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVA---------------LPL------ELAGTPK--AEIKAR--------VTELLELVGLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 147 --ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG----AVLFITHDRAFLQSLATRI 220
Cdd:PRK11153 132 dkADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelglTIVLITHEMDVVKRICDRV 211
|
....*....
gi 15598215 221 LELDRGHLI 229
Cdd:PRK11153 212 AVIDAGRLV 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-229 |
1.09e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 56.92 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAF-GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrAPALKIGElPQELP--RAD 79
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL-VSGIDTGD-FSKLQgiRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 80 ERIVFDVVAEGLaeVGKLLAEyhhlslnihtddDLArlsrVQQELEARDGWRLQQLVDSTLSRLQLPA--DKTLAELSGG 157
Cdd:PRK13644 79 VGIVFQNPETQF--VGRTVEE------------DLA----FGPENLCLPPIEIRKRVDRALAEIGLEKyrHRSPKTLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598215 158 WRRRVLLAQALVAEPDLLLLDEPTNHLDI-GAIAWLE--EALLGFNGAVLFITHDRAFLQSlATRILELDRGHLI 229
Cdd:PRK13644 141 QGQCVALAGILTMEPECLIFDEVTSMLDPdSGIAVLEriKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIV 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
317-514 |
1.14e-08 |
|
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: 55.80 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGTGkttllklllgdLQPTSGKIEV-GTKLEVAYFDQLR------ 389
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGkstllrllnglLKPTSGEVLVdGKDITKKNLRELRrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 390 -----HQL-EPeqTVIDNISEG-------REfiTIDGQNRHVLSYLG--DFlfspqrARTPVKALSGGERARLLLAK-LF 453
Cdd:COG1122 81 fqnpdDQLfAP--TVEEDVAFGpenlglpRE--EIRERVEEALELVGleHL------ADRPPHELSGGQKQRVAIAGvLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598215 454 SKPAnLLVLDEPTN--DLDVETLELLEEVLLGFQG-TVLMVSHDRAFLDNVVTSTLVFEgEGKV 514
Cdd:COG1122 151 MEPE-VLVLDEPTAglDPRGRRELLELLKRLNKEGkTVIIVTHDLDLVAELADRVIVLD-DGRI 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
299-466 |
1.22e-08 |
|
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: 57.76 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 299 QGKASFQLESADKSGKQVIVVEHVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV-G 377
Cdd:TIGR02868 317 VAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 378 TKLEVAYFDQLRHQ--LEPEQ------TVIDNISEGREFITiDGQNRHVLSY--LGDFLFS-PQRARTPV----KALSGG 442
Cdd:TIGR02868 397 VPVSSLDQDEVRRRvsVCAQDahlfdtTVRENLRLARPDAT-DEELWAALERvgLADWLRAlPDGLDTVLgeggARLSGG 475
|
170 180
....*....|....*....|....
gi 15598215 443 ERARLLLAKLFSKPANLLVLDEPT 466
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPT 499
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-181 |
1.30e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.04 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapaLKIGELPQELPRAde 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI-----VFDGKDITDWQTA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 RIVFDVVA---EGLAEVGKLLAEYhhlslNIHTDDDLARLSRVQQELEardgwRLQQLvdstLSRLQLPADKTLAELSGG 157
Cdd:PRK11614 76 KIMREAVAivpEGRRVFSRMTVEE-----NLAMGGFFAERDQFQERIK-----WVYEL----FPRLHERRIQRAGTMSGG 141
|
170 180
....*....|....*....|....
gi 15598215 158 WRRRVLLAQALVAEPDLLLLDEPT 181
Cdd:PRK11614 142 EQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
152-229 |
1.34e-08 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 57.03 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 152 AELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGA----IAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGH 227
Cdd:COG4148 132 ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkaeiLPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGR 211
|
..
gi 15598215 228 LI 229
Cdd:COG4148 212 VV 213
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-229 |
1.55e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 56.15 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 5 KFTDVSLAFGT--TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalKIgelpqelprADERI 82
Cdd:PRK13632 9 KVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI------KI---------DGITI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VFDVVAEGLAEVGKLLAEYHHLSLNIHTDDDLARlsrvqqELEAR--DGWRLQQLVDSTLSRLQLPA--DKTLAELSGGW 158
Cdd:PRK13632 74 SKENLKEIRKKIGIIFQNPDNQFIGATVEDDIAF------GLENKkvPPKKMKDIIDDLAKKVGMEDylDKEPQNLSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598215 159 RRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF----NGAVLFITHD--RAFlqsLATRILELDRGHLI 229
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITHDmdEAI---LADKVIVFSEGKLI 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-244 |
1.58e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQ-ADDGEVW--------RAPA----LKIGELPQElpRADERIVFD 85
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFingkpvdiRNPAqairAGIAMVPED--RKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 86 VvaeglaEVGKllaeyhhlSLNIHTDDDLARLSRVQQELEardgwrlQQLVDSTLSRLQLPA---DKTLAELSGGWRRRV 162
Cdd:TIGR02633 354 L------GVGK--------NITLSVLKSFCFKMRIDAAAE-------LQIIGSAIQRLKVKTaspFLPIGRLSGGNQQKA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 163 LLAQALVAEPDLLLLDEPTNHLDIGA---IAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLidwNGDYASFL 239
Cdd:TIGR02633 413 VLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL---KGDFVNHA 489
|
....*
gi 15598215 240 VHKEQ 244
Cdd:TIGR02633 490 LTQEQ 494
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
317-534 |
1.69e-08 |
|
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: 57.54 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGGQPLV-RDFSMVLQRGDRIGLLGAN-------GtgkttllKLLLGDLQPTSGKIEVGtKLEVAYFD-- 386
Cdd:COG2274 474 IELENVSFRYPGDSPPVlDNISLTIKPGERVAIVGRSgsgkstlL-------KLLLGLYEPTSGRILID-GIDLRQIDpa 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 387 QLRHQL-----EPEQ---TVIDNISEGREFITIDgQNRHVL--SYLGDFLFS-PQRARTPV----KALSGGERARLLLAK 451
Cdd:COG2274 546 SLRRQIgvvlqDVFLfsgTIRENITLGDPDATDE-EIIEAArlAGLHDFIEAlPMGYDTVVgeggSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 452 LFSKPANLLVLDEPTN--DLDVETLELLEEVLLGFQGTVLMVSHDRAFLDNvVTSTLVFEgEGKVREFvGGYQDWLRQGG 529
Cdd:COG2274 625 ALLRNPRILILDEATSalDAETEAIILENLRRLLKGRTVIIIAHRLSTIRL-ADRIIVLD-KGRIVED-GTHEELLARKG 701
|
....*
gi 15598215 530 TPRLL 534
Cdd:COG2274 702 LYAEL 706
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-227 |
1.80e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.64 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 20 DKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV-WRAPAL-KIGELPQELPRADERIVFDvvaEGLAE---- 93
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLGKDLlGMKDDEWRAVRSDIQMIFQ---DPLASlnpr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 94 --VGKLLAE----YH-HLSlnihtdddlarlsrvQQELEARdgwrlqqlVDSTLSRLQL-P--ADKTLAELSGGWRRRVL 163
Cdd:PRK15079 115 mtIGEIIAEplrtYHpKLS---------------RQEVKDR--------VKAMMLKVGLlPnlINRYPHEFSGGQCQRIG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 164 LAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL------LGFngAVLFITHDRAFLQSLATRILELDRGH 227
Cdd:PRK15079 172 IARALILEPKLIICDEPVSALDVSIQAQVVNLLqqlqreMGL--SLIFIAHDLAVVKHISDRVLVMYLGH 239
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-229 |
1.87e-08 |
|
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: 55.19 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAF--GTTPLLDKVSWQIGRGERVCVIGRNGTGKSS----LFKVVkgeqQADDGEVWrapalkIGELP-QELP 76
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSIL------IDGVDiSKIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 77 RADER----------IVFD-VVAEGLAevgkllaeyhhlSLNIHTDDDLAR-LSRVQqeleardgwrLQQLVDSTLSRLQ 144
Cdd:cd03244 73 LHDLRsrisiipqdpVLFSgTIRSNLD------------PFGEYSDEELWQaLERVG----------LKEFVESLPGGLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 145 LPADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL-LGFNGA-VLFITHdRafLQSLAT--RI 220
Cdd:cd03244 131 TVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIrEAFKDCtVLTIAH-R--LDTIIDsdRI 207
|
....*....
gi 15598215 221 LELDRGHLI 229
Cdd:cd03244 208 LVLDKGRVV 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
153-232 |
1.91e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.41 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 153 ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIA----WLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHL 228
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAqilqLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
....
gi 15598215 229 IDWN 232
Cdd:PRK15134 236 VEQN 239
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-209 |
2.33e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 55.53 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAF-GTTPL-LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQELpRADE 80
Cdd:PRK13648 7 IIVFKNVSFQYqSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL-RKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 RIVFDV-------------VAEGLaevgkllaEYHHLSLnihtdDDLARlsRVQQELEARDgwrlqqlvdsTLSRlqlpA 147
Cdd:PRK13648 86 GIVFQNpdnqfvgsivkydVAFGL--------ENHAVPY-----DEMHR--RVSEALKQVD----------MLER----A 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 148 DKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGA----IAWLEEALLGFNGAVLFITHD 209
Cdd:PRK13648 137 DYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDArqnlLDLVRKVKSEHNITIISITHD 202
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-238 |
2.35e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.78 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkIGE--LPQELPRADErivfdvVAEGLAEVGK 96
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTI------VGDyaIPANLKKIKE------VKRLRKEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 97 LLA--EYHHLSLNIHTDDDLARLSRVQQELEArdgwrlQQLVDSTLSRLQLPAD---KTLAELSGGWRRRVLLAQALVAE 171
Cdd:PRK13645 95 VFQfpEYQLFQETIEKDIAFGPVNLGENKQEA------YKKVPELLKLVQLPEDyvkRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598215 172 PDLLLLDEPTNHLDIGA----IAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLIDWNGDYASF 238
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
328-496 |
3.08e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 54.16 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 328 GGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEVAYFDQlrHQLEPEQ---TVIDNISE 404
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--RSEVPDSlplTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 405 GR-----EFITIDGQNRHVLSY------LGDFlfspqrARTPVKALSGGERARLLLAKLFSKPANLLVLDEPTN--DLDV 471
Cdd:NF040873 81 GRwarrgLWRRLTRDDRAAVDDalervgLADL------AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTglDAES 154
|
170 180
....*....|....*....|....*.
gi 15598215 472 ETLELLEEVLLGFQG-TVLMVSHDRA 496
Cdd:NF040873 155 RERIIALLAEEHARGaTVVVVTHDLE 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
319-509 |
3.09e-08 |
|
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: 53.40 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 319 VEHVSFAHpGGQPLVRDFSMVLQRGDRIGLLGANGtgkttllklllgdlqptSGKievgTklevAYFDQLRHQLEPeqtv 398
Cdd:cd00267 2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNG-----------------SGK----S----TLLRAIAGLLKP---- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 399 idniSEGRefITIDGQNRHVLS---YLGDFLFSPQrartpvkaLSGGERARLLLAKLFSKPANLLVLDEPTN--DLDVET 473
Cdd:cd00267 52 ----TSGE--ILIDGKDIAKLPleeLRRRIGYVPQ--------LSGGQRQRVALARALLLNPDLLLLDEPTSglDPASRE 117
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598215 474 LELLEEVLLGFQG-TVLMVSHDRAFLDNVVTSTLVFE 509
Cdd:cd00267 118 RLLELLRELAEEGrTVIIVTHDPELAELAADRVIVLK 154
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-242 |
3.13e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.57 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGT--TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapaLKIGELPQELPRADER 81
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI-----LLDGHDLRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 IVFDVVaeglaevgkllaeyhhlSLNIHT-DDDLA---------RLSRVQQELEARDGWRLQqlvdsTLSRLQLPADKTL 151
Cdd:PRK11176 417 NQVALV-----------------SQNVHLfNDTIAnniayarteQYSREQIEEAARMAYAMD-----FINKMDNGLDTVI 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 152 AE----LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDI---GAI-AWLEEalLGFNGAVLFITHDRAFLQSlATRILEL 223
Cdd:PRK11176 475 GEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTeseRAIqAALDE--LQKNRTSLVIAHRLSTIEK-ADEILVV 551
|
250
....*....|....*....
gi 15598215 224 DRGHLIDwNGDYASFLVHK 242
Cdd:PRK11176 552 EDGEIVE-RGTHAELLAQN 569
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-229 |
3.35e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.66 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MT-LLKFTDVSLAF----GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEvWRAPALKIGELPQEL 75
Cdd:PRK10535 1 MTaLLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGT-YRVAGQDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 76 PRADERIVFdvvaeglaevGKLLAEYH---HLSL--NIHTDDDLARLSRVQQELEARDgwrlqqlvdsTLSRLQLP--AD 148
Cdd:PRK10535 80 LAQLRREHF----------GFIFQRYHllsHLTAaqNVEVPAVYAGLERKQRLLRAQE----------LLQRLGLEdrVE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 149 KTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD----IGAIAWLEEaLLGFNGAVLFITHDRAFLQSlATRILELD 224
Cdd:PRK10535 140 YQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDshsgEEVMAILHQ-LRDRGHTVIIVTHDPQVAAQ-AERVIEIR 217
|
....*
gi 15598215 225 RGHLI 229
Cdd:PRK10535 218 DGEIV 222
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-239 |
3.52e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 18 LLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPAlkIGELPQE--LPRADER--IVFdvvaeglae 93
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS--IAYVPQQawIMNATVRgnILF--------- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 94 vgkllaeyhhlslniHTDDDLARLS---RVQQeLEARdgwrLQQLVdstlSRLQLPADKTLAELSGGWRRRVLLAQALVA 170
Cdd:PTZ00243 744 ---------------FDEEDAARLAdavRVSQ-LEAD----LAQLG----GGLETEIGEKGVNLSGGQKARVSLARAVYA 799
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598215 171 EPDLLLLDEPTNHLD--IGAIAwLEEALLG-FNGAVLFITHDRAFLQSLATRILELDRGHlIDWNGDYASFL 239
Cdd:PTZ00243 800 NRDVYLLDDPLSALDahVGERV-VEECFLGaLAGKTRVLATHQVHVVPRADYVVALGDGR-VEFSGSSADFM 869
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-208 |
3.74e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEqqaddgevwraPALKIgeLPQELPRADER 81
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-----------PAYKI--LEGDILFKGES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 IVfDVVAEGLAEVGKLLAEYHHLSLNIHTDDDLARLS----RVQQELEARDGWRLQQLVDSTLSRLQLPA---DKTLAE- 153
Cdd:CHL00131 73 IL-DLEPEERAHLGIFLAFQYPIEIPGVSNADFLRLAynskRKFQGLPELDPLEFLEIINEKLKLVGMDPsflSRNVNEg 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598215 154 LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEA---LLGFNGAVLFITH 208
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGinkLMTSENSIILITH 209
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-223 |
4.13e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.66 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVV------KGEQQADD-----GEVWRAPALKIGELP 72
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmnelESEVRVEGrveffNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 73 QEL------PRADERIVFDVVAEGLAEVGkllaeyHHLSLNIhtdDDLarlsrVQQELEARDGWrlqqlvDSTLSRLQlp 146
Cdd:PRK14258 88 RQVsmvhpkPNLFPMSVYDNVAYGVKIVG------WRPKLEI---DDI-----VESALKDADLW------DEIKHKIH-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 147 adKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL----LGFNGAVLFITHD----------RAF 212
Cdd:PRK14258 146 --KSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqslrLRSELTMVIVSHNlhqvsrlsdfTAF 223
|
250
....*....|.
gi 15598215 213 LQSLATRILEL 223
Cdd:PRK14258 224 FKGNENRIGQL 234
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
328-466 |
4.60e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.22 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 328 GGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVgtkLEVAYFDQLR------------HQLEPE 395
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV---LGVPVPARARlararigvvpqfDNLDLE 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598215 396 QTVIDN-ISEGREFITIDGQNRHVLSYLGDFLFSPQRARTPVKALSGGERARLLLAKLFSKPANLLVLDEPT 466
Cdd:PRK13536 129 FTVRENlLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-185 |
6.80e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.42 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 8 DVSLAFG------TTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQ--QADDGEVwrapALKIGELPQELPRAD 79
Cdd:COG2401 29 IVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV----DVPDNQFGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 80 erivfdvvaeglaevgkllaeyhHLSLNIHTDDDLARLSRVqqeleardgwrlqQLVDSTLSRlqlpadKTLAELSGGWR 159
Cdd:COG2401 105 -----------------------AIGRKGDFKDAVELLNAV-------------GLSDAVLWL------RRFKELSTGQK 142
|
170 180
....*....|....*....|....*.
gi 15598215 160 RRVLLAQALVAEPDLLLLDEPTNHLD 185
Cdd:COG2401 143 FRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
4-186 |
7.75e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 54.09 E-value: 7.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAfgTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPalKIGELPQE---LPRA-D 79
Cdd:cd03291 40 LFFSNLCLV--GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQFswiMPGTiK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 80 ERIVFDVVAEglaevgkllaEYHHLSL--NIHTDDDLARLSRVQQELEARDGwrlqqlvdstlsrlqlpadktlAELSGG 157
Cdd:cd03291 116 ENIIFGVSYD----------EYRYKSVvkACQLEEDITKFPEKDNTVLGEGG----------------------ITLSGG 163
|
170 180
....*....|....*....|....*....
gi 15598215 158 WRRRVLLAQALVAEPDLLLLDEPTNHLDI 186
Cdd:cd03291 164 QRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-185 |
9.37e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.24 E-value: 9.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 18 LLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRapalkigeLPQELPRADERIVFDVVAEglaEVGKL 97
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL--------VGQPLHQMDEEARAKLRAK---HVGFV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 98 LAEYHHL-SLNIHTDDDLARLSRVQQELEARDGWR--LQQLvdSTLSRL-QLPAdktlaELSGGWRRRVLLAQALVAEPD 173
Cdd:PRK10584 94 FQSFMLIpTLNALENVELPALLRGESSRQSRNGAKalLEQL--GLGKRLdHLPA-----QLSGGEQQRVALARAFNGRPD 166
|
170
....*....|..
gi 15598215 174 LLLLDEPTNHLD 185
Cdd:PRK10584 167 VLFADEPTGNLD 178
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-217 |
1.14e-07 |
|
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: 54.79 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 28 RGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAP-------------------ALKIGEL-----PQ---ELPRade 80
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPswdevlkrfrgtelqdyfkKLANGEIkvahkPQyvdLIPK--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 riVFDvvaeglAEVGKLLAEYhhlslnihtdDDLARLSRVQQELEardgwrLQQLVDstlsrlqlpadKTLAELSGGWRR 160
Cdd:COG1245 175 --VFK------GTVRELLEKV----------DERGKLDELAEKLG------LENILD-----------RDISELSGGELQ 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 161 RVLLAQALVAEPDLLLLDEPTNHLDIG---AIAWLEEALLGFNGAVLFITHDRAFLQSLA 217
Cdd:COG1245 220 RVAIAAALLRDADFYFFDEPSSYLDIYqrlNVARLIRELAEEGKYVLVVEHDLAILDYLA 279
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
328-466 |
1.42e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 53.66 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 328 GGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIE----------------VGTkleVAYFDqlrhQ 391
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsrarharqrVGV---VPQFD----N 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 392 LEPEQTVIDNISE-GREFITIDGQNRHVLSYLGDFLFSPQRARTPVKALSGGERARLLLAKLFSKPANLLVLDEPT 466
Cdd:PRK13537 91 LDPDFTVRENLLVfGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-185 |
1.43e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.17 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAF--GT---TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW-------RAPALKigel 71
Cdd:COG1101 2 LELKNLSKTFnpGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILidgkdvtKLPEYK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 72 pqelpRAdERI--VF-D---------VVAEGLAevgklLAEYHHLSLNIH---TDDDLA----RLSRVQQELEArdgwRL 132
Cdd:COG1101 78 -----RA-KYIgrVFqDpmmgtapsmTIEENLA-----LAYRRGKRRGLRrglTKKRRElfreLLATLGLGLEN----RL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598215 133 QQLVDStlsrlqlpadktlaeLSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD 185
Cdd:COG1101 143 DTKVGL---------------LSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-231 |
1.65e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 52.03 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGT--TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGevwrapalkigelpqelpradeR 81
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEG----------------------K 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 IVFDVVAEGLAEVGKLLAeyhhlSLNIHTDDDLARLSRVQQELEARDGWRLQQLVDStlsrlqLPADKTLAELSGGWRRR 161
Cdd:cd03369 65 IEIDGIDISTIPLEDLRS-----SLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGA------LRVSEGGLNLSQGQRQL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598215 162 VLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLG-FNGA-VLFITHDrafLQSLA--TRILELDRGHLIDW 231
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASIDYATDALIQKTIREeFTNStILTIAHR---LRTIIdyDKILVMDAGEVKEY 204
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
16-229 |
2.39e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.54 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 16 TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRapalkiGELPqelpraderivFDVVAEGLAE-- 93
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILF------DGKP-----------IDYSRKGLMKlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 94 --VGKLLAEYHH--LSLNIHTDDDLARLSRVQQELEardgwrLQQLVDSTLSRLQLP--ADKTLAELSGGWRRRVLLAQA 167
Cdd:PRK13636 82 esVGMVFQDPDNqlFSASVYQDVSFGAVNLKLPEDE------VRKRVDNALKRTGIEhlKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 168 LVAEPDLLLLDEPTNHLDIGAIAWLEEALL----GFNGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVemqkELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-239 |
2.48e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.18 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 12 AFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapALK--IGELPQEL----PRADERIVFd 85
Cdd:TIGR00957 647 ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV----HMKgsVAYVPQQAwiqnDSLRENILF- 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 86 vvaeglaevGKLLAEyhhlslnihtdddlarlSRVQQELEARdgwrlqqlvdSTLSRLQ-LPA-DKT-LAE----LSGGW 158
Cdd:TIGR00957 722 ---------GKALNE-----------------KYYQQVLEAC----------ALLPDLEiLPSgDRTeIGEkgvnLSGGQ 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 159 RRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAV-----LFITHDRAFLQSLATrILELDRGH------ 227
Cdd:TIGR00957 766 KQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLknktrILVTHGISYLPQVDV-IIVMSGGKisemgs 844
|
250
....*....|....*
gi 15598215 228 ---LIDWNGDYASFL 239
Cdd:TIGR00957 845 yqeLLQRDGAFAEFL 859
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-208 |
2.49e-07 |
|
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: 52.23 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 6 FTDVSLAFGTT-PLLDKVSWQIGRGERVCVIGRNGTGKSSLFK-------VVKGEQQADDGEV-------WRApalKIGE 70
Cdd:cd03253 3 FENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRllfrfydVSSGSILIDGQDIrevtldsLRR---AIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 71 LPQELPRADERIVFDVvaeglaEVGKLLAeyhhlslnihTDDDLARLSRVQQeleardgwrlqqlVDSTLSRLQLPADKT 150
Cdd:cd03253 80 VPQDTVLFNDTIGYNI------RYGRPDA----------TDEEVIEAAKAAQ-------------IHDKIMRFPDGYDTI 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598215 151 LAE----LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL--LGFNGAVLFITH 208
Cdd:cd03253 131 VGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALrdVSKGRTTIVIAH 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-188 |
2.56e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.48 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAfgttPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW--------RAP----ALKIG 69
Cdd:COG1129 255 VVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvriRSPrdaiRAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 70 ELPQElpRADERIVFDV-VAEglaevgkllaeyhhlslNIhTdddLARLSRVqqeleARDGW----RLQQLVDSTLSRLQ 144
Cdd:COG1129 331 YVPED--RKGEGLVLDLsIRE-----------------NI-T---LASLDRL-----SRGGLldrrRERALAEEYIKRLR 382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598215 145 LPA---DKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGA 188
Cdd:COG1129 383 IKTpspEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGA 429
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
316-467 |
2.91e-07 |
|
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: 52.17 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 316 VIVVEHVSFaHPGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV----------GTKLEVAYF 385
Cdd:COG4555 1 MIEVENLSK-KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgedvrkeprEARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 386 DQLRHqLEPEQTVIDNIsegREFITIDGQNRH-----VLSYLGDFLFSPQRARtPVKALSGGERARLLLAKLFSKPANLL 460
Cdd:COG4555 80 PDERG-LYDRLTVRENI---RYFAELYGLFDEelkkrIEELIELLGLEEFLDR-RVGELSTGMKKKVALARALVHDPKVL 154
|
....*..
gi 15598215 461 VLDEPTN 467
Cdd:COG4555 155 LLDEPTN 161
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
154-245 |
3.38e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.06 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 154 LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD---IGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLID 230
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDpelVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
90
....*....|....*
gi 15598215 231 wNGDYASFLVHKEQQ 245
Cdd:PRK11264 225 -QGPAKALFADPQQP 238
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
137-511 |
3.57e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 137 DSTLSRLQLPA--DKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIG-------AIAWLEEallgfNGAVLFIT 207
Cdd:PRK13409 194 DEVVERLGLENilDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRqrlnvarLIRELAE-----GKYVLVVE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 208 HDRAFLQSLA---------------------TR--ILELDRGHLIDWN---GDYA-SFLVH--KEQQLAAEEAANALFDK 258
Cdd:PRK13409 269 HDLAVLDYLAdnvhiaygepgaygvvskpkgVRvgINEYLKGYLPEENmriRPEPiEFEERppRDESERETLVEYPDLTK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 259 RLAqeevwirqgikarrtrnegrvralkemrreraerrerqgkaSFQLEsadksgkqvivVEhvsfahpGGQplvrdfsm 338
Cdd:PRK13409 349 KLG-----------------------------------------DFSLE-----------VE-------GGE-------- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 339 vLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGkiEVGTKLEVAYFDQlrhQLEPEQ--TVIDNISEGREfiTIDGqnr 416
Cdd:PRK13409 362 -IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG--EVDPELKISYKPQ---YIKPDYdgTVEDLLRSITD--DLGS--- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 417 hvlSYLGDFLFSP-------QRartPVKALSGGERARLLLAKLFSKPANLLVLDEPTN----DLDVETLELLEEVLLGFQ 485
Cdd:PRK13409 431 ---SYYKSEIIKPlqlerllDK---NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAhldvEQRLAVAKAIRRIAEERE 504
|
410 420
....*....|....*....|....*.
gi 15598215 486 GTVLMVSHDRAFLDNVVTSTLVFEGE 511
Cdd:PRK13409 505 ATALVVDHDIYMIDYISDRLMVFEGE 530
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-244 |
4.54e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.59 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 18 LLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalkigelpqelpRADERI------VFDVVAEGL 91
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKI----------------KVDGKVlyfgkdIFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 92 -AEVGKLLAE---YHHLS--------LNIHTDDDLARLSRVQQELEARDG-WRlqqlvdSTLSRLQLPAdktlAELSGGW 158
Cdd:PRK14246 89 rKEVGMVFQQpnpFPHLSiydniaypLKSHGIKEKREIKKIVEECLRKVGlWK------EVYDRLNSPA----SQLSGGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 159 RRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG--AVLFITHDRAFLQSLATRILELDRGHLIDWNGDYA 236
Cdd:PRK14246 159 QQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNE 238
|
....*...
gi 15598215 237 SFLVHKEQ 244
Cdd:PRK14246 239 IFTSPKNE 246
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
317-466 |
4.68e-07 |
|
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: 50.29 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGGQ-PLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV-GTKLEVAYFDQLRHQLE- 393
Cdd:cd03246 1 LEVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDPNELGDHVGy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 394 -PEQ------TVIDNIsegrefitidgqnrhvlsylgdflfspqrartpvkaLSGGERARLLLAKLFSKPANLLVLDEPT 466
Cdd:cd03246 81 lPQDdelfsgSIAENI------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-188 |
5.44e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 20 DKVSWQIGRGERVCVIGRNGTGK----SSLFKVVKGEQQaddGEVW--------RAP----ALKIGELPQElpRADERIV 83
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRtelvQCLFGAYPGRWE---GEIFidgkpvkiRNPqqaiAQGIAMVPED--RKRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 84 FDVvaeglaEVGK--LLAEYhhlslnihtdDDLARLSRVQQELEardgwrlQQLVDSTLSRLQLPA---DKTLAELSGGW 158
Cdd:PRK13549 354 PVM------GVGKniTLAAL----------DRFTGGSRIDDAAE-------LKTILESIQRLKVKTaspELAIARLSGGN 410
|
170 180 190
....*....|....*....|....*....|
gi 15598215 159 RRRVLLAQALVAEPDLLLLDEPTNHLDIGA 188
Cdd:PRK13549 411 QQKAVLAKCLLLNPKILILDEPTRGIDVGA 440
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
333-517 |
5.57e-07 |
|
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: 50.99 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 333 VRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKleVAYFDQLRHQLEPEQTVIDNI---------- 402
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--VSSLLGLGGGFNPELTGRENIylngrllgls 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 403 -SEGREFI--TIDgqnrhvLSYLGDFLfspqraRTPVKALSGGERARLLLAKLFSKPANLLVLDEPTN--Dldvetlell 477
Cdd:cd03220 116 rKEIDEKIdeIIE------FSELGDFI------DLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAvgD--------- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598215 478 eevlLGFQ--------------GTVLMVSHDRAFLDNVVTSTLVFEGeGKVREF 517
Cdd:cd03220 175 ----AAFQekcqrrlrellkqgKTVILVSHDPSSIKRLCDRALVLEK-GKIRFD 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
317-467 |
6.46e-07 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 50.83 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHpGGQPLVRDFSMVLQRGDRIGLLGANgtgkttllklllgdLQPTSGKIEVG----------TKLEVAYFD 386
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNgagktttirmllglLRPTSGEVRVLgedvardpaeVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 387 QlRHQLEPEQTVIDNISEGREFITIDGQNRH-----VLSYLGdfLfsPQRARTPVKALSGGERARLLLAKLFSKPANLLV 461
Cdd:COG1131 80 Q-EPALYPDLTVRENLRFFARLYGLPRKEARerideLLELFG--L--TDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
....*.
gi 15598215 462 LDEPTN 467
Cdd:COG1131 155 LDEPTS 160
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
319-514 |
7.29e-07 |
|
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: 50.33 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 319 VEHVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTK-------LEVAYF--DQLR 389
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerRKSIGYvmQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 390 HQLEpEQTVIDNISEGREFITIDGQN-RHVLSYLGDFLFSPQRARTpvkaLSGGERARLLLA-KLFSKPaNLLVLDEPTN 467
Cdd:cd03226 82 YQLF-TDSVREELLLGLKELDAGNEQaETVLKDLDLYALKERHPLS----LSGGQKQRLAIAaALLSGK-DLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598215 468 --DLDVETLELLEEVLLGFQG-TVLMVSHDRAFLDNVVtSTLVFEGEGKV 514
Cdd:cd03226 156 glDYKNMERVGELIRELAAQGkAVIVITHDYEFLAKVC-DRVLLLANGAI 204
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-237 |
7.62e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.15 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 16 TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKG-------------EQQADDGEVWRAPALKIGELPQeLPRADERi 82
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkingiELRELDPESWRKHLSWVGQNPQ-LPHGTLR- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 vfDVVAEGlaevgkllaeyhhlslNIHTDDDlarlsRVQQELEardgwrlQQLVDSTLSRLQLPADKTLAE----LSGGW 158
Cdd:PRK11174 441 --DNVLLG----------------NPDASDE-----QLQQALE-------NAWVSEFLPLLPQGLDTPIGDqaagLSVGQ 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 159 RRRVLLAQALVAEPDLLLLDEPTNHLDigaiAWLEEALL-GFNGA-----VLFITHDRAFLQSLATrILELDRGHLIDwN 232
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLD----AHSEQLVMqALNAAsrrqtTLMVTHQLEDLAQWDQ-IWVMQDGQIVQ-Q 564
|
....*
gi 15598215 233 GDYAS 237
Cdd:PRK11174 565 GDYAE 569
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-228 |
8.06e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 50.78 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADdgevwRAPALKIGELPQELPRADeR 81
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGD-----KSAGSHIELLGRTVQREG-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 IVFDVvAEGLAEVGKLLAEYHHLSlnihtdddlaRLSRVQQELEARDG----WRL---------QQLVDSTLSRLQLP-- 146
Cdd:PRK09984 77 LARDI-RKSRANTGYIFQQFNLVN----------RLSVLENVLIGALGstpfWRTcfswftreqKQRALQALTRVGMVhf 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 147 ADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFN---GAVLFIT-HDRAFLQSLATRILE 222
Cdd:PRK09984 146 AHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqndGITVVVTlHQVDYALRYCERIVA 225
|
....*.
gi 15598215 223 LDRGHL 228
Cdd:PRK09984 226 LRQGHV 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-229 |
8.38e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 50.85 E-value: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 16 TPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV--------WRAPAL-----KIGELPQE------LP 76
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepikYDKKSLlevrkTVGIVFQNpddqlfAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 77 RADERIVFDVVAEGLAEvgkllaeyhhlslnihtdDDLARlsRVQQELEARDgwrlqqlvdstlsrLQLPADKTLAELSG 156
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSK------------------EEVEK--RVKEALKAVG--------------MEGFENKPPHHLSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598215 157 GWRRRVLLAQALVAEPDLLLLDEPTNHLD-IGAIAwLEEALLGFN--GAVLFI-THDRAFLQSLATRILELDRGHLI 229
Cdd:PRK13639 141 GQKKRVAIAGILAMKPEIIVLDEPTSGLDpMGASQ-IMKLLYDLNkeGITIIIsTHDVDLVPVYADKVYVMSDGKII 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
317-466 |
8.56e-07 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 52.03 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPG-GQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV-GTKLEVAYFDQLRHQLEP 394
Cdd:TIGR02203 331 VEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 395 --------EQTVIDNISEGREFITIDGQNRHVL--SYLGDFL-FSPQRARTPVKA----LSGGERARLLLAKLFSKPANL 459
Cdd:TIGR02203 411 vsqdvvlfNDTIANNIAYGRTEQADRAEIERALaaAYAQDFVdKLPLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPI 490
|
....*..
gi 15598215 460 LVLDEPT 466
Cdd:TIGR02203 491 LILDEAT 497
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-229 |
8.91e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.89 E-value: 8.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLA------FGTTPLLDkVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapalKIGEL----- 71
Cdd:PRK13643 1 MIKFEKVNYTyqpnspFASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV------TVGDIvvsst 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 72 --PQELP--RADERIVFDVVAEGLAEvGKLLAEYHHLSLNIHTDDDLARlSRVQQELE----ARDGWrlqqlvdstlsrl 143
Cdd:PRK13643 74 skQKEIKpvRKKVGVVFQFPESQLFE-ETVLKDVAFGPQNFGIPKEKAE-KIAAEKLEmvglADEFW------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 144 qlpaDKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGA---IAWLEEALLGFNGAVLFITHDRAFLQSLATRI 220
Cdd:PRK13643 139 ----EKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTHLMDDVADYADYV 214
|
....*....
gi 15598215 221 LELDRGHLI 229
Cdd:PRK13643 215 YLLEKGHII 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
319-510 |
9.19e-07 |
|
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: 50.22 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 319 VEHVSFAHpGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV-GTKLE-----VAYFDQlRHQL 392
Cdd:cd03235 2 VEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLEkerkrIGYVPQ-RRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 393 EPEQ--TVIDNISEGRE-----FITIDGQNRHVLSY------LGDFlfspqrARTPVKALSGGERARLLLAKLFSKPANL 459
Cdd:cd03235 80 DRDFpiSVRDVVLMGLYghkglFRRLSKADKAKVDEalervgLSEL------ADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 460 LVLDEPTN--DLDVETLELLEEVLLGFQG-TVLMVSHD----RAFLDNVV--TSTLVFEG 510
Cdd:cd03235 154 LLLDEPFAgvDPKTQEDIYELLRELRREGmTILVVTHDlglvLEYFDRVLllNRTVVASG 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-230 |
1.43e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.18 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 17 PLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW--------RAPA----LKIGELPqelpraDERIvf 84
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRldgeditgLSPRerrrLGVAYIP------EDRL-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 85 dvvAEGLaeVGKL-LAEyhHLSLNIHTDDDLARLSRVQQElEARDgwRLQQLVDS---TLSRLQLPAdktlAELSGGWRR 160
Cdd:COG3845 344 ---GRGL--VPDMsVAE--NLILGRYRRPPFSRGGFLDRK-AIRA--FAEELIEEfdvRTPGPDTPA----RSLSGGNQQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598215 161 RVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALL-----GfnGAVLFITHDRAFLQSLATRILELDRGHLID 230
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLelrdaG--AAVLLISEDLDEILALSDRIAVMYEGRIVG 482
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-229 |
1.46e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.21 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 18 LLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQAD--------------DGEVWRA-PALKIGELPQELPRADERi 82
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvtgdvtlNGEPLAAiDAPRLARLRAVLPQAAQP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VFDVVAEGLAevgkLLAEYHHlslnihtdddlarlSRVQQELEARDG---WRLQQLVD-STLSRlqlpadKTLAELSGGW 158
Cdd:PRK13547 95 AFAFSAREIV----LLGRYPH--------------ARRAGALTHRDGeiaWQALALAGaTALVG------RDVTTLSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 159 RRRVLLAQAL---------VAEPDLLLLDEPTNHLDIGAIAWLEEALLG----FNGAVLFITHDRAFLQSLATRILELDR 225
Cdd:PRK13547 151 LARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRlardWNLGVLAIVHDPNLAARHADRIAMLAD 230
|
....
gi 15598215 226 GHLI 229
Cdd:PRK13547 231 GAIV 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-184 |
1.49e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.98 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKG--EQQADDGEV-WRAPALKIGELpqelpRAD 79
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIyWSGSPLKASNI-----RDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 80 ERIVFDVVAEGLAEVGKL-LAEY----HHLSLNIHTDDDLARLSRVQQeleardgwrlqqlvdsTLSRLQLPAD---KTL 151
Cdd:TIGR02633 76 ERAGIVIIHQELTLVPELsVAENiflgNEITLPGGRMAYNAMYLRAKN----------------LLRELQLDADnvtRPV 139
|
170 180 190
....*....|....*....|....*....|...
gi 15598215 152 AELSGGWRRRVLLAQALVAEPDLLLLDEPTNHL 184
Cdd:TIGR02633 140 GDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
316-467 |
2.08e-06 |
|
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: 49.66 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 316 VIVVEHVSFAHpGGQPLVRDFSMVLQRGDRIGLLGAN-------------GtgkttllklllgdLQPTSGKIEV-GTKLE 381
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNgsgkstllralagL-------------LKPSSGEVLLdGRDLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 382 ----------VAYFDQlRHQLEPEQTVIDNISEGR----EFITIDGQN-----RHVLSYLG--DFlfspqrARTPVKALS 440
Cdd:COG1120 67 slsrrelarrIAYVPQ-EPPAPFGLTVRELVALGRyphlGLFGRPSAEdreavEEALERTGleHL------ADRPVDELS 139
|
170 180
....*....|....*....|....*..
gi 15598215 441 GGERARLLLAKLFSKPANLLVLDEPTN 467
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTS 166
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-236 |
2.42e-06 |
|
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: 49.15 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTT--PLLDKVSWQIGRGERVCVIGRNGTGKSSL-------FKVVKGEQQADDGEVwRAPAL-----KIG 69
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLvnliprfYDVDSGRILIDGHDV-RDYTLaslrrQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 70 ELPQELpraderIVF-DVVAEGLAeVGKLLAeyhhlslnihTDDDLARLSRVQQeleardgwrLQQLVDSTLSRLQLPAD 148
Cdd:cd03251 80 LVSQDV------FLFnDTVAENIA-YGRPGA----------TREEVEEAARAAN---------AHEFIMELPEGYDTVIG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 149 KTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL--LGFNGAVLFITHDRAFLQSlATRILELDRG 226
Cdd:cd03251 134 ERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALerLMKNRTTFVIAHRLSTIEN-ADRIVVLEDG 212
|
250
....*....|....*....
gi 15598215 227 -------H--LIDWNGDYA 236
Cdd:cd03251 213 kivergtHeeLLAQGGVYA 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
316-494 |
2.47e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.34 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 316 VIVVEHVSFAHpGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEVAYFDQLRHqLEPe 395
Cdd:PRK09544 4 LVSLENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY-LDT- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 396 qTVIDNISegrEFITIDGQNRHvlsylGDFLFSPQRART------PVKALSGGERARLLLAK-LFSKPaNLLVLDEPTN- 467
Cdd:PRK09544 81 -TLPLTVN---RFLRLRPGTKK-----EDILPALKRVQAghlidaPMQKLSGGETQRVLLARaLLNRP-QLLVLDEPTQg 150
|
170 180 190
....*....|....*....|....*....|
gi 15598215 468 ---DLDVETLELLEEVLLGFQGTVLMVSHD 494
Cdd:PRK09544 151 vdvNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-185 |
2.67e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.43 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 18 LLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADdgeVWRAPALKIGELPQELPRADERIVFdvVAEGLAEVGKL 97
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKG---VKGSGSVLLNGMPIDAKEMRAISAY--VQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 98 LAEYH-----HLSLNIHTDDDlARLSRVQQELEArdgwrlQQLVDSTLSRLQLPADKTlaELSGGWRRRVLLAQALVAEP 172
Cdd:TIGR00955 115 TVREHlmfqaHLRMPRRVTKK-EKRERVDEVLQA------LGLRKCANTRIGVPGRVK--GLSGGERKRLAFASELLTDP 185
|
170
....*....|...
gi 15598215 173 DLLLLDEPTNHLD 185
Cdd:TIGR00955 186 PLLFCDEPTSGLD 198
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
333-517 |
3.66e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 48.54 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 333 VRDFSMVLQRGDRIGLLGANgtgkttllklllgdLQPTSGKIEVGTK----LEV-AYFDqlrhqlePEQTVIDNIsegrE 407
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNgagkstllkliagiLEPTSGRVEVNGRvsalLELgAGFH-------PELTGRENI----Y 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 408 FI-TIDGQNR--------HVLSY--LGDFLfspqraRTPVKALSGGERARLLLAKLFSKPANLLVLDEPTN--DLDvetl 474
Cdd:COG1134 111 LNgRLLGLSRkeidekfdEIVEFaeLGDFI------DQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAvgDAA---- 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598215 475 elleevllgFQ--------------GTVLMVSHDRAFLDNVVTSTLVFEGeGKVREF 517
Cdd:COG1134 181 ---------FQkkclarirelresgRTVIFVSHSMGAVRRLCDRAIWLEK-GRLVMD 227
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
137-229 |
3.86e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.35 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 137 DSTLSRLQL--PADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD--IGAIAWLEEALLGFNGA-VLFITHDRA 211
Cdd:NF000106 126 DELLERFSLteAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDprTRNEVWDEVRSMVRDGAtVLLTTQYME 205
|
90
....*....|....*...
gi 15598215 212 FLQSLATRILELDRGHLI 229
Cdd:NF000106 206 EAEQLAHELTVIDRGRVI 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-229 |
4.04e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.78 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 22 VSWQIGRGERVCVIGRNGTGKSSLFkvvkgeqqaddgevwrapALKIGELPQElpradERIVFDvvaeglaevGKLLAEY 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLL------------------ARMAGLLPGS-----GSIQFA---------GQPLEAW 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 102 HHLSLNIHTdddlARLSRVQQELEARDGWR--------------LQQLVDSTLSRLQLpADK---TLAELSGGWRRRVLL 164
Cdd:PRK03695 63 SAAELARHR----AYLSQQQTPPFAMPVFQyltlhqpdktrteaVASALNEVAEALGL-DDKlgrSVNQLSGGEWQRVRL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598215 165 AQAL-----VAEPD--LLLLDEPTNHLDIGAIAWLE---EALLGFNGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:PRK03695 138 AAVVlqvwpDINPAgqLLLLDEPMNSLDVAQQAALDrllSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-184 |
4.18e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkIGELPQELPRADE 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL------IDGQEMRFASTTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 81 RIvfdvvAEGLAEVGKLLaeyhHLSLNIHTDDDLArLSRvqqeLEARDGW----RLQQLVDSTLSRLQL---PADKtLAE 153
Cdd:PRK11288 76 AL-----AAGVAIIYQEL----HLVPEMTVAENLY-LGQ----LPHKGGIvnrrLLNYEAREQLEHLGVdidPDTP-LKY 140
|
170 180 190
....*....|....*....|....*....|.
gi 15598215 154 LSGGWRRRVLLAQALVAEPDLLLLDEPTNHL 184
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
154-229 |
4.94e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.10 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 154 LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDI----GAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-232 |
5.07e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAF--GTTPLLDKVSWQIGRGERVCVIGRNGTGKSS----LFKVV---KGEQQADDGEVWR------APALK 67
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSmlnaLFRIVeleKGRIMIDDCDVAKfgltdlRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 68 IgeLPQE--LPRADERIVFDVVAEglaevgkllaeyhhlslniHTDDDLarlsrvqqeLEARDGWRLQQLVDSTLSRLQL 145
Cdd:PLN03232 1314 I--IPQSpvLFSGTVRFNIDPFSE-------------------HNDADL---------WEALERAHIKDVIDRNPFGLDA 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 146 PADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALL-GFNGAVLFITHDRAFLQSLATRILELD 224
Cdd:PLN03232 1364 EVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIReEFKSCTMLVIAHRLNTIIDCDKILVLS 1443
|
....*...
gi 15598215 225 RGHLIDWN 232
Cdd:PLN03232 1444 SGQVLEYD 1451
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
316-467 |
5.97e-06 |
|
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: 47.47 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 316 VIVVEHVSFAHpGGQPLVRDFSMVLQRGDRIGLLGANGTGkttllklllgdLQPTSGKIEVG----TKLEVAYFDQLR-- 389
Cdd:COG4133 2 MLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGkttllrilaglLPPSAGEVLWNgepiRDAREDYRRRLAyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 390 -HQLE--PEQTVIDNI---SEGREFITIDGQNRHVLSYLGdfLfsPQRARTPVKALSGGERARLLLAKLFSKPANLLVLD 463
Cdd:COG4133 81 gHADGlkPELTVRENLrfwAALYGLRADREAIDEALEAVG--L--AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
....
gi 15598215 464 EPTN 467
Cdd:COG4133 157 EPFT 160
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-229 |
7.14e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 48.54 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 19 LDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV-------WR---APALKIG-------ELPQELPrader 81
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrvlgyvpFKrrkEFARRIGvvfgqrsQLWWDLP----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 ivfdvVAEGLaevgKLLAEYHHLSlnihtDDDLARlsrvqqeleardgwRLQQLVDstlsRLQLPA--DKTLAELSGGWR 159
Cdd:COG4586 113 -----AIDSF----RLLKAIYRIP-----DAEYKK--------------RLDELVE----LLDLGEllDTPVRQLSLGQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598215 160 RRVLLAQALVAEPDLLLLDEPTNHLDIGAiawlEEALLGF-------NGA-VLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVVS----KEAIREFlkeynreRGTtILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-226 |
8.47e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW------------RAPALKIGE 70
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITinninynkldhkLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 71 LPQELPRADERIVFdvvaEGLAeVGKLLAEyHHLSLNIhtdDDLARLSRVQQELEARDGwrlqqlvdstlsrLQLPADKT 150
Cdd:PRK09700 85 IYQELSVIDELTVL----ENLY-IGRHLTK-KVCGVNI---IDWREMRVRAAMMLLRVG-------------LKVDLDEK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598215 151 LAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWL---EEALLGFNGAVLFITHDRAFLQSLATRILELDRG 226
Cdd:PRK09700 143 VANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-190 |
9.31e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 22 VSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapaLKIGELPQELPraderivFDVVAEGLAEVGKLLAE- 100
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR----LNGKDISPRSP-------LDAVKKGMAYITESRRDn 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 101 --YHHLSL--NIHTDDDLaRLSRVQQELEARDGWRLQQLVDSTLSRLQLPA---DKTLAELSGGWRRRVLLAQALVAEPD 173
Cdd:PRK09700 351 gfFPNFSIaqNMAISRSL-KDGGYKGAMGLFHEVDEQRTAENQRELLALKChsvNQNITELSGGNQQKVLISKWLCCCPE 429
|
170
....*....|....*..
gi 15598215 174 LLLLDEPTNHLDIGAIA 190
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKA 446
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
316-516 |
9.93e-06 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 46.97 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 316 VIVVEHVSFAHPGGQPLVRDFSMVLQRGDR---IG--------LLgangtgkttllKLLLGDLQPTSGKIEVG----TKL 380
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFvflTGpsgagkstLL-----------KLLYGEERPTSGQVLVNgqdlSRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 381 ---EVAYfdqLR---------HQLEPEQTVIDNIS-----EGREFITIDGQNRHVLSYLGdfLfsPQRARTPVKALSGGE 443
Cdd:COG2884 70 krrEIPY---LRrrigvvfqdFRLLPDRTVYENVAlplrvTGKSRKEIRRRVREVLDLVG--L--SDKAKALPHELSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 444 RARLLLAK-LFSKPAnLLVLDEPT------------------NDldvetlelleevllgfQG-TVLMVSHDRAFLDNVVT 503
Cdd:COG2884 143 QQRVAIARaLVNRPE-LLLADEPTgnldpetsweimelleeiNR----------------RGtTVLIATHDLELVDRMPK 205
|
250
....*....|...
gi 15598215 504 STLVFEGeGKVRE 516
Cdd:COG2884 206 RVLELED-GRLVR 217
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-185 |
9.97e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 48.30 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAF-GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkIGElpqelprad 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIW------IGG--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 80 eRIVFDV-VAE-GLAEVGKLLAEYHHLS--------LNIhtdddlARLSRvqQELEARdgwrlqqlVDSTLSRLQLPA-- 147
Cdd:PRK11650 66 -RVVNELePADrDIAMVFQNYALYPHMSvrenmaygLKI------RGMPK--AEIEER--------VAEAARILELEPll 128
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598215 148 DKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD 185
Cdd:PRK11650 129 DRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
317-467 |
1.09e-05 |
|
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: 46.24 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFaHPGGQPLVRDFSMVLQRGDRIGLLGANGtgkttllklllgdlqptSGKievgTKLevayfdqLRH---QLE 393
Cdd:cd03230 1 IEVRNLSK-RYGKKTALDDISLTVEKGEIYGLLGPNG-----------------AGK----TTL-------IKIilgLLK 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 394 PeqtvidniSEGRefITIDGQN--RHVLSYLGDFLFSPQRARTP-------VKALSGGERARLLLAK-LFSKPaNLLVLD 463
Cdd:cd03230 52 P--------DSGE--IKVLGKDikKEPEEVKRRIGYLPEEPSLYenltvreNLKLSGGMKQRLALAQaLLHDP-ELLILD 120
|
....
gi 15598215 464 EPTN 467
Cdd:cd03230 121 EPTS 124
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-220 |
1.09e-05 |
|
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: 47.36 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 29 GERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAP-------------------ALKIGEL-----PQ---ELPRAder 81
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdeildefrgselqnyftKLLEGDVkvivkPQyvdLIPKA--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 82 ivfdvvAEGlaEVGKLLAEyhhlslnihtDDDLARLSRVQQELEardgwrLQQLVDSTLSrlqlpadktlaELSGGWRRR 161
Cdd:cd03236 103 ------VKG--KVGELLKK----------KDERGKLDELVDQLE------LRHVLDRNID-----------QLSGGELQR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598215 162 VLLAQALVAEPDLLLLDEPTNHLDIG---AIAWLEEALLGFNGAVLFITHDRAFLQSLATRI 220
Cdd:cd03236 148 VAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-230 |
1.22e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.39 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 17 PLLDKVSWQIGRGERVCVIGRNGTGKSslfkvvkgeqqaddgevwRAPALKIGELPQELPRADERIVFDVVAEGLAEV-G 95
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKS------------------LTCAAALGILPAGVRQTAGRVLLDGKPVAPCALrG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 96 KLLA---EYHHLSLN-IHTDDDLARLSRVQQELEARDGWRLQQLVDSTLSRLQLPADKTLAELSGGWRRRVLLAQALVAE 171
Cdd:PRK10418 79 RKIAtimQNPRSAFNpLHTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598215 172 PDLLLLDEPTNHLDIGA---IAWLEEALLGFNG-AVLFITHDRAFLQSLATRILELDRGHLID 230
Cdd:PRK10418 159 APFIIADEPTTDLDVVAqarILDLLESIVQKRAlGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-220 |
1.41e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.49 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAF----GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQaddgEVWRAPALKIG----ELP 72
Cdd:PRK15093 1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK----DNWRVTADRMRfddiDLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 73 QELPRADERIVFDVVAEGLAEVGKLLaeyhhlslnihtdDDLARLSRvqQELEA------------RDGWRLQQLVDsTL 140
Cdd:PRK15093 77 RLSPRERRKLVGHNVSMIFQEPQSCL-------------DPSERVGR--QLMQNipgwtykgrwwqRFGWRKRRAIE-LL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 141 SRLQLPADKTLA-----ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFN----GAVLFITHDRA 211
Cdd:PRK15093 141 HRVGIKDHKDAMrsfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqnnnTTILLISHDLQ 220
|
....*....
gi 15598215 212 FLQSLATRI 220
Cdd:PRK15093 221 MLSQWADKI 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
317-466 |
1.43e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 48.24 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANgtgkttllklllgDL-----QPTSGKIEVG----TKLEVayfDQ 387
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSgsgk-----stlvNLllrfyDPTSGRILIDgvdiRDLTL---ES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 388 LRHQL-----EP---EQTVIDNISEGREFITiDGQNRHVL--SYLGDFLFS-PQRARTPV----KALSGGERARLLLAKL 452
Cdd:COG1132 412 LRRQIgvvpqDTflfSGTIRENIRYGRPDAT-DEEVEEAAkaAQAHEFIEAlPDGYDTVVgergVNLSGGQRQRIAIARA 490
|
170
....*....|....
gi 15598215 453 FSKPANLLVLDEPT 466
Cdd:COG1132 491 LLKDPPILILDEAT 504
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
142-208 |
1.48e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 46.95 E-value: 1.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598215 142 RLQLPAdktlAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL--LGFNGAVLFITH 208
Cdd:COG1117 147 RLKKSA----LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELIleLKKDYTIVIVTH 211
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
340-511 |
1.73e-05 |
|
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: 46.63 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 340 LQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVgTKLEVAYFDQlrhQLEPEQ--TVIDNISEGREFITIDGQ-NR 416
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQ---YIKADYegTVRDLLSSITKDFYTHPYfKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 417 HVLSYLG-DFLFSPQrartpVKALSGGERARLLLAKLFSKPANLLVLDEPTNDLDVETLELLEEVLLGF----QGTVLMV 491
Cdd:cd03237 98 EIAKPLQiEQILDRE-----VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVV 172
|
170 180
....*....|....*....|
gi 15598215 492 SHDRAFLDNVVTSTLVFEGE 511
Cdd:cd03237 173 EHDIIMIDYLADRLIVFEGE 192
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-188 |
1.80e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 17 PLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGELPQELPRADerIVF---DVVAEGLAe 93
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANG--IVYiseDRKRDGLV- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 94 VGKLLAEyhHLSLNihtddDLARLSRVQQELEARDGwrlQQLVDS--TLSRLQLPA-DKTLAELSGGWRRRVLLAQALVA 170
Cdd:PRK10762 343 LGMSVKE--NMSLT-----ALRYFSRAGGSLKHADE---QQAVSDfiRLFNIKTPSmEQAIGLLSGGNQQKVAIARGLMT 412
|
170
....*....|....*...
gi 15598215 171 EPDLLLLDEPTNHLDIGA 188
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGA 430
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
317-465 |
1.89e-05 |
|
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: 46.52 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKlEVAYFD--QLRHQ--- 391
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE-DIREQDpvELRRKigy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 392 ------LEPEQTVIDNIS-----EGREFITIDGQNRHVLSYLGdflFSPQ--RARTPvKALSGGERARLLLAKLFSKPAN 458
Cdd:cd03295 80 viqqigLFPHMTVEENIAlvpklLKWPKEKIRERADELLALVG---LDPAefADRYP-HELSGGQQQRVGVARALAADPP 155
|
....*..
gi 15598215 459 LLVLDEP 465
Cdd:cd03295 156 LLLMDEP 162
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
331-466 |
1.96e-05 |
|
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: 46.56 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 331 PLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTklEVAYFDQLRH------------QLEPEQTV 398
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKKFlrrigvvfgqktQLWWDLPV 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 399 IDNISEGREFITID-GQNRHVLSYLGDFLFSPQRARTPVKALSGGERARL-LLAKLFSKPaNLLVLDEPT 466
Cdd:cd03267 113 IDSFYLLAAIYDLPpARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAeIAAALLHEP-EILFLDEPT 181
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-185 |
2.06e-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: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 13 FGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVkgeqqaddgevwrapALKIGElpqelpraDERIVFDVVAEGLA 92
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL---------------ANRTEG--------NVSVEGDIHYNGIP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 93 evGKLLAEYHHLSLNIHTDDDL--ARLSrVQQELEARdgwrlqqlvdstlsrLQLPADKTLAELSGGWRRRVLLAQALVA 170
Cdd:cd03233 74 --YKEFAEKYPGEIIYVSEEDVhfPTLT-VRETLDFA---------------LRCKGNEFVRGISGGERKRVSIAEALVS 135
|
170
....*....|....*
gi 15598215 171 EPDLLLLDEPTNHLD 185
Cdd:cd03233 136 RASVLCWDNSTRGLD 150
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-230 |
2.08e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.63 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 8 DVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWRAPALKIGelpqelpradeRIVFDV- 86
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGG-----------RSIFNYr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 87 -VAEGLAEVGKLLAEYHHLSLNIhTDDDLA--RLSRV--QQELEARDGWRLQQ--LVDSTLSRLqlpADKTLaELSGGWR 159
Cdd:PRK14271 95 dVLEFRRRVGMLFQRPNPFPMSI-MDNVLAgvRAHKLvpRKEFRGVAQARLTEvgLWDAVKDRL---SDSPF-RLSGGQQ 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598215 160 RRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL--LGFNGAVLFITHDRAFLQSLATRILELDRGHLID 230
Cdd:PRK14271 170 QLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIrsLADRLTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
316-467 |
2.09e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 46.52 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 316 VIVVEHVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVgTKLEVAYFDQLRHQLE-- 393
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV-SGIDTGDFSKLQGIRKlv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 394 ------PE-----QTVIDNISEGREFITIDGQN--RHVLSYLGDFLFSPQRARTPvKALSGGERARLLLAKLFSKPANLL 460
Cdd:PRK13644 80 givfqnPEtqfvgRTVEEDLAFGPENLCLPPIEirKRVDRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEPECL 158
|
....*..
gi 15598215 461 VLDEPTN 467
Cdd:PRK13644 159 IFDEVTS 165
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
319-467 |
2.26e-05 |
|
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: 45.50 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 319 VEHVSFAHpGGQPLVRDFSMVLQRGDRIGLLGANGtgkttllklllgdlqptSGKievgTKLevayFDQLRHQLEPEQtv 398
Cdd:cd03214 2 VENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNG-----------------AGK----STL----LKTLAGLLKPSS-- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 399 idniseGRefITIDGQNRHVLSYLgdflfspQRART-------------------PVKALSGGERARLLLAKLFSKPANL 459
Cdd:cd03214 54 ------GE--ILLDGKDLASLSPK-------ELARKiayvpqalellglahladrPFNELSGGERQRVLLARALAQEPPI 118
|
....*...
gi 15598215 460 LVLDEPTN 467
Cdd:cd03214 119 LLLDEPTS 126
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-229 |
2.37e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 46.95 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 23 SWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVwrapaLKIGELPQELPRADERivfDVVAEGLAEVGKLLAEYH 102
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQV-----LIDGVDIAKISDAELR---EVRRKKIAMVFQSFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 103 HLSL--NIHTDDDLARLSRVQQELEARDGWRLQQLVDStlsrlqlpADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEP 180
Cdd:PRK10070 120 HMTVldNTAFGMELAGINAEERREKALDALRQVGLENY--------AHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598215 181 TNHLDIGAIAWLEEALLGFNG----AVLFITHDRAFLQSLATRILELDRGHLI 229
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAkhqrTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
221-285 |
2.42e-05 |
|
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: 42.95 E-value: 2.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598215 221 LELDRGHLIDWNGDYASFLVHKEQQLAAEEAANALFDKRLAQEEVWI-RQGIKARRTR-NEGRVRAL 285
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIdRFRAKASKAKqAQSRIKAL 67
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
154-230 |
2.67e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 47.26 E-value: 2.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598215 154 LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL--LGFNGAVLFITHDRAFLQSlATRILELDRGHLID 230
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALdeLMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVE 549
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-228 |
2.83e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 47.41 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTP---LLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVW-----------RAPALKI 68
Cdd:TIGR00958 478 LIEFQDVSFSYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgvplvqydhHYLHRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 69 GELPQElPRADERIVFDVVAEGLaevgkllaeyhhlslnihTDDDLARLSRVQQELEARDG-WRLQQLVDSTLsrlqlpa 147
Cdd:TIGR00958 558 ALVGQE-PVLFSGSVRENIAYGL------------------TDTPDEEIMAAAKAANAHDFiMEFPNGYDTEV------- 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 148 DKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHDRAFLQSlATRILELDRGH 227
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGS 690
|
.
gi 15598215 228 L 228
Cdd:TIGR00958 691 V 691
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-181 |
2.83e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 20 DKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkigelpqelpraderiVF--DVVAEGLA---EV 94
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAW---------------------LFgqPVDAGDIAtrrRV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 95 G------KLLAEyhhLS----LNIHtdddlARLSRVQqelEARDGWRLQQLVDstlsRLQLP--ADKTLAELSGGWRRRV 162
Cdd:NF033858 342 GymsqafSLYGE---LTvrqnLELH-----ARLFHLP---AAEIAARVAEMLE----RFDLAdvADALPDSLPLGIRQRL 406
|
170
....*....|....*....
gi 15598215 163 LLAQALVAEPDLLLLDEPT 181
Cdd:NF033858 407 SLAVAVIHKPELLILDEPT 425
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
148-185 |
3.28e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 46.28 E-value: 3.28e-05
10 20 30
....*....|....*....|....*....|....*...
gi 15598215 148 DKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD 185
Cdd:PRK13649 140 EKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
153-185 |
3.32e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.17 E-value: 3.32e-05
10 20 30
....*....|....*....|....*....|...
gi 15598215 153 ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD 185
Cdd:PRK13634 145 ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
154-188 |
4.13e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 4.13e-05
10 20 30
....*....|....*....|....*....|....*
gi 15598215 154 LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGA 188
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGA 439
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
322-466 |
4.23e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 46.37 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 322 VSFahpGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV-GTKLEVAYFDQLRHQLE--PEQTV 398
Cdd:PRK09536 11 VEF---GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVaGDDVEALSARAASRRVAsvPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 399 I-------DNISEGR-----EFITIDGQNRHVLSYLGDFLFSPQRARTPVKALSGGERARLLLAKLFSKPANLLVLDEPT 466
Cdd:PRK09536 88 LsfefdvrQVVEMGRtphrsRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-188 |
4.35e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.80 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 5 KFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQ---------ADDGEVWRAPALKIGELPQEl 75
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnnftgtilANNRKPTKQILKRTGFVTQD- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 76 praderivfDVVaeglaevgkllaeYHHLSlnIHTDDDLARLSRVQQELEARDGWRLqqlVDSTLSRLQLP-------AD 148
Cdd:PLN03211 149 ---------DIL-------------YPHLT--VRETLVFCSLLRLPKSLTKQEKILV---AESVISELGLTkcentiiGN 201
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598215 149 KTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGA 188
Cdd:PLN03211 202 SFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
317-466 |
4.49e-05 |
|
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: 45.25 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVG----TKLEVAYFDQLRHQ- 391
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdiNKLKGKALRQLRRQi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 392 --------LEPEQTVIDNISEGRefitidgqnrhvLSYLGDF-----LFSPQ----------------RARTPVKALSGG 442
Cdd:cd03256 81 gmifqqfnLIERLSVLENVLSGR------------LGRRSTWrslfgLFPKEekqralaalervglldKAYQRADQLSGG 148
|
170 180
....*....|....*....|....
gi 15598215 443 ERARLLLAKLFSKPANLLVLDEPT 466
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPV 172
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
133-188 |
5.48e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 5.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598215 133 QQLVDSTlsRLQLPADKT-LAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGA 188
Cdd:PRK10982 372 QWVIDSM--RVKTPGHRTqIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGA 426
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
153-230 |
7.31e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 153 ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLG----FNGAVLFITHDRAFLQSLATRILELDRGHL 228
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDlqrdFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
..
gi 15598215 229 ID 230
Cdd:PRK10261 543 VE 544
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
317-495 |
7.73e-05 |
|
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: 44.40 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGG---QPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVG----TKLEVAYFDQLR 389
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdiSKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 390 ----------HQLEPEQTVIDNISEGREFITIDGQNRH-----VLSYLGdfLfsPQRARTPVKALSGGERARLLLAK-LF 453
Cdd:cd03255 81 rrhigfvfqsFNLLPDLTALENVELPLLLAGVPKKERReraeeLLERVG--L--GDRLNHYPSELSGGQQQRVAIARaLA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598215 454 SKPAnLLVLDEPT----NDLDVETLELLEEVLLGFQGTVLMVSHDR 495
Cdd:cd03255 157 NDPK-IILADEPTgnldSETGKEVMELLRELNKEAGTTIVVVTHDP 201
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
317-466 |
9.22e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 45.34 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV-GTKLEVAYFDQLRHQL--- 392
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIRTVTRASLRRNIavv 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 393 --EP---EQTVIDNISEGREfitiDGQNRHVLSYLG-----DFLF-SPQRARTPV----KALSGGERARLLLAKLFSKPA 457
Cdd:PRK13657 415 fqDAglfNRSIEDNIRVGRP----DATDEEMRAAAEraqahDFIErKPDGYDTVVgergRQLSGGERQRLAIARALLKDP 490
|
....*....
gi 15598215 458 NLLVLDEPT 466
Cdd:PRK13657 491 PILILDEAT 499
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
317-466 |
9.64e-05 |
|
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: 44.11 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGGQPLvRDFSMVLQRGdRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEVAYFDQLRHQLE--P 394
Cdd:cd03264 1 LQLENLTKRYGKKRAL-DGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGylP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 395 EQ-TVIDNISeGREFI------------TIDGQNRHVLSYLGdfLFspQRARTPVKALSGGERARLLLAK-LFSKPAnLL 460
Cdd:cd03264 79 QEfGVYPNFT-VREFLdyiawlkgipskEVKARVDEVLELVN--LG--DRAKKKIGSLSGGMRRRVGIAQaLVGDPS-IL 152
|
....*.
gi 15598215 461 VLDEPT 466
Cdd:cd03264 153 IVDEPT 158
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-228 |
1.19e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.04 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV------------WRAPALKIGE 70
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeiggnpcarltpAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 71 LPQE---LPR--ADERIVFDVVAEGLAE--VGKLLAEyhhlsLNIHTDDDLARLSrvqqeLEARDgwrlQQLVDstlsrl 143
Cdd:PRK15439 91 VPQEpllFPNlsVKENILFGLPKRQASMqkMKQLLAA-----LGCQLDLDSSAGS-----LEVAD----RQIVE------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 144 qlpadktlaelsggwrrrvlLAQALVAEPDLLLLDEPTNHLDIGAIAWL---EEALLGFNGAVLFITHDRAFLQSLATRI 220
Cdd:PRK15439 151 --------------------ILRGLMRDSRILILDEPTASLTPAETERLfsrIRELLAQGVGIVFISHKLPEIRQLADRI 210
|
....*...
gi 15598215 221 LELDRGHL 228
Cdd:PRK15439 211 SVMRDGTI 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-184 |
1.26e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.92 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 1 MTLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVK-----GEQQAD---DGEVWRAPALKigelp 72
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvyphGTYEGEiifEGEELQASNIR----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 73 qelpraderivfDVVAEGLAEVGKLLAEYHHLSL--NIHTDDDLARLSRVQ-QELEARDGWRLQQLvdstlsRLQLPADK 149
Cdd:PRK13549 78 ------------DTERAGIAIIHQELALVKELSVleNIFLGNEITPGGIMDyDAMYLRAQKLLAQL------KLDINPAT 139
|
170 180 190
....*....|....*....|....*....|....*
gi 15598215 150 TLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHL 184
Cdd:PRK13549 140 PVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
328-465 |
1.32e-04 |
|
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: 43.69 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 328 GGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVG----TKLEV--------AYFDQlrhqlEP- 394
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqdiTKLPMhkrarlgiGYLPQ-----EAs 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 395 ---EQTVIDNISEGREFITIDGQNRH--VLSYLGDFLFSPQRaRTPVKALSGGERARLLLAKLFSKPANLLVLDEP 465
Cdd:cd03218 86 ifrKLTVEENILAVLEIRGLSKKEREekLEELLEEFHITHLR-KSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
316-516 |
1.35e-04 |
|
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: 44.89 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 316 VIVVEHVSFAHPGGQ-PLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPT---SGKIEVGTKLEVAYFDQLR-- 389
Cdd:COG1123 4 LLEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 390 ----------HQLEPEqTVIDNISEGREFITIDGQNRH--VLSYLgDFLFSPQRARTPVKALSGGERARLLLA-KLFSKP 456
Cdd:COG1123 84 rigmvfqdpmTQLNPV-TVGDQIAEALENLGLSRAEARarVLELL-EAVGLERRLDRYPHQLSGGQRQRVAIAmALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598215 457 AnLLVLDEPTNDLDVETLELLEEVLLGFQG----TVLMVSHDRAFLDNVVTSTLVFEgEGKVRE 516
Cdd:COG1123 162 D-LLIADEPTTALDVTTQAEILDLLRELQRergtTVLLITHDLGVVAEIADRVVVMD-DGRIVE 223
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-208 |
1.51e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.01 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 3 LLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKG--EQQADDGEVwRAPALKIGEL-PQElpRAD 79
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTV-EFKGKDLLELsPED--RAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 80 ERIV----FDVVAEGLAEvgkllaeyhhlSLNIHTDDDLARLSRVQQELEARDgwrLQQLVDSTLSRLQLPAD----KTL 151
Cdd:PRK09580 78 EGIFmafqYPVEIPGVSN-----------QFFLQTALNAVRSYRGQEPLDRFD---FQDLMEEKIALLKMPEDlltrSVN 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 152 AELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEE---ALLGFNGAVLFITH 208
Cdd:PRK09580 144 VGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADgvnSLRDGKRSFIIVTH 203
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-185 |
1.78e-04 |
|
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: 43.69 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 14 GTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKV------VKGEQQAdDGEVWRAPALK-----IGELPQELpradeRI 82
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAflrllnTEGDIQI-DGVSWNSVPLQkwrkaFGVIPQKV-----FI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 83 VFDVVAEGLAEVGKllaeyhhlslniHTDDDLarlsrvqqeleardgWRLQQLVDSTLSRLQLPA--DKTLAE----LSG 156
Cdd:cd03289 89 FSGTFRKNLDPYGK------------WSDEEI---------------WKVAEEVGLKSVIEQFPGqlDFVLVDggcvLSH 141
|
170 180
....*....|....*....|....*....
gi 15598215 157 GWRRRVLLAQALVAEPDLLLLDEPTNHLD 185
Cdd:cd03289 142 GHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
317-468 |
2.19e-04 |
|
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: 42.99 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPG-GQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV-GTKLEVAYFDQLRHQLE- 393
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVRDYTLASLRRQIGl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 394 PEQ-------TVIDNISEGREFITiDGQNRHV--LSYLGDFLFS-PQRARTPVK----ALSGGERARLLLAKLFSKPANL 459
Cdd:cd03251 81 VSQdvflfndTVAENIAYGRPGAT-REEVEEAarAANAHEFIMElPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPI 159
|
....*....
gi 15598215 460 LVLDEPTND 468
Cdd:cd03251 160 LILDEATSA 168
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-221 |
2.37e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.13 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 22 VSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEV--------WRAP--ALKIGEL--PQElpRADERIV-FDVVA 88
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVyldgkpidIRSPrdAIRAGIMlcPED--RKAEGIIpVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 89 EGLAevgkLLAEYHHLS----LNIHTDDDLARLsrvqqeleardgwRLQQLVDSTLSRLQLpadktLAELSGGWRRRVLL 164
Cdd:PRK11288 350 DNIN----ISARRHHLRagclINNRWEAENADR-------------FIRSLNIKTPSREQL-----IMNLSGGNQQKAIL 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 165 AQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL--LGFNG-AVLFITHDRAFLQSLATRIL 221
Cdd:PRK11288 408 GRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIyeLAAQGvAVLFVSSDLPEVLGVADRIV 467
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
154-229 |
2.45e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 2.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598215 154 LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVlfithDRAFLqSLATRILELDRGHLI 229
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA-----DKTII-TIAHRIASIKRSDKI 1428
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
152-185 |
2.52e-04 |
|
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: 42.91 E-value: 2.52e-04
10 20 30
....*....|....*....|....*....|....
gi 15598215 152 AELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD 185
Cdd:cd03249 138 SQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
328-465 |
3.06e-04 |
|
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: 42.65 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 328 GGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVG------------TKLEVAYFDQlrhqlEP- 394
Cdd:TIGR04406 12 KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgqdithlpmherARLGIGYLPQ-----EAs 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598215 395 ---EQTVIDNIS---EGREFITIDGQNRHVLSYLGDFLFSPQRaRTPVKALSGGERARLLLAKLFSKPANLLVLDEP 465
Cdd:TIGR04406 87 ifrKLTVEENIMavlEIRKDLDRAEREERLEALLEEFQISHLR-DNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
317-466 |
3.19e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 42.69 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHpGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEVAYFD-QL------- 388
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLarrlall 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 389 -RHQLEPEQ-TVIDNISEGRE-----FITIDGQNRHVLSYLGDFLFSPQRARTPVKALSGGERARLLLAKLFSKPANLLV 461
Cdd:PRK11231 82 pQHHLTPEGiTVRELVAYGRSpwlslWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
....*
gi 15598215 462 LDEPT 466
Cdd:PRK11231 162 LDEPT 166
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
95-239 |
3.76e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 95 GKLLAEYHHLSLN---IHTDDDLARLSRVQQELEARDGwRLQQLVDSTLSRLQLpaDKTLAELSGGWRRRVLLAQALVAE 171
Cdd:PRK00635 418 GKTFAEFQQMSLQelfIFLSQLPSKSLSIEEVLQGLKS-RLSILIDLGLPYLTP--ERALATLSGGEQERTALAKHLGAE 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 172 PD--LLLLDEPT-------NHLDIGAIAWLEEAllgfNGAVLFITHDRAFLqSLATRILELDRGHLI-----DWNGDYAS 237
Cdd:PRK00635 495 LIgiTYILDEPSiglhpqdTHKLINVIKKLRDQ----GNTVLLVEHDEQMI-SLADRIIDIGPGAGIfggevLFNGSPRE 569
|
..
gi 15598215 238 FL 239
Cdd:PRK00635 570 FL 571
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
4-225 |
3.83e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.58 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAfgtTP----LLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVkgeqqaddGEVW--RAPAL------KIGEL 71
Cdd:TIGR00954 452 IKFENIPLV---TPngdvLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL--------GELWpvYGGRLtkpakgKLFYV 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 72 PQE----LPRADERIVFDVVAEGLAEVGkllaeyhhlslniHTDDDLAR-LSRVQQE--LEARDGWR-LQQLVDstlsrl 143
Cdd:TIGR00954 521 PQRpymtLGTLRDQIIYPDSSEDMKRRG-------------LSDKDLEQiLDNVQLThiLEREGGWSaVQDWMD------ 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 144 qlpadktlaELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNGAVLFITHdRAFLQSLATRILEL 223
Cdd:TIGR00954 582 ---------VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH-RKSLWKYHEYLLYM 651
|
..
gi 15598215 224 DR 225
Cdd:TIGR00954 652 DG 653
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
317-513 |
4.10e-04 |
|
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: 41.37 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGtgkttllklllgdlqptSGKievgTKLevayfdqLRhqlepeq 396
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSG-----------------TGK----SSL-------FR------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 397 tVIDNISE-GREFITIDGQNrhvlsylgDFLFSPQRARTPV------------KALSGGERARLLLAKLF-SKPAnLLVL 462
Cdd:cd03223 46 -ALAGLWPwGSGRIGMPEGE--------DLLFLPQRPYLPLgtlreqliypwdDVLSGGEQQRLAFARLLlHKPK-FVFL 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598215 463 DEPTN--DLDVETLELLEEVLLGFqgTVLMVSHdRAFLDNVVTSTLVFEGEGK 513
Cdd:cd03223 116 DEATSalDEESEDRLYQLLKELGI--TVISVGH-RPSLWKFHDRVLDLDGEGG 165
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
317-514 |
5.13e-04 |
|
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: 42.01 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV-GT---------------KL 380
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQdvsdlrgraipylrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 381 EVAYFDqlrHQLEPEQTVIDNISEGREFITIDGQ--NRHVLSYLgDFLFSPQRARTPVKALSGGERARLLLAKLFSKPAN 458
Cdd:cd03292 81 GVVFQD---FRLLPDRNVYENVAFALEVTGVPPReiRKRVPAAL-ELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598215 459 LLVLDEPTNDLDVETLELLEEVLLGFQ---GTVLMVSHDRAFLDNVVTSTLVFEgEGKV 514
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALE-RGKL 214
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
151-185 |
5.55e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 41.46 E-value: 5.55e-04
10 20 30
....*....|....*....|....*....|....*
gi 15598215 151 LAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD 185
Cdd:cd03232 106 LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
317-466 |
5.61e-04 |
|
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: 43.19 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLeVAYFDqlRHQLE--- 393
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS-LKDID--RHTLRqfi 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 394 ---PEQ------TVIDNISEG-REFITIDGQNRHV--LSYLGDFLFSPQRARTPVKA----LSGGERARLLLAKLFSKPA 457
Cdd:TIGR01193 551 nylPQEpyifsgSILENLLLGaKENVSQDEIWAACeiAEIKDDIENMPLGYQTELSEegssISGGQKQRIALARALLTDS 630
|
....*....
gi 15598215 458 NLLVLDEPT 466
Cdd:TIGR01193 631 KVLILDEST 639
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
328-467 |
6.38e-04 |
|
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: 41.43 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 328 GGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEVAYFDQLRH--------QLEPEQTVI 399
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRigalieapGFYPNLTAR 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 400 DNISEGREFITIDGQNRH-VLSYLGdflfSPQRARTPVKALSGGERARLLLAK-LFSKPaNLLVLDEPTN 467
Cdd:cd03268 91 ENLRLLARLLGIRKKRIDeVLDVVG----LKDSAKKKVKGFSLGMKQRLGIALaLLGNP-DLLILDEPTN 155
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
317-529 |
6.38e-04 |
|
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: 41.83 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV-GTKLEVAYFDQLRHQLE-- 393
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDIREVTLDSLRRAIGvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 394 PEQTVI------DNISEGREFITiDGQNRHV--LSYLGDFLFS-PQRARTPVKA----LSGGERARLLLAKLFSKPANLL 460
Cdd:cd03253 81 PQDTVLfndtigYNIRYGRPDAT-DEEVIEAakAAQIHDKIMRfPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598215 461 VLDEPTN--DLDVETLELLEEVLLGFQGTVLMVSHDrafLDNVVTSTLVFE-GEGKVREfVGGYQDWLRQGG 529
Cdd:cd03253 160 LLDEATSalDTHTEREIQAALRDVSKGRTTIVIAHR---LSTIVNADKIIVlKDGRIVE-RGTHEELLAKGG 227
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
154-216 |
6.96e-04 |
|
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: 41.44 E-value: 6.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598215 154 LSGGWRR------RVLLAQALVAEPDLLLLDEPTNHLDIGAIAW-----LEEALLGFNGAVLFITHDRAFLQSL 216
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
329-465 |
7.93e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 42.13 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 329 GQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV-GTKL-EVAYFDQ------LRHQLEPEQTVID 400
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdGVDLsHVPPYQRpinmmfQSYALFPHMTVEQ 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598215 401 NISEG-------REFITIDGQNRHVLSYLGDFlfspqRARTPvKALSGGERARLLLAKLFSKPANLLVLDEP 465
Cdd:PRK11607 111 NIAFGlkqdklpKAEIASRVNEMLGLVHMQEF-----AKRKP-HQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
132-223 |
7.94e-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: 40.77 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 132 LQQLVDSTLSRLQLpaDKTLAELSGGWRRRVLLAQALVAEPD--LLLLDEPTNHLDIGAIAWLEEAL--LGFNG-AVLFI 206
Cdd:cd03238 68 LQFLIDVGLGYLTL--GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIkgLIDLGnTVILI 145
|
90
....*....|....*..
gi 15598215 207 THDRAFLQSlATRILEL 223
Cdd:cd03238 146 EHNLDVLSS-ADWIIDF 161
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
409-466 |
7.99e-04 |
|
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: 40.49 E-value: 7.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598215 409 ITIDGQNRHVLSylgdflfsPQRAR----TPVKALSGGERARLLLAKLFSKPANLLVLDEPT 466
Cdd:cd03216 57 ILVDGKEVSFAS--------PRDARragiAMVYQLSVGERQMVEIARALARNARLLILDEPT 110
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
435-499 |
8.61e-04 |
|
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: 41.05 E-value: 8.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598215 435 PVKALSGGERA------RLLLAKLFSKPANLLVLDEPTN-------DLDVETLELLEEVLLGFQgtVLMVSHDRAFLD 499
Cdd:cd03240 112 MRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTnldeeniEESLAEIIEERKSQKNFQ--LIVITHDEELVD 187
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
317-466 |
9.66e-04 |
|
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: 41.20 E-value: 9.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHpGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGkievgtKLEVAYFDQLRHQLE--- 393
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG------RATVAGHDVVREPREvrr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 394 -----PEQTVIDNISEGREFITIDG------------QNRHVLSY--LGDFlfspqrARTPVKALSGGERARLLLAKLFS 454
Cdd:cd03265 74 rigivFQDLSVDDELTGWENLYIHArlygvpgaerreRIDELLDFvgLLEA------ADRLVKTYSGGMRRRLEIARSLV 147
|
170
....*....|..
gi 15598215 455 KPANLLVLDEPT 466
Cdd:cd03265 148 HRPEVLFLDEPT 159
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-209 |
1.05e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 41.31 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 2 TLLKFTDVSLAFGTTPLLDKVSWQIGRGERVCVIGRNGTGKSSLFKV------------VKGE----------QQADDGE 59
Cdd:PRK14243 9 TVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlipgfrVEGKvtfhgknlyaPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 60 VWRapalKIGELPQElPRADERIVFDVVAEGlaevgkllAEYHHLSLNIhtdDDLARLSRVQQEL--EARDgwrlqQLVD 137
Cdd:PRK14243 89 VRR----RIGMVFQK-PNPFPKSIYDNIAYG--------ARINGYKGDM---DELVERSLRQAALwdEVKD-----KLKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598215 138 STLSrlqlpadktlaeLSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEAL--LGFNGAVLFITHD 209
Cdd:PRK14243 148 SGLS------------LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMheLKEQYTIIIVTHN 209
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
316-466 |
1.27e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 41.37 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 316 VIVVEHVSFAHPGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKlEVAY----------- 384
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYsrkglmklres 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 385 ----FDQLRHQLEpEQTVIDNISEGREFITI--DGQNRHVLSYLGDFLFSPQRARtPVKALSGGERARLLLAKLFSKPAN 458
Cdd:PRK13636 84 vgmvFQDPDNQLF-SASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-PTHCLSFGQKKRVAIAGVLVMEPK 161
|
....*...
gi 15598215 459 LLVLDEPT 466
Cdd:PRK13636 162 VLVLDEPT 169
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-228 |
1.71e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 41.92 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 17 PLLDKVSWQIGRGERVCVIGRNGTGKSSLFKVVKGEQQADDGEVWrapalkIGElpqelprADERIVFDVVAEGLAEVGK 96
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL------VGG-------KDIETNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 97 LLAEYHHLSLNIHTDDDLARLSRVQQELEARdgwrLQQLVDSTlsRLQLPADKTLAELSGGWRRRVLLAQALVAEPDLLL 176
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLE----MEAMLEDT--GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598215 177 LDEPTNHLDIGAIAWLEEALLGFNGA--VLFITHDRAFLQSLATRILELDRGHL 228
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGrtIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
140-220 |
1.75e-03 |
|
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: 39.28 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 140 LSRLQLPADKTLAELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGF---------NGAVLFITHDR 210
Cdd:smart00382 47 DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRlllllksekNLTVILTTNDE 126
|
90
....*....|
gi 15598215 211 AFLQSLATRI 220
Cdd:smart00382 127 KDLGPALLRR 136
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
329-465 |
2.01e-03 |
|
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: 41.43 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 329 GQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKleVAYFDQLRHQLepEQTVIDNISEGref 408
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSPQTSWIM--PGTIKDNIIFG--- 510
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598215 409 ITIDG-QNRHVLSYLG---DFLFSPQRARTPVK----ALSGGERARLLLAKLFSKPANLLVLDEP 465
Cdd:TIGR01271 511 LSYDEyRYTSVIKACQleeDIALFPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSP 575
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
385-464 |
2.92e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 39.56 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 385 FDQLRHQLEPEQTVIDNISEGREFitidGQNRHVLSYLGdfLFSPQRARTPVKALSGGERARLLLAKLFSKPANLLVLDE 464
Cdd:COG2401 89 VDVPDNQFGREASLIDAIGRKGDF----KDAVELLNAVG--LSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDE 162
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
327-501 |
3.20e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 40.60 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 327 PGGQPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLqPTSGKIEV-GTKLEVAYFDQLRHQLE--------PEQT 397
Cdd:PRK11174 360 PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKInGIELRELDPESWRKHLSwvgqnpqlPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 398 VIDNISEGREFITiDGQNRHVL--SYLGDFLFS-PQRARTPVK----ALSGGERARLLLAKLFSKPANLLVLDEPTN--D 468
Cdd:PRK11174 439 LRDNVLLGNPDAS-DEQLQQALenAWVSEFLPLlPQGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTAslD 517
|
170 180 190
....*....|....*....|....*....|...
gi 15598215 469 LDVETLELLEEVLLGFQGTVLMVSHDRAFLDNV 501
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW 550
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
153-230 |
3.43e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 39.76 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 153 ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLD----IGAIAWLEEALLGFNGAVLFITHDRAFLQSLATRILELDRGHL 228
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
..
gi 15598215 229 ID 230
Cdd:PRK13646 225 VS 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
333-467 |
3.64e-03 |
|
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: 39.19 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 333 VRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV-------GTKLEVAYFDQLRhQLEPEQTVIDNIseg 405
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkpldiAARNRIGYLPEER-GLYPKMKVIDQL--- 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598215 406 REFITIDGQNRH-----VLSYLGDFLFSPQRARtPVKALSGGERARL-LLAKLFSKPAnLLVLDEPTN 467
Cdd:cd03269 92 VYLAQLKGLKKEearrrIDEWLERLELSEYANK-RVEELSKGNQQKVqFIAAVIHDPE-LLILDEPFS 157
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
317-465 |
4.28e-03 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 39.46 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGG---QPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKlEVAYFDQLR---- 389
Cdd:COG4525 4 LTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-PVTGPGADRgvvf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 390 --HQLEPEQTVIDNISEGREFITIDGQNRH-------VLSYLGDFlfspqrARTPVKALSGGERARLLLAK-LFSKPAnL 459
Cdd:COG4525 83 qkDALLPWLNVLDNVAFGLRLRGVPKAERRaraeellALVGLADF------ARRRIWQLSGGMRQRVGIARaLAADPR-F 155
|
....*.
gi 15598215 460 LVLDEP 465
Cdd:COG4525 156 LLMDEP 161
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
153-220 |
4.32e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 39.89 E-value: 4.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598215 153 ELSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIAWLEEALLGFNG----AVLFITHDRAFLQSLATRI 220
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqgtSILLISHDLESISQWADTI 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
317-466 |
5.01e-03 |
|
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: 39.01 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 317 IVVEHVSFAHPGGQPLV-RDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEV-GTKLEVAYFDQLRHQLEP 394
Cdd:cd03252 1 ITFEHVRFRYKPDGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 395 --------EQTVIDNISEGREfitidGQNRHVLSYLG------DFLFS-PQRARTPV----KALSGGERARLLLAKLFSK 455
Cdd:cd03252 81 vlqenvlfNRSIRDNIALADP-----GMSMERVIEAAklagahDFISElPEGYDTIVgeqgAGLSGGQRQRIAIARALIH 155
|
170
....*....|.
gi 15598215 456 PANLLVLDEPT 466
Cdd:cd03252 156 NPRILIFDEAT 166
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
333-466 |
6.75e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 38.91 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 333 VRDFSMVLQRGDRIGLLGANGtgkttllklllgdLQPTSGKIEVG----TKLEVAY-------FDQlRHQLEPEQTVID- 400
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGagksttikmltgiLVPTSGEVRVLgyvpFKRRKEFarrigvvFGQ-RSQLWWDLPAIDs 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 401 --------NISEGR------EFITIdgqnrhvLSyLGDFLfspqraRTPVKALSGGERARL-LLAKLFSKPAnLLVLDEP 465
Cdd:COG4586 117 frllkaiyRIPDAEykkrldELVEL-------LD-LGELL------DTPVRQLSLGQRMRCeLAAALLHRPK-ILFLDEP 181
|
.
gi 15598215 466 T 466
Cdd:COG4586 182 T 182
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
436-468 |
6.86e-03 |
|
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: 38.40 E-value: 6.86e-03
10 20 30
....*....|....*....|....*....|...
gi 15598215 436 VKALSGGERARLLLAKLFSKPANLLVLDEPTND 468
Cdd:cd03233 116 VRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-190 |
7.69e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.72 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 4 LKFTDVSLAFGTT--PLLDKVSWQIGRGERVCVIGRNGTGKSS----LFKVVKGEQqaddGEVWrapalkigelpqelpr 77
Cdd:PLN03130 1238 IKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSmlnaLFRIVELER----GRIL---------------- 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 78 ADErivFDVVAEGLAEVGKLLA-------------EYHHLSLNIHTDDDLarlsrvqqeLEARDGWRLQQLVdstlSRLQ 144
Cdd:PLN03130 1298 IDG---CDISKFGLMDLRKVLGiipqapvlfsgtvRFNLDPFNEHNDADL---------WESLERAHLKDVI----RRNS 1361
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598215 145 LPADKTLAE----LSGGWRRRVLLAQALVAEPDLLLLDEPTNHLDIGAIA 190
Cdd:PLN03130 1362 LGLDAEVSEagenFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
304-466 |
7.99e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 39.42 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 304 FQLESADKSGKQVIVVEHVSFAHPGG-QPLVRDFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEV 382
Cdd:PRK11160 326 FPTTSTAAADQVSLTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 383 AYF-DQLRHQLepeqTVI------------DNISEGREFITiDGQNRHVLSY--LGDFLFSPQRARTPV----KALSGGE 443
Cdd:PRK11160 406 DYSeAALRQAI----SVVsqrvhlfsatlrDNLLLAAPNAS-DEALIEVLQQvgLEKLLEDDKGLNAWLgeggRQLSGGE 480
|
170 180
....*....|....*....|...
gi 15598215 444 RARLLLAKLFSKPANLLVLDEPT 466
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPT 503
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
335-517 |
8.11e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 335 DFSMVLQRGDRIGLLGANGTGKTTLLKLLLGDLQPTSGKIEVGTKLEV-AYFDQLRHQLepeqTVIDNIsegrEF-ITID 412
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSViAISAGLSGQL----TGIENI----EFkMLCM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598215 413 GQNRHVL----------SYLGDFLFSpqrartPVKALSGGERARLLLAKLFSKPANLLVLDEPTNDLDVETLELLEEVLL 482
Cdd:PRK13546 114 GFKRKEIkamtpkiiefSELGEFIYQ------PVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIY 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598215 483 GFQ---GTVLMVSHDRAFLDNVVTSTLVFEGeGKVREF 517
Cdd:PRK13546 188 EFKeqnKTIFFVSHNLGQVRQFCTKIAWIEG-GKLKDY 224
|
|
| |
