|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-634 |
0e+00 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 1336.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRNIG 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 GSVFDFVAEGVAEQAEHLKAYHAISHLVESDPSEKNLARMAQIMEILDHQGLWQLDSRISEVLLQLGLNGDAELSSLSGG 160
Cdd:PRK11147 81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 161 WLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPGNYDL 240
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 241 YLQSKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRVERSQRREVMGTAKMQVEEATRSGKIVF 320
Cdd:PRK11147 241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRSGKIVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQHRADLDPERTV 400
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 401 MDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:PRK11147 401 MDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 481 ELIDGYQGTVLLVSHDRQFVDNSVTECWIFEGNGVINAFVGGYYDAHHQRATAKPIRQAAPSASKPAAEKKAEQPKKTAA 560
Cdd:PRK11147 481 ELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSK 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505190249 561 KLSYNLLRELEQLPQRLEQLEAEIEALQAQMSDADFFTRPHSETQEVLTALADAEQALEQAFARWEELEAMKNG 634
Cdd:PRK11147 561 KLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLADLADAEQELEVAFERWEELEALKNG 634
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-525 |
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: 665.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 6 MSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRNIGGSVFD 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 86 FVAEGVAEQAEHLKAYHAISHLVESdpSEKNLARMAQIMEILDHQGLWQLDSRISEVLLQLGLNG---DAELSSLSGGWL 162
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAE--PDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEedlDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 163 RKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPGNYDLYL 242
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 243 QSKEEALRVEELQNAEFDRKLAQEEVWIRQ-GIKARR-TRNEGRVRALKALRVERSQRREvmGTAKMQVEEATRSGKIVF 320
Cdd:COG0488 239 EQRAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARKaKQAQSRIKALEKLEREEPPRRD--KTVEIRFPPPERLGKKVL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQHRADLDPERTV 400
Cdd:COG0488 317 ELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 401 MDNLAEGKQevmvNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:COG0488 397 LDELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 505190249 481 ELIDGYQGTVLLVSHDRQFVDNSVTECWIFEgNGVINAFVGGYYD 525
Cdd:COG0488 473 EALDDFPGTVLLVSHDRYFLDRVATRILEFE-DGGVREYPGGYDD 516
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-530 |
3.35e-130 |
|
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: 393.92 E-value: 3.35e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 34 LVGRNGAGKSTLLKI---LGKEIpldDGRVIYEQDLIVARLQQDPPRNIGGSVFDFVAEGVAEQAEHLKAYHAISHLV-- 108
Cdd:TIGR03719 36 VLGLNGAGKSTLLRImagVDKDF---NGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEISAKYae 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 109 ESDPSEKNLARMAQIMEILDHQGLWQLDSRISEVLLQLGL-NGDAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHL 187
Cdd:TIGR03719 113 PDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCpPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 188 DIETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPGNYDLYLQSKEEALRVEELQNAEFDRKLAQEE 267
Cdd:TIGR03719 193 DAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLEQEEKEESARQKTLKREL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 268 VWIRQGIKARRTRNEGRVRALKALRVERSQRREvmGTAKMQVEEATRSGKIVFELEDVNYQVGEKVLVRGFSAQVQRGDK 347
Cdd:TIGR03719 273 EWVRQSPKGRQAKSKARLARYEELLSQEFQKRN--ETAEIYIPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGI 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 348 IALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQHRADLDPERTVMDNLAEGKQEVMVNGRPRHVLGYLQDF 427
Cdd:TIGR03719 351 VGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRF 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 428 LFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELIDGYQGTVLLVSHDRQFVDNSVTEC 507
Cdd:TIGR03719 431 NFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHI 510
|
490 500
....*....|....*....|....*
gi 505190249 508 WIFEGNGVINAFVGGY--YDAHHQR 530
Cdd:TIGR03719 511 LAFEGDSHVEWFEGNFseYEEDKKR 535
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-525 |
6.47e-126 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 382.93 E-value: 6.47e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 34 LVGRNGAGKSTLLKILG---KEIpldDGRVIYEQDLIVARLQQDPPRNIGGSVFDFVAEGVAEQAEHLKAYHAISHLV-- 108
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAgvdKEF---EGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRFNEIYAAYae 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 109 ESDPSEKNLARMAQIMEILDHQGLWQLDSRISEVLLQLGL-NGDAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHL 187
Cdd:PRK11819 115 PDADFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCpPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 188 DIETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPGNYDLYLQSKEEALRVEELQNAEFDRKLAQEE 267
Cdd:PRK11819 195 DAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAKRLAQEEKQEAARQKALKREL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 268 VWIRQGIKARRTRNEGRVRALKALRVERSQRREvmGTAKMQVEEATRSGKIVFELEDVNYQVGEKVLVRGFSAQVQRGDK 347
Cdd:PRK11819 275 EWVRQSPKARQAKSKARLARYEELLSEEYQKRN--ETNEIFIPPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGI 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 348 IALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQHRADLDPERTVMDNLAEGKQEVMVNGRPRHVLGYLQDF 427
Cdd:PRK11819 353 VGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKVGNREIPSRAYVGRF 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 428 LFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELIDGYQGTVLLVSHDRQFVDNSVTEC 507
Cdd:PRK11819 433 NFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI 512
|
490
....*....|....*...
gi 505190249 508 WIFEGNGVINAFVGGYYD 525
Cdd:PRK11819 513 LAFEGDSQVEWFEGNFQE 530
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-525 |
2.33e-85 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 276.77 E-value: 2.33e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRNIGGS 82
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 VFDFVAEGVAEQAEHLKAYHAISHLVESdpSEKNLARMAQI-MEILDHQGlWQLDSRISEVLLQLGL-----NGdaELSS 156
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQERDRIYALPEM--SEEDGMKVADLeVKFAEMDG-YTAEARAGELLLGVGIpeeqhYG--LMSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 157 LSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPG 236
Cdd:PRK15064 156 VAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 237 NYDLYLQSKEEAlrvEELQNAEFDRKLAQ-EEVwirQGIKARRTRNegrvrALKAlRVERSQRREVmgtAKMQVEEATRS 315
Cdd:PRK15064 236 NYDEYMTAATQA---RERLLADNAKKKAQiAEL---QSFVSRFSAN-----ASKA-KQATSRAKQI---DKIKLEEVKPS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 316 GK----IVFE-----------LEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGT 380
Cdd:PRK15064 301 SRqnpfIRFEqdkklhrnaleVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 381 KLEVAYFDQ-HRADLDPERTVMDNLAEGKQ----EVMVngrpRHVLGYLqdfLFHPKRAMTPVKALSGGERNRLLLAKLF 455
Cdd:PRK15064 381 NANIGYYAQdHAYDFENDLTLFDWMSQWRQegddEQAV----RGTLGRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLM 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 456 LKPSNLLILDEPTNDLDVETLELLEELIDGYQGTVLLVSHDRQFVDNSVTECWIFEGNGVINaFVGGYYD 525
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVD-FSGTYEE 522
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-631 |
1.53e-63 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 221.58 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 18 LLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRnIGGSVFDFVAEGVAEQAEh 97
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPA-LPQPALEYVIDGDREYRQ- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 98 LKAYHAIShlvesdpSEKNLAR-MAQIMEILDHQGLWQLDSRISEVLLQLGLNGDA---ELSSLSGGWLRKAALGRALVS 173
Cdd:PRK10636 94 LEAQLHDA-------NERNDGHaIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQlerPVSDFSGGWRMRLNLAQALIC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 174 SPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPGNYDLYLQSKEEALRVEE 253
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 254 LQNAEFDRKLAQEEVWI-RQGIKARRTRN-EGRVRALKalRVERSQRREVMGTAKMQVEEATRSGKIVFELEDVNYQVGE 331
Cdd:PRK10636 247 AMYESQQERVAHLQSYIdRFRAKATKAKQaQSRIKMLE--RMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSAGYGD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 332 KVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQH-----RADLDPERTvMDNLAE 406
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHqleflRADESPLQH-LARLAP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 407 GKQEvmvngrpRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELIDGY 486
Cdd:PRK10636 404 QELE-------QKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 487 QGTVLLVSHDRQFVDNSVTECWIFEgNGVINAFVGGYYDAHH-----QRATAKPIRQAAPSASKPAAEKKaEQPKKTAA- 560
Cdd:PRK10636 477 EGALVVVSHDRHLLRSTTDDLYLVH-DGKVEPFDGDLEDYQQwlsdvQKQENQTDEAPKENNANSAQARK-DQKRREAEl 554
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 561 -KLSYNLLRELEQLPQRLEQLEAEIEALQAQMSDADFFTRPH-SETQEVLTALADAEQALEQAFARW----EELEAM 631
Cdd:PRK10636 555 rTQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRkAELTACLQQQASAKSGLEECEMAWleaqEQLEQM 631
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-525 |
2.20e-55 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 200.47 E-value: 2.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 34 LVGRNGAGKSTLLKILGKE----IPLDDGRVIYEQDLI---VARLQ----QDPPRNiggSVFDFVAEGVAEQAE-HLKAY 101
Cdd:PLN03073 208 LVGRNGTGKTTFLRYMAMHaidgIPKNCQILHVEQEVVgddTTALQcvlnTDIERT---QLLEEEAQLVAQQRElEFETE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 102 HAISHLVESDPSEKNLA--RMAQIMEILDHQGLWQLDSRISEVLLQLGLNGDAEL---SSLSGGWLRKAALGRALVSSPR 176
Cdd:PLN03073 285 TGKGKGANKDGVDKDAVsqRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVkatKTFSGGWRMRIALARALFIEPD 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 177 VLLLDEPTNHLDIETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPGNYDLYLQSKEEALRVEELQN 256
Cdd:PLN03073 365 LLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAF 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 257 AEFDRKLAQEEVWI---RQGIKaRRTRNEGRVRALKALrverSQRREVMGTAKMQVEEAT---RSGKIVFELEDVNYQV- 329
Cdd:PLN03073 445 ESNERSRSHMQAFIdkfRYNAK-RASLVQSRIKALDRL----GHVDAVVNDPDYKFEFPTpddRPGPPIISFSDASFGYp 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 330 GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQHRAD-LDPERTVMDNLAEgk 408
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDgLDLSSNPLLYMMR-- 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 409 qevMVNGRPRHVL-GYLQDFLFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELIDGYQ 487
Cdd:PLN03073 598 ---CFPGVPEQKLrAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQ 674
|
490 500 510
....*....|....*....|....*....|....*...
gi 505190249 488 GTVLLVSHDRQFVDNSVTECWIFEgNGVINAFVGGYYD 525
Cdd:PLN03073 675 GGVLMVSHDEHLISGSVDELWVVS-EGKVTPFHGTFHD 711
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
321-514 |
2.70e-50 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 171.09 E-value: 2.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQhradldpertv 400
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 401 mdnlaegkqevmvngrprhvlgylqdflfhpkramtpvkaLSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd03221 71 ----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190
....*....|....*....|....*....|....
gi 505190249 481 ELIDGYQGTVLLVSHDRQFVDNSVTECWIFEGNG 514
Cdd:cd03221 111 EALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-243 |
3.62e-44 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 165.24 E-value: 3.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQD----PPRN 78
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHqeelDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 79 iggSVFDFVAEGVAEQAE-HLKAYhaishlvesdpseknLARMaqimeildhqglwqldsrisevllqlGLNGD---AEL 154
Cdd:COG0488 395 ---TVLDELRDGAPGGTEqEVRGY---------------LGRF--------------------------LFSGDdafKPV 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 155 SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSW 234
Cdd:COG0488 431 GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
....*....
gi 505190249 235 PGNYDLYLQ 243
Cdd:COG0488 511 PGGYDDYLE 519
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-230 |
2.01e-43 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 152.22 E-value: 2.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQdpprniggsv 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 84 fdfvaegvaeqaehlkayhaishlvesdpseknlarmaqimeildhqglwqldsrisevllqlglngdaelssLSGGWLR 163
Cdd:cd03221 71 -------------------------------------------------------------------------LSGGEKM 77
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 164 KAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03221 78 RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-496 |
5.89e-41 |
|
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: 156.22 E-value: 5.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFS----DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPlDDGRVIYEQDLIVARLQQDPPRNIGGSVfdf 86
Cdd:COG1123 10 LSVRypggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLP-HGGRISGEVLLDGRDLLELSEALRGRRI--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 87 vaegvaeqaehlkayhaisHLVESDP-SEKNLAR-MAQIMEILDHQGL--WQLDSRISEVLLQLGLN--GDAELSSLSGG 160
Cdd:COG1123 86 -------------------GMVFQDPmTQLNPVTvGDQIAEALENLGLsrAEARARVLELLEAVGLErrLDRYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 161 WLRKAALGRALVSSPRVLLLDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVswpg 236
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIV---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 237 nydlylqskeEALRVEELQnaefdrklaqeevwirqgikarrtrneGRVRALKAlrversqrREVMGTAKMQVEEATRSG 316
Cdd:COG1123 223 ----------EDGPPEEIL---------------------------AAPQALAA--------VPRLGAARGRAAPAAAAA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 317 KIVFELEDVNY-----QVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLEVAYF 387
Cdd:COG1123 258 EPLLEVRNLSKrypvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkdlTKLSRRSL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 388 DQHRAD-----------LDPERTVMDNLAEGkqeVMVNG------RPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLL 450
Cdd:COG1123 338 RELRRRvqmvfqdpyssLNPRMTVGDIIAEP---LRLHGllsraeRRERVAELLERVGLPPDLADRYPHELSGGQRQRVA 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 505190249 451 LAK-LFLKPSnLLILDEPTNDLDVETLELLEELIDGYQ----GTVLLVSHD 496
Cdd:COG1123 415 IARaLALEPK-LLILDEPTSALDVSVQAQILNLLRDLQrelgLTYLFISHD 464
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
11-234 |
2.37e-32 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 125.54 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFS--DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE-QDL----------IVARLQQDPPR 77
Cdd:COG1120 7 LSVGygGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgRDLaslsrrelarRIAYVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 78 NIGGSVFDFVAegvaeqaehlkayhaishlvesdpseknLARMAqimeildHQGLWQLDSR-----ISEVLLQLGLNGDA 152
Cdd:COG1120 87 PFGLTVRELVA----------------------------LGRYP-------HLGLFGRPSAedreaVEEALERTGLEHLA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 153 E--LSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDL 226
Cdd:COG1120 132 DrpVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLL 211
|
....*...
gi 505190249 227 DRGKLVSW 234
Cdd:COG1120 212 KDGRIVAQ 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
320-498 |
1.24e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 119.15 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 320 FELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKL-----------EVAYFD 388
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 389 QhRADLDPErTVMDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAK-LFLKPSNLLiLDEP 467
Cdd:COG4619 81 Q-EPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRaLLLQPDVLL-LDEP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 505190249 468 TNDLDVETLELLEELIDGY----QGTVLLVSHDRQ 498
Cdd:COG4619 158 TSALDPENTRRVEELLREYlaeeGRAVLWVSHDPE 192
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
319-502 |
5.80e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 117.19 E-value: 5.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 319 VFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLEVAYFDQ----- 389
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgepiRDAREDYRRRlaylg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 390 HRADLDPERTVMDNL---AEGKQEVMVNGRPRHVLGYLQdfLfhPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDE 466
Cdd:COG4133 82 HADGLKPELTVRENLrfwAALYGLRADREAIDEALEAVG--L--AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 505190249 467 PTNDLDVETLELLEELIDGY---QGTVLLVSHDRQFVDN 502
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAA 196
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-267 |
9.57e-30 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 117.65 E-value: 9.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEqDLIVARLQQDPPRNIGgsvfdFVAEGV 91
Cdd:COG4555 10 KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID-GEDVRKEPREARRQIG-----VLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 92 aEQAEHLKAyhaishlvesdpsEKNLARMAQIMEILDHqglwQLDSRISEVLLQLGLNGDAE--LSSLSGGWLRKAALGR 169
Cdd:COG4555 84 -GLYDRLTV-------------RENIRYFAELYGLFDE----ELKKRIEELIELLGLEEFLDrrVGELSTGMKKKVALAR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 170 ALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF---DGSIVFISHDRSFIRNMATRIVDLDRGKLVswpgnydlYLQSKE 246
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVV--------AQGSLD 217
|
250 260
....*....|....*....|...
gi 505190249 247 E--ALRVEELQNAEFDRKLAQEE 267
Cdd:COG4555 218 ElrEEIGEENLEDAFVALIGSEE 240
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-257 |
2.53e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 116.73 E-value: 2.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGkEIPLDDGRV-IYEQDLIVARL------Q 72
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILG-LLPPTSGTVrLFGKPPRRARRrigyvpQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 73 QdppRNIGG----SVFDFVAEGVAEQAEHLKAYHAISHlvesdpseknlarmAQIMEILDHQGLWQL-DSRISEvllqlg 147
Cdd:COG1121 83 R---AEVDWdfpiTVRDVVLMGRYGRRGLFRRPSRADR--------------EAVDEALERVGLEDLaDRPIGE------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 148 lngdaelssLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DG-SIVFISHDRSFIRNMATRIV 224
Cdd:COG1121 140 ---------LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDLGAVREYFDRVL 210
|
250 260 270
....*....|....*....|....*....|...
gi 505190249 225 DLDRGKlvswpgnydLYLQSKEEALRVEELQNA 257
Cdd:COG1121 211 LLNRGL---------VAHGPPEEVLTPENLSRA 234
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-245 |
4.77e-29 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 121.54 E-value: 4.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDpprniggSVFDFvaegv 91
Cdd:PRK15064 328 GFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQD-------HAYDF----- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 92 aeqaehlkayhaishlvESDpseknlarmaqiMEILDHQGLWQ----LDSRISEVLLQLGLNGD---AELSSLSGGWLRK 164
Cdd:PRK15064 396 -----------------END------------LTLFDWMSQWRqegdDEQAVRGTLGRLLFSQDdikKSVKVLSGGEKGR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 165 AALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPGNYDLYLQS 244
Cdd:PRK15064 447 MLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRS 526
|
.
gi 505190249 245 K 245
Cdd:PRK15064 527 Q 527
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-230 |
1.10e-28 |
|
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: 113.72 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFS----DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRNIgGSVFD- 85
Cdd:cd03225 5 LSFSypdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV-GLVFQn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 86 ----FVAEGVAEQaehlkayhaishlVESDPseKNLARMAQIMEildhqglwqldSRISEVLLQLGLNG--DAELSSLSG 159
Cdd:cd03225 84 pddqFFGPTVEEE-------------VAFGL--ENLGLPEEEIE-----------ERVEEALELVGLEGlrDRSPFTLSG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505190249 160 GWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DG-SIVFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03225 138 GQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
12-232 |
1.29e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 114.39 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDliVARLQQDPPRNIGgsvfdFVAEG 90
Cdd:COG1131 9 RYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrVLGED--VARDPAEVRRRIG-----YVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 91 VAeQAEHLKAYhaishlvesdpseKNLARMAQIMEIldhqGLWQLDSRISEVLLQLGLNGDAE--LSSLSGGWLRKAALG 168
Cdd:COG1131 82 PA-LYPDLTVR-------------ENLRFFARLYGL----PRKEARERIDELLELFGLTDAADrkVGTLSGGMKQRLGLA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 169 RALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFIS-HDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVAIIDKGRIV 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-231 |
1.81e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.99 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLI-----------VARLQ 72
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLsampppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 73 QDPPRnIGGSVfdfvaegvaeqAEHLKAYHAISHLVESDPseknlarmaqimeildhqglwqldsRISEVLLQLGLNG-- 150
Cdd:COG4619 81 QEPAL-WGGTV-----------RDNLPFPFQLRERKFDRE-------------------------RALELLERLGLPPdi 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 151 -DAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET----IDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVD 225
Cdd:COG4619 124 lDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLT 203
|
....*.
gi 505190249 226 LDRGKL 231
Cdd:COG4619 204 LEAGRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-230 |
2.80e-28 |
|
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: 112.57 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIvARLQQDPPRNIGgs 82
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 vfdFVAE--GVAEQ---AEHLKAYHAIShlvesdpseknlarmaqimeildhqGLWQLDSRISEVLLQLGLNG--DAELS 155
Cdd:COG4133 79 ---YLGHadGLKPEltvRENLRFWAALY-------------------------GLRADREAIDEALEAVGLAGlaDLPVR 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 156 SLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF---DGSIVFISHDRSFIRnmATRIVDLDRGK 230
Cdd:COG4133 131 QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-501 |
2.82e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.65 E-value: 2.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 319 VFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTKLE-----VAYFDQhRA 392
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlFGKPPRrarrrIGYVPQ-RA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 393 DLDPER--TVMDnlaegkqeVMVNGRPRHvLGylqdFLFHPKRA-------------MT-----PVKALSGGERNRLLLA 452
Cdd:COG1121 85 EVDWDFpiTVRD--------VVLMGRYGR-RG----LFRRPSRAdreavdealervgLEdladrPIGELSGGQQQRVLLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505190249 453 KLFLKPSNLLILDEPTNDLDVETLELLEELIDGYQG---TVLLVSHD----RQFVD 501
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDlgavREYFD 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
321-507 |
3.05e-28 |
|
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: 112.63 E-value: 3.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTKLE-----VAYFDQHRaDL 394
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvFGKPLEkerkrIGYVPQRR-SI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 DPER--TVMDnlaegkqeVMVNGRPRHVlgylqDFLFHPKRA-------------MT-----PVKALSGGERNRLLLAKL 454
Cdd:cd03235 80 DRDFpiSVRD--------VVLMGLYGHK-----GLFRRLSKAdkakvdealervgLSeladrQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505190249 455 FLKPSNLLILDEPTNDLDVETLELLEELIDGYQG---TVLLVSHDRQFVDNSVTEC 507
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRV 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
335-469 |
5.51e-28 |
|
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: 109.66 E-value: 5.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 335 VRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG-----------TKLEVAYFDQHRAdLDPERTVMDN 403
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQDPQ-LFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505190249 404 LAEGKQEVMV-----NGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:pfam00005 80 LRLGLLLKGLskrekDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-233 |
2.76e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 110.14 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFS-DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIY-EQDLivARLQQD--PP--R 77
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQDL--SRLKRReiPYlrR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 78 NIGgSVF-DF-------VAEGVAeqaehlkayhaishlvesdpseknLArmaqiMEILDHQGLwQLDSRISEVLLQLGLN 149
Cdd:COG2884 80 RIG-VVFqDFrllpdrtVYENVA------------------------LP-----LRVTGKSRK-EIRRRVREVLDLVGLS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 150 GDAEL--SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFI-SHDRSFIRNMATRIV 224
Cdd:COG2884 129 DKAKAlpHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRMPKRVL 208
|
....*....
gi 505190249 225 DLDRGKLVS 233
Cdd:COG2884 209 ELEDGRLVR 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-231 |
6.33e-27 |
|
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: 107.48 E-value: 6.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEqdlivarlqqdpprniGGSV 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL----------------GKDI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 84 FDfvaegvaeqaEHLKAYHAISHLVESDPSEKNLarmaQIMEILDhqglwqldsrisevllqlglngdaelssLSGGWLR 163
Cdd:cd03230 65 KK----------EPEEVKRRIGYLPEEPSLYENL----TVRENLK----------------------------LSGGMKQ 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505190249 164 KAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF---DGSIVFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03230 103 RLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
17-232 |
1.01e-26 |
|
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: 109.12 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 17 PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRNIGgSVFdfvaegvaeQae 96
Cdd:COG1124 19 PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQ-MVF---------Q-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 97 hlkayHAISHLvesDPseknlaRM---AQIMEILDHQGLWQLDSRISEVLLQLGLngDAEL-----SSLSGGWLRKAALG 168
Cdd:COG1124 87 -----DPYASL---HP------RHtvdRILAEPLRIHGLPDREERIAELLEQVGL--PPSFldrypHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 169 RALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-232 |
3.17e-26 |
|
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: 107.42 E-value: 3.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFS---DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE-QDLIVARLQ----------QDPp 76
Cdd:COG1122 6 LSFSypgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgKDITKKNLRelrrkvglvfQNP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 77 RN--IGGSVFDFVAEGvaeqaehlkayhaishlvesdPseKNLArmaqimeiLDHQglwQLDSRISEVLLQLGLNG--DA 152
Cdd:COG1122 85 DDqlFAPTVEEDVAFG---------------------P--ENLG--------LPRE---EIRERVEEALELVGLEHlaDR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 153 ELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDG---SIVFISHDRSFIRNMATRIVDLDRG 229
Cdd:COG1122 131 PPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDG 210
|
...
gi 505190249 230 KLV 232
Cdd:COG1122 211 RIV 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-233 |
4.81e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 105.21 E-value: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDLivarlqqdpprniggsvfdfvae 89
Cdd:cd03214 7 VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlLDGKDL----------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 90 gvaeqaehlkayhaishlveSDPSEKNLAR----MAQIMEILdhqGLWQLDSRisevllqlglngdaELSSLSGGWLRKA 165
Cdd:cd03214 64 --------------------ASLSPKELARkiayVPQALELL---GLAHLADR--------------PFNELSGGERQRV 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505190249 166 ALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVS 233
Cdd:cd03214 107 LLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
345-607 |
1.22e-25 |
|
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: 111.57 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 345 GDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQhRADLDPERTVMDNLAEGKQEVmvngrpRHVL--- 421
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQ-EPQLDPTKTVRENVEEGVAEI------KDALdrf 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 422 ---------------------GYLQDFLFHPK---------RAM---------TPVKALSGGERNRLLLAKLFLKPSNLL 462
Cdd:TIGR03719 104 neisakyaepdadfdklaaeqAELQEIIDAADawdldsqleIAMdalrcppwdADVTKLSGGERRRVALCRLLLSKPDML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 463 ILDEPTNDLDVETLELLEELIDGYQGTVLLVSHDRQFVDNsVTEcWIFE---GNGVinAFVGGYYDAHHQRatakpirqa 539
Cdd:TIGR03719 184 LLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDN-VAG-WILEldrGRGI--PWEGNYSSWLEQK--------- 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505190249 540 apsaskpaaEKKAEQPKKTAAKLSYNLLRELEQLPQ----RLEQLEAEIEALQaQMSDADFFTRPhsETQEV 607
Cdd:TIGR03719 251 ---------QKRLEQEEKEESARQKTLKRELEWVRQspkgRQAKSKARLARYE-ELLSQEFQKRN--ETAEI 310
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
321-496 |
1.31e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 105.53 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTKLE---------VAYFDQH 390
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVArdpaevrrrIGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 391 RAdLDPERTVMDNL-----AEGKQEVMVNGRPRHVLGYLQdfLfhPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILD 465
Cdd:COG1131 82 PA-LYPDLTVRENLrffarLYGLPRKEARERIDELLELFG--L--TDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190
....*....|....*....|....*....|....
gi 505190249 466 EPTNDLDVETLELLEELIDGY--QG-TVLLVSHD 496
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELaaEGkTVLLSTHY 190
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
321-496 |
2.13e-25 |
|
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: 103.25 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGrvhcgtklEVAYFDQhradldpertv 400
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSG--------EIKVLGK----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 401 mdNLAEGKQEVmvngrpRHVLGYL-QDFLFHPKraMTP--VKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLE 477
Cdd:cd03230 63 --DIKKEPEEV------KRRIGYLpEEPSLYEN--LTVreNLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180
....*....|....*....|..
gi 505190249 478 LLEELIDGY---QGTVLLVSHD 496
Cdd:cd03230 133 EFWELLRELkkeGKTILLSSHI 154
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-496 |
2.29e-25 |
|
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: 103.28 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTKL------EVAyfdQHRAD 393
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILlDGKDLaslspkELA---RKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 394 LdP---ERTVMDNLAEgkqevmvngRprhvlgylqdflfhpkramtPVKALSGGERNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:cd03214 78 V-PqalELLGLAHLAD---------R--------------------PFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190
....*....|....*....|....*....|
gi 505190249 471 LDVETLELLEELI----DGYQGTVLLVSHD 496
Cdd:cd03214 128 LDIAHQIELLELLrrlaRERGKTVVMVLHD 157
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-511 |
4.03e-25 |
|
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: 101.94 E-value: 4.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHcgtklevaYFDQHRADLDPERtv 400
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL--------IDGKDIAKLPLEE-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 401 mdnlaegkqevmvngRPRHVLGYLQdflfhpkramtpvkaLSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd00267 71 ---------------LRRRIGYVPQ---------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....
gi 505190249 481 ELIDGYQG---TVLLVSHDRQFVDNSVTECWIFE 511
Cdd:cd00267 121 ELLRELAEegrTVIIVTHDPELAELAADRVIVLK 154
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-232 |
5.45e-25 |
|
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: 110.31 E-value: 5.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFS----DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIY-EQDLivarlQQDPP----RNIG- 80
Cdd:COG2274 479 VSFRypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdGIDL-----RQIDPaslrRQIGv 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 ---------GSVFDFVAEGvAEQAEHLKAYHAishlvesdpseknlARMAQIME-ILDHQGlwQLDSRISEvllqlglNG 150
Cdd:COG2274 554 vlqdvflfsGTIRENITLG-DPDATDEEIIEA--------------ARLAGLHDfIEALPM--GYDTVVGE-------GG 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 151 daelSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET----IDWLEGFLKefDGSIVFISHDRSFIRNmATRIVDL 226
Cdd:COG2274 610 ----SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETeaiiLENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVL 682
|
....*.
gi 505190249 227 DRGKLV 232
Cdd:COG2274 683 DKGRIV 688
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
321-495 |
6.16e-25 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 101.69 E-value: 6.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVN--YQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtklevaYFDQHradldper 398
Cdd:cd03228 2 EFKNVSfsYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI---------LIDGV-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 399 tvmdNLAEGKQEVMvngrpRHVLGYL-QD-FLFHpkraMTpVKA--LSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03228 65 ----DLRDLDLESL-----RKNIAYVpQDpFLFS----GT-IREniLSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180
....*....|....*....|...
gi 505190249 475 TLELLEELIDGYQG--TVLLVSH 495
Cdd:cd03228 131 TEALILEALRALAKgkTVIVIAH 153
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-230 |
8.11e-25 |
|
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: 100.78 E-value: 8.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 5 SMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYeqdlivarlqqdpprniggsvf 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 85 dfvaegvaeqaehlkayhaishlvesdpseknlarmaqimeilDHQGLWQLDSRisEVLLQLGLngdaeLSSLSGGWLRK 164
Cdd:cd00267 59 -------------------------------------------DGKDIAKLPLE--ELRRRIGY-----VPQLSGGQRQR 88
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 165 AALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF---DGSIVFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd00267 89 VALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-232 |
2.78e-24 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 101.43 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 17 PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE-QDLI--VARLQQDPPRNIgGSVFdfvaegvae 93
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgKDLLklSRRLRKIRRKEI-QMVF--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 94 QAehlkAYHAIshlvesDPseknlaRM---AQIMEILDHQGLWQLDSRISEVLLQL--GLNGDAELSS-----LSGGWLR 163
Cdd:cd03257 89 QD----PMSSL------NP------RMtigEQIAEPLRIHGKLSKKEARKEAVLLLlvGVGLPEEVLNrypheLSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505190249 164 KAALGRALVSSPRVLLLDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
310-502 |
6.72e-24 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 106.00 E-value: 6.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 310 EEATRSGKIVFELEDVNYQ-VGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGtklevayfD 388
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN--------G 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 389 QHRADLDPER-----------------TVMDNLAEGK-----QEVmvngrpRHVLG--YLQDFLfhpkRAM-----TPV- 438
Cdd:COG4988 399 VDLSDLDPASwrrqiawvpqnpylfagTIRENLRLGRpdasdEEL------EAALEaaGLDEFV----AALpdgldTPLg 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 439 ---KALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELIDGY-QG-TVLLVSHDRQFVDN 502
Cdd:COG4988 469 eggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaKGrTVILITHRLALLAQ 537
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
345-511 |
6.84e-24 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 105.97 E-value: 6.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 345 GDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQhRADLDPERTVMDNLAEGKQEVM--------VN-- 414
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ-EPQLDPEKTVRENVEEGVAEVKaaldrfneIYaa 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 415 -GRPRHVL-------GYLQDFLFHP---------KRAM---------TPVKALSGGERNRLLLAKLFLKPSNLLILDEPT 468
Cdd:PRK11819 112 yAEPDADFdalaaeqGELQEIIDAAdawdldsqlEIAMdalrcppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505190249 469 NDLDVETLELLEELIDGYQGTVLLVSHDRQFVDNsVTEcWIFE 511
Cdd:PRK11819 192 NHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDN-VAG-WILE 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
321-511 |
1.54e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 99.08 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQV--GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKLEVAYFDQHRADL--- 394
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLTKLSLKELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 --DPER-----TVMDNLAEGkqevMVN-GRPRH-----VLGYLQDFLFHPKRAmTPVKALSGGERNRLLLAK-LFLKPsN 460
Cdd:cd03225 81 fqNPDDqffgpTVEEEVAFG----LENlGLPEEeieerVEEALELVGLEGLRD-RSPFTLSGGQKQRVAIAGvLAMDP-D 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505190249 461 LLILDEPTNDLDVETLELLEELIDGYQG---TVLLVSHDRQFVDNSVTECWIFE 511
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLE 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-496 |
2.41e-23 |
|
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: 99.73 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 319 VFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTKLE----------VAYF 387
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLlDGRDLAslsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 388 DQHRAdlDPER-TVMDnlaegkqeVMVNGRPRHvlgylQDFLFHPK--------RAMT----------PVKALSGGERNR 448
Cdd:COG1120 81 PQEPP--APFGlTVRE--------LVALGRYPH-----LGLFGRPSaedreaveEALErtglehladrPVDELSGGERQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505190249 449 LLLAKLFLKPSNLLILDEPTNDLDVetlelleelidGYQ---------------GTVLLVSHD 496
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDL-----------AHQlevlellrrlarergRTVVMVLHD 197
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
330-532 |
2.76e-23 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 104.48 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 330 GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQHRADLDpeRTVMDNLAEGKQ 409
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALP--QPALEYVIDGDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 410 E--------------------VMVNG----------RPR-----HVLGYLQDFLFHPkramtpVKALSGGERNRLLLAKL 454
Cdd:PRK10636 90 EyrqleaqlhdanerndghaiATIHGkldaidawtiRSRaasllHGLGFSNEQLERP------VSDFSGGWRMRLNLAQA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 455 FLKPSNLLILDEPTNDLDVETLELLEELIDGYQGTVLLVSHDRQFVDNSVTECWIFEgNGVINAFVGGYYDAHHQRAT 532
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIE-QQSLFEYTGNYSSFEVQRAT 240
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-232 |
3.33e-23 |
|
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: 98.66 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARlqqdPPRNI----------------GGS 82
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL----PPHEIarlgigrtfqiprlfpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 VFDFVAegVAEQAehlkayHAISHLVESDPSEKNLARMAQIMEILDHQGLWQLdsrisevllqlglnGDAELSSLSGGWL 162
Cdd:cd03219 92 VLENVM--VAAQA------RTGSGLLLARARREEREARERAEELLERVGLADL--------------ADRPAGELSYGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505190249 163 RKAALGRALVSSPRVLLLDEPT---NHLDIE-TIDWLEGfLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAaglNPEETEeLAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
320-516 |
3.86e-23 |
|
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: 98.17 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 320 FELEDVNYQV-GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTKLEVAYFDQHRADL--- 394
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvDGKDITKKNLRELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 --DPER-----TVMD-------NLAEGKQEvmVNGRPRHVLGY--LQDFLFHpkramtPVKALSGGERNRLLLAK-LFLK 457
Cdd:COG1122 81 fqNPDDqlfapTVEEdvafgpeNLGLPREE--IRERVEEALELvgLEHLADR------PPHELSGGQKQRVAIAGvLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505190249 458 PSnLLILDEPTNDLDVETLELLEELIDGYQG---TVLLVSHDRQFVDNSVTECWIFEGNGVI 516
Cdd:COG1122 153 PE-VLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
12-232 |
4.00e-23 |
|
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: 97.98 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDliVARLqqdPP--RNIgGSVFDFva 88
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlIDGRD--VTGV---PPerRNI-GMVFQD-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 89 egvaeqaehlkaYHAISHL-VesdpsEKNLA---RMAQIMEIldhqglwQLDSRISEVLLQLGLNGDAEL--SSLSGGWL 162
Cdd:cd03259 81 ------------YALFPHLtV-----AENIAfglKLRGVPKA-------EIRARVRELLELVGLEGLLNRypHELSGGQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505190249 163 RKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLK----EFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03259 137 QRVALARALAREPSLLLLDEPLSALDAKLREELREELKelqrELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
17-231 |
4.55e-23 |
|
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: 97.95 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 17 PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIY---------EQDLIVARLqqdppRNIGgSVFDFv 87
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdgtdisklsEKELAAFRR-----RHIG-FVFQS- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 88 aegvaeqaehlkaYHAISHLVESDpsekNLArMAQImeiLDHQGLWQLDSRISEVLLQLGLNGDAEL--SSLSGGWLRKA 165
Cdd:cd03255 91 -------------FNLLPDLTALE----NVE-LPLL---LAGVPKKERRERAEELLERVGLGDRLNHypSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 166 ALGRALVSSPRVLLLDEPTNHLDIET----IDWLEGFLKEFDGSIVFISHDRSFIRnMATRIVDLDRGKL 231
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
19-232 |
7.77e-23 |
|
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: 98.19 E-value: 7.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE-QDLI------VARL------QQdpPRNIGG-SVF 84
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgRDITglpphrIARLgiartfQN--PRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 85 DFVAEGvAEQAEHLKAYHAISHLVESDPSEKNLARMAqiMEILDhqglwqldsrisevllQLGLNGDAEL--SSLSGGWL 162
Cdd:COG0411 98 ENVLVA-AHARLGRGLLAALLRLPRARREEREARERA--EELLE----------------RVGLADRADEpaGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505190249 163 RKAALGRALVSSPRVLLLDEPT---NHLDI-ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAaglNPEETeELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-234 |
8.46e-23 |
|
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: 96.83 E-value: 8.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 5 SMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGkEIPLDDGRVIyeqdlIVARLQQDPPRNIG--- 80
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILG-LLKPTSGSIR-----VFGKPLEKERKRIGyvp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 ----------GSVFDFVAEGVAEQAEHLKAYHAishlvesdpseknlARMAQIMEILDHQGLWQL-DSRISEvllqlgln 149
Cdd:cd03235 75 qrrsidrdfpISVRDVVLMGLYGHKGLFRRLSK--------------ADKAKVDEALERVGLSELaDRQIGE-------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 150 gdaelssLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DG-SIVFISHDRSFIRNMATRIVDL 226
Cdd:cd03235 133 -------LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrrEGmTILVVTHDLGLVLEYFDRVLLL 205
|
....*...
gi 505190249 227 DRgKLVSW 234
Cdd:cd03235 206 NR-TVVAS 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-250 |
8.59e-23 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 97.57 E-value: 8.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE----QDLIVARLQQDPpRNI 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgediSGLSEAELYRLR-RRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 80 G-----GSVFD--FVAEGVA-EQAEHLKayhaishLVEsdpseknlarmaqimeildhqglWQLDSRISEVLLQLGLNGD 151
Cdd:cd03261 80 GmlfqsGALFDslTVFENVAfPLREHTR-------LSE-----------------------EEIREIVLEKLEAVGLRGA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 152 AEL--SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLD-------IETIDWLEgflKEFDGSIVFISHDRSFIRNMATR 222
Cdd:cd03261 130 EDLypAELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLK---KELGLTSIMVTHDLDTAFAIADR 206
|
250 260
....*....|....*....|....*...
gi 505190249 223 IVDLDRGKLVsWPGNYDLYLQSKEEALR 250
Cdd:cd03261 207 IAVLYDGKIV-AEGTPEELRASDDPLVR 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
30-232 |
8.89e-23 |
|
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: 102.29 E-value: 8.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 30 ERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE-QDliVARLQQDPPRNIGGS---VF-DfvaegvaeqaehlkAYHAI 104
Cdd:COG1123 292 ETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgKD--LTKLSRRSLRELRRRvqmVFqD--------------PYSSL 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 105 shlvesDPseknlaRM---AQIMEILDHQGLW---QLDSRISEVLLQLGLngDAEL-----SSLSGGWLRKAALGRALVS 173
Cdd:COG1123 356 ------NP------RMtvgDIIAEPLRLHGLLsraERRERVAELLERVGL--PPDLadrypHELSGGQRQRVAIARALAL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505190249 174 SPRVLLLDEPTNHLDIET----IDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1123 422 EPKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
292-501 |
9.15e-23 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 102.54 E-value: 9.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 292 RVERSQRR--EVMGTA---KMQVEEATRSGKIVFELEDVN--YQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKL 364
Cdd:COG4987 301 RVRAAARRlnELLDAPpavTEPAEPAPAPGGPSLELEDVSfrYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 365 MLGQLKADSGRVHC-GTKLE----------VAYFDQhRADL--DperTVMDNLAEGKQEV----MvngrpRHVLG--YLQ 425
Cdd:COG4987 381 LLRFLDPQSGSITLgGVDLRdldeddlrrrIAVVPQ-RPHLfdT---TLRENLRLARPDAtdeeL-----WAALErvGLG 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 426 DFLFH-PKRAMTPV----KALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELIDGYQG--TVLLVSHDRQ 498
Cdd:COG4987 452 DWLAAlPDGLDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLA 531
|
...
gi 505190249 499 FVD 501
Cdd:COG4987 532 GLE 534
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-232 |
1.26e-22 |
|
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: 97.46 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIY---EQ-------DL---- 66
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgERrggedvwELrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 67 -IV-ARLQQDPPRNIggSVFDFVAEGvaeqaehlkAYHAISHLVESDPSEKNLARmaQIMEILdhqGLWQLdsrisevll 144
Cdd:COG1119 81 gLVsPALQLRFPRDE--TVLDVVLSG---------FFDSIGLYREPTDEQRERAR--ELLELL---GLAHL--------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 145 qlglnGDAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET----IDWLEGFLKEFDGSIVFISHDRSFIRNMA 220
Cdd:COG1119 136 -----ADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTHHVEEIPPGI 210
|
250
....*....|..
gi 505190249 221 TRIVDLDRGKLV 232
Cdd:COG1119 211 THVLLLKDGRVV 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
315-502 |
1.31e-22 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 102.60 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 315 SGKIvfELEDVN--YQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtklevaYFDQH-R 391
Cdd:COG2274 471 KGDI--ELENVSfrYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI---------LIDGIdL 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 392 ADLDP-----------------ERTVMDNLAEGKQEV----------MVNgrprhvlgyLQDFL-FHPKRAMTPV----K 439
Cdd:COG2274 540 RQIDPaslrrqigvvlqdvflfSGTIRENITLGDPDAtdeeiieaarLAG---------LHDFIeALPMGYDTVVgeggS 610
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 440 ALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELIDGYQG--TVLLVSHDRQFVDN 502
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL 675
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
12-232 |
2.27e-22 |
|
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: 95.36 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVArlQQDPPRNIgGSVFD---FVA 88
Cdd:cd03268 9 TYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRI-GALIEapgFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 89 EGVAEqaEHLkayhaishlvesdpseKNLARMAQImeildhqglwqLDSRISEVLLQLGLNGDAEL--SSLSGGWLRKAA 166
Cdd:cd03268 86 NLTAR--ENL----------------RLLARLLGI-----------RKKRIDEVLDVVGLKDSAKKkvKGFSLGMKQRLG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 167 LGRALVSSPRVLLLDEPTNHLDIETIDWLEGF---LKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-502 |
2.83e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 100.65 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 13 FSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILG--KEIPLDDGRVIYEQDLIVARLQQDPPRNIGGSVFdfVAEG 90
Cdd:TIGR03269 10 FDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmDQYEPTSGRIIYHVALCEKCGYVERPSKVGEPCP--VCGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 91 VAEQAEhlkayhaISHLVESDPSEKNLARMAQIMeILDHQGLWQLDSRISEV---LLQLGLNGD------AEL------- 154
Cdd:TIGR03269 88 TLEPEE-------VDFWNLSDKLRRRIRKRIAIM-LQRTFALYGDDTVLDNVleaLEEIGYEGKeavgraVDLiemvqls 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 155 -------SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDW----LEGFLKEFDGSIVFISHDRSFIRNMATRI 223
Cdd:TIGR03269 160 hrithiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 224 VDLDRGKLVSwPGNYD----LYLQSKEEALRVEElqnaefdrklaqeevwIRQGIKARRTRNEGRvralKALRVERsqrr 299
Cdd:TIGR03269 240 IWLENGEIKE-EGTPDevvaVFMEGVSEVEKECE----------------VEVGEPIIKVRNVSK----RYISVDR---- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 300 evmGTAKMqveeatrsgkivfeledvnyqvgekvlVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG 379
Cdd:TIGR03269 295 ---GVVKA---------------------------VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 380 --------TKLEVayFDQHRA-----------DLDPERTVMDNLAE--GKQEVMVNGRPRHVLgYLQDFLFHPKRAMTPV 438
Cdd:TIGR03269 345 vgdewvdmTKPGP--DGRGRAkryigilhqeyDLYPHRTVLDNLTEaiGLELPDELARMKAVI-TLKMVGFDEEKAEEIL 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505190249 439 K----ALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELI----DGYQGTVLLVSHDRQFVDN 502
Cdd:TIGR03269 422 DkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTFIIVSHDMDFVLD 493
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-250 |
5.55e-22 |
|
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: 95.43 E-value: 5.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE-QDL--IVARLQQDPPRNI 79
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDgQDItgLSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 80 G-----GSVFDF--VAEGVA---EQAEHLkayhaishlvesdpSEKnlarmaqimEILDhqglwqldsRISEVLLQLGLN 149
Cdd:COG1127 85 GmlfqgGALFDSltVFENVAfplREHTDL--------------SEA---------EIRE---------LVLEKLELVGLP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 150 GDAEL--SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET---IDWLEGFL-KEFDGSIVFISHDRSFIRNMATRI 223
Cdd:COG1127 133 GAADKmpSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITsavIDELIRELrDELGLTSVVVTHDLDSAFAIADRV 212
|
250 260
....*....|....*....|....*..
gi 505190249 224 VDLDRGKLVsWPGNYDLYLQSKEEALR 250
Cdd:COG1127 213 AVLADGKII-AEGTPEELLASDDPWVR 238
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
561-630 |
1.22e-21 |
|
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: 88.68 E-value: 1.22e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 561 KLSYNLLRELEQLPQRLEQLEAEIEALQAQMSDADFFTRpHSETQEVLTALADAEQALEQAFARWEELEA 630
Cdd:pfam16326 1 KLSYKEQRELEELEAEIEKLEEEIAELEAQLADPELYSD-YEKLQELSAELEELEAELEELYERWEELEE 69
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-232 |
1.53e-21 |
|
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: 93.09 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGKEIPlDDGRvIYEQDLIVARLqqdPP--RNIg 80
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRmIAGLEEP-TSGR-IYIGGRDVTDL---PPkdRDI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 GSVFDFVAegvaeQAEHLKAYHAISH---LVESDPSEKNlARMAQIMEILdhqglwqldsRISEVLlqlglngDAELSSL 157
Cdd:cd03301 75 AMVFQNYA-----LYPHMTVYDNIAFglkLRKVPKDEID-ERVREVAELL----------QIEHLL-------DRKPKQL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 158 SGGWLRKAALGRALVSSPRVLLLDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03301 132 SGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
321-472 |
2.75e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.87 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTKL-EVAYFDQHRA------ 392
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlCGEPVpSRARHARQRVgvvpqf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 393 -DLDPERTVMDNL-AEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK13537 89 dNLDPDFTVRENLlVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
..
gi 505190249 471 LD 472
Cdd:PRK13537 169 LD 170
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-473 |
4.48e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.01 E-value: 4.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE------------QDLIVAR 70
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgepvrfrsprdaQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 71 LQQDPprniggSVFDF--VAEGVAeqaehlkayhaishlvesdpseknLARMAQIMEILDHQglwQLDSRISEVLLQLGL 148
Cdd:COG1129 84 IHQEL------NLVPNlsVAENIF------------------------LGREPRRGGLIDWR---AMRRRARELLARLGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 149 NGD--AELSSLSGGwlRKA--ALGRALVSSPRVLLLDEPTNHLDIETIDWLegF-----LKEFDGSIVFISHDRSFIRNM 219
Cdd:COG1129 131 DIDpdTPVGDLSVA--QQQlvEIARALSRDARVLILDEPTASLTEREVERL--FriirrLKAQGVAIIYISHRLDEVFEI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 220 ATRIVDLDRGKLvswpgnydlylqskeealrVEELQNAEFDRklaqEEVwIRQ--GikarrtrnegrvRALKALRVERsq 297
Cdd:COG1129 207 ADRVTVLRDGRL-------------------VGTGPVAELTE----DEL-VRLmvG------------RELEDLFPKR-- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 298 rrevmgtakmqveeATRSGKIVFELEDVNyqVGEKvlVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH 377
Cdd:COG1129 249 --------------AAAPGEVVLEVEGLS--VGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 378 -CGTKLE-----------VAYF--DQHRADLDPERTVMDNLAEGKQEVMVNGRP-------RHVLGYLQDFLFHPKRAMT 436
Cdd:COG1129 311 lDGKPVRirsprdairagIAYVpeDRKGEGLVLDLSIRENITLASLDRLSRGGLldrrrerALAEEYIKRLRIKTPSPEQ 390
|
490 500 510
....*....|....*....|....*....|....*..
gi 505190249 437 PVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:COG1129 391 PVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDV 427
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-231 |
4.70e-21 |
|
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: 92.09 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 15 DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDLIVARLQQDP--PRNIGGSVFDFvaegv 91
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrVNGQDVSDLRGRAIPylRRKIGVVFQDF----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 92 aEQAEHLKAYHAIshlvesdpseknlarmAQIMEILDHQG-LWQldSRISEVLLQLGLNG--DAELSSLSGGWLRKAALG 168
Cdd:cd03292 88 -RLLPDRNVYENV----------------AFALEVTGVPPrEIR--KRVPAALELVGLSHkhRALPAELSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505190249 169 RALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFD---GSIVFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
327-496 |
5.12e-21 |
|
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: 91.80 E-value: 5.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 327 YQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----------TKLEVAYFDQHRAdLDP 396
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgysirtdrkaARQSLGYCPQFDA-LFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 397 ERTVMDNL---AegkqevMVNGRPRH-----VLGYLQDFLFHPKRAmTPVKALSGGERNRLLLAKLFLKPSNLLILDEPT 468
Cdd:cd03263 89 ELTVREHLrfyA------RLKGLPKSeikeeVELLLRVLGLTDKAN-KRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190
....*....|....*....|....*....|
gi 505190249 469 NDLDVETLELLEELIDGYQG--TVLLVSHD 496
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-185 |
6.79e-21 |
|
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: 89.63 E-value: 6.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRNIGgsvfdfvaegVAEQAEHL 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIG----------YVFQDPQL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 99 KAYHAIshlvesdpsEKNLARMAQIMEILDHQglwqLDSRISEVLLQLGLNGDAE------LSSLSGGWLRKAALGRALV 172
Cdd:pfam00005 71 FPRLTV---------RENLRLGLLLKGLSKRE----KDARAEEALEKLGLGDLADrpvgerPGTLSGGQRQRVAIARALL 137
|
170
....*....|...
gi 505190249 173 SSPRVLLLDEPTN 185
Cdd:pfam00005 138 TKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
11-232 |
9.19e-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: 96.37 E-value: 9.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFS---DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDLivARLQQDPPRN-------- 78
Cdd:COG4988 342 VSFSypgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlINGVDL--SDLDPASWRRqiawvpqn 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 79 ---IGGSVfdfvaegvaeqAEHLKayhaishLVESDPSEknlarmAQIMEILDHQGLWQ--------LDSRISEvllqlg 147
Cdd:COG4988 420 pylFAGTI-----------RENLR-------LGRPDASD------EELEAALEAAGLDEfvaalpdgLDTPLGE------ 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 148 lNGdaelSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKE-FDGSIV-FISHDRSFIRNmATRIVD 225
Cdd:COG4988 470 -GG----RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGRTViLITHRLALLAQ-ADRILV 543
|
....*..
gi 505190249 226 LDRGKLV 232
Cdd:COG4988 544 LDDGRIV 550
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-501 |
9.92e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 96.42 E-value: 9.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 34 LVGRNGAGKSTLLKIL-GKEIP-LDDGRVIYEQDLIVAR-----LQQdpprniggsVFDFVAEGvaeqaeHLKAYHAISH 106
Cdd:PRK13409 104 ILGPNGIGKTTAVKILsGELIPnLGDYEEEPSWDEVLKRfrgteLQN---------YFKKLYNG------EIKVVHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 107 lVESDPseKNL-ARMAQIMEILDHQGLWqldsriSEVLLQLGLNG--DAELSSLSGGWLRKAALGRALVSSPRVLLLDEP 183
Cdd:PRK13409 169 -VDLIP--KVFkGKVRELLKKVDERGKL------DEVVERLGLENilDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 184 TNHLDI-------ETIdwlegflKEF--DGSIVFISHDRSfIRNMATRIVDLDRGKlvswPGNYDLYLQSKEealrVEEL 254
Cdd:PRK13409 240 TSYLDIrqrlnvaRLI-------RELaeGKYVLVVEHDLA-VLDYLADNVHIAYGE----PGAYGVVSKPKG----VRVG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 255 QNAEFDRKLAQEEVWIRQgikarrtrnegrvralKALRVE-RSQRREVmgtakmqveeatrSGKIVFELEDVNYQVGEKV 333
Cdd:PRK13409 304 INEYLKGYLPEENMRIRP----------------EPIEFEeRPPRDES-------------ERETLVEYPDLTKKLGDFS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 334 L-VRGfsAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcGTKLEVAYFDQHRADlDPERTVMDNLAEGKQEVM 412
Cdd:PRK13409 355 LeVEG--GEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYIKP-DYDGTVEDLLRSITDDLG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 413 VNgrprhvlgYLQDFLFHP---KRAMT-PVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELI----D 484
Cdd:PRK13409 430 SS--------YYKSEIIKPlqlERLLDkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIrriaE 501
|
490
....*....|....*..
gi 505190249 485 GYQGTVLLVSHDRQFVD 501
Cdd:PRK13409 502 EREATALVVDHDIYMID 518
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
19-233 |
1.45e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 90.87 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE-QDLI------VARLQQdppRNIGgsvfdFVaegv 91
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgQDISslsereLARLRR---RHIG-----FV---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 92 aeqaehLKAYHAISHL--VEsdpsekNLArMAQImeiLDHQGLWQLDSRISEVLLQLGLNGDAEL--SSLSGGWLRKAAL 167
Cdd:COG1136 92 ------FQFFNLLPELtaLE------NVA-LPLL---LAGVSRKERRERARELLERVGLGDRLDHrpSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 168 GRALVSSPRVLLLDEPTNHLDIET----IDWLEGFLKEFDGSIVFISHDRsFIRNMATRIVDLDRGKLVS 233
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-232 |
2.58e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 92.85 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDliVARLqqdPP--R 77
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlLDGRD--VTGL---PPekR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 78 NIGgSVF-DF-------VAEGVAEqaeHLKAyhaishlvesdpseKNLARmAQImeildhqglwqlDSRISEVLLQLGLN 149
Cdd:COG3842 78 NVG-MVFqDYalfphltVAENVAF---GLRM--------------RGVPK-AEI------------RARVAELLELVGLE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 150 GDAEL--SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHDRS--FIrnMAT 221
Cdd:COG3842 127 GLADRypHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQEeaLA--LAD 204
|
250
....*....|.
gi 505190249 222 RIVDLDRGKLV 232
Cdd:COG3842 205 RIAVMNDGRIE 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-230 |
3.90e-20 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 88.01 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE-QDLIVARLQQDPPRNIGGS 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 VF-DFVAegvaeqaehlkayhaISHlvesdpseknlarmaqiMEILDHQGLwqldsrisevllqlglngdaelsSLSGGW 161
Cdd:cd03229 81 VFqDFAL---------------FPH-----------------LTVLENIAL-----------------------GLSGGQ 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505190249 162 LRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLK----EFDGSIVFISHDRSFIRNMATRIVDLDRGK 230
Cdd:cd03229 106 QQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKslqaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
321-502 |
4.85e-20 |
|
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: 89.53 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV-HCG---------TKLEVAYFDQH 390
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlIDGedvrkepreARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 391 RAdLDPERTVMDNLaegKQEVMVNGRPRHVLGYLQDFLFH----PKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDE 466
Cdd:COG4555 83 RG-LYDRLTVRENI---RYFAELYGLFDEELKKRIEELIEllglEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505190249 467 PTNDLDVETLELLEELI-----DGyqGTVLLVSHDRQFVDN 502
Cdd:COG4555 159 PTNGLDVMARRLLREILralkkEG--KTVLFSSHIMQEVEA 197
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-500 |
5.06e-20 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 88.01 E-value: 5.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 320 FELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQHRAD------ 393
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrrigm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 394 ------LDPERTVMDNLAEGkqevmvngrprhvlgylqdflfhpkramtpvkaLSGGERNRLLLAK-LFLKPsNLLILDE 466
Cdd:cd03229 81 vfqdfaLFPHLTVLENIALG---------------------------------LSGGQQQRVALARaLAMDP-DVLLLDE 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 505190249 467 PTNDLDVETLELLEELI----DGYQGTVLLVSHDRQFV 500
Cdd:cd03229 127 PTSALDPITRREVRALLkslqAQLGITVVLVTHDLDEA 164
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-224 |
9.35e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 89.38 E-value: 9.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSDA----PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE--------QDLIV 68
Cdd:COG1116 5 APALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDgkpvtgpgPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 69 ArLQQD---PPRniggSVFDFVAEGVaEQAEHLKAyhaishlvesdpseknlARMAQIMEILDhqglwqldsrisevllQ 145
Cdd:COG1116 85 V-FQEPallPWL----TVLDNVALGL-ELRGVPKA-----------------ERRERARELLE----------------L 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 146 LGLNGDAEL--SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETI----DWLEGFLKEFDGSIVFISHDrsfIRN- 218
Cdd:COG1116 126 VGLAGFEDAypHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRerlqDELLRLWQETGKTVLFVTHD---VDEa 202
|
....*...
gi 505190249 219 --MATRIV 224
Cdd:COG1116 203 vfLADRVV 210
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
312-497 |
1.05e-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: 92.73 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 312 ATRSGKIVFELEDVNYQVGEKVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKL-------- 382
Cdd:TIGR02857 316 AAPASSLEFSGVSVAYPGRRPAL-RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLadadadsw 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 383 --EVAYFDQHRADLdpERTVMDNLAEGKQEV---MVNGRPRHVlgYLQDFLFH-PKRAMTPV----KALSGGERNRLLLA 452
Cdd:TIGR02857 395 rdQIAWVPQHPFLF--AGTIAENIRLARPDAsdaEIREALERA--GLDEFVAAlPQGLDTPIgeggAGLSGGQAQRLALA 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505190249 453 KLFLKPSNLLILDEPTNDLDVETLELLEELIDGY-QG-TVLLVSHDR 497
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaQGrTVLLVTHRL 517
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
320-472 |
1.43e-19 |
|
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: 86.60 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 320 FELEDVNYQVGE--KVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtklevaYFDQHradldPE 397
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGV-----PV 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 398 RTVMDNLAegKQEVMVNGRPrhvlgylqdFLFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03247 67 SDLEKALS--SLISVLNQRP---------YLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-231 |
1.48e-19 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 88.17 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 13 FSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPlDDGRVIYEQDLIVARLQQDppRNIG----------- 80
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIaGLERP-DSGTILFGGEDATDVPVQE--RNVGfvfqhyalfrh 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 GSVFDFVAEGvaeqaehLKAYHAishlvESDPSEKNLARmaQIMEILDhqglwqldsrisevLLQLGLNGDAELSSLSGG 160
Cdd:cd03296 89 MTVFDNVAFG-------LRVKPR-----SERPPEAEIRA--KVHELLK--------------LVQLDWLADRYPAQLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 161 WLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSI----VFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03296 141 QRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
11-232 |
1.68e-19 |
|
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: 92.52 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFS----DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV---------IYEQDL--IVARLQQDP 75
Cdd:COG4987 339 VSFRypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdlrdLDEDDLrrRIAVVPQRP 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 76 PrniggsVFDfvaegvAEQAEHLKayhaishLVESDPSEknlarmAQIMEILDHQGLWQLDSRisevlLQLGLngDAEL- 154
Cdd:COG4987 419 H------LFD------TTLRENLR-------LARPDATD------EELWAALERVGLGDWLAA-----LPDGL--DTWLg 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 155 ---SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETID-WLEGFLKEFDG-SIVFISHDRSFIRNMaTRIVDLDRG 229
Cdd:COG4987 467 eggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQaLLADLLEALAGrTVLLITHRLAGLERM-DRILVLEDG 545
|
...
gi 505190249 230 KLV 232
Cdd:COG4987 546 RIV 548
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-501 |
1.96e-19 |
|
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: 92.15 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 34 LVGRNGAGKSTLLKIL-GKEIP-LDDGRVIYEQDLIVARLQqdpprniGGSVFDF---VAEGvaeqaeHLKAYHAISHlV 108
Cdd:COG1245 104 ILGPNGIGKSTALKILsGELKPnLGDYDEEPSWDEVLKRFR-------GTELQDYfkkLANG------EIKVAHKPQY-V 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 109 ESDPSE-KNLARmaQIMEILDHQGLWqldsriSEVLLQLGLNG--DAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTN 185
Cdd:COG1245 170 DLIPKVfKGTVR--ELLEKVDERGKL------DELAEKLGLENilDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 186 HLDI-------ETIdwlEGFLKEfDGSIVFISHDRSfIRNMATRIVDLDRGKlvswPGNYDLYLQSKEealrVEELQNAE 258
Cdd:COG1245 242 YLDIyqrlnvaRLI---RELAEE-GKYVLVVEHDLA-ILDYLADYVHILYGE----PGVYGVVSKPKS----VRVGINQY 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 259 FDRKLAQEEVWIRQgikarrtrnegrvralKALRVE-RSQRREVMGTAKMQVEEATRS-GKivFELEdvnyqvgekvlVR 336
Cdd:COG1245 309 LDGYLPEENVRIRD----------------EPIEFEvHAPRREKEEETLVEYPDLTKSyGG--FSLE-----------VE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 337 GfsAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHcgTKLEVAYFDQH-RADLDpeRTVMDNLAEGKQEVMVNg 415
Cdd:COG1245 360 G--GEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKISYKPQYiSPDYD--GTVEEFLRSANTDDFGS- 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 416 rprhvlGYLQDFLFHP---KRAMT-PVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELI----DGYQ 487
Cdd:COG1245 433 ------SYYKTEIIKPlglEKLLDkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIrrfaENRG 506
|
490
....*....|....
gi 505190249 488 GTVLLVSHDRQFVD 501
Cdd:COG1245 507 KTAMVVDHDIYLID 520
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-230 |
1.98e-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: 85.90 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFS----DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDLivarlqqdppRNIGgsvfd 85
Cdd:cd03228 6 VSFSypgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlIDGVDL----------RDLD----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 86 fvaegvaeqaehLKAYHAISHLVESDPseknlarmaqimeildhqglWQLDSRISEVLLqlglngdaelsslSGGWLRKA 165
Cdd:cd03228 71 ------------LESLRKNIAYVPQDP--------------------FLFSGTIRENIL-------------SGGQRQRI 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 166 ALGRALVSSPRVLLLDEPTNHLDIET-IDWLEGFLKEFDG-SIVFISHDRSFIRnMATRIVDLDRGK 230
Cdd:cd03228 106 AIARALLRDPPILILDEATSALDPETeALILEALRALAKGkTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-232 |
2.46e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 89.82 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPlDDGRVIY-EQDLIVARLQQDppRNIGgsvFDF--- 86
Cdd:COG1118 11 RFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIaGLETP-DSGRIVLnGRDLFTNLPPRE--RRVG---FVFqhy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 87 -------VAEGVAEQAEHLKayhaishlvesdPSEKnlARMAQIMEILDhqglwqldsrisevLLQL-GLnGDAELSSLS 158
Cdd:COG1118 85 alfphmtVAENIAFGLRVRP------------PSKA--EIRARVEELLE--------------LVQLeGL-ADRYPSQLS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 159 GGWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG1118 136 GGQRQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-232 |
2.48e-19 |
|
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: 86.87 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 14 SDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGKEIPlDDGRVIYEQdlivARLQQDPP----RNIGgsvfdFVA 88
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKlLAGLYKP-TSGSVLLDG----TDIRQLDPadlrRNIG-----YVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 89 EGVAEQAEHLKAYHAISHLVESDpseknlarmAQIMEILDHQGLWQLDSRISEVL-LQLGLNGDaelsSLSGGWLRKAAL 167
Cdd:cd03245 85 QDVTLFYGTLRDNITLGAPLADD---------ERILRAAELAGVTDFVNKHPNGLdLQIGERGR----GLSGGQRQAVAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 168 GRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFISHDRSFIrNMATRIVDLDRGKLV 232
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-245 |
2.81e-19 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 87.25 E-value: 2.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 14 SDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPlDDGRVIYeQDLIVARLQQDPPRNIG---GSVFdfvae 89
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInGLERP-TSGSVLV-DGTDLTLLSGKELRKARrriGMIF----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 90 gvaeQAEHL----KAYHAISHLVEsdpseknlarmaqimeiLDHQGLWQLDSRISEVLLQLGLNG--DAELSSLSGGWLR 163
Cdd:cd03258 89 ----QHFNLlssrTVFENVALPLE-----------------IAGVPKAEIEERVLELLELVGLEDkaDAYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 164 KAALGRALVSSPRVLLLDEPTNHLDIET----IDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPGNYD 239
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
....*.
gi 505190249 240 LYLQSK 245
Cdd:cd03258 228 VFANPQ 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
333-496 |
3.03e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.13 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 333 VLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQHRADLD--PeRTVMDNLAEGK-Q 409
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDslP-LTVRDLVAMGRwA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 410 EVMVNGRPRHV-----------LGyLQDFLfhpKRamtPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLEL 478
Cdd:NF040873 85 RRGLWRRLTRDdraavddalerVG-LADLA---GR---QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180
....*....|....*....|.
gi 505190249 479 LEELID---GYQGTVLLVSHD 496
Cdd:NF040873 158 IIALLAeehARGATVVVVTHD 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-224 |
3.25e-19 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 86.76 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSDA----PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVAR-------LQ 72
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPgpdrgyvFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 73 QD---PPRNIGGSV-FDFVAEGVAeqaehlkayhaishlvesdpseknlarMAQIMEildhqglwqldsRISEVLLQLGL 148
Cdd:cd03293 81 QDallPWLTVLDNVaLGLELQGVP---------------------------KAEARE------------RAEELLELVGL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 149 NGDAEL--SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET----IDWLEGFLKEFDGSIVFISHDrsfIRN---M 219
Cdd:cd03293 122 SGFENAypHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHD---IDEavfL 198
|
....*
gi 505190249 220 ATRIV 224
Cdd:cd03293 199 ADRVV 203
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
321-496 |
3.56e-19 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 87.17 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtklevaYFDQH------RADL 394
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEV---------LIDGEdisglsEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 DPER----------------TVMDNLA------EGKQEVMVNGRprhVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLA 452
Cdd:cd03261 73 YRLRrrmgmlfqsgalfdslTVFENVAfplrehTRLSEEEIREI---VLEKLEAVGLRGAEDLYPAE-LSGGMKKRVALA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505190249 453 K-LFLKPSnLLILDEPTNDLDVETLELLEELI----DGYQGTVLLVSHD 496
Cdd:cd03261 149 RaLALDPE-LLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHD 196
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-232 |
4.04e-19 |
|
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: 84.79 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIyeqdlivarlqqdpprnIGGSV 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL-----------------VDGKE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 84 FDFvaegvaeqaehlkayhaishlveSDPSEKNLARMAQImeildHQglwqldsrisevllqlglngdaelssLSGGWLR 163
Cdd:cd03216 64 VSF-----------------------ASPRDARRAGIAMV-----YQ--------------------------LSVGERQ 89
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505190249 164 KAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DG-SIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03216 90 MVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
321-501 |
4.18e-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: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVG----EKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTKL------------- 382
Cdd:cd03255 2 ELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvDGTDIsklsekelaafrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 383 -EVAY-FDQHRadLDPERTVMDNLA-----EGKQEVMVNGRPRHVLGYLQdfLfhPKRAMTPVKALSGGERNRLLLAKLF 455
Cdd:cd03255 82 rHIGFvFQSFN--LLPDLTALENVElplllAGVPKKERRERAEELLERVG--L--GDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505190249 456 LKPSNLLILDEPTNDLDVETLELLEELI----DGYQGTVLLVSHDRQFVD 501
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLrelnKEAGTTIVVVTHDPELAE 205
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-249 |
4.83e-19 |
|
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: 90.76 E-value: 4.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPlDDGRVIYEQDLIVARLQQ-----DPPRNiggsVFD 85
Cdd:TIGR03719 331 AFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMItGQEQP-DSGTIEIGETVKLAYVDQsrdalDPNKT----VWE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 86 FVAEGvaeqaehlkayhaishlvesdpseknlarmAQIMEIldhqGLWQLDSRisEVLLQLGLNGDAE---LSSLSGGWL 162
Cdd:TIGR03719 406 EISGG------------------------------LDIIKL----GKREIPSR--AYVGRFNFKGSDQqkkVGQLSGGER 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 163 RKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSW-PGNYDLY 241
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWfEGNFSEY 529
|
....*...
gi 505190249 242 LQSKEEAL 249
Cdd:TIGR03719 530 EEDKKRRL 537
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
321-496 |
5.56e-19 |
|
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: 86.41 E-value: 5.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNY----QVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV----HCGTKLEVAYFDQHRA 392
Cdd:cd03257 3 EVKNLSVsfptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgKDLLKLSRRLRKIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 393 D-----------LDPERTVMDNLAEG--KQEVMVNGRPRHVLGYLQDFLFH-PKRAMT--PVkALSGGERNRLLLAK-LF 455
Cdd:cd03257 83 EiqmvfqdpmssLNPRMTIGEQIAEPlrIHGKLSKKEARKEAVLLLLVGVGlPEEVLNryPH-ELSGGQRQRVAIARaLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505190249 456 LKPSnLLILDEPTNDLDVETLELLEELI----DGYQGTVLLVSHD 496
Cdd:cd03257 162 LNPK-LLIADEPTSALDVSVQAQILDLLkklqEELGLTLLFITHD 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
321-502 |
9.64e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.49 E-value: 9.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVN--YQVGEKVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTKL------EVAY----- 386
Cdd:COG2884 3 RFENVSkrYPGGREAL-SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvNGQDLsrlkrrEIPYlrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 387 ---FDQHRadLDPERTVMDNLA-----EGKQEVMVNGRPRHVLGYLQdfLFHPKRAMTPvkALSGGERNRLLLAKLFL-K 457
Cdd:COG2884 82 gvvFQDFR--LLPDRTVYENVAlplrvTGKSRKEIRRRVREVLDLVG--LSDKAKALPH--ELSGGEQQRVAIARALVnR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505190249 458 PSnLLILDEPTNDLDVETLELLEELIDGY--QG-TVLLVSHDRQFVDN 502
Cdd:COG2884 156 PE-LLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDR 202
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
321-497 |
9.84e-19 |
|
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: 85.26 E-value: 9.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKL---------EVAYFDQHR 391
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvpperrNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 392 AdLDPERTVMDNLAEG--KQEVMVNGRPRHVLGYLQ--DFLFHPKRamtPVKALSGGERNRLLLAK-LFLKPSnLLILDE 466
Cdd:cd03259 82 A-LFPHLTVAENIAFGlkLRGVPKAEIRARVRELLElvGLEGLLNR---YPHELSGGQQQRVALARaLAREPS-LLLLDE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 505190249 467 PTNDLDVETLELLEELIDGYQG----TVLLVSHDR 497
Cdd:cd03259 157 PLSALDAKLREELREELKELQRelgiTTIYVTHDQ 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
321-495 |
1.18e-18 |
|
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: 84.96 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgTKLEVAYFDQHRA-------- 392
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---TFDGKSYQKNIEAlrrigali 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 393 ---DLDPERTVMDNLAEGKQEVMV-NGRPRHVLGY--LQDflfHPKRamtPVKALSGGERNRLLLAKLFLKPSNLLILDE 466
Cdd:cd03268 79 eapGFYPNLTARENLRLLARLLGIrKKRIDEVLDVvgLKD---SAKK---KVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190
....*....|....*....|....*....|..
gi 505190249 467 PTNDLD---VETLELLEELIDGYQGTVLLVSH 495
Cdd:cd03268 153 PTNGLDpdgIKELRELILSLRDQGITVLISSH 184
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
321-495 |
1.77e-18 |
|
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: 83.95 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTK---------LEVAYFDQHR 391
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdepHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 392 ADLDPERTVMDNLAEGkqevmvngrpRHVLGYLQDFLFHPKRAM-------TPVKALSGGERNRLLLAKLFLKPSNLLIL 464
Cdd:TIGR01189 82 PGLKPELSALENLHFW----------AAIHGGAQRTIEDALAAVgltgfedLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 505190249 465 DEPTNDLDVETLELLEELIDGY---QGTVLLVSH 495
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
321-496 |
1.83e-18 |
|
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: 84.45 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQ----VGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH------CGTKLEVAY-FDQ 389
Cdd:cd03293 2 EVRNVSKTygggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYvFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 390 HRadLDPERTVMDNLAEGkqeVMVNGRPR-----HVLGY-----LQDFLFH-PkramtpvKALSGGERNRLLLAK-LFLK 457
Cdd:cd03293 82 DA--LLPWLTVLDNVALG---LELQGVPKaeareRAEELlelvgLSGFENAyP-------HQLSGGMRQRVALARaLAVD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505190249 458 PsNLLILDEPTNDLDVETLELLEELI----DGYQGTVLLVSHD 496
Cdd:cd03293 150 P-DVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
321-499 |
1.88e-18 |
|
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: 84.23 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLV-RGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV-------HCGTKLEVAYF-DQHR 391
Cdd:cd03226 1 RIENISFSYKKGTEIlDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpiKAKERRKSIGYvMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 392 ADLDPERTVMDNLAEGKQEV-MVNGRPRHVLGYLQDFLF---HPkramtpvKALSGGERNRLLLAKLFLKPSNLLILDEP 467
Cdd:cd03226 81 DYQLFTDSVREELLLGLKELdAGNEQAETVLKDLDLYALkerHP-------LSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190
....*....|....*....|....*....|....*
gi 505190249 468 TNDLDVETLELLEELIDGYQG---TVLLVSHDRQF 499
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAqgkAVIVITHDYEF 188
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
283-496 |
2.15e-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: 88.57 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 283 GRVRAlKALRVERSQRREVMGTAKMQVEEATR-SGKIVFELEDVNYQV-GEKVLVRGFSAQVQRGDKIALVGPNGCGKTT 360
Cdd:TIGR02868 298 TRVRA-AAERIVEVLDAAGPVAEGSAPAAGAVgLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKST 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 361 LLKLMLGQLKADSGRV-----------HCGTKLEVAYFDQhradlDP---ERTVMDNLAEGK-----QEVMVNGRPRHVL 421
Cdd:TIGR02868 377 LLATLAGLLDPLQGEVtldgvpvssldQDEVRRRVSVCAQ-----DAhlfDTTVRENLRLARpdatdEELWAALERVGLA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 422 GYLQDFlfhPKRAMTPV----KALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELI-DGYQG-TVLLVSH 495
Cdd:TIGR02868 452 DWLRAL---PDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLlAALSGrTVVLITH 528
|
.
gi 505190249 496 D 496
Cdd:TIGR02868 529 H 529
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-247 |
2.36e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 84.96 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLD-----------DGRVIYEQDLIVA 69
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvsgevylDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 70 RLQ-------QDPPRNIggSVFDFVAEGVAeqaehlkayhaISHLVESdpsEKNLarMAQIMEILDHQGLWQldsrisEV 142
Cdd:PRK14247 81 RRRvqmvfqiPNPIPNL--SIFENVALGLK-----------LNRLVKS---KKEL--QERVRWALEKAQLWD------EV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 143 LLQLglngDAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFISHdrsfIRNMA 220
Cdd:PRK14247 137 KDRL----DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELkkDMTIVLVTH----FPQQA 208
|
250 260 270
....*....|....*....|....*....|.
gi 505190249 221 TRIVD----LDRGKLVSWPGNYDLYLQSKEE 247
Cdd:PRK14247 209 ARISDyvafLYKGQIVEWGPTREVFTNPRHE 239
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
318-472 |
2.44e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.81 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 318 IVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgTKLEVAYFDQHRA----- 392
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI---TVLGVPVPARARLarari 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 393 -------DLDPERTVMDNL-AEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLIL 464
Cdd:PRK13536 117 gvvpqfdNLDLEFTVRENLlVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
....*...
gi 505190249 465 DEPTNDLD 472
Cdd:PRK13536 197 DEPTTGLD 204
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-287 |
2.71e-18 |
|
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: 86.70 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 26 IEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIV---ARLQQDPPRNIGGSVFdfvaegvaEQAEHLKAYH 102
Cdd:TIGR02142 20 LPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdsrKGIFLPPEKRRIGYVF--------QEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 103 AISHLV----ESDPSEKNlARMAQIMEILdhqGLwqldsrisEVLLQLGLNgdaelsSLSGGWLRKAALGRALVSSPRVL 178
Cdd:TIGR02142 92 VRGNLRygmkRARPSERR-ISFERVIELL---GI--------GHLLGRLPG------RLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 179 LLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVS-------WpGNYDLYLQSKEE 247
Cdd:TIGR02142 154 LMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAagpiaevW-ASPDLPWLARED 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 505190249 248 ALRVEELQNAEFDRK-------LAQEEVWIRQGIKARRTRNEGRVRA 287
Cdd:TIGR02142 233 QGSLIEGVVAEHDQHygltalrLGGGHLWVPENLGPTGARLRLRVPA 279
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-232 |
3.29e-18 |
|
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: 83.71 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEqDLIVARLQQDPPRNIG-----GSVFD-FVAEgva 92
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN-GYSIRTDRKAARQSLGycpqfDALFDeLTVR--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 93 eqaEHLKAYHAISHLVESDpSEKNLARMAQIMEILDHQglwqlDSRISEvllqlglngdaelssLSGGWLRKAALGRALV 172
Cdd:cd03263 94 ---EHLRFYARLKGLPKSE-IKEEVELLLRVLGLTDKA-----NKRART---------------LSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505190249 173 SSPRVLLLDEPTNHLDIETIDWLEGFLKEFDG--SIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-232 |
3.82e-18 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 83.77 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLD-----------DGRVIYEQDLIVARLq 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdegevllDGKDIYDLDVDVLEL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 73 qdpPRNIG----------GSVFDFVAEGVAEQAEHLKAyhaishlvESDPSEKNLARMAqimeildhqGLWQldsrisEV 142
Cdd:cd03260 80 ---RRRVGmvfqkpnpfpGSIYDNVAYGLRLHGIKLKE--------ELDERVEEALRKA---------ALWD------EV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 143 LLQLGLngdaelSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFISHDRSFIRNMA 220
Cdd:cd03260 134 KDRLHA------LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHNMQQAARVA 207
|
250
....*....|..
gi 505190249 221 TRIVDLDRGKLV 232
Cdd:cd03260 208 DRTAFLLNGRLV 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
319-495 |
5.67e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 83.98 E-value: 5.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 319 VFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMlgqlkadSGRVHCGTKLEVAYFDQHR------- 391
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLI-------TGDLPPTYGNDVRLFGERRggedvwe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 392 -------------ADLDPERTVMDNLAEGKQEVMvnGRPRHV-----------LGYLQdfLFHpkRAMTPVKALSGGERN 447
Cdd:COG1119 76 lrkriglvspalqLRFPRDETVLDVVLSGFFDSI--GLYREPtdeqrerarelLELLG--LAH--LADRPFGTLSQGEQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505190249 448 RLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELIDGY--QG--TVLLVSH 495
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTH 201
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
320-495 |
6.99e-18 |
|
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: 83.02 E-value: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 320 FELEDVN--YQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtKLEVAYFDQ-HRADL-- 394
Cdd:cd03245 3 IEFRNVSfsYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV----LLDGTDIRQlDPADLrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 -------DPER---TVMDNLAEGK-----QEVMVNGRprhvLGYLQDFL-FHPKRAMTPV----KALSGGERNRLLLAKL 454
Cdd:cd03245 79 nigyvpqDVTLfygTLRDNITLGApladdERILRAAE----LAGVTDFVnKHPNGLDLQIgergRGLSGGQRQAVALARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505190249 455 FLKPSNLLILDEPTNDLDVETLELLEELIDGYQG--TVLLVSH 495
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH 197
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-232 |
9.95e-18 |
|
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: 81.92 E-value: 9.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 18 LLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVAR--------LQQDPPRNIGG-SVFDFVA 88
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKerrksigyVMQDVDYQLFTdSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 89 EGvaeqaehlkayhaishlveSDPSEKNLARMAQIMEILDhqgLWQLDsrisevllqlglngDAELSSLSGGWLRKAALG 168
Cdd:cd03226 95 LG-------------------LKELDAGNEQAETVLKDLD---LYALK--------------ERHPLSLSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 169 RALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF---DGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
320-495 |
1.00e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 81.11 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 320 FELEDVNYQVG--EKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKLEVAYFDQHRadldp 396
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDPNELG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 397 ertvmdnlaegkqevmvngrpRHVlGYL-QDFLFHPKRAMTPVkaLSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03246 76 ---------------------DHV-GYLpQDDELFSGSIAENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180
....*....|....*....|...
gi 505190249 476 LELLEELI---DGYQGTVLLVSH 495
Cdd:cd03246 132 ERALNQAIaalKAAGATRIVIAH 154
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-232 |
1.03e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 85.12 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPlDDGRVIYEqDLIVARLqqdPP--R 77
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIaGLEDP-TSGEILIG-GRDVTDL---PPkdR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 78 NIG-----------GSVFDFVAEGvaeqaehLKAYHAishlvesDPSEKN--LARMAQIMEILDHqglwqLDSRISEvll 144
Cdd:COG3839 76 NIAmvfqsyalyphMTVYENIAFP-------LKLRKV-------PKAEIDrrVREAAELLGLEDL-----LDRKPKQ--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 145 qlglngdaelssLSGGWLRKAALGRALVSSPRVLLLDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHDRSFIRNMA 220
Cdd:COG3839 134 ------------LSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLA 201
|
250
....*....|..
gi 505190249 221 TRIVDLDRGKLV 232
Cdd:COG3839 202 DRIAVMNDGRIQ 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-473 |
1.24e-17 |
|
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: 86.28 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 17 PLLDNTEIHIEDNERVCLVGRNGAGKS----TLLKILGKEIPLDDGRVIYE-QDLivarLQQDPP--RNIGGS----VFD 85
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDgQDL----LGLSERelRRIRGNriamIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 86 fvaegvaEQAEHLKAYHAIshlvesdpsEKnlarmaQIMEILD-HQGLW--QLDSRISEVLLQLGLNgDAE--LSS---- 156
Cdd:COG4172 100 -------EPMTSLNPLHTI---------GK------QIAEVLRlHRGLSgaAARARALELLERVGIP-DPErrLDAyphq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 157 LSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIeTI-----DWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVqaqilDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 232 VswpgnydlylqskeEALRVEELqnaeFDrklAQEEVWIRQGIKARRTRNEGRVRAlkalrversQRREVMGTAKMQVEE 311
Cdd:COG4172 236 V--------------EQGPTAEL----FA---APQHPYTRKLLAAEPRGDPRPVPP---------DAPPLLEARDLKVWF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 312 ATRSGkiVFeledvNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGqLKADSGRVH-CGTKLEVAYFDQ- 389
Cdd:COG4172 286 PIKRG--LF-----RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRfDGQDLDGLSRRAl 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 390 --HRAD-----------LDPERTVMDNLAEG---------KQEvmvngRPRHVLgylqdflfhpkRAMTPVK-------- 439
Cdd:COG4172 358 rpLRRRmqvvfqdpfgsLSPRMTVGQIIAEGlrvhgpglsAAE-----RRARVA-----------EALEEVGldpaarhr 421
|
490 500 510
....*....|....*....|....*....|....*...
gi 505190249 440 ---ALSGGERNRLLLAK-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG4172 422 yphEFSGGQRQRIAIARaLILEPK-LLVLDEPTSALDV 458
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-232 |
1.49e-17 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 82.38 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQdlivARLQQDPP--RNIGgsvfdFVAEGVAeQAE 96
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG----KDITNLPPekRDIS-----YVPQNYA-LFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 97 HLKAYHAISH-LVESDPSEKNLARmaQIMEILDHQGlwqldsrISEVLlqlglngDAELSSLSGGWLRKAALGRALVSSP 175
Cdd:cd03299 85 HMTVYKNIAYgLKKRKVDKKEIER--KVLEIAEMLG-------IDHLL-------NRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505190249 176 RVLLLDEPTNHLDIET----IDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03299 149 KILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
319-473 |
1.75e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 319 VFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV-HCGTKLEV-AYFDQ-----HR 391
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkLDGGDIDDpDVAEAchylgHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 392 ADLDPERTVMDNLAEGKQevMVNGRPRHVLGYLQDF----LFHpkramTPVKALSGGERNRLLLAKLFLKPSNLLILDEP 467
Cdd:PRK13539 82 NAMKPALTVAENLEFWAA--FLGGEELDIAAALEAVglapLAH-----LPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
....*.
gi 505190249 468 TNDLDV 473
Cdd:PRK13539 155 TAALDA 160
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-247 |
3.09e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.02 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLI-----VARLQQDPPR 77
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 78 NIGGSVFDfvaegVAEQAEHLKAYHAISHLVESDPSEKNLARMAQIMEILDHQGLWQldsrisEVLLQLglngDAELSSL 157
Cdd:PRK14246 90 KEVGMVFQ-----QPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWK------EVYDRL----NSPASQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 158 SGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDG--SIVFISHDRSFIRNMATRIVDLDRGKLVSWP 235
Cdd:PRK14246 155 SGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
250
....*....|..
gi 505190249 236 GNYDLYLQSKEE 247
Cdd:PRK14246 235 SSNEIFTSPKNE 246
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-232 |
3.85e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.66 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSDAPL---------LDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPlDDGRVIYeQDLIVAR 70
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLsgkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLvGLESP-SQGNVSW-RGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 71 LQQdpprniggsvfdfvaegvaeqaEHLKAYHAISHLVESD-PSEKNLARM--AQIMEILDHqgLWQLD-----SRISEV 142
Cdd:PRK10419 79 LNR----------------------AQRKAFRRDIQMVFQDsISAVNPRKTvrEIIREPLRH--LLSLDkaerlARASEM 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 143 LLQLGLngDAELSS-----LSGGWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDR 213
Cdd:PRK10419 135 LRAVDL--DDSVLDkrppqLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDL 212
|
250
....*....|....*....
gi 505190249 214 SFIRNMATRIVDLDRGKLV 232
Cdd:PRK10419 213 RLVERFCQRVMVMDNGQIV 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
321-496 |
6.97e-17 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 79.61 E-value: 6.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLE-----VAYFDQHR 391
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvTDLPpkdrdIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 392 AdLDPERTVMDNLAEG-----KQEVMVNGRPRHVLGYLQ-DFLFHPKramtpVKALSGGERNRLLLAKLFLKPSNLLILD 465
Cdd:cd03301 82 A-LYPHMTVYDNIAFGlklrkVPKDEIDERVREVAELLQiEHLLDRK-----PKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190
....*....|....*....|....*....|....*
gi 505190249 466 EPTNDLDVETLELLEELIDGYQ----GTVLLVSHD 496
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQqrlgTTTIYVTHD 190
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
34-232 |
7.82e-17 |
|
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: 79.54 E-value: 7.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 34 LVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDL---------IVARLQQDPPRNIGGSVFDFVaegvaeqaehlkAYHA 103
Cdd:cd03264 30 LLGPNGAGKTTLMRILATLTPPSSGTIrIDGQDVlkqpqklrrRIGYLPQEFGVYPNFTVREFL------------DYIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 104 ISHLVESDpseknlarmaqimeildhqglwQLDSRISEVLLQLGLNG--DAELSSLSGGWLRKAALGRALVSSPRVLLLD 181
Cdd:cd03264 98 WLKGIPSK----------------------EVKARVDEVLELVNLGDraKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505190249 182 EPTNHLDIETIDWLEGFLKEF--DGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELgeDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-473 |
1.22e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.30 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRViyeqdlivarlqqdpprNIGGS 82
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI-----------------TINNI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 VFDFVAEGVAEQAEHLKAYHAISHLVESDPSE-----KNLARMAQIMEILDHQglwQLDSRISEVLLQLGLNGDAE--LS 155
Cdd:PRK09700 68 NYNKLDHKLAAQLGIGIIYQELSVIDELTVLEnlyigRHLTKKVCGVNIIDWR---EMRVRAAMMLLRVGLKVDLDekVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 156 SLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDG---SIVFISHDRSFIRNMATRIVDLDRGKlv 232
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDRYTVMKDGS-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 233 swpgnydlYLQSKEealrVEELQNAEFDRKLAQEEvwirqgIKARRTrnegrvralkalrversqrrevmgtaKMQVEEA 312
Cdd:PRK09700 223 --------SVCSGM----VSDVSNDDIVRLMVGRE------LQNRFN--------------------------AMKENVS 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 313 TRSGKIVFELEDVNYQVGEKVlvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKLE-------- 383
Cdd:PRK09700 259 NLAHETVFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLnGKDISprspldav 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 384 ---VAYFDQHRAD--LDPERTVMDNLAEGKQevMVNGRPRHVLGylqdfLFHPK---------RAMTPVKA--------- 440
Cdd:PRK09700 337 kkgMAYITESRRDngFFPNFSIAQNMAISRS--LKDGGYKGAMG-----LFHEVdeqrtaenqRELLALKChsvnqnite 409
|
490 500 510
....*....|....*....|....*....|...
gi 505190249 441 LSGGERNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
321-496 |
1.51e-16 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 79.30 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GT--------KLEVAYFDQHR 391
Cdd:cd03299 2 KVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKditnlppeKRDISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 392 AdLDPERTVMDNLAEG--KQEVMVNGRPRHVL---GYLQ-DFLFHPKramtpVKALSGGERNRLLLAK-LFLKPSnLLIL 464
Cdd:cd03299 81 A-LFPHMTVYKNIAYGlkKRKVDKKEIERKVLeiaEMLGiDHLLNRK-----PETLSGGEQQRVAIARaLVVNPK-ILLL 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 505190249 465 DEPTNDLDVETLELLEELI----DGYQGTVLLVSHD 496
Cdd:cd03299 154 DEPFSALDVRTKEKLREELkkirKEFGVTVLHVTHD 189
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
322-500 |
1.63e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.77 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 322 LEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQhRADLDP----- 396
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ-KLYLDTtlplt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 397 -ERTVMDNLAEGKQEVMvNGRPRHVLGYLQDFlfhpkramtPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:PRK09544 86 vNRFLRLRPGTKKEDIL-PALKRVQAGHLIDA---------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*....
gi 505190249 476 LELLEELIDGYQGT----VLLVSHDRQFV 500
Cdd:PRK09544 156 QVALYDLIDQLRREldcaVLMVSHDLHLV 184
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
321-467 |
2.02e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 79.36 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVN--YQV--GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC------GTKLEVAY-FDQ 389
Cdd:COG1116 9 ELRGVSkrFPTggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGVvFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 390 HRadLDPERTVMDNLAEGkqeVMVNGRPR-----HVLGY-----LQDFL-FHPkramtpvKALSGGERNRLLLAK-LFLK 457
Cdd:COG1116 89 PA--LLPWLTVLDNVALG---LELRGVPKaerreRARELlelvgLAGFEdAYP-------HQLSGGMRQRVAIARaLAND 156
|
170
....*....|
gi 505190249 458 PSnLLILDEP 467
Cdd:COG1116 157 PE-VLLMDEP 165
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-241 |
2.07e-16 |
|
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: 78.82 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPlDDGRVIYEqDLIVARLqqdPP--RNIG 80
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIaGFETP-TSGEILLD-GKDITNL---PPhkRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 gSVFdfvaegvaeqaehlKAYHAISHLVesdpSEKNLA---RMAQIMEIldhqglwQLDSRISEVLLQLGLNGDA--ELS 155
Cdd:cd03300 76 -TVF--------------QNYALFPHLT----VFENIAfglRLKKLPKA-------EIKERVAEALDLVQLEGYAnrKPS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 156 SLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSI----VFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03300 130 QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgitfVFVTHDQEEALTMSDRIAVMNKGKI 209
|
250
....*....|
gi 505190249 232 VSWPGNYDLY 241
Cdd:cd03300 210 QQIGTPEEIY 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-233 |
2.46e-16 |
|
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: 78.11 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 28 DNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIV-ARLQQD-PP--RNIGgSVFdfvaegvaEQAE---HLKA 100
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdSRKKINlPPqqRKIG-LVF--------QQYAlfpHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 101 YHAISHLVESDPSEKNLARMAQIMEILDHQGLwqLDSRISEvllqlglngdaelssLSGGWLRKAALGRALVSSPRVLLL 180
Cdd:cd03297 93 RENLAFGLKRKRNREDRISVDELLDLLGLDHL--LNRYPAQ---------------LSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 181 DEPTNHLDIETIDWLEGFLKE----FDGSIVFISHDRSFIRNMATRIVDLDRGKLVS 233
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQikknLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-232 |
2.71e-16 |
|
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: 78.43 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 17 PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE----QDLIVARLQqdppRNIG----------GS 82
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvRDYTLASLR----RQIGlvsqdvflfnDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 VFDFVAEGV--AEQAEHLKAyhaishlvesdpseknlARMAQIMEILDH--QGlwqLDSRISEvllqlglNGdaelSSLS 158
Cdd:cd03251 92 VAENIAYGRpgATREEVEEA-----------------ARAANAHEFIMElpEG---YDTVIGE-------RG----VKLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505190249 159 GGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFISHDRSFIRNmATRIVDLDRGKLV 232
Cdd:cd03251 141 GGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAHRLSTIEN-ADRIVVLEDGKIV 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
315-472 |
2.71e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.13 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 315 SGKIVFEleDVN--YQVGEKVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtklevaYFDQHR- 391
Cdd:COG1132 337 RGEIEFE--NVSfsYPGDRPVL-KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI---------LIDGVDi 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 392 ADLDPE-----------------RTVMDNLAEGK-----QEVmvngrpRHVLG--YLQDFLfhpkRAM-----TPV---- 438
Cdd:COG1132 405 RDLTLEslrrqigvvpqdtflfsGTIRENIRYGRpdatdEEV------EEAAKaaQAHEFI----EALpdgydTVVgerg 474
|
170 180 190
....*....|....*....|....*....|....
gi 505190249 439 KALSGGERNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALD 508
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-226 |
3.18e-16 |
|
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: 81.95 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSDA-PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDLI----------VARL 71
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIaVNGVPLAdadadswrdqIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 72 QQDPprnigGSVFDFVAEGVAeqaehlkayhaishLVESDPSEknlarmAQIMEILDHQGLWQLDSRISEVL-LQLGLNG 150
Cdd:TIGR02857 402 PQHP-----FLFAGTIAENIR--------------LARPDASD------AEIREALERAGLDEFVAALPQGLdTPIGEGG 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 151 daelSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET-IDWLEGFLKEFDG-SIVFISHDRSFIRNmATRIVDL 226
Cdd:TIGR02857 457 ----AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETeAEVLEALRALAQGrTVLLVTHRLALAAL-ADRIVVL 529
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
337-496 |
3.52e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.73 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 337 GFSAQVQRGDKIALVGPNGCGKTTLLKLMLGqLKADSGRVHC-GTKLE---VAYFDQHRADL---DPERTVMD------- 402
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLnGRPLSdwsAAELARHRAYLsqqQSPPFAMPvfqylal 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 403 NLAEGKQEVMVNGRPRHVLGYLQ--DFLfhpkraMTPVKALSGGERNRLLLAKLFLK-------PSNLLILDEPTNDLDV 473
Cdd:COG4138 93 HQPAGASSEAVEQLLAQLAEALGleDKL------SRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDV 166
|
170 180
....*....|....*....|....*.
gi 505190249 474 ETLELLEELIDGY---QGTVLLVSHD 496
Cdd:COG4138 167 AQQAALDRLLRELcqqGITVVMSSHD 192
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
331-496 |
3.65e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 78.14 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 331 EKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC--------------------GTKLEVA----- 385
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaglvpwkrrkkflrrigvvfGQKTQLWwdlpv 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 386 ----YFDQHRADLDPER--TVMDNLAEgkqevMVNgrprhvlgyLQDFLFhpkramTPVKALSGGERNRLLLAKLFLKPS 459
Cdd:cd03267 113 idsfYLLAAIYDLPPARfkKRLDELSE-----LLD---------LEELLD------TPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505190249 460 NLLILDEPTNDLDVETLELLEELIDGY----QGTVLLVSHD 496
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHY 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
321-496 |
3.80e-16 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 78.10 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHcgtklevaYFDQHRADLDPER-- 398
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIL--------VDGQDITGLSEKEly 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 399 -------------------TVMDNLA----E----GKQEV---------MVNgrprhvlgyLQDFlfhpkRAMTPvKALS 442
Cdd:COG1127 79 elrrrigmlfqggalfdslTVFENVAfplrEhtdlSEAEIrelvlekleLVG---------LPGA-----ADKMP-SELS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 443 GGERNRLLLAK-LFLKPSnLLILDEPTNDLDVETLELLEELI----DGYQGTVLLVSHD 496
Cdd:COG1127 144 GGMRKRVALARaLALDPE-ILLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHD 201
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
316-500 |
4.26e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 78.54 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 316 GKIVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHcgtklevayFDQHR-ADL 394
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIL---------FDGRDiTGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 DPER-------------------TVMDNlaegkqeVMVNGRPRHVLGYLQDFLFHPK----------RAM---------- 435
Cdd:COG0411 72 PPHRiarlgiartfqnprlfpelTVLEN-------VLVAAHARLGRGLLAALLRLPRarreereareRAEellervglad 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505190249 436 ---TPVKALSGGERNRLLLAK-LFLKPSnLLILDEPT---NDLDVETLELLEELIDGYQG-TVLLVSHDRQFV 500
Cdd:COG0411 145 radEPAGNLSYGQQRRLEIARaLATEPK-LLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLV 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-232 |
4.43e-16 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 78.69 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 16 APLLDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGKEIPlDDGRVIYE-QDLIvarlQQDPprniggsvfdfvaegvae 93
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARlLLGLEKP-AQGTVSFRgQDLY----QLDR------------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 94 qaEHLKAYHAISHLVESD-PSEKNLARMAQ--IMEILDHqgLWQLD-----SRISEVLLQLGLNG---DAELSSLSGGWL 162
Cdd:TIGR02769 81 --KQRRAFRRDVQLVFQDsPSAVNPRMTVRqiIGEPLRH--LTSLDeseqkARIAELLDMVGLRSedaDKLPRQLSGGQL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505190249 163 RKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
321-473 |
4.56e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.66 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHcgtkleVAYFDQHRADldpERTV 400
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVL------VAGDDVEALS---ARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 401 MDNLAEGKQEVMVN-----------GRPRHvlgyLQDFLFHP-------KRAMT----------PVKALSGGERNRLLLA 452
Cdd:PRK09536 76 SRRVASVPQDTSLSfefdvrqvvemGRTPH----RSRFDTWTetdraavERAMErtgvaqfadrPVTSLSGGERQRVLLA 151
|
170 180
....*....|....*....|.
gi 505190249 453 KLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDI 172
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
34-233 |
4.72e-16 |
|
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: 78.32 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 34 LVGRNGAGKSTLLKILGKEIPLDDGRVIY-----------EQDLIVARLQQDPPRNIGGSVFDFVAegvaeqaehlkayh 102
Cdd:TIGR03873 32 LLGPNGSGKSTLLRLLAGALRPDAGTVDLagvdlhglsrrARARRVALVEQDSDTAVPLTVRDVVA-------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 103 aishlvesdpseknLARMAqimeildHQGLWQLDSR-----ISEVLLQLGLN--GDAELSSLSGGWLRKAALGRALVSSP 175
Cdd:TIGR03873 98 --------------LGRIP-------HRSLWAGDSPhdaavVDRALARTELShlADRDMSTLSGGERQRVHVARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505190249 176 RVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFIS-HDRSFIRNMATRIVDLDRGKLVS 233
Cdd:TIGR03873 157 KLLLLDEPTNHLDVRAQLETLALVRELaaTGVTVVAAlHDLNLAASYCDHVVVLDGGRVVA 217
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-258 |
5.92e-16 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 81.37 E-value: 5.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQdpprniggs 82
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ--------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 vfdfvaegvaEQAEHLKAYHA-ISHLVESDPSEknlarmaqimeildhqglwqLDSRISEVLLQLGLNGDA---ELSSLS 158
Cdd:PRK10636 383 ----------HQLEFLRADESpLQHLARLAPQE--------------------LEQKLRDYLGGFGFQGDKvteETRRFS 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 159 GGwlRKAALGRALV--SSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPG 236
Cdd:PRK10636 433 GG--EKARLVLALIvwQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDG 510
|
250 260
....*....|....*....|..
gi 505190249 237 NYDLYLQSKEEALRVEELQNAE 258
Cdd:PRK10636 511 DLEDYQQWLSDVQKQENQTDEA 532
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
338-496 |
5.93e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.05 E-value: 5.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 338 FSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKAdSGRVHC-GTKLE---VAYFDQHRADLDPERT------VMDNLAEG 407
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFaGQPLEawsAAELARHRAYLSQQQTppfampVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 408 KQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAKLFLK------P-SNLLILDEPTNDLDVETLELLE 480
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinPaGQLLLLDEPMNSLDVAQQAALD 173
|
170
....*....|....*....
gi 505190249 481 ELIDGY--QG-TVLLVSHD 496
Cdd:PRK03695 174 RLLSELcqQGiAVVMSSHD 192
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
321-500 |
6.01e-16 |
|
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: 77.48 E-value: 6.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTklEVAYFDQHR-------- 391
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfDGE--DITGLPPHEiarlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 392 ----ADLDPERTVMDNlaegkqeVMVNGRPRHVLGYLQDFLFHPKRAM------------------TPVKALSGGERNRL 449
Cdd:cd03219 80 tfqiPRLFPELTVLEN-------VMVAAQARTGSGLLLARARREEREAreraeellervgladladRPAGELSYGQQRRL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 450 LLAK-LFLKPSnLLILDEPT---NDLDVETLELLEELIDGYQGTVLLVSHDRQFV 500
Cdd:cd03219 153 EIARaLATDPK-LLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVV 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-212 |
7.62e-16 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 80.87 E-value: 7.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFS---DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIyeqdlivarLQQDPPRNIGGSVFDFV 87
Cdd:TIGR02868 340 LSAGypgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT---------LDGVPVSSLDQDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 88 AEGVAEQAehlkayhaisHLVESDPSEkNL------ARMAQIMEILDHQGL--WqLDSRISEVLLQLGLNGdaelSSLSG 159
Cdd:TIGR02868 411 VSVCAQDA----------HLFDTTVRE-NLrlarpdATDEELWAALERVGLadW-LRALPDGLDTVLGEGG----ARLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 160 GWLRKAALGRALVSSPRVLLLDEPTNHLDIETID-WLEGFLKEFDG-SIVFISHD 212
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADeLLEDLLAALSGrTVVLITHH 529
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
19-232 |
9.36e-16 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 77.22 E-value: 9.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE----QDLIVARLQQdpPRNIGGSVF-DFvaegvae 93
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdiNKLKGKALRQ--LRRQIGMIFqQF------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 94 qaehlkayhaisHLVESDPSEKN-----LARMAQImeildhQGLWQLDSRI-----SEVLLQLGLNGDAEL--SSLSGGW 161
Cdd:cd03256 88 ------------NLIERLSVLENvlsgrLGRRSTW------RSLFGLFPKEekqraLAALERVGLLDKAYQraDQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 162 LRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF---DGSIVFIS-HDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDLAREYADRIVGLKDGRIV 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-232 |
1.08e-15 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 78.56 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILG--KEIPLDDGRVIYE-QDLivARLQQDPPRNIGGS----VFdfvaeg 90
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARaILGllPPPGITSGEILFDgEDL--LKLSEKELRKIRGReiqmIF------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 91 vaeQAehlkayhAISHLvesDPseknlaRM---AQIMEILDHQGLW---QLDSRISEVLLQLGLNGDAE-LSS----LSG 159
Cdd:COG0444 93 ---QD-------PMTSL---NP------VMtvgDQIAEPLRIHGGLskaEARERAIELLERVGLPDPERrLDRypheLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 160 GWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVtiqaQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
321-496 |
1.23e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 76.25 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC----------GTKLEVAYFDQH 390
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvreprEVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 391 RAdLDPERTVMDNLA-EGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:cd03265 82 LS-VDDELTGWENLYiHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190
....*....|....*....|....*....|.
gi 505190249 470 DLDVETLELLEELIDGYQG----TVLLVSHD 496
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEefgmTILLTTHY 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-496 |
1.78e-15 |
|
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: 79.56 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 319 VFELED--VNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKAD---SGRVHCGTKLEVAYFDQHRAD 393
Cdd:COG1123 4 LLEVRDlsVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 394 L------DPER-----TVMDNLAEGKQEVMVNG--RPRHVLGYLQDFLFhPKRAMTPVKALSGGERNRLLLA-KLFLKPS 459
Cdd:COG1123 84 RigmvfqDPMTqlnpvTVGDQIAEALENLGLSRaeARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAmALALDPD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505190249 460 nLLILDEPTNDLDVETLELLEELIDGYQG----TVLLVSHD 496
Cdd:COG1123 163 -LLIADEPTTALDVTTQAEILDLLRELQRergtTVLLITHD 202
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-226 |
1.87e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.96 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQdpprniggsvfdfvaegv 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 92 aeqaehlkayhaISHLVESDPseknlARMAQIMEI--LDHQGLWQLDSR-----ISEVLLQLGLNG--DAELSSLSGGWL 162
Cdd:NF040873 63 ------------RSEVPDSLP-----LTVRDLVAMgrWARRGLWRRLTRddraaVDDALERVGLADlaGRQLGELSGGQR 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 163 RKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDG---SIVFISHDRSFIRNmATRIVDL 226
Cdd:NF040873 126 QRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELVRR-ADPCVLL 191
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
317-472 |
2.51e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 75.47 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 317 KIVFELEDVN--YQVGE---KVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTKL------EV 384
Cdd:COG1136 2 SPLLELRNLTksYGTGEgevTAL-RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLiDGQDIsslserEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 385 AYFdqhRAD----------LDPERTVMDNLA-----EGKQEVMVNGRPRHVLGYLQdfLFHpkRAMTPVKALSGGERNRL 449
Cdd:COG1136 81 ARL---RRRhigfvfqffnLLPELTALENVAlplllAGVSRKERRERARELLERVG--LGD--RLDHRPSQLSGGQQQRV 153
|
170 180
....*....|....*....|....
gi 505190249 450 LLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:COG1136 154 AIARaLVNRPK-LILADEPTGNLD 176
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
321-495 |
2.67e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 75.01 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKlEVAYFDQHRADLDPE--- 397
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-PLDIAARNRIGYLPEerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 398 ----RTVMDNL---AE----GKQEVMvngrpRHVLGYLQDFLFHPKRAmTPVKALSGGERNRLLLAKLFLKPSNLLILDE 466
Cdd:cd03269 81 lypkMKVIDQLvylAQlkglKKEEAR-----RRIDEWLERLELSEYAN-KRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190
....*....|....*....|....*....|..
gi 505190249 467 PTNDLDVETLELLEELIDGYQG---TVLLVSH 495
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARagkTVILSTH 186
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
321-473 |
2.99e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.84 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTKLE---VAYFDQ-----HR 391
Cdd:PRK13538 3 EARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwQGEPIRrqrDEYHQDllylgHQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 392 ADLDPERTVMDNLA-------EGKQEVMVNGRPRHVLGylqdflfhpKRAMTPVKALSGGERNRLLLAKLFLKPSNLLIL 464
Cdd:PRK13538 83 PGIKTELTALENLRfyqrlhgPGDDEALWEALAQVGLA---------GFEDVPVRQLSAGQQRRVALARLWLTRAPLWIL 153
|
....*....
gi 505190249 465 DEPTNDLDV 473
Cdd:PRK13538 154 DEPFTAIDK 162
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
15-232 |
3.63e-15 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 74.78 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 15 DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEqdlivarlqqdpPRNIGG-SVFDFVAEGVAE 93
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD------------GRDITGlPPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 94 QAEHLKAYHAIShlVesdpsEKNLaRMAqIMEILDHQGLWQLDS------RISEVLLQLGlngdaelSSLSGGWLRKAAL 167
Cdd:cd03224 80 VPEGRRIFPELT--V-----EENL-LLG-AYARRRAKRKARLERvyelfpRLKERRKQLA-------GTLSGGEQQMLAI 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505190249 168 GRALVSSPRVLLLDEPTNHL------DI-ETIDWlegfLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLapkiveEIfEAIRE----LRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
330-500 |
4.17e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.12 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 330 GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTK----LEVAyfdqhrADLDPERTVMDNla 405
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsalLELG------AGFHPELTGREN-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 406 egkqeVMVNGRprhVLGY-----------------LQDFLfhpkraMTPVKALSGGERNRLLLA-KLFLKPsNLLILDEP 467
Cdd:COG1134 109 -----IYLNGR---LLGLsrkeidekfdeivefaeLGDFI------DQPVKTYSSGMRARLAFAvATAVDP-DILLVDEV 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 505190249 468 TNDLDVETLELLEELIDGYQ---GTVLLVSHDRQFV 500
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELResgRTVIFVSHSMGAV 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
321-502 |
4.26e-15 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 74.75 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVL-VRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKL------EVAYFDQHRA 392
Cdd:cd03292 2 EFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 393 ------DLDPERTVMDNLAEGKQEVMVNGR--PRHVLGYLQDF-LFHPKRAMTpvKALSGGERNRLLLAKLFLKPSNLLI 463
Cdd:cd03292 82 vvfqdfRLLPDRNVYENVAFALEVTGVPPReiRKRVPAALELVgLSHKHRALP--AELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505190249 464 LDEPTNDLDVETLELLEELIDGYQ---GTVLLVSHDRQFVDN 502
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDT 201
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
320-498 |
4.27e-15 |
|
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: 74.91 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 320 FELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGtklEVAYFDQHRADLDPER- 398
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEG---EVLLDGKDIYDLDVDVl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 399 ------------------TVMDNLAEG------KQEVMVNGRPRHVL------GYLQDFLfhpkramtPVKALSGGERNR 448
Cdd:cd03260 78 elrrrvgmvfqkpnpfpgSIYDNVAYGlrlhgiKLKEELDERVEEALrkaalwDEVKDRL--------HALGLSGGQQQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505190249 449 LLLAK-LFLKPSNLLiLDEPTNDLDVETLELLEELIDGYQG--TVLLVSHDRQ 498
Cdd:cd03260 150 LCLARaLANEPEVLL-LDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQ 201
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-232 |
4.91e-15 |
|
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: 74.71 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEqDLIVARLQQDPPRNIGgsvFDFVAEGVAEQ--AE 96
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD-GFDVVKEPAEARRRLG---FVSDSTGLYDRltAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 97 HLKAYHAISHLVESDPSEKNLARMAQIMEILDHqglwqLDSRISEvllqlglngdaelssLSGGWLRKAALGRALVSSPR 176
Cdd:cd03266 97 ENLEYFAGLYGLKGDELTARLEELADRLGMEEL-----LDRRVGG---------------FSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 177 VLLLDEPTNHLDIETIDWLEGFLKEFDG---SIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
317-505 |
5.45e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.75 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 317 KIVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtklevaYFDQHR-ADLD 395
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL---------LFEGEDiSTLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 396 PER-----------------TVMDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRL-LLAKLFLK 457
Cdd:PRK10247 76 PEIyrqqvsycaqtptlfgdTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRIsLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 458 PSNLLiLDEPTNDLDVETLELLEELIDGY----QGTVLLVSHDR---QFVDNSVT 505
Cdd:PRK10247 156 PKVLL-LDEITSALDESNKHNVNEIIHRYvreqNIAVLWVTHDKdeiNHADKVIT 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-500 |
6.21e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.82 E-value: 6.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 20 DNTEIHIEDNERVCLVGRNGAGKS-TLLKILGKeipLDDGRVIYEQDLIV----ARLQQDPP--RNIGGsvfDFVAEGVA 92
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRL---LPSPPVVYPSGDIRfhgeSLLHASEQtlRGVRG---NKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 93 EQAEHLKAYHAIshlvesdpsEKNLARM-------------AQIMEILDHQGLWQLDSRISEVLLQLglngdaelsslSG 159
Cdd:PRK15134 100 EPMVSLNPLHTL---------EKQLYEVlslhrgmrreaarGEILNCLDRVGIRQAAKRLTDYPHQL-----------SG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 160 GWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSwp 235
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVsvqaQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 236 GNYDLYLQSKEEALRVEELQNAEfdrklaqeevwirqgikarrtrNEGRVRALKA-----LRVERsqrrevmgtakMQVE 310
Cdd:PRK15134 238 QNRAATLFSAPTHPYTQKLLNSE----------------------PSGDPVPLPEpasplLDVEQ-----------LQVA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 311 EATRSGKIvfeledvNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTT----LLKLML--GQLKADSGRVHCGT---- 380
Cdd:PRK15134 285 FPIRKGIL-------KRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIWFDGQPLHNLNrrql 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 381 -----KLEVAYFDQHRAdLDPERTVMDNLAEGKQ----EVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLL 451
Cdd:PRK15134 358 lpvrhRIQVVFQDPNSS-LNPRLNVLQIIEEGLRvhqpTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAI 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 505190249 452 AK-LFLKPSnLLILDEPTNDLDVETLELLEELIDGYQGT----VLLVSHDRQFV 500
Cdd:PRK15134 437 ARaLILKPS-LIILDEPTSSLDKTVQAQILALLKSLQQKhqlaYLFISHDLHVV 489
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-232 |
6.51e-15 |
|
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: 74.44 E-value: 6.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 15 DAPL-LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE-QDLIVArlqqDPP---RNIGgsvfdfvae 89
Cdd:cd03252 13 DGPViLDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDgHDLALA----DPAwlrRQVG--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 90 gVAEQAEHLKAYHAISHLVESDPSeknlARMAQIMEILDHQGLWQLDSRISEVLLQ-LGLNGdaelSSLSGGWLRKAALG 168
Cdd:cd03252 80 -VVLQENVLFNRSIRDNIALADPG----MSMERVIEAAKLAGAHDFISELPEGYDTiVGEQG----AGLSGGQRQRIAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505190249 169 RALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF-DG-SIVFISHDRSFIRNmATRIVDLDRGKLV 232
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDIcAGrTVIIIAHRLSTVKN-ADRIIVMEKGRIV 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-232 |
7.87e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 77.51 E-value: 7.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFS---DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDliVARLQQDP-PRNIG----- 80
Cdd:COG1132 345 VSFSypgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlIDGVD--IRDLTLESlRRQIGvvpqd 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 -----GSVFDFVAEGV--AEQAEHLKAyhaishlvesdpseknlARMAQIMEILDH--QGLwqlDSRISEvllqlglNGd 151
Cdd:COG1132 423 tflfsGTIRENIRYGRpdATDEEVEEA-----------------AKAAQAHEFIEAlpDGY---DTVVGE-------RG- 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 152 aelSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET---IdwLEGFLKEFDGSIVF-ISHDRSFIRNmATRIVDLD 227
Cdd:COG1132 475 ---VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETealI--QEALERLMKGRTTIvIAHRLSTIRN-ADRILVLD 548
|
....*
gi 505190249 228 RGKLV 232
Cdd:COG1132 549 DGRIV 553
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-231 |
8.32e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.22 E-value: 8.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGkeipLDDgrvIYEQDLIVA--RLQQDPP- 76
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRmIAG----LED---ITSGDLFIGekRMNDVPPa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 77 -RNIgGSVFdfvaegvaeqaehlKAYHAISHLVESDpsekNLA---RMAQIMEIldhqglwQLDSRISEV--LLQLGLNG 150
Cdd:PRK11000 74 eRGV-GMVF--------------QSYALYPHLSVAE----NMSfglKLAGAKKE-------EINQRVNQVaeVLQLAHLL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 151 DAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLD--------IEtIDWLEgflKEFDGSIVFISHDRSFIRNMATR 222
Cdd:PRK11000 128 DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmrIE-ISRLH---KRLGRTMIYVTHDQVEAMTLADK 203
|
....*....
gi 505190249 223 IVDLDRGKL 231
Cdd:PRK11000 204 IVVLDAGRV 212
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
11-239 |
8.50e-15 |
|
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: 77.86 E-value: 8.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFS---DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGK-------EIPLDdGRVIYEQDLIVAR-----LQQDP 75
Cdd:TIGR01193 479 VSYSygyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGffqarsgEILLN-GFSLKDIDRHTLRqfinyLPQEP 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 76 pRNIGGSVFDFVAEGVAEQAEHLKAYHAIShLVESDPSEKNLArmaqimeildhQGLwqlDSRISEvllqlglngdaELS 155
Cdd:TIGR01193 558 -YIFSGSILENLLLGAKENVSQDEIWAACE-IAEIKDDIENMP-----------LGY---QTELSE-----------EGS 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 156 SLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET---IdwLEGFLKEFDGSIVFISHdRSFIRNMATRIVDLDRGKLV 232
Cdd:TIGR01193 611 SISGGQKQRIALARALLTDSKVLILDESTSNLDTITekkI--VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKII 687
|
....*..
gi 505190249 233 SwPGNYD 239
Cdd:TIGR01193 688 E-QGSHD 693
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-232 |
9.17e-15 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 77.45 E-value: 9.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 15 DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRNI---GGSVF---DFVA 88
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQValvSQDVVlfnDTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 89 EGVAeqaehlkaYHAISHLVESDPSEknLARMAQIMEILDhqglwQLDSRISEvllQLGLNGdaelSSLSGGWLRKAALG 168
Cdd:TIGR02203 424 NNIA--------YGRTEQADRAEIER--ALAAAYAQDFVD-----KLPLGLDT---PIGENG----VLLSGGQRQRLAIA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 169 RALVSSPRVLLLDEPTNHLDIET----IDWLEGFLKEFDGSIvfISHDRSFIRNmATRIVDLDRGKLV 232
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESerlvQAALERLMQGRTTLV--IAHRLSTIEK-ADRIVVMDDGRIV 546
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-232 |
9.99e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 73.91 E-value: 9.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 13 FSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRViyeqdlivarlqqdpprniggSVFDFVAegVA 92
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV---------------------RVAGLVP--WK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 93 EQAEHLKAYHAI----SHLVESDPSEKNLARMAQIMEILDHQGLWQLDsRISEvLLQLGLNGDAELSSLSGGWLRKAALG 168
Cdd:cd03267 88 RRKKFLRRIGVVfgqkTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLD-ELSE-LLDLEELLDTPVRQLSLGQRMRAEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 169 RALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF----DGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
26-232 |
1.02e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 74.28 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 26 IEDNERVCLVGRNGAGKSTLLKILG-KEIPlDDGRViyeqdlivarlqqdpprNIGGSVFDFVAEGVAEQAEHLK----- 99
Cdd:PRK11124 25 CPQGETLVLLGPSGAGKSSLLRVLNlLEMP-RSGTL-----------------NIAGNHFDFSKTPSDKAIRELRrnvgm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 100 ---AYHAISH------LVESDPSEKNLAR---MAQIMEILDHqglwqldsrisevlLQLGLNGDAELSSLSGGWLRKAAL 167
Cdd:PRK11124 87 vfqQYNLWPHltvqqnLIEAPCRVLGLSKdqaLARAEKLLER--------------LRLKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 168 GRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGS-I--VFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgItqVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
318-472 |
1.51e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.04 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 318 IVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHcgtklevaYFDQHRADLDPE 397
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR--------LNGRPLADWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 398 -----RTVM--------DNLAEgkqEVMVNGRPRHVLGYLQDFLfHPKRAMTPV----------KALSGGERNRLLLAKL 454
Cdd:PRK13548 73 elarrRAVLpqhsslsfPFTVE---EVVAMGRAPHGLSRAEDDA-LVAAALAQVdlahlagrdyPQLSGGEQQRVQLARV 148
|
170 180
....*....|....*....|....
gi 505190249 455 FL------KPSNLLILDEPTNDLD 472
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALD 172
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-232 |
1.80e-14 |
|
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: 72.95 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIyeqdlivarlqqdpprnIGGSVFDFVAEGVAEQAEhL 98
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT-----------------VRGRVSSLLGLGGGFNPE-L 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 99 KAyhaishlvesdpsEKNLARMAQIMEILDHqglwQLDSRISEVL--LQLGLNGDAELSSLSGGWLRKAALGRALVSSPR 176
Cdd:cd03220 100 TG-------------RENIYLNGRLLGLSRK----EIDEKIDEIIefSELGDFIDLPVKTYSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 177 VLLLDEPTNHLDIETIDWLEGFLKEF---DGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRRLRELlkqGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-232 |
1.88e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 75.11 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPlDDGRVIY---------EQDLIVARlqqdppRNIGgSVF-DF- 86
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInLLERP-TSGSVLVdgvdltalsERELRAAR------RKIG-MIFqHFn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 87 ------VAEGVA---EQAEHLKAyhaishlvesdpseknlarmaqimEIldhqglwqlDSRISEvLLQL-GLNG--DAEL 154
Cdd:COG1135 93 llssrtVAENVAlplEIAGVPKA------------------------EI---------RKRVAE-LLELvGLSDkaDAYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 155 SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLK----EFDGSIVFISHDRSFIRNMATRIVDLDRGK 230
Cdd:COG1135 139 SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKdinrELGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
..
gi 505190249 231 LV 232
Cdd:COG1135 219 IV 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
321-472 |
1.92e-14 |
|
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: 72.61 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGdKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtklevaYFDqhraDLDPERtv 400
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI---------RID----GQDVLK-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 401 mdnlaeGKQEVmvngrpRHVLGYL-QDFLFHPK------------------------------------RAMTPVKALSG 443
Cdd:cd03264 66 ------QPQKL------RRRIGYLpQEFGVYPNftvrefldyiawlkgipskevkarvdevlelvnlgdRAKKKIGSLSG 133
|
170 180
....*....|....*....|....*....
gi 505190249 444 GERNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03264 134 GMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-249 |
2.13e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 76.31 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGKEIPlDDGRVIyeqdlivarlqqdpprnIGGSVfdfvaeg 90
Cdd:PRK11819 333 SFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKmITGQEQP-DSGTIK-----------------IGETV------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 91 vaeqaehlkayhaisHLVESDPSEKNLArmaqimeilDHQGLWQLdsrISEVLLQLGLnGDAELSS-------------- 156
Cdd:PRK11819 388 ---------------KLAYVDQSRDALD---------PNKTVWEE---ISGGLDIIKV-GNREIPSrayvgrfnfkggdq 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 157 ------LSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGK 230
Cdd:PRK11819 440 qkkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDS 519
|
250 260
....*....|....*....|
gi 505190249 231 LVSW-PGNYDLYLQSKEEAL 249
Cdd:PRK11819 520 QVEWfEGNFQEYEEDKKRRL 539
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
17-232 |
2.45e-14 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 73.10 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 17 PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV------IYEQDLIVARlqqdppRNIGGsvfdfvaeg 90
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedIREQDPVELR------RKIGY--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 91 VAEQA---EHLKAyhaishlvesdpsEKNLARMAQIMEILDHQglwqLDSRISEVLLQLGLnGDAEL-----SSLSGGWL 162
Cdd:cd03295 80 VIQQIglfPHMTV-------------EENIALVPKLLKWPKEK----IRERADELLALVGL-DPAEFadrypHELSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505190249 163 RKAALGRALVSSPRVLLLDEPTNHLDIETIDWL-EGFLK---EFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03295 142 QRVGVARALAADPPLLLMDEPFGALDPITRDQLqEEFKRlqqELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
341-495 |
2.70e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.19 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 341 QVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTK--------LEVAYFDqHRADLDPERTVMDNLAegkqevM 412
Cdd:PRK13543 33 HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsRFMAYLG-HLPGLKADLSTLENLH------F 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 413 VNG----RPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELIDGY-- 486
Cdd:PRK13543 106 LCGlhgrRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHlr 185
|
170
....*....|
gi 505190249 487 -QGTVLLVSH 495
Cdd:PRK13543 186 gGGAALVTTH 195
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-250 |
3.02e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.86 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILG------------KEIPLDDGRVIYEQDLIV 68
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpeagtirvGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 69 ARLQQDPprnigGSVFdfvaegvaeQAEHLKAYH-AISHLVESDPSEKNLARMAQImeildhqglwqldSRISEVLLQLG 147
Cdd:PRK11264 81 RQLRQHV-----GFVF---------QNFNLFPHRtVLENIIEGPVIVKGEPKEEAT-------------ARARELLAKVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 148 LNG--DAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIE-------TIDWlegfLKEFDGSIVFISHDRSFIRN 218
Cdd:PRK11264 134 LAGkeTSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPElvgevlnTIRQ----LAQEKRTMVIVTHEMSFARD 209
|
250 260 270
....*....|....*....|....*....|..
gi 505190249 219 MATRIVDLDRGKLVSWPGNYDLYLQSKEEALR 250
Cdd:PRK11264 210 VADRAIFMDQGRIVEQGPAKALFADPQQPRTR 241
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
321-472 |
3.06e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 74.34 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGtklevayfDQHRADLDPER-- 398
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIG--------GRDVTDLPPKDrn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 399 --------------TVMDNLAEG-------KQEvmVNGRPRHVLGYLQ--DFLfhpKRamtPVKALSGGERNRLLLA--- 452
Cdd:COG3839 77 iamvfqsyalyphmTVYENIAFPlklrkvpKAE--IDRRVREAAELLGleDLL---DR---KPKQLSGGQRQRVALGral 148
|
170 180
....*....|....*....|....
gi 505190249 453 ----KLFLkpsnlliLDEPTNDLD 472
Cdd:COG3839 149 vrepKVFL-------LDEPLSNLD 165
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-225 |
4.23e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.49 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRNIg 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 GSV-------FDFVAEGVAEQAEHlkayhaiSHLVESDPSEKnlARMAQIMEILDHQGLWQLdsrisevllqlglnGDAE 153
Cdd:PRK09536 80 ASVpqdtslsFEFDVRQVVEMGRT-------PHRSRFDTWTE--TDRAAVERAMERTGVAQF--------------ADRP 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 154 LSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDI-ETIDWLEGF--LKEFDGSIVFISHDrsfiRNMATRIVD 225
Cdd:PRK09536 137 VTSLSGGERQRVLLARALAQATPVLLLDEPTASLDInHQVRTLELVrrLVDDGKTAVAAIHD----LDLAARYCD 207
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
327-496 |
4.38e-14 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 70.91 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 327 YQVGEKVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKlEVAYfdqHRADL------------ 394
Cdd:TIGR01166 1 YPGGPEVL-KGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGE-PLDY---SRKGLlerrqrvglvfq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 DPER-----TVMDNLA-----EGKQEVMVNGRPRHVLGYLqDFLFHPKRamtPVKALSGGERNRLLLA-KLFLKPsNLLI 463
Cdd:TIGR01166 76 DPDDqlfaaDVDQDVAfgplnLGLSEAEVERRVREALTAV-GASGLRER---PTHCLSGGEKKRVAIAgAVAMRP-DVLL 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 505190249 464 LDEPTNDLDVETLELLEELIDGY--QGTVLLVS-HD 496
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRLraEGMTVVIStHD 186
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
321-468 |
5.41e-14 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 71.70 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGT-----------KLEVAYFD 388
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfDGRditglppheraRAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 389 QHRaDLDPERTVMDNL---AEGKQEVMVNGRPRHVLGylqdfLFhPK---RAMTPVKALSGGERNRLLLAK-LFLKPSnL 461
Cdd:cd03224 82 EGR-RIFPELTVEENLllgAYARRRAKRKARLERVYE-----LF-PRlkeRRKQLAGTLSGGEQQMLAIARaLMSRPK-L 153
|
....*..
gi 505190249 462 LILDEPT 468
Cdd:cd03224 154 LLLDEPS 160
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
304-472 |
5.54e-14 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 75.14 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 304 TAKMQVEEATrsGKIVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKL 382
Cdd:TIGR02203 319 TGTRAIERAR--GDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdGHDL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 383 E----------VAYFDQHRADLDPerTVMDNLAEGKQEVMVNGRPRHVL--GYLQDFLFH-PKRAMTPVKA----LSGGE 445
Cdd:TIGR02203 397 AdytlaslrrqVALVSQDVVLFND--TIANNIAYGRTEQADRAEIERALaaAYAQDFVDKlPLGLDTPIGEngvlLSGGQ 474
|
170 180
....*....|....*....|....*..
gi 505190249 446 RNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALD 501
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
329-500 |
7.30e-14 |
|
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: 71.02 E-value: 7.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 329 VGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV--HCGTK--LEVAYFdqhradLDPERTVMDNl 404
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtvRGRVSslLGLGGG------FNPELTGREN- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 405 aegkqeVMVNGRprhVLGYLQDFLfhpkRAM---------------TPVKALSGGERNRLLLA-KLFLKPsNLLILDEPT 468
Cdd:cd03220 105 ------IYLNGR---LLGLSRKEI----DEKideiiefselgdfidLPVKTYSSGMKARLAFAiATALEP-DILLIDEVL 170
|
170 180 190
....*....|....*....|....*....|....*
gi 505190249 469 NDLDVETLELLEELIDGYQ---GTVLLVSHDRQFV 500
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLkqgKTVILVSHDPSSI 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
317-472 |
7.50e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 70.27 E-value: 7.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 317 KIVFELEDVNYQV------GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLK--ADSGrvhcgtklevayfd 388
Cdd:cd03213 1 GVTLSFRNLTVTVksspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 389 qhradldpertvmdnlaegkqEVMVNGRPRH------VLGY-LQDFLFHPKraMTPVKAL---------SGGERNRLLLA 452
Cdd:cd03213 67 ---------------------EVLINGRPLDkrsfrkIIGYvPQDDILHPT--LTVRETLmfaaklrglSGGERKRVSIA 123
|
170 180
....*....|....*....|.
gi 505190249 453 -KLFLKPSnLLILDEPTNDLD 472
Cdd:cd03213 124 lELVSNPS-LLFLDEPTSGLD 143
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
337-518 |
7.50e-14 |
|
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: 71.67 E-value: 7.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 337 GFSAQVQRGD-----KIALVGPNGCGKTTLLKLMLGQLKADSGRVhcGTKLE-VAYFDQHrADLDPERTVMDNLAEgkqe 410
Cdd:cd03237 12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--EIELDtVSYKPQY-IKADYEGTVRDLLSS---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 411 vmvngrprhvlgYLQDFLFHPK---RAMTP----------VKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLE 477
Cdd:cd03237 85 ------------ITKDFYTHPYfktEIAKPlqieqildreVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505190249 478 LLEELIDGY----QGTVLLVSHDRQFVDNSVTECWIFEG----NGVINA 518
Cdd:cd03237 153 MASKVIRRFaennEKTAFVVEHDIIMIDYLADRLIVFEGepsvNGVANP 201
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-233 |
7.63e-14 |
|
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: 71.31 E-value: 7.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 2 SLISMSGAWLSFSDA--PL--LDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPlDDGRV-IYEQDLivARLQQDP 75
Cdd:COG4181 7 PIIELRGLTKTVGTGagELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLaGLDRP-TSGTVrLAGQDL--FALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 76 -----PRNIGgSVFdfvaegvaeQAEHLkayhaISHL--VE--SDPSEknLARMAQIMEildhqglwqldsRISEVLLQL 146
Cdd:COG4181 84 rarlrARHVG-FVF---------QSFQL-----LPTLtaLEnvMLPLE--LAGRRDARA------------RARALLERV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 147 GLNG--DAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET----IDWLEGFLKEFDGSIVFISHDRSFIRnMA 220
Cdd:COG4181 135 GLGHrlDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLVTHDPALAA-RC 213
|
250
....*....|...
gi 505190249 221 TRIVDLDRGKLVS 233
Cdd:COG4181 214 DRVLRLRAGRLVE 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-473 |
9.81e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.91 E-value: 9.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 23 EIHiednervCLVGRNGAGKSTLLKIL-GKEIPlDDGRVIYEqdlivarlqqDPPRNIGGSVfdfvaegvaeqaehlkay 101
Cdd:COG3845 32 EIH-------ALLGENGAGKSTLMKILyGLYQP-DSGEILID----------GKPVRIRSPR------------------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 102 HAISH----------LVES-----------DPSEKNLARMAQIMEildhqglwqldsRISEVLLQLGL--NGDAELSSLS 158
Cdd:COG3845 76 DAIALgigmvhqhfmLVPNltvaenivlglEPTKGGRLDRKAARA------------RIRELSERYGLdvDPDAKVEDLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 159 GGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DG-SIVFISHDRSFIRNMATRIVDLDRGKLVswp 235
Cdd:COG3845 144 VGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITHKLREVMAIADRVTVLRRGKVV--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 236 gnydlylqskeEALRVEELQNAEfdrkLAQ----EEVwirqgikarrtrnegrvralkALRVERsqrrevmgtakmqveE 311
Cdd:COG3845 221 -----------GTVDTAETSEEE----LAElmvgREV---------------------LLRVEK---------------A 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 312 ATRSGKIVFELEDVNYQVGEKVL-VRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTKLE------ 383
Cdd:COG3845 250 PAEPGEVVLEVENLSVRDDRGVPaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRlDGEDITglspre 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 384 -----VAYF--DQHRADLDPERTVMDNLAEGKQE-------VMVNGRP--RHVLGYLQDFLFHPKRAMTPVKALSGGERN 447
Cdd:COG3845 330 rrrlgVAYIpeDRLGRGLVPDMSVAENLILGRYRrppfsrgGFLDRKAirAFAEELIEEFDVRTPGPDTPARSLSGGNQQ 409
|
490 500
....*....|....*....|....*.
gi 505190249 448 RLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDV 435
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-495 |
1.14e-13 |
|
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: 68.99 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 320 FELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGrvhcgtklevayfdqhradldpert 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 400 vmdnlaegkqEVMVNGRPRHVLGylqdflfhPKRAM----TPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03216 56 ----------EILVDGKEVSFAS--------PRDARragiAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180
....*....|....*....|...
gi 505190249 476 LELLEELIDGY--QG-TVLLVSH 495
Cdd:cd03216 118 VERLFKVIRRLraQGvAVIFISH 140
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
34-232 |
1.31e-13 |
|
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: 70.48 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 34 LVGRNGAGKSTLLKILGKEIPLDDGR-VIYEQDliVARLQQDPPRNIGGSVFDFVAEGVAEQAEHLKAYHAISHLvesdp 112
Cdd:cd03265 31 LLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHD--VVREPREVRRRIGIVFQDLSVDDELTGWENLYIHARLYGV----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 113 seKNLARMAQIMEILDHQGLWQLDSRIsevllqlglngdaeLSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETI 192
Cdd:cd03265 104 --PGAERRERIDELLDFVGLLEAADRL--------------VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505190249 193 D--W--LEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03265 168 AhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
320-495 |
1.34e-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: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 320 FELEDVNYQVGE-KVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQhradldper 398
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQ--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 399 tvmdnlaegkqevmvngRPRHVLGYLQDFLFHPKRamtpvKALSGGERNRLLLAKLFL-KPSnLLILDEPTNDLDVETLE 477
Cdd:cd03223 72 -----------------RPYLPLGTLREQLIYPWD-----DVLSGGEQQRLAFARLLLhKPK-FVFLDEATSALDEESED 128
|
170
....*....|....*...
gi 505190249 478 LLEELIDGYQGTVLLVSH 495
Cdd:cd03223 129 RLYQLLKELGITVISVGH 146
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-248 |
1.47e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSlISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILG-KEIPlDDGRViyeqdlivarlqqdpprNI 79
Cdd:COG4161 1 MS-IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNlLETP-DSGQL-----------------NI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 80 GGSVFDFVAEGVAEQAEHLK--------AYHAISHLVESDpsekNLarMAQIMEILDhQGLWQLDSRISEVLLQLGLNGD 151
Cdd:COG4161 62 AGHQFDFSQKPSEKAIRLLRqkvgmvfqQYNLWPHLTVME----NL--IEAPCKVLG-LSKEQAREKAMKLLARLRLTDK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 152 AEL--SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGS-I--VFISHDRSFIRNMATRIVDL 226
Cdd:COG4161 135 ADRfpLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgItqVIVTHEVEFARKVASQVVYM 214
|
250 260
....*....|....*....|..
gi 505190249 227 DRGKLVSWpGNYDLYLQSKEEA 248
Cdd:COG4161 215 EKGRIIEQ-GDASHFTQPQTEA 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
322-496 |
1.77e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.86 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 322 LEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQHR-----ADLDP 396
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRlmfqdARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 397 ERTVMDNLAEGKQEvmvNGRPR-----HVLGyLQDflfhpkRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:PRK11247 95 WKKVIDNVGLGLKG---QWRDAalqalAAVG-LAD------RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180
....*....|....*....|....*....
gi 505190249 472 DVETLELLEELIDG----YQGTVLLVSHD 496
Cdd:PRK11247 165 DALTRIEMQDLIESlwqqHGFTVLLVTHD 193
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
321-472 |
2.05e-13 |
|
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: 70.06 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTK---------LEVAYFDQHR 391
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqeRNVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 392 AdLDPERTVMDNLAEGKQEVMVNGRP---------RHVLGYLQ-DFLF--HPKRamtpvkaLSGGERNRLLLAKLFLKPS 459
Cdd:cd03296 84 A-LFRHMTVFDNVAFGLRVKPRSERPpeaeirakvHELLKLVQlDWLAdrYPAQ-------LSGGQRQRVALARALAVEP 155
|
170
....*....|...
gi 505190249 460 NLLILDEPTNDLD 472
Cdd:cd03296 156 KVLLLDEPFGALD 168
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-189 |
2.65e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 70.14 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE---------QDLivAR----LQQDPPR 77
Cdd:COG4559 9 VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrplaawspWEL--ARrravLPQHSSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 78 NiggsvFDFVAEGVAeqaehlkayhAISHLVESDPSEKNLARMAQIMEILDHQGLWQLDSRisevllqlglngdaelsSL 157
Cdd:COG4559 87 A-----FPFTVEEVV----------ALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQ-----------------TL 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 505190249 158 SGGWLRKAALGRALV-------SSPRVLLLDEPTNHLDI 189
Cdd:COG4559 135 SGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDL 173
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-241 |
2.80e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 72.97 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 2 SLISMSGAWLSFSDAPLL-DNTEIHIEDNERVCLVGRNGAGKSTLLKilgkeiplddgrviyeqdLIVARLQQdpprnIG 80
Cdd:PLN03073 507 PIISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILK------------------LISGELQP-----SS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 GSVFDFVAEGVAEQAEHlkayhaisHLVESDPSEKNLARMAQIMEILDHQglwqldsRISEVLLQLGLNGDAELSS---L 157
Cdd:PLN03073 564 GTVFRSAKVRMAVFSQH--------HVDGLDLSSNPLLYMMRCFPGVPEQ-------KLRAHLGSFGVTGNLALQPmytL 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 158 SGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPGN 237
Cdd:PLN03073 629 SGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGT 708
|
....
gi 505190249 238 YDLY 241
Cdd:PLN03073 709 FHDY 712
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
337-496 |
2.81e-13 |
|
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: 69.25 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 337 GFSAQVQ---RGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG---------------TKLEVAYFDQHRAdLDPER 398
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrkkinlppQQRKIGLVFQQYA-LFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 399 TVMDNLAEG---KQEVMVNGRPRHVLGYLQdfLFHPKRAmtPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03297 91 NVRENLAFGlkrKRNREDRISVDELLDLLG--LDHLLNR--YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180
....*....|....*....|....*
gi 505190249 476 LELLEELID----GYQGTVLLVSHD 496
Cdd:cd03297 167 RLQLLPELKqikkNLNIPVIFVTHD 191
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
333-473 |
3.81e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 68.93 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 333 VLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtklEVAYFDQHRADLDPER-------------- 398
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA------TVDGFDVVKEPAEARRrlgfvsdstglydr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 399 -TVMDNLA-----EGKQEVMVNGRPRHVLGYLQDFLFHPKRamtpVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03266 93 lTARENLEyfaglYGLKGDELTARLEELADRLGMEELLDRR----VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
.
gi 505190249 473 V 473
Cdd:cd03266 169 V 169
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
321-497 |
4.73e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 70.90 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLE-----VAYFDQHR 391
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvTGLPpekrnVGMVFQDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 392 AdLDPERTVMDNLAEG-------KQEV---------MVNgrprhvlgyLQDFLfhpKRAmtpVKALSGGERNRLLLAK-L 454
Cdd:COG3842 87 A-LFPHLTVAENVAFGlrmrgvpKAEIrarvaelleLVG---------LEGLA---DRY---PHQLSGGQQQRVALARaL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505190249 455 FLKPSnLLILDEPTNDLDVETLELLEELIDGYQ----GTVLLVSHDR 497
Cdd:COG3842 151 APEPR-VLLLDEPLSALDAKLREEMREELRRLQrelgITFIYVTHDQ 196
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-473 |
5.94e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.62 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRViyeqdlivarlqqdpprNIGGS 82
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL-----------------EIGGN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 VFdfvAEGVAEQAEHLKAYhaishLVESDP--------SEKNLARMAQimeildHQGLwqlDSRISEVLLQLG--LNGDA 152
Cdd:PRK15439 74 PC---ARLTPAKAHQLGIY-----LVPQEPllfpnlsvKENILFGLPK------RQAS---MQKMKQLLAALGcqLDLDS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 153 ELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLD-IETiDWLEGFLKEF---DGSIVFISHDRSFIRNMATRIVDLDR 228
Cdd:PRK15439 137 SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAET-ERLFSRIRELlaqGVGIVFISHKLPEIRQLADRISVMRD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 229 GKLVswpgnydlyLQSKEEALRVEELQNAefdrklaqeevwirqgiKARRTRNEGRVRALKA-LRVERSQRREVMGTAKM 307
Cdd:PRK15439 216 GTIA---------LSGKTADLSTDDIIQA-----------------ITPAAREKSLSASQKLwLELPGNRRQQAAGAPVL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 308 QVEEATrsgkivfeledvnyqvGEkvlvrGF---SAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV-------- 376
Cdd:PRK15439 270 TVEDLT----------------GE-----GFrniSLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRImlngkein 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 377 HCGTKLEVA----YFDQHRAD----LD-PER----TVMDNL----AEGKQEVMVNGRPRHVLGYLqdfLFHPKRamtPVK 439
Cdd:PRK15439 329 ALSTAQRLArglvYLPEDRQSsglyLDaPLAwnvcALTHNRrgfwIKPARENAVLERYRRALNIK---FNHAEQ---AAR 402
|
490 500 510
....*....|....*....|....*....|....
gi 505190249 440 ALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK15439 403 TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
330-473 |
5.94e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.27 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 330 GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTK-----------LEVAYFDQHRadLDPER 398
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlaRRLALLPQHH--LTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 399 -TVmdnlaegkQEVMVNGRPRHV--LGYL-QDFLFHPKRAMT----------PVKALSGGERNRLLLAKLFLKPSNLLIL 464
Cdd:PRK11231 91 iTV--------RELVAYGRSPWLslWGRLsAEDNARVNQAMEqtrinhladrRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
....*....
gi 505190249 465 DEPTNDLDV 473
Cdd:PRK11231 163 DEPTTYLDI 171
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-231 |
6.18e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.50 E-value: 6.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSlISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE-QDliVARLQ-QDppRN 78
Cdd:PRK10851 1 MS-IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgTD--VSRLHaRD--RK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 79 IGgsvfdFVAEGVAeQAEHLKAYHAISHLVESDPSEKNLARMA---QIMEILDhqglwqldsrisevLLQLGLNGDAELS 155
Cdd:PRK10851 76 VG-----FVFQHYA-LFRHMTVFDNIAFGLTVLPRRERPNAAAikaKVTQLLE--------------MVQLAHLADRYPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 156 SLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK10851 136 QLSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
321-496 |
6.26e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 68.63 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLvrGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLEVA------YFDQH 390
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqdlTALPPAerpvsmLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 391 raDLDPERTVMDNLAEG-----------KQEVM-----VNgrprhvLGYLQDFLfhpkramtPvKALSGGERNRLLLAKL 454
Cdd:COG3840 81 --NLFPHLTVAQNIGLGlrpglkltaeqRAQVEqalerVG------LAGLLDRL--------P-GQLSGGQRQRVALARC 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505190249 455 FLKPSNLLILDEPTNDLDVETLELLEELIDG----YQGTVLLVSHD 496
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDElcreRGLTVLMVTHD 189
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-232 |
7.51e-13 |
|
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: 67.90 E-value: 7.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 26 IEDNERVCLVGRNGAGKSTLLK-ILGKEIPLDDGRVIYEQDLIVArlqqDPPRNIGGSVFdfvaegvaeQAEHLkayhaI 104
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNlIAGFETPQSGRVLINGVDVTAA----PPADRPVSMLF---------QENNL-----F 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 105 SHL-VESD------PSEKNLARMAQIME-ILDHQGLWQLDSRISEvllqlglngdaelsSLSGGWLRKAALGRALVSSPR 176
Cdd:cd03298 83 AHLtVEQNvglglsPGLKLTAEDRQAIEvALARVGLAGLEKRLPG--------------ELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 177 VLLLDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03298 149 VLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-231 |
7.89e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.58 E-value: 7.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGrviyeqDLIVARLQQDPP----RNI---GGSVF 84
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG------DLIVDGLKVNDPkvdeRLIrqeAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 85 dfvaegvaeqaehlKAYHAISHL-----VESDP-----SEKNLARmAQIMEILDHQGLWQldsrisevllqlglNGDAEL 154
Cdd:PRK09493 84 --------------QQFYLFPHLtalenVMFGPlrvrgASKEEAE-KQARELLAKVGLAE--------------RAHHYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 155 SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DG-SIVFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK09493 135 SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLaeEGmTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
34-232 |
8.43e-13 |
|
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: 70.13 E-value: 8.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 34 LVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLivarLQQD------PP--RNIGgSVFdfvaegvaeQAEHLkayhaIS 105
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV----LQDSargiflPPhrRRIG-YVF---------QEARL-----FP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 106 HL-VESD--------PSEKNLARMAQIMEILDHQGLwqLDSRISevllqlglngdaelsSLSGGWLRKAALGRALVSSPR 176
Cdd:COG4148 91 HLsVRGNllygrkraPRAERRISFDEVVELLGIGHL--LDRRPA---------------TLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 177 VLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG4148 154 LLLMDEPLAALDLarkaEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
24-184 |
1.36e-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: 67.70 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 24 IHIEDNERVCLVGRNGAGKSTLLK-ILGkEIPLDDGRVIYE-QDLivARLqqdPP-----RNIGgsvfdFVAEG------ 90
Cdd:COG0410 24 LEVEEGEIVALLGRNGAGKTTLLKaISG-LLPPRSGSIRFDgEDI--TGL---PPhriarLGIG-----YVPEGrrifps 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 91 --VaeqAEHLKAyhAISHLVESDPSEKNLARMAQIMEILDhqglwqldsrisEVLLQLGlngdaelSSLSGGWLRKAALG 168
Cdd:COG0410 93 ltV---EENLLL--GAYARRDRAEVRADLERVYELFPRLK------------ERRRQRA-------GTLSGGEQQMLAIG 148
|
170
....*....|....*.
gi 505190249 169 RALVSSPRVLLLDEPT 184
Cdd:COG0410 149 RALMSRPKLLLLDEPS 164
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-232 |
1.60e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 67.71 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPlDDGRVIYEQDLIvarlqQDPPRNIG- 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCInLLEEP-DSGTITVDGEDL-----TDSKKDINk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 -----GSVF-DF-------VAEGVAE-QAEHLKAyhaishlvesDPSEknlARmAQIMEILDHQGLwqLDSRisevllql 146
Cdd:COG1126 75 lrrkvGMVFqQFnlfphltVLENVTLaPIKVKKM----------SKAE---AE-ERAMELLERVGL--ADKA-------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 147 glngDAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DG-SIVFISHDRSFIRNMATRI 223
Cdd:COG1126 131 ----DAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLakEGmTMVVVTHEMGFAREVADRV 206
|
....*....
gi 505190249 224 VDLDRGKLV 232
Cdd:COG1126 207 VFMDGGRIV 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-233 |
1.61e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.87 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDL----------IVARLQQDPPRNi 79
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrLNGRPLadwspaelarRRAVLPQHSSLS- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 80 ggsvFDF-VAEGVAeqaehlkayhaishlvesdpseknlarmaqiMEILDHQGLWQLDSRI-SEVLLQLGLNGDAELS-- 155
Cdd:PRK13548 89 ----FPFtVEEVVA-------------------------------MGRAPHGLSRAEDDALvAAALAQVDLAHLAGRDyp 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 156 SLSGGWLRKAALGRALV------SSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDrsfiRNMAT---- 221
Cdd:PRK13548 134 QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD----LNLAAryad 209
|
250
....*....|..
gi 505190249 222 RIVDLDRGKLVS 233
Cdd:PRK13548 210 RIVLLHQGRLVA 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-211 |
1.66e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 66.61 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 17 PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYeQDLIVARLQQDPPRNIggsvfdfvaegvaeqae 96
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRW-NGTPLAEQRDEPHENI----------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 97 hlkayHAISHLvesdPSEKNLARMAQIMEIL--DHQGlwqLDSRISEVLLQLGLNG--DAELSSLSGGWLRKAALGRALV 172
Cdd:TIGR01189 76 -----LYLGHL----PGLKPELSALENLHFWaaIHGG---AQRTIEDALAAVGLTGfeDLPAAQLSAGQQRRLALARLWL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505190249 173 SSPRVLLLDEPTNHLDIETIDWLEGFLKEF---DGSIVFISH 211
Cdd:TIGR01189 144 SRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
12-232 |
1.69e-12 |
|
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: 66.92 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEqdlivarlqqdpprnigGSVFDFvaegv 91
Cdd:cd03269 9 RFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD-----------------GKPLDI----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 92 aeqaehlKAYHAISHLvesdPSEKNLARMAQIMEILDH----QGLWQLD--SRISEVLLQLGLNGDAE--LSSLSGGWLR 163
Cdd:cd03269 67 -------AARNRIGYL----PEERGLYPKMKVIDQLVYlaqlKGLKKEEarRRIDEWLERLELSEYANkrVEELSKGNQQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505190249 164 KAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDG---SIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03269 136 KVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-229 |
1.70e-12 |
|
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: 67.46 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 17 PLLDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGKEIPlDDGRVIYEQDLIVARLQQDPPRNIG-------GSV--F-- 84
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKcIYGNYLP-DSGSILVRHDGGWVDLAQASPREILalrrrtiGYVsqFlr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 85 --------DFVAE-----GVAEQAEHLKAYHAISHLvesdpsekNLArmaqimeildhQGLWQLDSrisevllqlglngd 151
Cdd:COG4778 104 viprvsalDVVAEpllerGVDREEARARARELLARL--------NLP-----------ERLWDLPP-------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 152 aelSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET----IDWLEGfLKEFDGSIVFISHDRSFIRNMATRIVDLD 227
Cdd:COG4778 151 ---ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEE-AKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
..
gi 505190249 228 RG 229
Cdd:COG4778 227 PF 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
318-472 |
1.90e-12 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 67.26 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 318 IVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhCGTKLEVAYFDqhradLDPE 397
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRI-LIDGHDVRDYT-----LASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 398 R---------------TVMDNLAEGK-----QEVMVNGRprhvLGYLQDFLFH-PKRAMTPVK----ALSGGERNRLLLA 452
Cdd:cd03251 75 RrqiglvsqdvflfndTVAENIAYGRpgatrEEVEEAAR----AANAHEFIMElPEGYDTVIGergvKLSGGQRQRIAIA 150
|
170 180
....*....|....*....|
gi 505190249 453 KLFLKPSNLLILDEPTNDLD 472
Cdd:cd03251 151 RALLKDPPILILDEATSALD 170
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
12-232 |
2.25e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.09 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPLDDGRVIYEQDLivarlQQDPP--RNIGgsvfdfva 88
Cdd:PRK11607 28 SFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLaGFEQPTAGQIMLDGVDL-----SHVPPyqRPIN-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 89 egvaeqaEHLKAYHAISHLVesdpSEKNLA-RMAQimeilDHQGLWQLDSRISEVLLQLGLNGDAELS--SLSGGWLRKA 165
Cdd:PRK11607 95 -------MMFQSYALFPHMT----VEQNIAfGLKQ-----DKLPKAEIASRVNEMLGLVHMQEFAKRKphQLSGGQRQRV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 166 ALGRALVSSPRVLLLDEPTNHLD--------IETIDWLEgflkEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILE----RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-231 |
2.38e-12 |
|
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: 66.73 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 14 SDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVI--------YEQDLI---VARLQQDPPRnIGGS 82
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgkpisqYEHKYLhskVSLVGQEPVL-FARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 VFDFVAEGVAEqaehlkayhaishlvesdpseknlarmAQIMEILDHQGLWQLDSRISEvlLQLGLNGDA--ELSSLSGG 160
Cdd:cd03248 104 LQDNIAYGLQS---------------------------CSFECVKEAAQKAHAHSFISE--LASGYDTEVgeKGSQLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505190249 161 WLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFISHDRSFIRNmATRIVDLDRGKL 231
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
306-473 |
2.80e-12 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 69.77 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 306 KMQVEEATRSGKIVFELEDVNYQVGEKVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLeVA 385
Cdd:TIGR01193 462 KKRTELNNLNGDIVINDVSYSYGYGSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS-LK 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 386 YFDQH--RADLD--PER------TVMDNL----AEGKQEVMVNGRPRHV----------LGYLQDFLFHPKramtpvkAL 441
Cdd:TIGR01193 540 DIDRHtlRQFINylPQEpyifsgSILENLllgaKENVSQDEIWAACEIAeikddienmpLGYQTELSEEGS-------SI 612
|
170 180 190
....*....|....*....|....*....|..
gi 505190249 442 SGGERNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR01193 613 SGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
321-497 |
3.13e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 68.25 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTklEVAYFD------------ 388
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--RDLFTNlpprerrvgfvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 389 QHRAdLDPERTVMDNLAEGKQevmVNGRPRH-----VLGYLQdfLFH--------PKRamtpvkaLSGGERNRLLLAK-L 454
Cdd:COG1118 82 QHYA-LFPHMTVAENIAFGLR---VRPPSKAeirarVEELLE--LVQlegladryPSQ-------LSGGQRQRVALARaL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505190249 455 FLKPSnLLILDEPTNDLDVETLELL----EELIDGYQGTVLLVSHDR 497
Cdd:COG1118 149 AVEPE-VLLLDEPFGALDAKVRKELrrwlRRLHDELGGTTVFVTHDQ 194
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
316-473 |
3.85e-12 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 66.09 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 316 GKIVFEleDVNYQVGEKVLV-RGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKLE---------- 383
Cdd:cd03254 1 GEIEFE--NVNFSYDEKKPVlKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdGIDIRdisrkslrsm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 384 VAYFDQhradlDP---ERTVMDNLAEGKQ-----EVMVNGRPRHvlgyLQDFLFH-PKRAMTPV----KALSGGERNRLL 450
Cdd:cd03254 79 IGVVLQ-----DTflfSGTIMENIRLGRPnatdeEVIEAAKEAG----AHDFIMKlPNGYDTVLgengGNLSQGERQLLA 149
|
170 180
....*....|....*....|...
gi 505190249 451 LAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDT 172
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
327-501 |
4.11e-12 |
|
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: 66.30 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 327 YQVGEKVL--VRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV---HCGTKLEVAyfdqhRAdldPERTVM 401
Cdd:COG4778 17 HLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrHDGGWVDLA-----QA---SPREIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 402 DnLaegkqevmvngRpRHVLGYLQDFLfhpkRAMTPVKAL---------------------------------------- 441
Cdd:COG4778 89 A-L-----------R-RRTIGYVSQFL----RVIPRVSALdvvaepllergvdreearararellarlnlperlwdlppa 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 442 --SGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELIDGY--QGTVLL-VSHDRQFVD 501
Cdd:COG4778 152 tfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkaRGTAIIgIFHDEEVRE 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
321-473 |
4.23e-12 |
|
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: 66.10 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVN--YQVGEKVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtklevaYFDQHR---ADLD 395
Cdd:cd03253 2 EFENVTfaYDPGRPVL-KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSI---------LIDGQDireVTLD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 396 PER---------------TVMDNLAEGK-----QEVMVNGRPRHVLGYLQDFlfhPKRAMTPVKA----LSGGERNRLLL 451
Cdd:cd03253 72 SLRraigvvpqdtvlfndTIGYNIRYGRpdatdEEVIEAAKAAQIHDKIMRF---PDGYDTIVGErglkLSGGEKQRVAI 148
|
170 180
....*....|....*....|..
gi 505190249 452 AKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDT 170
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
321-496 |
4.63e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 66.26 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCgtklevayfdqhrADLDPERTV 400
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLV-------------DGLDVATTP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 401 MDNLAEG----KQEVMVN------------------GRP-----RHV---LGYLQdflfhpkraMTPVKA-----LSGGE 445
Cdd:COG4604 70 SRELAKRlailRQENHINsrltvrelvafgrfpyskGRLtaedrEIIdeaIAYLD---------LEDLADryldeLSGGQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 446 RNRLLLAKLFLKPSNLLILDEPTNDLD----VETLELLEELIDGYQGTVLLVSHD 496
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADELGKTVVIVLHD 195
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-247 |
4.74e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.52 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGKEIPlDDGRVIY---------EQDLIVARlqqdppRNIG-------- 80
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRcINLLERP-TSGRVLVdgqdltalsEKELRKAR------RQIGmifqhfnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 ---GSVFDFVAEgvaeqaehlkayhaishlvesdPSEknLARM--AQImeildhqglwqlDSRISEVLLQLGLN--GDAE 153
Cdd:PRK11153 94 lssRTVFDNVAL----------------------PLE--LAGTpkAEI------------KARVTELLELVGLSdkADRY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 154 LSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET----IDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRG 229
Cdd:PRK11153 138 PAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATtrsiLELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
250
....*....|....*...
gi 505190249 230 KLVSWPGNYDLYLQSKEE 247
Cdd:PRK11153 218 RLVEQGTVSEVFSHPKHP 235
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
331-496 |
4.77e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.42 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 331 EKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CG---TKLEVAY-------------------- 386
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGyvpFKRRKEFarrigvvfgqrsqlwwdlpa 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 387 ---FDQHRA--DLDPE--RTVMDNLAEgkqevmvngrprhVLGyLQDFLfhpkraMTPVKALSGGERNRL-LLAKLFLKP 458
Cdd:COG4586 114 idsFRLLKAiyRIPDAeyKKRLDELVE-------------LLD-LGELL------DTPVRQLSLGQRMRCeLAAALLHRP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505190249 459 SnLLILDEPTNDLDVETLELLEELI----DGYQGTVLLVSHD 496
Cdd:COG4586 174 K-ILFLDEPTIGLDVVSKEAIREFLkeynRERGTTILLTSHD 214
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-232 |
5.06e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.89 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 15 DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE----QDLIVARLQQDpprniggsvfdfVAeg 90
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDghdlRDYTLASLRNQ------------VA-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 91 VAEQAEHL--------KAYHAISHLveSDPSEKNLARMAQIMEILDH--QGLwqlDSRISEvllqlglNGdaelSSLSGG 160
Cdd:PRK11176 421 LVSQNVHLfndtiannIAYARTEQY--SREQIEEAARMAYAMDFINKmdNGL---DTVIGE-------NG----VLLSGG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505190249 161 WLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFISHDRSFIRNmATRIVDLDRGKLV 232
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELqkNRTSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
321-498 |
5.46e-12 |
|
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: 65.72 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKlEVAYFD----------QH 390
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK-DITNLPphkrpvntvfQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 391 RAdLDPERTVMDNLAEG-----------KQEVMVNGRPRHVLGYLQDFlfhpkramtpVKALSGGERNRLLLAK-LFLKP 458
Cdd:cd03300 81 YA-LFPHLTVFENIAFGlrlkklpkaeiKERVAEALDLVQLEGYANRK----------PSQLSGGQQQRVAIARaLVNEP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505190249 459 SnLLILDEPTNDLDVETLELLEELIDGYQG----TVLLVSHDRQ 498
Cdd:cd03300 150 K-VLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQE 192
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-232 |
6.81e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.60 E-value: 6.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFS-----DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-------GKEIPLDDGRVI-YEQDLI---VARLQQDP 75
Cdd:TIGR00958 485 SFSypnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLqnlyqptGGQVLLDGVPLVqYDHHYLhrqVALVGQEP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 76 PRnIGGSVFDFVAEGVaeqaehlkayhaishlvesdpsekNLARMAQIMEILDHQGLwqlDSRISEVLLQLGLNGDAELS 155
Cdd:TIGR00958 565 VL-FSGSVRENIAYGL------------------------TDTPDEEIMAAAKAANA---HDFIMEFPNGYDTEVGEKGS 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 156 SLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSIVFISHDRSFIRNmATRIVDLDRGKLV 232
Cdd:TIGR00958 617 QLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVV 692
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
12-231 |
8.34e-12 |
|
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: 64.86 E-value: 8.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQ-DPPRNIGGSVF-DF--- 86
Cdd:cd03262 9 SFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGMVFqQFnlf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 87 ----VAEGVAE---QAEHLKAYHAIshlvesdpseknlarmAQIMEILDHQGLwqlDSRIsevllqlglngDAELSSLSG 159
Cdd:cd03262 89 phltVLENITLapiKVKGMSKAEAE----------------ERALELLEKVGL---ADKA-----------DAYPAQLSG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 160 GWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DG-SIVFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03262 139 GQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeEGmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-232 |
8.96e-12 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 64.49 E-value: 8.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 10 WLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGkeiplddGRVIYEQdlivarlqqdpprnIGGSVFdfvae 89
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA-------GRRTGLG--------------VSGEVL----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 90 gVAEQAEHLKAYHAISHLVESDpseknlarmaqimeildhqglwqlDSRISEVLLQLGLNGDAELSSLSGGWLRKAALGR 169
Cdd:cd03213 70 -INGRPLDKRSFRKIIGYVPQD------------------------DILHPTLTVRETLMFAAKLRGLSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 170 ALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DG-SIVFISHD-RSFIRNMATRIVDLDRGKLV 232
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLadTGrTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
330-495 |
9.55e-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: 64.44 E-value: 9.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 330 GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV---------HCGTKLEVAYFDQHRADLDPERTV 400
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggpldfQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 401 MDNL----AEGKQEVMVNGRPRHVLGYLQDflfhpkramTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETL 476
Cdd:cd03231 91 LENLrfwhADHSDEQVEEALARVGLNGFED---------RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|..
gi 505190249 477 ELLEELIDGYQ---GTVLLVSH 495
Cdd:cd03231 162 ARFAEAMAGHCargGMVVLTTH 183
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-467 |
1.00e-11 |
|
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: 65.26 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 320 FELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLEV--------AYF 387
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqdiTKLPMhkrarlgiGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 388 DQhRADLDPERTVMDNLAEGKQEVMVNGRPRH-VLGYLQDfLFHPKR-AMTPVKALSGGERNRLLLAK-LFLKPSNLLiL 464
Cdd:cd03218 81 PQ-EASIFRKLTVEENILAVLEIRGLSKKEREeKLEELLE-EFHITHlRKSKASSLSGGERRRVEIARaLATNPKFLL-L 157
|
...
gi 505190249 465 DEP 467
Cdd:cd03218 158 DEP 160
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
332-472 |
1.17e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.56 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 332 KVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLG------QLKADsgrvhcGTKLEVAYFDQHRADLD--------PE 397
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgSLKIN------GIELRELDPESWRKHLSwvgqnpqlPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 398 RTVMDNLAEGKQEvMVNGRPRHVL--GYLQDFLF-HPKRAMTPVK----ALSGGERNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK11174 437 GTLRDNVLLGNPD-ASDEQLQQALenAWVSEFLPlLPQGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
..
gi 505190249 471 LD 472
Cdd:PRK11174 516 LD 517
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-192 |
1.18e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.51 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 17 PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDlivarlQQDPPRniggsvfdfvaegVAEQAe 96
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG------DIDDPD-------------VAEAC- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 97 hlkayHAISHLvesDPSEKNLArmaqIMEILDhqgLW-----QLDSRISEVLLQLGLNGDAEL--SSLSGGWLRKAALGR 169
Cdd:PRK13539 76 -----HYLGHR---NAMKPALT----VAENLE---FWaaflgGEELDIAAALEAVGLAPLAHLpfGYLSAGQKRRVALAR 140
|
170 180
....*....|....*....|...
gi 505190249 170 ALVSSPRVLLLDEPTNHLDIETI 192
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAAV 163
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
318-472 |
1.18e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 318 IVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKadsGRVHCGTklevayFDQHRADLDPE 397
Cdd:COG2401 29 IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK---GTPVAGC------VDVPDNQFGRE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 398 RTVMDNLAEgKQEVMVNGRPRHVLGYLQDFLFhpkraMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:COG2401 100 ASLIDAIGR-KGDFKDAVELLNAVGLSDAVLW-----LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
330-467 |
1.18e-11 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 64.99 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 330 GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV------------HCGTKLEVAYFDQhRADLDPE 397
Cdd:TIGR04406 12 KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIlidgqdithlpmHERARLGIGYLPQ-EASIFRK 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505190249 398 RTVMDNLA---EGKQEVMVNGRPRHVLGYLQDF-LFHPKRAmtPVKALSGGERNRLLLAKLFLKPSNLLILDEP 467
Cdd:TIGR04406 91 LTVEENIMavlEIRKDLDRAEREERLEALLEEFqISHLRDN--KAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
14-212 |
1.38e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.54 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 14 SDAPL-LDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGKEIPlDDGRVIYEQDLIVARLQQDPPRNIgGSVF-----DF 86
Cdd:PRK13648 19 SDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKlMIGIEKV-KSGEIFYNNQAITDDNFEKLRKHI-GIVFqnpdnQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 87 VAEGVAEQAehlkAYHAISHLVesdPSEKNLARMAQIMEILDhqglwQLDSRisevllqlglngDAELSSLSGGWLRKAA 166
Cdd:PRK13648 97 VGSIVKYDV----AFGLENHAV---PYDEMHRRVSEALKQVD-----MLERA------------DYEPNALSGGQKQRVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505190249 167 LGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF----DGSIVFISHD 212
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITHD 202
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
10-245 |
1.39e-11 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 64.55 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 10 WLSF-SDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIY-EQDL----------IVARLQQDPPR 77
Cdd:cd03254 9 NFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdGIDIrdisrkslrsMIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 78 nIGGSVFDFVAegvaeqaehlkayhaISHLVESDPSEKNLARMAQIMEILDH--QGLwqlDSRISEvllqlglNGdaelS 155
Cdd:cd03254 89 -FSGTIMENIR---------------LGRPNATDEEVIEAAKEAGAHDFIMKlpNGY---DTVLGE-------NG----G 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 156 SLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWL-EGFLKEFDGSIVF-ISHDRSFIRNmATRIVDLDRGKLVS 233
Cdd:cd03254 139 NLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIqEALEKLMKGRTSIiIAHRLSTIKN-ADKILVLDDGKIIE 217
|
250
....*....|..
gi 505190249 234 wPGNYDLYLQSK 245
Cdd:cd03254 218 -EGTHDELLAKK 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
321-468 |
1.65e-11 |
|
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: 64.62 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVN--YqvGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLE--------VAY 386
Cdd:COG0410 5 EVENLHagY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgediTGLPphriarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 387 FDQHR---ADLdperTVMDNLAEG----KQEVMVNGRPRHVLGY---LQDFLFHpkRAMTpvkaLSGGERNRLLLAK-LF 455
Cdd:COG0410 83 VPEGRrifPSL----TVEENLLLGayarRDRAEVRADLERVYELfprLKERRRQ--RAGT----LSGGEQQMLAIGRaLM 152
|
170
....*....|...
gi 505190249 456 LKPSnLLILDEPT 468
Cdd:COG0410 153 SRPK-LLLLDEPS 164
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
12-231 |
1.77e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 64.70 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-------GKEI-----PL----DDGRVIYeQDlivARLQqdP 75
Cdd:PRK11247 21 RYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLagletpsAGELlagtaPLaearEDTRLMF-QD---ARLL--P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 76 PRniggSVFDFVAEGVaeqaehlkayhaishlvesdpseknlarmaqimeildhQGLWQLDSRisEVLLQLGLNGDAE-- 153
Cdd:PRK11247 95 WK----KVIDNVGLGL--------------------------------------KGQWRDAAL--QALAAVGLADRANew 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 154 LSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRG 229
Cdd:PRK11247 131 PAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
..
gi 505190249 230 KL 231
Cdd:PRK11247 211 KI 212
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
324-472 |
1.90e-11 |
|
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: 64.51 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 324 DVNYQVGEKVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLEVAYFDQHRAD------ 393
Cdd:cd03256 7 SKTYPNGKKAL-KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdiNKLKGKALRQLRRQigmifq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 394 ---LDPERTVMDNlaegkqeVMVnGRprhvLGYLQDF-----LFHP----------------KRAMTPVKALSGGERNRL 449
Cdd:cd03256 86 qfnLIERLSVLEN-------VLS-GR----LGRRSTWrslfgLFPKeekqralaalervgllDKAYQRADQLSGGQQQRV 153
|
170 180
....*....|....*....|...
gi 505190249 450 LLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLD 176
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
320-498 |
1.91e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 63.65 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 320 FELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKAD---SGRVhcgtklevaYFDQHR-ADLD 395
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEV---------LLNGRRlTALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 396 PER----------------TVMDNLA------EGKQEvmvngRPRHVLGYLQDfLFHPKRAMTPVKALSGGERNRL-LLA 452
Cdd:COG4136 73 AEQrrigilfqddllfphlSVGENLAfalpptIGRAQ-----RRARVEQALEE-AGLAGFADRDPATLSGGQRARVaLLR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505190249 453 KLFLKPSNLLiLDEPTNDLDVETLELLEE----LIDGYQGTVLLVSHDRQ 498
Cdd:COG4136 147 ALLAEPRALL-LDEPFSKLDAALRAQFREfvfeQIRQRGIPALLVTHDEE 195
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-472 |
1.92e-11 |
|
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: 63.70 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 320 FELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKL------------EVAY 386
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdGLKLtddkkninelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 387 FDQHrADLDPERTVMDNLAEGkqEVMVNGRPR-----HVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLAK-LFLKPSn 460
Cdd:cd03262 81 VFQQ-FNLFPHLTVLENITLA--PIKVKGMSKaeaeeRALELLEKVGLADKADAYPAQ-LSGGQQQRVAIARaLAMNPK- 155
|
170
....*....|..
gi 505190249 461 LLILDEPTNDLD 472
Cdd:cd03262 156 VMLFDEPTSALD 167
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
321-495 |
2.17e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 63.31 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKAdsgRVhcgTKLEVAYFDQHRADLDPERTV 400
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKY---EV---TEGEILFKGEDITDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 401 MDNLAEGKQEvmvngrPRHVLGY-LQDFLfhpkRAMTpvKALSGGERNRL-LLAKLFLKPSnLLILDEPTNDLDVETLEL 478
Cdd:cd03217 76 RLGIFLAFQY------PPEIPGVkNADFL----RYVN--EGFSGGEKKRNeILQLLLLEPD-LAILDEPDSGLDIDALRL 142
|
170 180
....*....|....*....|
gi 505190249 479 LEELIDGYQG---TVLLVSH 495
Cdd:cd03217 143 VAEVINKLREegkSVLIITH 162
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
329-472 |
2.38e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.72 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 329 VGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKlEVAYFDQH-RADL------DPER--- 398
Cdd:COG1101 16 VNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK-DVTKLPEYkRAKYigrvfqDPMMgta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 399 ---TVMDNLA----EGKQEVMVNGRPRHVLGYLQDFLFH-----PKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDE 466
Cdd:COG1101 95 psmTIEENLAlayrRGKRRGLRRGLTKKRRELFRELLATlglglENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDE 174
|
....*.
gi 505190249 467 PTNDLD 472
Cdd:COG1101 175 HTAALD 180
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-225 |
4.26e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.65 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 31 RVC-LVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLI-----------VARLQQDPPRNIGGSVFDFVAEGvaeqaehl 98
Cdd:PRK10575 38 KVTgLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsskafarkVAYLPQQLPAAEGMTVRELVAIG-------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 99 kAYhaishlvesdPSEKNLARMAQimeiLDHQglwqldsRISEVLLQLGLNGDAE--LSSLSGGWLRKAALGRALVSSPR 176
Cdd:PRK10575 110 -RY----------PWHGALGRFGA----ADRE-------KVEEAISLVGLKPLAHrlVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505190249 177 VLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDrsfiRNMATRIVD 225
Cdd:PRK10575 168 CLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHD----INMAARYCD 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
324-497 |
4.49e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.66 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 324 DVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC---GTKLEVAYFDQ------HRADL 394
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFerqSIKKDLCTYQKqlcfvgHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 DPERTVMDN------LAEGKQEVMVNGRpRHVLGYLQDFlfhpkramtPVKALSGGERNRLLLAKLFLKPSNLLILDEPT 468
Cdd:PRK13540 86 NPYLTLRENclydihFSPGAVGITELCR-LFSLEHLIDY---------PCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|..
gi 505190249 469 NDLDVETLELLEELIDGYQ---GTVLLVSHDR 497
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
30-232 |
5.00e-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: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 30 ERVCLVGRNGAGKSTL-LKILGkeipLDD--GRVIYE-QDL----------IVARLQ---QDP-----PRNiggSVFDFV 87
Cdd:COG4172 313 ETLGLVGESGSGKSTLgLALLR----LIPseGEIRFDgQDLdglsrralrpLRRRMQvvfQDPfgslsPRM---TVGQII 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 88 AEGVAeqaehlkayhaiSHLVESDPSEknlaRMAQIMEILDhqglwqldsrisEVllqlGLNGDA------ElssLSGGW 161
Cdd:COG4172 386 AEGLR------------VHGPGLSAAE----RRARVAEALE------------EV----GLDPAArhryphE---FSGGQ 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 162 LRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVsvqaQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-231 |
5.07e-11 |
|
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: 61.85 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 15 DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGKEIPLDdGRViyeqdlivaRLqqdpprniggsvfdfvaEGVAE 93
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARlILGLLRPTS-GRV---------RL-----------------DGADI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 94 QAEHLKAYHaishlvesdpseknlarmaqimeilDHQGlwqldsriseVLLQlglngDAELSS-------LSGGWLRKAA 166
Cdd:cd03246 67 SQWDPNELG-------------------------DHVG----------YLPQ-----DDELFSgsiaeniLSGGQRQRLG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 167 LGRALVSSPRVLLLDEPTNHLDIETIDWLE---GFLKEFDGSIVFISHDRSFIRnMATRIVDLDRGKL 231
Cdd:cd03246 107 LARALYGNPRILVLDEPNSHLDVEGERALNqaiAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-233 |
5.46e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 63.32 E-value: 5.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 26 IEDNERVCLVGRNGAGKSTLLKILGKEIP-----LDDGRVIYEQDLI-VARL------QQDPPRNIGgsVFDFVAEGVAE 93
Cdd:COG4138 19 VNAGELIHLIGPNGAGKSTLLARMAGLLPgqgeiLLNGRPLSDWSAAeLARHraylsqQQSPPFAMP--VFQYLALHQPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 94 QAEHLKAYHAISHLVESDPSEKNLARMAqimeildHQ---GLWQlDSRISEVLLQL--GLNGDAELsslsggwlrkaalg 168
Cdd:COG4138 97 GASSEAVEQLLAQLAEALGLEDKLSRPL-------TQlsgGEWQ-RVRLAAVLLQVwpTINPEGQL-------------- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 169 ralvssprvLLLDEPTNHLDIETIDWLEGFLKEF---DGSIVFISHDRSFIRNMATRIVDLDRGKLVS 233
Cdd:COG4138 155 ---------LLLDEPMNSLDVAQQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVA 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
30-211 |
5.78e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 62.13 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 30 ERVCLVGRNGAGKSTLLKILGKEIPLDDGRViyeqdlivaRLQQDPPrnigGSVFDFVAEGVAeQAEHLKAYHAISHLVE 109
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAGRV---------LLNGGPL----DFQRDSIARGLL-YLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 110 sdpsekNLARMAQIMEildhqglwqlDSRISEVLLQLGLNG--DAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHL 187
Cdd:cd03231 93 ------NLRFWHADHS----------DEQVEEALARVGLNGfeDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*..
gi 505190249 188 DIETIDWLEGFLK---EFDGSIVFISH 211
Cdd:cd03231 157 DKAGVARFAEAMAghcARGGMVVLTTH 183
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
311-472 |
6.47e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.58 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 311 EATRSGKIVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH----CGTKL---- 382
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMldgqDITHVpaen 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 383 -EVAYFDQHRAdLDPERTVMDNLAEG-------KQEVmvngRPRhVLG-----YLQDFlfhpkrAMTPVKALSGGERNRL 449
Cdd:PRK09452 86 rHVNTVFQSYA-LFPHMTVFENVAFGlrmqktpAAEI----TPR-VMEalrmvQLEEF------AQRKPHQLSGGQQQRV 153
|
170 180
....*....|....*....|...
gi 505190249 450 LLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALD 176
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
325-472 |
6.66e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 63.34 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 325 VNYQVG--EKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV--------HCGTKLEVAYfdQHRAdL 394
Cdd:COG4525 11 VRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEItldgvpvtGPGADRGVVF--QKDA-L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 DPERTVMDNLAEGKQevmVNGRPRH-----------VLGyLQDFlfhpkrAMTPVKALSGGERNRLLLAKLFLKPSNLLI 463
Cdd:COG4525 88 LPWLNVLDNVAFGLR---LRGVPKAerraraeellaLVG-LADF------ARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
....*....
gi 505190249 464 LDEPTNDLD 472
Cdd:COG4525 158 MDEPFGALD 166
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
331-472 |
7.27e-11 |
|
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: 62.29 E-value: 7.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 331 EKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMlgqlkadSGRVHCG------------------TKLEVAYFDQHrA 392
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAI-------SGRVEGGgttsgqilfngqprkpdqFQKCVAYVRQD-D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 393 DLDPERTVMDNLA-------------EGKQEVMVNGRPRHVlgylqdflfhpkrAMTPV-----KALSGGERNRLLLAKL 454
Cdd:cd03234 91 ILLPGLTVRETLTytailrlprkssdAIRKKRVEDVLLRDL-------------ALTRIggnlvKGISGGERRRVSIAVQ 157
|
170
....*....|....*...
gi 505190249 455 FLKPSNLLILDEPTNDLD 472
Cdd:cd03234 158 LLWDPKVLILDEPTSGLD 175
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-232 |
7.97e-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: 61.18 E-value: 7.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFS----DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIyeqdlivarLQQDPPRNIGGSVFDF 86
Cdd:cd03247 6 VSFSypeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT---------LDGVPVSDLEKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 87 VaeGVAEQAEHLKAyhaishlvesdpseknlarmAQIMEILDHQglwqldsrisevllqlglngdaelssLSGGWLRKAA 166
Cdd:cd03247 77 I--SVLNQRPYLFD--------------------TTLRNNLGRR--------------------------FSGGERQRLA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 167 LGRALVSSPRVLLLDEPTNHLDIET-IDWLEGFLKEF-DGSIVFISHDRSFIRNMaTRIVDLDRGKLV 232
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITeRQLLSLIFEVLkDKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-232 |
9.01e-11 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 62.13 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSD--APLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIY-EQDLIVARLQ-------- 72
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdGVDISKIGLHdlrsrisi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 73 --QDPprniggsvfdFVAEG-VAEQAEHLKAYhaishlveSDpseknlarmAQIMEILDHQGLW--------QLDSRISE 141
Cdd:cd03244 83 ipQDP----------VLFSGtIRSNLDPFGEY--------SD---------EELWQALERVGLKefveslpgGLDTVVEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 142 VllqlGLNgdaelssLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFISHdRsfIRNM 219
Cdd:cd03244 136 G----GEN-------LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAH-R--LDTI 201
|
250
....*....|....*
gi 505190249 220 AT--RIVDLDRGKLV 232
Cdd:cd03244 202 IDsdRILVLDKGRVV 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
330-516 |
9.09e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.46 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 330 GEKVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLM------------LGQLKADSGRVHCGTKLEVAYFDQHRA----- 392
Cdd:PRK11264 15 GQTVL-HGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARSLSQQKGLIRQLRQHVGfvfqn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 393 -DLDPERTVMDNLAEGKqeVMVNGRPRHVLGYLQDFLF-----------HPKRamtpvkaLSGGERNRLLLAKLFLKPSN 460
Cdd:PRK11264 94 fNLFPHRTVLENIIEGP--VIVKGEPKEEATARARELLakvglagketsYPRR-------LSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 461 LLILDEPTNDLDVETLELLEELIDGY---QGTVLLVSHDRQFVDNsVTECWIFEGNGVI 516
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARD-VADRAIFMDQGRI 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-232 |
9.61e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 62.70 E-value: 9.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFS----DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-------GKEIPLdDGRVIYEQDLIVAR-----LQQD 74
Cdd:PRK13632 13 VSFSypnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILtgllkpqSGEIKI-DGITISKENLKEIRkkigiIFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 75 PPRN-IGGSVFDFVAEGVAEQAEhlkayhaishlvesDPSEknlarMAQImeildhqglwqldsrISEVLLQLGLNG--D 151
Cdd:PRK13632 92 PDNQfIGATVEDDIAFGLENKKV--------------PPKK-----MKDI---------------IDDLAKKVGMEDylD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 152 AELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLD-------IETIDWLEgflKEFDGSIVFISHDRSFIRNmATRIV 224
Cdd:PRK13632 138 KEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkreiKKIMVDLR---KTRKKTLISITHDMDEAIL-ADKVI 213
|
....*...
gi 505190249 225 DLDRGKLV 232
Cdd:PRK13632 214 VFSEGKLI 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
320-473 |
9.88e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 9.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 320 FELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKL-----------EVAYFD 388
Cdd:PRK10575 12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 389 QHradLDPertvmdnlAEGK--QEVMVNGR-PRHvlGYLQDFLFHPKR---------AMTP-----VKALSGGERNRLLL 451
Cdd:PRK10575 92 QQ---LPA--------AEGMtvRELVAIGRyPWH--GALGRFGAADREkveeaislvGLKPlahrlVDSLSGGERQRAWI 158
|
170 180
....*....|....*....|..
gi 505190249 452 AKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDI 180
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-473 |
1.00e-10 |
|
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: 64.46 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLD--DGRVIYEQDLIVARLQQDPPRNiG 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERA-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 GSVFDFVAEGVAEQ--AEHLKAYHAISHlvesdpsekNLARMAQIMEILdhqglwqldsRISEVLLQLGLNGDA---ELS 155
Cdd:TIGR02633 80 IVIIHQELTLVPELsvAENIFLGNEITL---------PGGRMAYNAMYL----------RAKNLLRELQLDADNvtrPVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 156 SLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDG---SIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:TIGR02633 141 DYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 233 swpgnydlylqskeealrveelqnaefdrklaqeevwirqGIKARRTRNEGRVRALKALRVERSqrrevmgtakMQVEEA 312
Cdd:TIGR02633 221 ----------------------------------------ATKDMSTMSEDDIITMMVGREITS----------LYPHEP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 313 TRSGKIVFELEDVN-YQVGEKVLVR--GFSAQVQRGDKIALVGPNGCGKTTLLKLMLGqlkADSGRvHCGTklevAYFDQ 389
Cdd:TIGR02633 251 HEIGDVILEARNLTcWDVINPHRKRvdDVSFSLRRGEILGVAGLVGAGRTELVQALFG---AYPGK-FEGN----VFING 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 390 HRADLdpeRTVMDNLAEGKqeVMV-NGRPRH------------VLGYLQDFLFHPK-----------RAMT--------- 436
Cdd:TIGR02633 323 KPVDI---RNPAQAIRAGI--AMVpEDRKRHgivpilgvgkniTLSVLKSFCFKMRidaaaelqiigSAIQrlkvktasp 397
|
490 500 510
....*....|....*....|....*....|....*....
gi 505190249 437 --PVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR02633 398 flPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-237 |
1.05e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.75 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILG-KEIPLDDGRVIYEQDliVARLQQDPPRNIGGSVFDFVaegvaeqaeh 97
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGcLDKPTSGTYRVAGQD--VATLDADALAQLRREHFGFI---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 98 LKAYHAISHLVesdpSEKNLarmaQIMEILDHQGLWQLDSRISEVLLQLGLNG--DAELSSLSGGWLRKAALGRALVSSP 175
Cdd:PRK10535 92 FQRYHLLSHLT----AAQNV----EVPAVYAGLERKQRLLRAQELLQRLGLEDrvEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 176 RVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFI-SHDRSfIRNMATRIVDLDRGKLVSWPGN 237
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLrdRGHTVIIvTHDPQ-VAAQAERVIEIRDGEIVRNPPA 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
338-495 |
1.35e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.91 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 338 FSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV------HCGT---KLEVAYFDQHRaDLDPERTVMDNLAEG- 407
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdHTTTppsRRPVSMLFQEN-NLFSHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 408 --------KQEVMVNGRPRHVlgYLQDFLfhpkrAMTPvKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELL 479
Cdd:PRK10771 97 npglklnaAQREKLHAIARQM--GIEDLL-----ARLP-GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180
....*....|....*....|
gi 505190249 480 EELIDGY----QGTVLLVSH 495
Cdd:PRK10771 169 LTLVSQVcqerQLTLLMVSH 188
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-232 |
1.92e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 61.64 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDL----------IVARLQ 72
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVlVDGLDVattpsrelakRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 73 QDPPRNIGGSVFDFVAEGvaeqaehlkayhaishlvesdpseknlaRMAQimeildHQG-LWQLDSR-ISEVLLQLGLNG 150
Cdd:COG4604 82 QENHINSRLTVRELVAFG----------------------------RFPY------SKGrLTAEDREiIDEAIAYLDLED 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 151 --DAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIV 224
Cdd:COG4604 128 laDRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHDINFASCYADHIV 207
|
....*...
gi 505190249 225 DLDRGKLV 232
Cdd:COG4604 208 AMKDGRVV 215
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-232 |
2.02e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 61.64 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIyeqdlivarlqqdpprnIGGSVfdfvaegvaeqaehl 98
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE-----------------VNGRV--------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 99 kayhaiSHLVES----DPS---EKNLARMAQIMeildhqGL--WQLDSRISEVLL--QLGLNGDAELSSLSGGwlRKAAL 167
Cdd:COG1134 90 ------SALLELgagfHPEltgRENIYLNGRLL------GLsrKEIDEKFDEIVEfaELGDFIDQPVKTYSSG--MRARL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 168 GRALVSS--PRVLLLDEptnhldietidWL-----------EGFLKEF---DGSIVFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:COG1134 156 AFAVATAvdPDILLVDE-----------VLavgdaafqkkcLARIRELresGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
.
gi 505190249 232 V 232
Cdd:COG1134 225 V 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
310-472 |
2.03e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.69 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 310 EEATRSGKIVFELEDVN--YQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYF 387
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSftYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 388 DQH-RADLD--PER------TVMDNLAEGK----QEVMVNGRPRHVLGYLQDflfhpkrAMTPVKA--------LSGGER 446
Cdd:PRK11160 409 EAAlRQAISvvSQRvhlfsaTLRDNLLLAApnasDEALIEVLQQVGLEKLLE-------DDKGLNAwlgeggrqLSGGEQ 481
|
170 180
....*....|....*....|....*.
gi 505190249 447 NRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-367 |
2.18e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.50 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDG----------RVIYE--QDLIV 68
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshitRLSFEqlQKLVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 69 ARLQQ-------DPPRNIGGSVFDFVAEGVAEQA--EHLKAYHAISHLvesdpseknlarmaqimeildhqglwqLDSRi 139
Cdd:PRK10938 81 DEWQRnntdmlsPGEDDTGRTTAEIIQDEVKDPArcEQLAQQFGITAL---------------------------LDRR- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 140 sevllqlglngdaeLSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGS---IVFISHDRSFI 216
Cdd:PRK10938 133 --------------FKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSgitLVLVLNRFDEI 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 217 RNMATRIVDLDRGKLVswpgnydlyLQSKEEALrveeLQNAEFdRKLAQEEvwirqgikarrtrnegrvralkalRVERS 296
Cdd:PRK10938 199 PDFVQFAGVLADCTLA---------ETGEREEI----LQQALV-AQLAHSE------------------------QLEGV 240
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505190249 297 QRREvmgTAKMQVEEATRSGKIVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLG 367
Cdd:PRK10938 241 QLPE---PDEPSARHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
155-233 |
2.40e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.58 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 155 SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGK 230
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
...
gi 505190249 231 LVS 233
Cdd:PRK11144 207 VKA 209
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-243 |
2.44e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 61.74 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 14 SDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRNIGgsvfdFVAEGVAE 93
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG-----LVFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 94 QAehlkayhaISHLVESDPS--EKNLArmaqimeiLDHQglwQLDSRISEVLLQLGLNG--DAELSSLSGGWLRKAALGR 169
Cdd:PRK13652 90 QI--------FSPTVEQDIAfgPINLG--------LDEE---TVAHRVSSALHMLGLEElrDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 170 ALVSSPRVLLLDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPGNYDLYLQ 243
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-232 |
2.51e-10 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 60.75 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 14 SDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGKeipLDDGRVIYEQDLI--VARLQQDPPRNIG-GSVFDFVAE 89
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDaISGR---VEGGGTTSGQILFngQPRKPDQFQKCVAyVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 90 GVAeQAEHLkAYHAISHLvesdPSEKNLARMAQIMEIldhqglwqldsrisEVLLQLGLN--GDAELSSLSGGWLRKAAL 167
Cdd:cd03234 95 GLT-VRETL-TYTAILRL----PRKSSDAIRKKRVED--------------VLLRDLALTriGGNLVKGISGGERRRVSI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 168 GRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFIS-HD-RSFIRNMATRIVDLDRGKLV 232
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLarRNRIVILTiHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
316-473 |
2.58e-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: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 316 GKIVFELEDVnyqvGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG------------TKLE 383
Cdd:cd03215 1 GEPVLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkpvtrrsprdaIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 384 VAYF--DQHRADLDPERTVMDNLAegkqevmvngrprhvLGYLqdflfhpkramtpvkaLSGGERNRLLLAKLFLKPSNL 461
Cdd:cd03215 77 IAYVpeDRKREGLVLDLSVAENIA---------------LSSL----------------LSGGNQQKVVLARWLARDPRV 125
|
170
....*....|..
gi 505190249 462 LILDEPTNDLDV 473
Cdd:cd03215 126 LILDEPTRGVDV 137
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-249 |
2.83e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.56 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQ-----DPPRNIGgSVFDFvaegvae 93
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikevkRLRKEIG-LVFQF------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 94 qaehlKAYHAISHLVESDPSEKNLARMAQIMEILdhqglwqldSRISEVLLQLGLNGDAELSS---LSGGWLRKAALGRA 170
Cdd:PRK13645 99 -----PEYQLFQETIEKDIAFGPVNLGENKQEAY---------KKVPELLKLVQLPEDYVKRSpfeLSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 171 LVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPGNYDLYlqSKE 246
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF--SNQ 242
|
...
gi 505190249 247 EAL 249
Cdd:PRK13645 243 ELL 245
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
224-300 |
2.84e-10 |
|
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: 56.81 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 224 VDLDRGKLVSWPGNYDLYLQSKEEALRVEELQNAEFDRKLAQEEVWI-RQGIKARRTR-NEGRVRALKAL-RVERSQRRE 300
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIdRFRAKASKAKqAQSRIKALEKMeRIEKPERDK 80
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
321-495 |
2.95e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 60.20 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLvrGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLEVA------YFDQH 390
Cdd:cd03298 2 RLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvTAAPPAdrpvsmLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 391 raDLDPERTVMDNLAEGKQevmvngrPRHVLGYLQDFLFHPKRAMTPV--------KALSGGERNRLLLAKLFLKPSNLL 462
Cdd:cd03298 80 --NLFAHLTVEQNVGLGLS-------PGLKLTAEDRQAIEVALARVGLaglekrlpGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 505190249 463 ILDEPTNDLDVETLELLEELIDGY----QGTVLLVSH 495
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLhaetKMTVLMVTH 187
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
34-223 |
2.99e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 62.06 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 34 LVGRNGAGKSTLLKILGKEIPLDDGRVIYE-QDLIVA----------RLQ---QDP-----PRNiggSVFDFVAEGVaeq 94
Cdd:COG4608 49 LVGESGCGKSTLGRLLLRLEEPTSGEILFDgQDITGLsgrelrplrrRMQmvfQDPyaslnPRM---TVGDIIAEPL--- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 95 aehlkayhaishlvesdpseknlarmaQIMEILDHQglwQLDSRISEVLLQLGLNGDA------ELSslsGGWLRKAALG 168
Cdd:COG4608 123 ---------------------------RIHGLASKA---ERRERVAELLELVGLRPEHadryphEFS---GGQRQRIGIA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 169 RALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRI 223
Cdd:COG4608 170 RALALNPKLIVCDEPVSALDVsiqaQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRV 228
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-257 |
3.28e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.81 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFS---DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLI-----------VARLQQDPP 76
Cdd:PRK10790 346 VSFAyrdDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsslshsvlrqgVAMVQQDPV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 77 RnIGGSVFDFVAEGvaeqaehlkayhaishlveSDPSEknlarmAQIMEILDHQGLWQLDSRISEVL-LQLGLNGdaelS 155
Cdd:PRK10790 426 V-LADTFLANVTLG-------------------RDISE------EQVWQALETVQLAELARSLPDGLyTPLGEQG----N 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 156 SLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFISHDRSFIRNmATRIVDLDRGKLVS 233
Cdd:PRK10790 476 NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
250 260
....*....|....*....|....
gi 505190249 234 wPGNYDLYLQSKEEALRVEELQNA 257
Cdd:PRK10790 555 -QGTHQQLLAAQGRYWQMYQLQLA 577
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-245 |
4.27e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.53 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGawLSFS----DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRN 78
Cdd:PRK11160 338 SLTLNN--VSFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 79 IGgsvfdfvaegVAEQAEHLKayhaishlveSDPSEKNLaRMAQIMEIldhqglwqlDSRISEVLLQLGL----NGDAEL 154
Cdd:PRK11160 416 IS----------VVSQRVHLF----------SATLRDNL-LLAAPNAS---------DEALIEVLQQVGLekllEDDKGL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 155 SS--------LSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFISHDRSFIRNMaTRIV 224
Cdd:PRK11160 466 NAwlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRLTGLEQF-DRIC 544
|
250 260
....*....|....*....|.
gi 505190249 225 DLDRGKLVSwPGNYDLYLQSK 245
Cdd:PRK11160 545 VMDNGQIIE-QGTHQELLAQQ 564
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
330-467 |
4.33e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 60.43 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 330 GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLE--------VAYFDQH----RaD 393
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDgediTHLPmhkrarlgIGYLPQEasifR-K 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 394 LdperTVMDNL---AEgKQEVMVNGRPRHVLGYLQDF-LFHPKRamTPVKALSGGERNRLLLAK-LFLKPSNLLiLDEP 467
Cdd:COG1137 93 L----TVEDNIlavLE-LRKLSKKEREERLEELLEEFgITHLRK--SKAYSLSGGERRRVEIARaLATNPKFIL-LDEP 163
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-231 |
4.47e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.21 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 18 LLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEqdlivarlqqdpprniGGSVFDFVAEGVAEQAEH 97
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN----------------GQPMSKLSSAAKAELRNQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 98 -LKAYHAISHLVESDPSEKNLArmaqiMEIL-DHQGLWQLDSRISEVLLQLGLNGDAE--LSSLSGGWLRKAALGRALVS 173
Cdd:PRK11629 88 kLGFIYQFHHLLPDFTALENVA-----MPLLiGKKKPAEINSRALEMLAAVGLEHRANhrPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505190249 174 SPRVLLLDEPTNHLDIETIDWLEGFLKEFD----GSIVFISHDRSFIRNMaTRIVDLDRGKL 231
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-232 |
4.87e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.89 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 6 MSGAWLSFSDAplLDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGKEIPlDDGRVIYEQDLIVARLQQDPP---RNIGg 81
Cdd:PRK10908 7 VSKAYLGGRQA--LQGVTFHMRPGEMAFLTGHSGAGKSTLLKlICGIERP-SAGKIWFSGHDITRLKNREVPflrRQIG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 82 SVFdfvaegvaeQAEHL----KAYHAIS-HLVESDPSEKNLARmaqimeildhqglwqldsRISEVLLQLGLNGDAE--L 154
Cdd:PRK10908 83 MIF---------QDHHLlmdrTVYDNVAiPLIIAGASGDDIRR------------------RVSAALDKVGLLDKAKnfP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 155 SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDG---SIVFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
.
gi 505190249 232 V 232
Cdd:PRK10908 216 H 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-232 |
5.00e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 60.83 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQ-DLIVARLQQDPPRNIGGSVFDFVAEGVAEQAEH 97
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvDITDKKVKLSDIRKKVGLVFQYPEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 98 LKAYHAISHLVESDPSEKNlaRMAQIMEI--LDHQGLwqldsrisevllqlglnGDAELSSLSGGWLRKAALGRALVSSP 175
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIEN--RVKRAMNIvgLDYEDY-----------------KDKSPFELSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505190249 176 RVLLLDEPTNHLDIETIDWLEGFLK----EFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKelhkEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-472 |
5.35e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.89 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHcgtklevayFDQHRADLDP---- 396
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVL---------WDGEPLDPEDrrri 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 397 -----ER------TVMDNL-----------AEGKQEVMVngrprhvlgYLQDF-LfhPKRAMTPVKALSGGERNRL-LLA 452
Cdd:COG4152 74 gylpeERglypkmKVGEQLvylarlkglskAEAKRRADE---------WLERLgL--GDRANKKVEELSKGNQQKVqLIA 142
|
170 180
....*....|....*....|
gi 505190249 453 KLFLKPSnLLILDEPTNDLD 472
Cdd:COG4152 143 ALLHDPE-LLILDEPFSGLD 161
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
315-473 |
6.27e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.90 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 315 SGKIVFEleDVNYQV-GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLM-------LGQLKAD----------SGRV 376
Cdd:PRK13657 332 KGAVEFD--DVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILIDgtdirtvtraSLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 377 HCGTKLEVA-YFDqhradldpeRTVMDNLAEGK-----QEVMVNGRPRHVLgylqDFLF-HPKRAMTPV----KALSGGE 445
Cdd:PRK13657 410 NIAVVFQDAgLFN---------RSIEDNIRVGRpdatdEEMRAAAERAQAH----DFIErKPDGYDTVVgergRQLSGGE 476
|
170 180
....*....|....*....|....*...
gi 505190249 446 RNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDV 504
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-188 |
6.27e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.10 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 18 LLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIyeqdlivarlqqdpprnIGGsvfdfvaEGVAEQAEH 97
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL-----------------IDG-------KDVTKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 98 LKAYHaISHlVESDPS---------EKNLA-----------RMAqimeiLDHQGLWQLDSRISEvlLQLGLNG--DAELS 155
Cdd:COG1101 77 KRAKY-IGR-VFQDPMmgtapsmtiEENLAlayrrgkrrglRRG-----LTKKRRELFRELLAT--LGLGLENrlDTKVG 147
|
170 180 190
....*....|....*....|....*....|....
gi 505190249 156 SLSGGWlRKA-ALGRALVSSPRVLLLDEPTNHLD 188
Cdd:COG1101 148 LLSGGQ-RQAlSLLMATLTKPKLLLLDEHTAALD 180
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-232 |
6.65e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.51 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQdlivARLQQDPPRNIGgsvfdFVAE-- 89
Cdd:COG4152 10 RFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG----EPLDPEDRRRIG-----YLPEer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 90 ------GVAEQAEHLKAYHAIShlvesdpseKNLARmAQIMEILDhqglwqldsrisevLLQLGLNGDAELSSLSGGWLR 163
Cdd:COG4152 81 glypkmKVGEQLVYLARLKGLS---------KAEAK-RRADEWLE--------------RLGLGDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505190249 164 KAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DG-SIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGtTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-230 |
7.82e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.12 E-value: 7.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPlDDGRVIYE-QDliVARLqqdPP-- 76
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIaGFETP-DSGRIMLDgQD--ITHV---PAen 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 77 RNIGG-----------SVFDFVAEGVaeqaehlkayhaishlvesdpseknlaRMAQIMEIldhqglwQLDSRISEVL-- 143
Cdd:PRK09452 86 RHVNTvfqsyalfphmTVFENVAFGL---------------------------RMQKTPAA-------EITPRVMEALrm 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 144 LQLGLNGDAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLD--------IEtidwLEGFLKEFDGSIVFISHDRSF 215
Cdd:PRK09452 132 VQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrkqmqNE----LKALQRKLGITFVFVTHDQEE 207
|
250
....*....|....*
gi 505190249 216 IRNMATRIVDLDRGK 230
Cdd:PRK09452 208 ALTMSDRIVVMRDGR 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-250 |
7.95e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 59.38 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 25 HIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE-QDLI--------VARLQQDppRNIGG--SVFDFVAEGVae 93
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgQDLTalppaerpVSMLFQE--NNLFPhlTVAQNIGLGL-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 94 qaehlkayhaishlvesDPSEK-NLARMAQIMEILDHQGLWQLDSRISEvllqlglngdaelsSLSGGWLRKAALGRALV 172
Cdd:COG3840 97 -----------------RPGLKlTAEQRAQVEQALERVGLAGLLDRLPG--------------QLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 173 SSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKlVSWPGNYDLYLQSK-EE 247
Cdd:COG3840 146 RKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGR-IAADGPTAALLDGEpPP 224
|
...
gi 505190249 248 ALR 250
Cdd:COG3840 225 ALA 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-239 |
9.90e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.49 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 26 IEDNERVCLVGRNGAGKSTLLKIL--------GK-EIpldDGRVIYEQdlivarlQQDPPRNIGgSVFdfvaeG------ 90
Cdd:COG4586 45 IEPGEIVGFIGPNGAGKSTTIKMLtgilvptsGEvRV---LGYVPFKR-------RKEFARRIG-VVF-----Gqrsqlw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 91 ----VAEQAEHLKAYHAIshlvesDPSE--KNLARMAQIMEILDhqglwQLDSRISEvlLQLGLNGDAELsslsggwlrk 164
Cdd:COG4586 109 wdlpAIDSFRLLKAIYRI------PDAEykKRLDELVELLDLGE-----LLDTPVRQ--LSLGQRMRCEL---------- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 165 AAlgrALVSSPRVLLLDEPTNHLDIETIDWLEGFLKE----FDGSIVFISHDRSFIRNMATRIVDLDRGKLVswpgnYD 239
Cdd:COG4586 166 AA---ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynreRGTTILLTSHDMDDIEALCDRVIVIDHGRII-----YD 236
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
335-473 |
1.03e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 60.52 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 335 VRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLEVAYFDQHRAD-----------LDPERT 399
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqdiTGLSGRELRPLRRRmqmvfqdpyasLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 400 VMDNLAEG--------KQEV---------MVNGRPRHVLGYLQDFlfhpkramtpvkalSGGERNRLLLAK-LFLKPSnL 461
Cdd:COG4608 114 VGDIIAEPlrihglasKAERrervaelleLVGLRPEHADRYPHEF--------------SGGQRQRIGIARaLALNPK-L 178
|
170
....*....|..
gi 505190249 462 LILDEPTNDLDV 473
Cdd:COG4608 179 IVCDEPVSALDV 190
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-243 |
1.28e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.12 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPLDDGRVIYEQDLIVARLQQdppRNIGgSVFdfvaeg 90
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVaGLEKPTEGQIFIDGEDVTHRSIQQ---RDIC-MVF------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 91 vaeqaehlKAYHAISHLVESDPSEKNLaRMaqimeildhQGL--WQLDSRISEVLLQLGLNG--DAELSSLSGGWLRKAA 166
Cdd:PRK11432 85 --------QSYALFPHMSLGENVGYGL-KM---------LGVpkEERKQRVKEALELVDLAGfeDRYVDQISGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 167 LGRALVSSPRVLLLDEPTNHLDI-------ETIDWLEgflKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPGNYD 239
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQ---QQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
....
gi 505190249 240 LYLQ 243
Cdd:PRK11432 224 LYRQ 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
339-472 |
1.43e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 60.23 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 339 SAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKLE--------VAYFDQHRAdLDPERTVMDNLAEG-K 408
Cdd:PRK11607 39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdGVDLShvppyqrpINMMFQSYA-LFPHMTVEQNIAFGlK 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 409 QEVM----VNGRPRHVLG--YLQDFlfhpkrAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11607 118 QDKLpkaeIASRVNEMLGlvHMQEF------AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-229 |
1.49e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.98 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 14 SDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL------GkeipldDGRVIYEQDLIVARLQQDP--PrniGGSvfd 85
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpyG------SGRIARPAGARVLFLPQRPylP---LGT--- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 86 fvaegvaeqaehLKAyhAISH-LVESDPSEknlarmAQIMEILDHQGLWQLDSRISEVLlqlglNGDAELSslsGGWLRK 164
Cdd:COG4178 442 ------------LRE--ALLYpATAEAFSD------AELREALEAVGLGHLAERLDEEA-----DWDQVLS---LGEQQR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 165 AALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKE--FDGSIVFISHdRSFIRNMATRIVDLDRG 229
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-234 |
1.51e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 58.19 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 17 PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDLIVARLQ----------QDPprniggSVFd 85
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeIDGIDISTIPLEdlrssltiipQDP------TLF- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 86 fvaegvaeqaehlkayhaiSHLVESDPSEKNLARMAQIMEILdhqglwqldsRISEVllqlGLNgdaelssLSGGWLRKA 165
Cdd:cd03369 95 -------------------SGTIRSNLDPFDEYSDEEIYGAL----------RVSEG----GLN-------LSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505190249 166 ALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFL-KEFDGS-IVFISHDRSFIRNMAtRIVDLDRGKLVSW 234
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIrEEFTNStILTIAHRLRTIIDYD-KILVMDAGEVKEY 204
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
344-500 |
1.54e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.00 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 344 RGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtklevayfdqhradldpertvmdnlaegkqeVMVNGRPRHvlgY 423
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----------------------------------IYIDGEDIL---E 43
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 424 LQDFLFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELIDGYQGTVLLVSHDRQFV 500
Cdd:smart00382 44 EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
321-472 |
1.58e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.94 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC------GTKLEVAYFDQHRAdL 394
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpveGPGAERGVVFQNEG-L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 DPERTVMDNLAEGKQEVMVNGRPRHVLGylQDFL-------FHPKRamtpVKALSGGERNRLLLAKLFLKPSNLLILDEP 467
Cdd:PRK11248 82 LPWRNVQDNVAFGLQLAGVEKMQRLEIA--HQMLkkvglegAEKRY----IWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
....*
gi 505190249 468 TNDLD 472
Cdd:PRK11248 156 FGALD 160
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
316-501 |
1.59e-09 |
|
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: 58.64 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 316 GKIVFELEDVNYQVGEKVLV-RGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV----HCGTKLEVAYFDQH 390
Cdd:cd03248 10 GIVKFQNVTFAYPTRPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 391 RADLDPE-----RTVMDNLAEGKQ-----EVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGGERNRLLLAKLFL 456
Cdd:cd03248 90 VSLVGQEpvlfaRSLQDNIAYGLQscsfeCVKEAAQKAHAHSFISEL---ASGYDTEVgekgSQLSGGQKQRVAIARALI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505190249 457 KPSNLLILDEPTNDLDVETLELLEELIdgYQG----TVLLVSHDRQFVD 501
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQAL--YDWperrTVLVIAHRLSTVE 213
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
316-503 |
1.78e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 60.89 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 316 GKIVFELEDVNYQVGEKVLV-RGFSAQVQRGDKIALVGPNGCGKTTLLKLML-------GQLKADSGRVhcgTKLEVAYF 387
Cdd:TIGR00958 477 GLIEFQDVSFSYPNRPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQnlyqptgGQVLLDGVPL---VQYDHHYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 388 DQHRADLDPE-----RTVMDNLAEG-----KQEVMVNGRPRHVLGYLQDFlfhPKRAMTPVKA----LSGGERNRLLLAK 453
Cdd:TIGR00958 554 HRQVALVGQEpvlfsGSVRENIAYGltdtpDEEIMAAAKAANAHDFIMEF---PNGYDTEVGEkgsqLSGGQKQRIAIAR 630
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505190249 454 LFLKPSNLLILDEPTNDLDVETLELLEELIDGYQGTVLLVSHDRQFVDNS 503
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERA 680
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-245 |
1.81e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.02 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEqDLIVARLQQD----PPRNIGGSVFDFVaegvaeq 94
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDkyirPVRKRIGMVFQFP------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 95 aehlkayhaishlvESDPSEKNLARmaqimEILD-----HQGLWQLDSRISEVLLQLGLNGDAELSS---LSGGWLRKAA 166
Cdd:PRK13646 95 --------------ESQLFEDTVER-----EIIFgpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQSpfqMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 167 LGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF----DGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPGNYDLYL 242
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqtdeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
...
gi 505190249 243 QSK 245
Cdd:PRK13646 236 DKK 238
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
307-467 |
2.29e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 57.48 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 307 MQVEEAT-----RSGKIVFELEDVNYQVgekvlvrgfsaqvQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTK 381
Cdd:cd03250 1 ISVEDASftwdsGEQETSFTLKDINLEV-------------PKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 382 leVAYFDQ----HRAdldperTVMDNLAEGKQevMVNGRPRHVL---GYLQDFLFHPKRAMTPVK----ALSGGERNRLL 450
Cdd:cd03250 68 --IAYVSQepwiQNG------TIRENILFGKP--FDEERYEKVIkacALEPDLEILPDGDLTEIGekgiNLSGGQKQRIS 137
|
170
....*....|....*..
gi 505190249 451 LAKLFLKPSNLLILDEP 467
Cdd:cd03250 138 LARAVYSDADIYLLDDP 154
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
322-472 |
3.17e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.27 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 322 LEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKL---------EVAYFDQHRA 392
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRmndvppaerGVGMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 393 dLDPERTVMDNLAEG-------KQEvmVNGRPRHVLGYLQ-DFLFHPKramtPvKALSGGERNRLLLAKLFLKPSNLLIL 464
Cdd:PRK11000 86 -LYPHLSVAENMSFGlklagakKEE--INQRVNQVAEVLQlAHLLDRK----P-KALSGGQRQRVAIGRTLVAEPSVFLL 157
|
....*...
gi 505190249 465 DEPTNDLD 472
Cdd:PRK11000 158 DEPLSNLD 165
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
332-472 |
3.19e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.82 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 332 KVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-----------------GTKLEVAYFDQHRADL 394
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpagarvlflpqrpylplGTLREALLYPATAEAF 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 DPE--RTVMDnlaegkqevMVNgrprhvLGYLQDFLFHPKRAMtpvKALSGGERNRLLLAKLFL-KPSnLLILDEPTNDL 471
Cdd:COG4178 456 SDAelREALE---------AVG------LGHLAERLDEEADWD---QVLSLGEQQRLAFARLLLhKPD-WLFLDEATSAL 516
|
.
gi 505190249 472 D 472
Cdd:COG4178 517 D 517
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-232 |
3.37e-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: 59.82 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEqdlivarlqqdpprnIGGSVFDFVAEGVAEQAEhL 98
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR---------------VGDEWVDMTKPGPDGRGR-A 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 99 KAYHAISH--------------LVESDPSE--KNLARMAQIMeILDHQGLwqLDSRISEVLlqlglngDAELSSLSGGWL 162
Cdd:TIGR03269 364 KRYIGILHqeydlyphrtvldnLTEAIGLElpDELARMKAVI-TLKMVGF--DEEKAEEIL-------DKYPDELSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505190249 163 RKAALGRALVSSPRVLLLDEPTNHLD-IETIDWLEGFLK---EFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILKareEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-233 |
3.77e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.64 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 26 IEDNERVCLVGRNGAGKSTLL-----------KILGKEIPLDDGRViYEQDLIVARL--QQDPPRNIggSVFDFVAEGVA 92
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLarmagllpgsgSIQFAGQPLEAWSA-AELARHRAYLsqQQTPPFAM--PVFQYLTLHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 93 EQAEHLKAYHAISHLVESDPSEKNLARMAQIMEildhQGLWQlDSRISEVLLQLglngdaelsslsggWlrkaalgRALV 172
Cdd:PRK03695 96 DKTRTEAVASALNEVAEALGLDDKLGRSVNQLS----GGEWQ-RVRLAAVVLQV--------------W-------PDIN 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505190249 173 SSPRVLLLDEPTNHLDIETIDWLEGFLKEF---DGSIVFISHDRSFIRNMATRIVDLDRGKLVS 233
Cdd:PRK03695 150 PAGQLLLLDEPMNSLDVAQQAALDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA 213
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
30-232 |
4.19e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.63 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 30 ERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYeqdlivarlqqdppRNIGGSVFDFVAEGVAEQAEHLKAYHAIshlVE 109
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSARLAPDAGEVHY--------------RMRDGQLRDLYALSEAERRRLLRTEWGF---VH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 110 SDPSEKnlARM-----AQIMEILDHQGlWQLDSRI--------SEVLLQLGLNGDAElSSLSGGWLRKAALGRALVSSPR 176
Cdd:PRK11701 96 QHPRDG--LRMqvsagGNIGERLMAVG-ARHYGDIratagdwlERVEIDAARIDDLP-TTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 177 VLLLDEPTNHLDIET----IDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK11701 172 LVFMDEPTGGLDVSVqarlLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-212 |
4.31e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.85 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQD---------LIVAR- 70
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrsrLYTVRk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 71 ----LQQDPPRNIGGSVFDFVAEGVAEQAehlkayhaishlvesdpseknlarmaQIMEILDHqglwqldsriSEVLLQL 146
Cdd:PRK11831 85 rmsmLFQSGALFTDMNVFDNVAYPLREHT--------------------------QLPAPLLH----------STVMMKL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 147 ---GLNGDAEL--SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSI----VFISHD 212
Cdd:PRK11831 129 eavGLRGAAKLmpSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvtcVVVSHD 203
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
11-232 |
4.46e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 57.72 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDLI----------VARLQQDPPRNI 79
Cdd:PRK11231 10 VGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVfLGDKPISmlssrqlarrLALLPQHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 80 GGSVFDFVAEGvaeQAEHLKAYHAIShlvesdpsEKNLARMAQIMEildhqglwqlDSRISEVllqlglnGDAELSSLSG 159
Cdd:PRK11231 90 GITVRELVAYG---RSPWLSLWGRLS--------AEDNARVNQAME----------QTRINHL-------ADRRLTDLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 160 GWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDwLEGFLKEFDGSIVFISHDrsfiRNMATRIVD----LDRGKL 231
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDInhqvELMR-LMRELNTQGKTVVTVLHD----LNQASRYCDhlvvLANGHV 216
|
.
gi 505190249 232 V 232
Cdd:PRK11231 217 M 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-190 |
5.55e-09 |
|
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: 57.03 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRNiGGSVFDFVAEGVAEQAEHl 98
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADY-EGTVRDLLSSITKDFYTH- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 99 kAYHaishlvesdpsEKNLARMAQIMEILDHQglwqldsrisevllqlglngdaeLSSLSGGWLRKAALGRALVSSPRVL 178
Cdd:cd03237 93 -PYF-----------KTEIAKPLQIEQILDRE-----------------------VPELSGGELQRVAIAACLSKDADIY 137
|
170
....*....|..
gi 505190249 179 LLDEPTNHLDIE 190
Cdd:cd03237 138 LLDEPSAYLDVE 149
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
155-231 |
5.80e-09 |
|
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: 55.90 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 155 SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DG-SIVFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:cd03215 103 SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELadAGkAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
349-498 |
6.00e-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: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 349 ALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GT--------------KLEVAYFDQhRADLDPERTVMDNLAEGKQEVMV 413
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLnGRtlfdsrkgiflppeKRRIGYVFQ-EARLFPHLSVRGNLRYGMKRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 414 ---NGRPRHVLGYLQdfLFHPKRamTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELI----DGY 486
Cdd:TIGR02142 106 serRISFERVIELLG--IGHLLG--RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLerlhAEF 181
|
170
....*....|..
gi 505190249 487 QGTVLLVSHDRQ 498
Cdd:TIGR02142 182 GIPILYVSHSLQ 193
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
311-498 |
6.09e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.36 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 311 EATRSGKIVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKleVAYFDQH 390
Cdd:PRK14246 2 EAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK--VLYFGKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 391 RADLD------------------PERTVMDNLAEGKQEVMVNGRpRHVLGYLQDFLFHP-------KRAMTPVKALSGGE 445
Cdd:PRK14246 80 IFQIDaiklrkevgmvfqqpnpfPHLSIYDNIAYPLKSHGIKEK-REIKKIVEECLRKVglwkevyDRLNSPASQLSGGQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505190249 446 RNRLLLAK-LFLKPSnLLILDEPTNDLDVETLELLEELIDGYQG--TVLLVSHDRQ 498
Cdd:PRK14246 159 QQRLTIARaLALKPK-VLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQ 213
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-226 |
6.28e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 57.35 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLD-----DGRV------IYEQDLIVARLQQD----- 74
Cdd:PRK14258 15 FYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVeffnqnIYERRVNLNRLRRQvsmvh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 75 -PPRNIGGSVFDFVAEGVAEQAEHLKAyhAISHLVESdpseknlarmaqimeILDHQGLW-QLDSRISEVLLQlglngda 152
Cdd:PRK14258 95 pKPNLFPMSVYDNVAYGVKIVGWRPKL--EIDDIVES---------------ALKDADLWdEIKHKIHKSALD------- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 153 elssLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF----DGSIVFISHDRSFIrnmaTRIVDL 226
Cdd:PRK14258 151 ----LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHNLHQV----SRLSDF 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
321-497 |
7.10e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.81 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLEVAYFD-----QHR 391
Cdd:PRK11432 8 VLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgedvTHRSIQQRDicmvfQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 392 AdLDPERTVMDNLAEG-------KQEvmVNGRPRHVLGyLQDFLFHPKRAmtpVKALSGGERNRLLLAK-LFLKPSNLLi 463
Cdd:PRK11432 88 A-LFPHMSLGENVGYGlkmlgvpKEE--RKQRVKEALE-LVDLAGFEDRY---VDQISGGQQQRVALARaLILKPKVLL- 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 505190249 464 LDEPTNDLDVETLELLEELIDGYQG----TVLLVSHDR 497
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQqfniTSLYVTHDQ 197
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
331-472 |
8.14e-09 |
|
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: 56.12 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 331 EKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKAD---SGRVHCGTKLEVAYFDQHRADL---------DPER 398
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIiyvseedvhFPTL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 399 TV---MDNLAEGKQEVMVNGrprhvlgylqdflfhpkramtpvkaLSGGERNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03233 99 TVretLDFALRCKGNEFVRG-------------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
318-472 |
8.33e-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: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 318 IVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKLEVAYFDQHRADLDP 396
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 397 --------ERTVMDNLAEGKQevmvnGRPRHVLGYL------QDFLFH-PKRAMTPV----KALSGGERNRLLLAKLFLK 457
Cdd:cd03252 81 vlqenvlfNRSIRDNIALADP-----GMSMERVIEAaklagaHDFISElPEGYDTIVgeqgAGLSGGQRQRIAIARALIH 155
|
170
....*....|....*
gi 505190249 458 PSNLLILDEPTNDLD 472
Cdd:cd03252 156 NPRILIFDEATSALD 170
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-239 |
8.80e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.32 E-value: 8.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTL-------------LKILG---KEIPLDDGRviyEQdliVARLQQD 74
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLlnallgflpyqgsLKINGielRELDPESWR---KH---LSWVGQN 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 75 PpRNIGGSVFDFVAEGvAEQAehlkayhaishlveSDPSEKNLARMAQIMEILDHQGLwQLDSRISEvllqlglngdaEL 154
Cdd:PRK11174 432 P-QLPHGTLRDNVLLG-NPDA--------------SDEQLQQALENAWVSEFLPLLPQ-GLDTPIGD-----------QA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 155 SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKE--FDGSIVFISHDRSFIRNMATrIVDLDRGKLV 232
Cdd:PRK11174 484 AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAasRRQTTLMVTHQLEDLAQWDQ-IWVMQDGQIV 562
|
....*..
gi 505190249 233 SwPGNYD 239
Cdd:PRK11174 563 Q-QGDYA 568
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
330-500 |
1.06e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 56.62 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 330 GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKLEVAYFDQHRA--------------DL 394
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWrGEPLAKLNRAQRKAfrrdiqmvfqdsisAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 DPERTVMDNLAEGKQEVMV---NGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:PRK10419 103 NPRKTVREIIREPLRHLLSldkAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190
....*....|....*....|....*....|...
gi 505190249 472 DVETLELLEELIDGYQ---GTV-LLVSHDRQFV 500
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQqqfGTAcLFITHDLRLV 215
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
15-228 |
1.14e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 55.57 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 15 DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLD---DGRVIY-EQDL----IVAR----LQQDPPRNIGGS 82
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLnGRRLtalpAEQRrigiLFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 VFDFVAEGVAeqaehlkayhaishlvesdPSEKNLARMAQIMEILDhqglwqldsrisevllQLGLNG--DAELSSLSGG 160
Cdd:COG4136 93 VGENLAFALP-------------------PTIGRAQRRARVEQALE----------------EAGLAGfaDRDPATLSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505190249 161 WLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGF----LKEFDGSIVFISHDRSFIRNmATRIVDLDR 228
Cdd:COG4136 138 QRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
319-472 |
1.36e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 56.56 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 319 VFELEDVNYQV--GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKLEVAYFDQHRADL- 394
Cdd:PRK13635 5 IIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVgGMVLSEETVWDVRRQVg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 ----DPER-----TVMDNLAEGKQEvmvNGRPR-----------HVLGyLQDFLFH-PKRamtpvkaLSGGERNRLLLAK 453
Cdd:PRK13635 85 mvfqNPDNqfvgaTVQDDVAFGLEN---IGVPReemvervdqalRQVG-MEDFLNRePHR-------LSGGQKQRVAIAG 153
|
170 180
....*....|....*....|
gi 505190249 454 -LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13635 154 vLALQPD-IIILDEATSMLD 172
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-212 |
1.39e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.56 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 18 LLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKeipLDDGrviyeqdlivarlQQDPPRNIGGSVFDFVAEGVAE-QAE 96
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAG---LDDG-------------SSGEVSLVGQPLHQMDEEARAKlRAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 97 HLKAYHAISHLVESDPSEKNLarmaQIMEILDHQGLWQLDSRISEVLLQLGLNG--DAELSSLSGGWLRKAALGRALVSS 174
Cdd:PRK10584 89 HVGFVFQSFMLIPTLNALENV----ELPALLRGESSRQSRNGAKALLEQLGLGKrlDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505190249 175 PRVLLLDEPTNHLDIETIDWLEGFL----KEFDGSIVFISHD 212
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-184 |
1.39e-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: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVarlqQDPPRNIggsvfdfVAEGVAEQAEHL 98
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT----DWQTAKI-------MREAVAIVPEGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 99 KAYHAIShlvesdpSEKNLArMAQIMEilDHQGLWQLDSRISEVLLQLGLNGDAELSSLSGGWLRKAALGRALVSSPRVL 178
Cdd:PRK11614 90 RVFSRMT-------VEENLA-MGGFFA--ERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
....*.
gi 505190249 179 LLDEPT 184
Cdd:PRK11614 160 LLDEPS 165
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-232 |
1.48e-08 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 55.62 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 15 DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-------GKEIPLDdGRVIYEQDL-----IVARLQQDP------- 75
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEILLD-GVDIRDLNLrwlrsQIGLVSQEPvlfdgti 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 76 PRNIGGSVFDFVAEGVAEQAEHLKAYHAISHLVEsdpseknlarmaqimeildhqglwQLDSRIsevllqlGLNGdaelS 155
Cdd:cd03249 94 AENIRYGKPDATDEEVEEAAKKANIHDFIMSLPD------------------------GYDTLV-------GERG----S 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 156 SLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET----IDWLEGFLKEFdgSIVFISHDRSFIRNmATRIVDLDRGKL 231
Cdd:cd03249 139 QLSGGQKQRIAIARALLRNPKILLLDEATSALDAESeklvQEALDRAMKGR--TTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
.
gi 505190249 232 V 232
Cdd:cd03249 216 V 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-227 |
1.54e-08 |
|
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: 54.47 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 14 SDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYeqdlivarlqqdPPRNiggSVFdFVAEgvae 93
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM------------PEGE---DLL-FLPQ---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 94 qaehlKAYHAISHLvesdpseknlarmaqiMEILDHqgLWQldsrisevllqlglngdaelSSLSGGWLRKAALGRALVS 173
Cdd:cd03223 72 -----RPYLPLGTL----------------REQLIY--PWD--------------------DVLSGGEQQRLAFARLLLH 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505190249 174 SPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSIVFISHdRSFIRNMATRIVDLD 227
Cdd:cd03223 109 KPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-233 |
1.56e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 18 LLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLD--------------DGRVIYEQD-LIVARLQ----QDPPRN 78
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvtgdvtlNGEPLAAIDaPRLARLRavlpQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 79 IGGSVFDFVAEGvaeQAEHLKAYHAISHlvesdpSEKNLARMAqimeiLDHQGLWQLDSRisevllqlglngdaELSSLS 158
Cdd:PRK13547 96 FAFSAREIVLLG---RYPHARRAGALTH------RDGEIAWQA-----LALAGATALVGR--------------DVTTLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 159 GGWLRKAALGRAL---------VSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVD 225
Cdd:PRK13547 148 GGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLahqhRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAM 227
|
....*...
gi 505190249 226 LDRGKLVS 233
Cdd:PRK13547 228 LADGAIVA 235
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
319-472 |
2.01e-08 |
|
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: 54.56 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 319 VFELEDVNYQV----GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMlgqlkadSGRVHCGTklevayfdqhradl 394
Cdd:cd03232 3 VLTWKNLNYTVpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL-------AGRKTAGV-------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 dpertvmdnlAEGkqEVMVNGRP-----RHVLGYLQDFLFHPK--------RAMTPVKALSGGERNRLLLA-KLFLKPSn 460
Cdd:cd03232 62 ----------ITG--EILINGRPldknfQRSTGYVEQQDVHSPnltvrealRFSALLRGLSVEQRKRLTIGvELAAKPS- 128
|
170
....*....|..
gi 505190249 461 LLILDEPTNDLD 472
Cdd:cd03232 129 ILFLDEPTSGLD 140
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
330-500 |
2.02e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.65 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 330 GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHcgTKLEVAYFDQhRADLDPErTVMDNLAEGKQ 409
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH--MKGSVAYVPQ-QAWIQND-SLRENILFGKA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 410 evMVNGRPRHVL---GYLQDFLFHPKRAMTPVKA----LSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEEL 482
Cdd:TIGR00957 725 --LNEKYYQQVLeacALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802
|
170 180
....*....|....*....|...
gi 505190249 483 IDGYQG-----TVLLVSHDRQFV 500
Cdd:TIGR00957 803 VIGPEGvlknkTRILVTHGISYL 825
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
332-472 |
2.09e-08 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 55.24 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 332 KVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLEVAYFDQHRADLDPE-----RTVMD 402
Cdd:cd03249 17 PIL-KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDgvdiRDLNLRWLRSQIGLVSQEpvlfdGTIAE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 403 NLAEGK---QEVMVNGRPRhvLGYLQDFLFH-PKRAMTPVKA----LSGGERNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03249 96 NIRYGKpdaTDEEVEEAAK--KANIHDFIMSlPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-237 |
2.14e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.25 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 20 DNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIY-EQDLI-------------VARLQQDP-----PR-NI 79
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlGKDLLgmkddewravrsdIQMIFQDPlaslnPRmTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 80 GgsvfDFVAEGvaeqaehLKAYHAishlvesdpsekNLARmAQIMEildhqglwqldsRISEVLLQLGLngdaeLSSL-- 157
Cdd:PRK15079 118 G----EIIAEP-------LRTYHP------------KLSR-QEVKD------------RVKAMMLKVGL-----LPNLin 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 158 ------SGGWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIvdld 227
Cdd:PRK15079 157 ryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVsiqaQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRV---- 232
|
250
....*....|
gi 505190249 228 rgkLVSWPGN 237
Cdd:PRK15079 233 ---LVMYLGH 239
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-232 |
2.22e-08 |
|
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: 55.73 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 26 IEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE-QDLIV---ARLQQDPPRNIG-----------GSVFDFVA-- 88
Cdd:cd03294 47 VREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgQDIAAmsrKELRELRRKKISmvfqsfallphRTVLENVAfg 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 89 ---EGVAEQAEHLKAyhaishlvesdpseknlarmaqimeildhqglwqldsriSEVLLQLGLNGDAE--LSSLSGGWLR 163
Cdd:cd03294 127 levQGVPRAEREERA---------------------------------------AEALELVGLEGWEHkyPDELSGGMQQ 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505190249 164 KAALGRALVSSPRVLLLDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:cd03294 168 RVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
321-472 |
2.74e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.25 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLML-------GQLK---ADSGRVHCGTKlEVAYFDQH 390
Cdd:PRK10851 4 EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAglehqtsGHIRfhgTDVSRLHARDR-KVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 391 RAdLDPERTVMDNLAEGKQEVMVNGRP-RHVLGY----LQDFLFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILD 465
Cdd:PRK10851 83 YA-LFRHMTVFDNIAFGLTVLPRRERPnAAAIKAkvtqLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
....*..
gi 505190249 466 EPTNDLD 472
Cdd:PRK10851 162 EPFGALD 168
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-229 |
2.77e-08 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 54.78 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPlDDGRVIYEQDLIVArlqQDPPRNIGGSVFDFVAEGVAEQAEH 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLIsGLAQP-TSGGVILEGKQITE---PGPDRMVVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 98 LKAYHAISHLVESDpseknlaRMAQIMEILDhqglwqldsrisevLLQLGLNGDAELSSLSGGWLRKAALGRALVSSPRV 177
Cdd:TIGR01184 77 LAVDRVLPDLSKSE-------RRAIVEEHIA--------------LVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505190249 178 LLLDEPTNHLDIETIDWLEGFL----KEFDGSIVFISHDRSFIRNMATRIVDLDRG 229
Cdd:TIGR01184 136 LLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-188 |
3.77e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.61 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGR--VIYEQDLIVARLQQdpprnigg 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitVLGVPVPARARLAR-------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 82 svfdfVAEGVAEQAEHLKAYHAIshlvesdpsEKNLarmaqimeiLDHQGLWQLDSRISEVLL-------QLGLNGDAEL 154
Cdd:PRK13536 114 -----ARIGVVPQFDNLDLEFTV---------RENL---------LVFGRYFGMSTREIEAVIpsllefaRLESKADARV 170
|
170 180 190
....*....|....*....|....*....|....
gi 505190249 155 SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLD 188
Cdd:PRK13536 171 SDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
157-473 |
3.96e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 157 LSGGWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 233 SWPGNYDL-------YLQSKEEAL-RVEELQNAEFDRKLAqeevWIRQGIKARRTRnegrvralkalrvERSQRREVMGT 304
Cdd:PRK10261 249 ETGSVEQIfhapqhpYTRALLAAVpQLGAMKGLDYPRRFP----LISLEHPAKQEP-------------PIEQDTVVDGE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 305 AKMQVEEAT-----RSGKIvfeledvNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTT----LLKLM---LGQLKAD 372
Cdd:PRK10261 312 PILQVRNLVtrfplRSGLL-------NRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVesqGGEIIFN 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 373 SGRVHC--GTKLEVA------YFDQHRADLDPERTVMDNLAEG-KQEVMVNGRP--RHVLGYLQDFLFHPKRAMTPVKAL 441
Cdd:PRK10261 385 GQRIDTlsPGKLQALrrdiqfIFQDPYASLDPRQTVGDSIMEPlRVHGLLPGKAaaARVAWLLERVGLLPEHAWRYPHEF 464
|
330 340 350
....*....|....*....|....*....|...
gi 505190249 442 SGGERNRLLLAK-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK10261 465 SGGQRQRICIARaLALNP-KVIIADEAVSALDV 496
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
349-467 |
4.63e-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: 55.49 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 349 ALVGPNGCGKTTLLKLMLGQLKADSGRVHCGtklEVAYFDQHR-----------------ADLDPERTVMDNLAEG-KQE 410
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLG---GEVLQDSARgiflpphrrrigyvfqeARLFPHLSVRGNLLYGrKRA 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505190249 411 VMVNGRPRH-----VLGyLQDFLfhpKRAMTpvkALSGGERNRLLLAK-LFLKPSnLLILDEP 467
Cdd:COG4148 106 PRAERRISFdevveLLG-IGHLL---DRRPA---TLSGGERQRVAIGRaLLSSPR-LLLMDEP 160
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-183 |
4.90e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 54.09 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 17 PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIV-------AR-----LQQDPprniggSVF 84
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITklpmhkrARlgigyLPQEA------SIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 85 D--FVAE---GVAEQAEHLKAYhaishlvesdpseknlaRMAQIMEILDhqglwqlDSRISEVLLQLGlngdaelSSLSG 159
Cdd:cd03218 88 RklTVEEnilAVLEIRGLSKKE-----------------REEKLEELLE-------EFHITHLRKSKA-------SSLSG 136
|
170 180
....*....|....*....|....
gi 505190249 160 GWLRKAALGRALVSSPRVLLLDEP 183
Cdd:cd03218 137 GERRRVEIARALATNPKFLLLDEP 160
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-233 |
5.04e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 54.74 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 14 SDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLI-----------VARLQQDPPRN-IGG 81
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteenvwdirhkIGMVFQNPDNQfVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 82 SVFDFVAEGVAEQAehlkayhaishlvesdpseknlarmaqimeiLDHQglwQLDSRISEVLLQLGLNG--DAELSSLSG 159
Cdd:PRK13650 98 TVEDDVAFGLENKG-------------------------------IPHE---EMKERVNEALELVGMQDfkEREPARLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 160 GWLRKAALGRALVSSPRVLLLDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHDRSFIrNMATRIVDLDRGKLVS 233
Cdd:PRK13650 144 GQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVES 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-233 |
5.26e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 54.64 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 15 DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDG------RVIYEQDLIVARLQ-----QDPPRN-IGGS 82
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGtitvggMVLSEETVWDVRRQvgmvfQNPDNQfVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 VFDFVAEGvaeqaehlkayhaishlvesdpseknlarmaqimeiLDHQGLWQLD--SRISEVLLQLGLNG--DAELSSLS 158
Cdd:PRK13635 99 VQDDVAFG------------------------------------LENIGVPREEmvERVDQALRQVGMEDflNREPHRLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 159 GGWLRKAALGRALVSSPRVLLLDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHDRSFIRNmATRIVDLDRGKLVS 233
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
334-513 |
5.36e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.66 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 334 LVRGFSAQVQRGDKIALVGPNGCGKTTLLKlMLGQLKADSGRVHCGTKLEvaYFDQH----RADLDPER----------- 398
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGRVE--FFNQNiyerRVNLNRLRrqvsmvhpkpn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 399 ----TVMDNLAEGKQevMVNGRPRHVLGYLQDFLFHPKRAMTPVK--------ALSGGERNRLLLAK-LFLKPsNLLILD 465
Cdd:PRK14258 99 lfpmSVYDNVAYGVK--IVGWRPKLEIDDIVESALKDADLWDEIKhkihksalDLSGGQQQRLCIARaLAVKP-KVLLMD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505190249 466 EPTNDLDVETLELLEELIDGY----QGTVLLVSHDRQFVDNSVTECWIFEGN 513
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHNLHQVSRLSDFTAFFKGN 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-232 |
5.42e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 54.27 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-------------GkEIPLDdGRVIYEQDLIVARLQqdppR 77
Cdd:COG1117 19 VYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipgarveG-EILLD-GEDIYDPDVDVVELR----R 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 78 NIG----------GSVFDFVAEGvaeqaehLKaYHAIshlvesdpseKNLARMAQIMEI-LDHQGLWqldsriSEV---L 143
Cdd:COG1117 93 RVGmvfqkpnpfpKSIYDNVAYG-------LR-LHGI----------KSKSELDEIVEEsLRKAALW------DEVkdrL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 144 LQLGLngdaelsSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLD------IE-TIDwlEgfLKEfDGSIVFISHdrsfi 216
Cdd:COG1117 149 KKSAL-------GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistakIEeLIL--E--LKK-DYTIVIVTH----- 211
|
250 260
....*....|....*....|..
gi 505190249 217 rNM--ATRIVD----LDRGKLV 232
Cdd:COG1117 212 -NMqqAARVSDytafFYLGELV 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-232 |
5.83e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.61 E-value: 5.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDA-PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEqdlivarlqqdpprniGG 81
Cdd:PRK13644 1 MIRLENVSYSYPDGtPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVS----------------GI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 82 SVFDFvaegvaeqaEHLKAYHAISHLVESDPSEKNLARMAQIMEILDHQGLW----QLDSRISEVLLQLGLNGDAELS-- 155
Cdd:PRK13644 65 DTGDF---------SKLQGIRKLVGIVFQNPETQFVGRTVEEDLAFGPENLClppiEIRKRVDRALAEIGLEKYRHRSpk 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 156 SLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET-IDWLEGF--LKEFDGSIVFISHDRSFIRNmATRIVDLDRGKLV 232
Cdd:PRK13644 136 TLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIkkLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIV 214
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
332-496 |
5.84e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.32 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 332 KVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKAD----SGRVHC-GTKLE--------VAYFDQH-RADLDPE 397
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLdGKPVApcalrgrkIATIMQNpRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 398 RTVMDNLAEGKQEVMVNGRPRHVLGYLQDF-LFHPKRA--MTPVKaLSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVE 474
Cdd:PRK10418 96 HTMHTHARETCLALGKPADDATLTAALEAVgLENAARVlkLYPFE-MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174
|
170 180
....*....|....*....|....*.
gi 505190249 475 TLELLEELIDGYQGT----VLLVSHD 496
Cdd:PRK10418 175 AQARILDLLESIVQKralgMLLVTHD 200
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-232 |
6.10e-08 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 53.77 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 17 PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDliVARLQQDPPRNiggsvfdfvAEGVAEQA 95
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlIDGQD--IREVTLDSLRR---------AIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 96 EHL---KAYHAISH--LVESDPSEKNLARMAQImeildHQGLWQLDSRISEVLLQLGLngdaelsSLSGGWLRKAALGRA 170
Cdd:cd03253 84 TVLfndTIGYNIRYgrPDATDEEVIEAAKAAQI-----HDKIMRFPDGYDTIVGERGL-------KLSGGEKQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505190249 171 LVSSPRVLLLDEPTNHLDIET---IdwLEGFLKEFDG-SIVFISHDRSFIRNmATRIVDLDRGKLV 232
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTereI--QAALRDVSKGrTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
330-472 |
6.23e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.13 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 330 GEKVlVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV------------HCGTKLEVAYFDQhRADLDPE 397
Cdd:PRK10895 15 GRRV-VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplHARARRGIGYLPQ-EASIFRR 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 398 RTVMDNLA---EGKQEVMVNGRPRHVLGYLQDF-LFHPKRAMTpvKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK10895 93 LSVYDNLMavlQIRDDLSAEQREDRANELMEEFhIEHLRDSMG--QSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
321-496 |
6.50e-08 |
|
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: 53.84 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGE-KVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKlEVAYFDQHR-------- 391
Cdd:cd03295 2 EFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE-DIREQDPVElrrkigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 392 ---ADLDPERTVMDNLA-----EGKQEVMVNGRPRHVLGYLqdflfhpkrAMTPVK-------ALSGGERNRLLLAKLFL 456
Cdd:cd03295 81 iqqIGLFPHMTVEENIAlvpklLKWPKEKIRERADELLALV---------GLDPAEfadryphELSGGQQQRVGVARALA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505190249 457 KPSNLLILDEPTNDLDVETLELLEELIDGYQ----GTVLLVSHD 496
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHD 195
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
319-499 |
6.93e-08 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 53.51 E-value: 6.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 319 VFELEDVN--YQVGEKVL--VRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQHRADL 394
Cdd:TIGR02211 1 LLKCENLGkrYQEGKLDTrvLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 D--------------PERTVMDNLAE----GKQEVMVNGRPRHVLgyLQDF-LFHpkRAMTPVKALSGGERNRLLLAKLF 455
Cdd:TIGR02211 81 RnkklgfiyqfhhllPDFTALENVAMplliGKKSVKEAKERAYEM--LEKVgLEH--RINHRPSELSGGERQRVAIARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505190249 456 LKPSNLLILDEPTNDLDVETLELLEELI---DGYQGT-VLLVSHDRQF 499
Cdd:TIGR02211 157 VNQPSLVLADEPTGNLDNNNAKIIFDLMlelNRELNTsFLVVTHDLEL 204
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
341-500 |
7.59e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 53.49 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 341 QVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLE---------------VAYFDQHRADLDPerTVMDNLA 405
Cdd:cd03290 23 RIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKPWLLNA--TVEENIT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 406 EG----KQevmvngRPRHVLG--YLQ---DFLFHPKRAMTPVKA--LSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03290 101 FGspfnKQ------RYKAVTDacSLQpdiDLLPFGDQTEIGERGinLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190
....*....|....*....|....*....|.
gi 505190249 475 TLELLEEL-----IDGYQGTVLLVSHDRQFV 500
Cdd:cd03290 175 LSDHLMQEgilkfLQDDKRTLVLVTHKLQYL 205
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
321-473 |
7.69e-08 |
|
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: 54.67 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELED--VNYQVGEKVL--VRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKA---DSGRV-HCGTKL---------- 382
Cdd:COG0444 3 EVRNlkVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEIlFDGEDLlklsekelrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 383 ----EVAY-FdQhraD----LDPERTVMDNLAE--------GKQEVMvngrpRHVLGYLQDF-LFHPKRAMtpvKA---- 440
Cdd:COG0444 83 irgrEIQMiF-Q---DpmtsLNPVMTVGDQIAEplrihgglSKAEAR-----ERAIELLERVgLPDPERRL---DRyphe 150
|
170 180 190
....*....|....*....|....*....|....
gi 505190249 441 LSGGERNRLLLAK-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG0444 151 LSGGMRQRVMIARaLALEPK-LLIADEPTTALDV 183
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-237 |
9.20e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.97 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLL--------------KILGKEIpldDGRVIYEQDLIVARLQQDPPRNI-GGSV 83
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLlhlngiylpqrgrvKVMGREV---NAENEKWVRSKVGLVFQDPDDQVfSSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 84 FDFVAEGvaeqaehlkayhaishlvesdPSEKNLARMaqimeildhqglwQLDSRISEVLLQLGLNGDAELSS--LSGGW 161
Cdd:PRK13647 98 WDDVAFG---------------------PVNMGLDKD-------------EVERRVEEALKAVRMWDFRDKPPyhLSYGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 162 LRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFIS-HDRSFIRNMATRIVDLDRGKLVSWPGN 237
Cdd:PRK13647 144 KKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhnQGKTVIVAtHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
321-376 |
9.74e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 53.62 E-value: 9.74e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV 376
Cdd:PRK11831 9 DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-212 |
1.22e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.19 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVA----RLQQDPP 76
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGyvpqKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 77 RNIGGSVFDFVAEGVaeqaehlkayhaishlvesdpseknlaRMAQIMEILDHqglwqldsrisevlLQLGLNGDAELSS 156
Cdd:PRK09544 82 LPLTVNRFLRLRPGT---------------------------KKEDILPALKR--------------VQAGHLIDAPMQK 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 157 LSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIE----TIDWLEGFLKEFDGSIVFISHD 212
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNgqvaLYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
30-232 |
1.30e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.71 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 30 ERVCLVGRNGAGKST----LLKILGK--EIPLDDG---RVIYEQDLIV-ARLQ---QDP-----PRNiggSVFDFVAEGV 91
Cdd:PRK15134 313 ETLGLVGESGSGKSTtglaLLRLINSqgEIWFDGQplhNLNRRQLLPVrHRIQvvfQDPnsslnPRL---NVLQIIEEGL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 92 AEQAEHLKAYhaishlvesdpseknlarmaqimeildhqglwQLDSRISEVLLQLGLngDAEL-----SSLSGGWLRKAA 166
Cdd:PRK15134 390 RVHQPTLSAA--------------------------------QREQQVIAVMEEVGL--DPETrhrypAEFSGGQRQRIA 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 167 LGRALVSSPRVLLLDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK15134 436 IARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
330-473 |
1.33e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.45 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 330 GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtklevaYFD----QHRADLDPERTVmDNLA 405
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV---------WLDgehiQHYASKEVARRI-GLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 406 EGK--------QEVMVNGRprhvlgYLQDFLFHPKR-------------------AMTPVKALSGGERNRLLLAKLFLKP 458
Cdd:PRK10253 88 QNAttpgditvQELVARGR------YPHQPLFTRWRkedeeavtkamqatgithlADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170
....*....|....*
gi 505190249 459 SNLLILDEPTNDLDV 473
Cdd:PRK10253 162 TAIMLLDEPTTWLDI 176
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
331-495 |
1.36e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.51 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 331 EKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtklevaYFDqhraDLDP-ERTVmdNLAEGKQ 409
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI---------IID----GVDItDKKV--KLSDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 410 EV-MVNGRPRHVL---GYLQDFLFHP--------------KRAMTPVK------------ALSGGERNRLLLAKLF-LKP 458
Cdd:PRK13637 84 KVgLVFQYPEYQLfeeTIEKDIAFGPinlglseeeienrvKRAMNIVGldyedykdkspfELSGGQKRRVAIAGVVaMEP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505190249 459 SnLLILDEPTNDLDVETLELLEELI----DGYQGTVLLVSH 495
Cdd:PRK13637 164 K-ILILDEPTAGLDPKGRDEILNKIkelhKEYNMTIILVSH 203
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-232 |
1.43e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.21 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 15 DAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPlDDGRVIYEQDLIVARLQQDPPRNIG---GSVFDFVAEG 90
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLnGLHVP-TQGSVRVDDTLITSTSKNKDIKQIRkkvGLVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 91 VAEQAEhLK--AYHAISHLVESDPSEKnLARmaqimEILDHQGlwqldsrISEVLLqlglngDAELSSLSGGWLRKAALG 168
Cdd:PRK13649 98 LFEETV-LKdvAFGPQNFGVSQEEAEA-LAR-----EKLALVG-------ISESLF------EKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 169 RALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGS---IVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgmtIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-250 |
1.47e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 53.27 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 14 SDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-GKEIPLDDGRVIYEQDLI-------------VARLQQDPPRN- 78
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLInGLLLPDDNPNSKITVDGItltaktvwdirekVGIVFQNPDNQf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 79 IGGSVFDFVAEGVAEQAEhlkayhaishlvesdPSEKnlarMAQImeildhqglwqldsrISEVLLQLGLNG--DAELSS 156
Cdd:PRK13640 98 VGATVGDDVAFGLENRAV---------------PRPE----MIKI---------------VRDVLADVGMLDyiDSEPAN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 157 LSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIE----TIDWLEGFLKEFDGSIVFISHDRSFIrNMATRIVDLDRGKLV 232
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAgkeqILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLL 222
|
250
....*....|....*...
gi 505190249 233 SWPGNYDLYlqSKEEALR 250
Cdd:PRK13640 223 AQGSPVEIF--SKVEMLK 238
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
335-473 |
1.55e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 53.56 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 335 VRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTKLEVAYFDQHR--------------ADLDPERT 399
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLGMKDDEWRavrsdiqmifqdplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 400 VMDNLAE---------GKQEVM---------VNGRPRHVLGYLQDFlfhpkramtpvkalSGGERNRLLLAK-LFLKPsN 460
Cdd:PRK15079 117 IGEIIAEplrtyhpklSRQEVKdrvkammlkVGLLPNLINRYPHEF--------------SGGQCQRIGIARaLILEP-K 181
|
170
....*....|...
gi 505190249 461 LLILDEPTNDLDV 473
Cdd:PRK15079 182 LIICDEPVSALDV 194
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
18-193 |
1.58e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.97 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 18 LLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGR-VIYEQDLIVARLQQDPPRNIG-----GSVFdfvaegv 91
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiIIDDEDISLLPLHARARRGIGylpqeASIF------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 92 aeqaEHLKAYH---AISHLVESDPSEKNLARMAQIMEildhqglwqlDSRISEVLLQLGlngdaelSSLSGGWLRKAALG 168
Cdd:PRK10895 91 ----RRLSVYDnlmAVLQIRDDLSAEQREDRANELME----------EFHIEHLRDSMG-------QSLSGGERRRVEIA 149
|
170 180
....*....|....*....|....*.
gi 505190249 169 RALVSSPRVLLLDEPTNHLD-IETID 193
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDpISVID 175
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
24-183 |
1.63e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 52.72 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 24 IHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDL------IVAR-----LQQDPprniggSVFD--FVAE 89
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIfLDGEDIthlpmhKRARlgigyLPQEA------SIFRklTVED 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 90 GVAeqaehlkayhAISHLVESDPSEKNlARMAQIMEILdhqglwqldsRISEVLLQLGlngdaelSSLSGGWLRKAALGR 169
Cdd:COG1137 98 NIL----------AVLELRKLSKKERE-ERLEELLEEF----------GITHLRKSKA-------YSLSGGERRRVEIAR 149
|
170
....*....|....
gi 505190249 170 ALVSSPRVLLLDEP 183
Cdd:COG1137 150 ALATNPKFILLDEP 163
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-224 |
1.67e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 52.94 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSF----SDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVA----R-- 70
Cdd:COG4525 1 MSMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpgadRgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 71 -LQQD---PPRNiggsVFDFVA-----EGVAEQAEHLKAyhaishlvesdpsEKNLARMAqimeiLDHQGlwqlDSRISE 141
Cdd:COG4525 81 vFQKDallPWLN----VLDNVAfglrlRGVPKAERRARA-------------EELLALVG-----LADFA----RRRIWQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 142 vllqlglngdaelssLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFL----KEFDGSIVFISHDRSFIR 217
Cdd:COG4525 135 ---------------LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLldvwQRTGKGVFLITHSVEEAL 199
|
....*..
gi 505190249 218 NMATRIV 224
Cdd:COG4525 200 FLATRLV 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-230 |
1.68e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 52.09 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSD-----APLLDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGkEIPLDDGRVIYE-------QdliVAR 70
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLG-ELEKLSGSVSVPgsiayvsQ---EPW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 71 LQQDPPR-NI-GGSVFDfvaegvaeQAEHLKAYHAiSHLvESDpseknlarmaqiMEILDHQGLwqldsriSEVllqlGL 148
Cdd:cd03250 77 IQNGTIReNIlFGKPFD--------EERYEKVIKA-CAL-EPD------------LEILPDGDL-------TEI----GE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 149 NGdaelSSLSGGwlRKA--ALGRALVSSPRVLLLDEPTNHLDIETIDWL-----EGFLKEfDGSIVFISHDRSFIRNmAT 221
Cdd:cd03250 124 KG----INLSGG--QKQriSLARAVYSDADIYLLDDPLSAVDAHVGRHIfenciLGLLLN-NKTRILVTHQLQLLPH-AD 195
|
....*....
gi 505190249 222 RIVDLDRGK 230
Cdd:cd03250 196 QIVVLDNGR 204
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
335-496 |
1.78e-07 |
|
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: 52.47 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 335 VRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGrvhcGTKLEVAYFDQHRAD---------LDPERTVMDNLA 405
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSG----GVILEGKQITEPGPDrmvvfqnysLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 406 EGKQEVMVN---GRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAK-LFLKPSnLLILDEPTNDLDVETLELLEE 481
Cdd:TIGR01184 77 LAVDRVLPDlskSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARaLSIRPK-VLLLDEPFGALDALTRGNLQE 155
|
170
....*....|....*....
gi 505190249 482 LI----DGYQGTVLLVSHD 496
Cdd:TIGR01184 156 ELmqiwEEHRVTVLMVTHD 174
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-224 |
1.88e-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: 54.02 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 23 EIHIedNERVCLVGRNGAGKSTLLKILGKEIPLDDGRViyEQDLIVARLQQDPPRNIGGSVFDFVAEgvaeqaehlkayh 102
Cdd:COG1245 362 EIRE--GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGTVEEFLRS------------- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 103 AISHLVESDPSEKNLARMAQIMEILdhqglwqldsrisevllqlglngDAELSSLSGGWLRKAALGRALVSSPRVLLLDE 182
Cdd:COG1245 425 ANTDDFGSSYYKTEIIKPLGLEKLL-----------------------DKNVKDLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505190249 183 PTNHLDIE-------TIdwlEGFLKEFDGSIVFISHDRSFIRNMATRIV 224
Cdd:COG1245 482 PSAHLDVEqrlavakAI---RRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
30-239 |
1.90e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.20 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 30 ERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYE----QDLIVARLQqdppRNIGgSVFD----F---VAEGV------A 92
Cdd:PRK13657 362 QTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDgtdiRTVTRASLR----RNIA-VVFQdaglFnrsIEDNIrvgrpdA 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 93 EQAEHLKAyhaishlvesdpseknlARMAQIMEILDHQGLwQLDSRISEvllqlglNGdaelSSLSGGWLRKAALGRALV 172
Cdd:PRK13657 437 TDEEMRAA-----------------AERAQAHDFIERKPD-GYDTVVGE-------RG----RQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 173 SSPRVLLLDEPTNHLDIETIDWLEGFLKEF-DGSIVF-ISHDRSFIRNmATRIVDLDRGKLVSwPGNYD 239
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELmKGRTTFiIAHRLSTVRN-ADRILVFDNGRVVE-SGSFD 554
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-473 |
1.95e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.85 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYeqdlivarlqQDPPRNIGGS 82
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILY----------LGKEVTFNGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 vfdfvaegVAEQAEHLKAYHAISHLVESDPSEKN--LARmaqimEILDHQG--LWQLDSRISEVLLQ-LGLNGDAE--LS 155
Cdd:PRK10762 74 --------KSSQEAGIGIIHQELNLIPQLTIAENifLGR-----EFVNRFGriDWKKMYAEADKLLArLNLRFSSDklVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 156 SLSGGWLRKAALGRALVSSPRVLLLDEPTNHL-DIETIDWLE--GFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10762 141 ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRviRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 233 SwpgnydlylQSKEEALRVEELQNAEFDRKLaqEEVWIRqgikarrtrnegrvralkaLRVERsqrrevmGTAKMQVEEA 312
Cdd:PRK10762 221 A---------EREVADLTEDSLIEMMVGRKL--EDQYPR-------------------LDKAP-------GEVRLKVDNL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 313 TRSGkivfeledvnyqvgekvlVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV------------HCGT 380
Cdd:PRK10762 264 SGPG------------------VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVtldghevvtrspQDGL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 381 KLEVAYF--DQHRADLDPERTVMDNLA--------------EGKQEVMVNGrprhvlgylqDF--LFHPKramTP----- 437
Cdd:PRK10762 326 ANGIVYIseDRKRDGLVLGMSVKENMSltalryfsraggslKHADEQQAVS----------DFirLFNIK---TPsmeqa 392
|
490 500 510
....*....|....*....|....*....|....*..
gi 505190249 438 VKALSGGERNRLLLAK-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK10762 393 IGLLSGGNQQKVAIARgLMTRP-KVLILDEPTRGVDV 428
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
319-472 |
2.10e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.93 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 319 VFELEDVNYQVGEKV-LVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKlevayfdqhraDLDPE 397
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-----------PIDYS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 398 RTVMDNLaegKQEV-MVNGRPRHVL---GYLQDFLFHP--------------KRAMT----------PVKALSGGERNRL 449
Cdd:PRK13636 74 RKGLMKL---RESVgMVFQDPDNQLfsaSVYQDVSFGAvnlklpedevrkrvDNALKrtgiehlkdkPTHCLSFGQKKRV 150
|
170 180
....*....|....*....|...
gi 505190249 450 LLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLD 173
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-233 |
2.47e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.81 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 13 FSDAPLLDnTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQD---PPRNIGGSVFDFVAE 89
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikPVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 90 GVAEQAEhLK--AYHAISHLVESDPSEKNLARMAQIMEIldHQGLWQLDSrisevllqlglngdaelSSLSGGWLRKAAL 167
Cdd:PRK13643 96 QLFEETV-LKdvAFGPQNFGIPKEKAEKIAAEKLEMVGL--ADEFWEKSP-----------------FELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 168 GRALVSSPRVLLLDEPTNHLD----IETIDWLEGfLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVS 233
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDpkarIEMMQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-188 |
2.57e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 52.89 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 4 ISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGKEIPlDDGRVIYEQDLIVARLQQDPPRniggs 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRmLLGLTHP-DAGSISLCGEPVPSRARHARQR----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 vfdfvaEGVAEQAEHLkayhaishlvesDPS---EKNLARMAQIMEILDHQglwqLDSRISEVL--LQLGLNGDAELSSL 157
Cdd:PRK13537 82 ------VGVVPQFDNL------------DPDftvRENLLVFGRYFGLSAAA----ARALVPPLLefAKLENKADAKVGEL 139
|
170 180 190
....*....|....*....|....*....|.
gi 505190249 158 SGGWLRKAALGRALVSSPRVLLLDEPTNHLD 188
Cdd:PRK13537 140 SGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-224 |
2.86e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 23 EIHIedNERVCLVGRNGAGKSTLLKILGKEIPLDDGRViyEQDLIVA----RLQQDPPrnigGSVFDFVAEgvaeqaehl 98
Cdd:PRK13409 361 EIYE--GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISykpqYIKPDYD----GTVEDLLRS--------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 99 kayhaISHLVESDPSEKNLARMAQIMEILDHqglwqldsrisevllqlglngdaELSSLSGGWLRKAALGRALVSSPRVL 178
Cdd:PRK13409 424 -----ITDDLGSSYYKSEIIKPLQLERLLDK-----------------------NVKDLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505190249 179 LLDEPTNHLDIE-------TIdwlEGFLKEFDGSIVFISHDRSFIRNMATRIV 224
Cdd:PRK13409 476 LLDEPSAHLDVEqrlavakAI---RRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
34-473 |
3.38e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 34 LVGRNGAGKSTLLKILGKEIPLDDGRViyeqdLIVARLQQdpprniGGSVFDFVAEGVAEQAEHLkayhaisHLVESDPS 113
Cdd:PRK11288 35 LMGENGAGKSTLLKILSGNYQPDAGSI-----LIDGQEMR------FASTTAALAAGVAIIYQEL-------HLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 114 EKN--LARMAQIMEILDHQglwQLDSRISEVLLQLGLNGD--AELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDI 189
Cdd:PRK11288 97 AENlyLGQLPHKGGIVNRR---LLNYEAREQLEHLGVDIDpdTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 190 ETIDWLEGFLKEF--DGS-IVFISHDRSFIRNMATRIVDLDRGKLVSwpgnydlylqskeealRVEELQNAEFDRkLAQE 266
Cdd:PRK11288 174 REIEQLFRVIRELraEGRvILYVSHRMEEIFALCDAITVFKDGRYVA----------------TFDDMAQVDRDQ-LVQA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 267 EVWiR--QGIKARRTRNEGRVRalkaLRVErsqrrEVMGTAkmqveeatrsgkivfeledvnyqvgekvLVRGFSAQVQR 344
Cdd:PRK11288 237 MVG-ReiGDIYGYRPRPLGEVR----LRLD-----GLKGPG----------------------------LREPISFSVRA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 345 GDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTKLEVAY-FDQHRAD--LDPE----------RTVMDNLAegkqe 410
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYlDGKPIDIRSpRDAIRAGimLCPEdrkaegiipvHSVADNIN----- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 411 vmVNGRPRHVLGylqDFLFHPKR------------------AMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11288 354 --ISARRHHLRA---GCLINNRWeaenadrfirslniktpsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
.
gi 505190249 473 V 473
Cdd:PRK11288 429 V 429
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-211 |
3.45e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLD--DGRVIYEQDLIVARlqqdpprnig 80
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQAS---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 gSVFDFVAEGVaeqaehlkayhAISH----LVESDPSEKNLARMAQIME--ILDHQGLWQldsRISEVL--LQLGLNGDA 152
Cdd:PRK13549 75 -NIRDTERAGI-----------AIIHqelaLVKELSVLENIFLGNEITPggIMDYDAMYL---RAQKLLaqLKLDINPAT 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505190249 153 ELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHL-DIET---IDWLEGfLKEFDGSIVFISH 211
Cdd:PRK13549 140 PVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLtESETavlLDIIRD-LKAHGIACIYISH 201
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
327-498 |
3.48e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 51.74 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 327 YQVGE---KVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV----HCGTKLEVAyfdqHRADLD---- 395
Cdd:PRK11629 15 YQEGSvqtDVL-HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngQPMSKLSSA----AKAELRnqkl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 396 ----------PERTVMDNLAE-----GKQEVMVNGRPRHVLGYLQdflfHPKRAMTPVKALSGGERNRLLLAKLFLKPSN 460
Cdd:PRK11629 90 gfiyqfhhllPDFTALENVAMplligKKKPAEINSRALEMLAAVG----LEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505190249 461 LLILDEPTNDLDVETLE---LLEELIDGYQGTV-LLVSHDRQ 498
Cdd:PRK11629 166 LVLADEPTGNLDARNADsifQLLGELNRLQGTAfLVVTHDLQ 207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
318-500 |
3.50e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.41 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 318 IVFELEDVNYQVGEKVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV----HCGTKL---EVAY---- 386
Cdd:PRK10908 2 IRFEHVSKAYLGGRQAL-QGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsgHDITRLknrEVPFlrrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 387 ----FDQHRADLDpeRTVMDNLAegkQEVMVNGRP-----RHVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLAKLFLK 457
Cdd:PRK10908 81 igmiFQDHHLLMD--RTVYDNVA---IPLIIAGASgddirRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505190249 458 PSNLLILDEPTNDLDVETLELLEELIDGYQG---TVLLVSHDRQFV 500
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLI 200
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-188 |
3.51e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.13 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 18 LLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIP---------LDDGRVI--YEQDLIVARLQQDpprniggsvfD- 85
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvkgsgsvLLNGMPIdaKEMRAISAYVQQD----------Dl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 86 FVAEGVAEqaEHLkAYHAISHLVESDPSEKnlaRMAQIMEILDHQGLWQL-DSRIsevllqlGLNGDaeLSSLSGGWLRK 164
Cdd:TIGR00955 110 FIPTLTVR--EHL-MFQAHLRMPRRVTKKE---KRERVDEVLQALGLRKCaNTRI-------GVPGR--VKGLSGGERKR 174
|
170 180
....*....|....*....|....
gi 505190249 165 AALGRALVSSPRVLLLDEPTNHLD 188
Cdd:TIGR00955 175 LAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
320-472 |
3.69e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.77 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 320 FELEDVNYQV--GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLM--LGQLKADSgRVHCgtklEVAYF--DQHRAD 393
Cdd:PRK14267 3 FAIETVNLRVyyGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEEA-RVEG----EVRLFgrNIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 394 LDPER------------------TVMDNLAEGkqeVMVNG--RPRHVLGYLQDFLFHPKRAMTPVK--------ALSGGE 445
Cdd:PRK14267 78 VDPIEvrrevgmvfqypnpfphlTIYDNVAIG---VKLNGlvKSKKELDERVEWALKKAALWDEVKdrlndypsNLSGGQ 154
|
170 180
....*....|....*....|....*...
gi 505190249 446 RNRLLLAK-LFLKPsNLLILDEPTNDLD 472
Cdd:PRK14267 155 RQRLVIARaLAMKP-KILLMDEPTANID 181
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-233 |
3.87e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.91 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRNIGgsvfdfvaeg 90
Cdd:PRK10253 15 LGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIG---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 91 vaeqaehLKAYHAIShlvESDPSEKNLARMAQimeiLDHQGL---WQLDSR--ISEVLLQLGLN--GDAELSSLSGGWLR 163
Cdd:PRK10253 85 -------LLAQNATT---PGDITVQELVARGR----YPHQPLftrWRKEDEeaVTKAMQATGIThlADQSVDTLSGGQRQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 164 KAALGRALVSSPRVLLLDEPTNHLDI-ETIDWLEgFLKEFDG----SIVFISHDRSFIRNMATRIVDLDRGKLVS 233
Cdd:PRK10253 151 RAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLE-LLSELNRekgyTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
324-516 |
3.94e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.89 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 324 DVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKL---------EVAYFDQHRADL 394
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgQLKVADKNQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 DPER--------------TVMDNLAEGKQEVM----VNGRPRHVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLAKLFL 456
Cdd:PRK10619 90 LRTRltmvfqhfnlwshmTVLENVMEAPIQVLglskQEARERAVKYLAKVGIDERAQGKYPVH-LSGGQQQRVSIARALA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505190249 457 KPSNLLILDEPTNDLD---VETLELLEELIDGYQGTVLLVSHDRQFVDNsVTECWIFEGNGVI 516
Cdd:PRK10619 169 MEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARH-VSSHVIFLHQGKI 230
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
349-501 |
4.04e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.07 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 349 ALVGPNGCGKTTLLKLML----GQLKADS-GRVH----CGTKLEVAYFDQH-RADLDPERTVMDNLAEGKQEVMVNgrpr 418
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltGELPPNSkGGAHdpklIREGEVRAQVKLAfENANGKKYTITRSLAILENVIFCH---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 419 hvlgylQDFLFHPkrAMTPVKALSGGERN------RLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELI-DGYQGT-- 489
Cdd:cd03240 102 ------QGESNWP--LLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIiEERKSQkn 173
|
170
....*....|....
gi 505190249 490 --VLLVSHDRQFVD 501
Cdd:cd03240 174 fqLIVITHDEELVD 187
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
330-516 |
4.08e-07 |
|
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: 51.73 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 330 GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLEVAYFDQHRADL----------- 394
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqdlYQLDRKQRRAFRRDVqlvfqdspsav 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 DPERTVMDNLAEGKQEVM---VNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAK-LFLKPsNLLILDEPTND 470
Cdd:TIGR02769 102 NPRMTVRQIIGEPLRHLTsldESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARaLAVKP-KLIVLDEAVSN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505190249 471 LDVETLELLEELIDGYQ---GTV-LLVSHDRQFVDNSVTECWIFEGNGVI 516
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQqafGTAyLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
311-472 |
4.66e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.68 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 311 EATRSGKIVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtklevaYFDQH 390
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI---------FYNNQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 391 RADLD---------------PER-----TVMDNLAEGKQEVMVNGRPRH--VLGYLQDFLFHPKRAMTPvKALSGGERNR 448
Cdd:PRK13648 72 AITDDnfeklrkhigivfqnPDNqfvgsIVKYDVAFGLENHAVPYDEMHrrVSEALKQVDMLERADYEP-NALSGGQKQR 150
|
170 180
....*....|....*....|....*
gi 505190249 449 LLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13648 151 VAIAGvLALNPS-VIILDEATSMLD 174
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
342-512 |
4.99e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 50.26 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 342 VQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtklevayfdqhraDLDPERTVMdnlaegkqevmvngRPRHVl 421
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND----------------EWDGITPVY--------------KPQYI- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 422 gylqdflfhpkramtpvkALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELIDGY----QGTVLLVSHDR 497
Cdd:cd03222 71 ------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDL 132
|
170
....*....|....*
gi 505190249 498 QFVDNSVTECWIFEG 512
Cdd:cd03222 133 AVLDYLSDRIHVFEG 147
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
336-473 |
5.25e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.47 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 336 RGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC----GTKLEVA----------------YFDQHRAD-L 394
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdGQLRDLYalseaerrrllrtewgFVHQHPRDgL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 DPERTVMDNLAEgkqEVMVNGRpRH-------VLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEP 467
Cdd:PRK11701 103 RMQVSAGGNIGE---RLMAVGA-RHygdiratAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEP 178
|
....*.
gi 505190249 468 TNDLDV 473
Cdd:PRK11701 179 TGGLDV 184
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
312-472 |
5.45e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 52.51 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 312 ATRSGKIVFEleDVN--YQVGEKVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKL-EVAyf 387
Cdd:COG5265 352 VVGGGEVRFE--NVSfgYDPERPIL-KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIdGQDIrDVT-- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 388 dQH--RADLD--PERTVM------DNLAEGK-----QEVMVNGRprhvLGYLQDFLFH-PKRAMTPV-----KaLSGGER 446
Cdd:COG5265 427 -QAslRAAIGivPQDTVLfndtiaYNIAYGRpdaseEEVEAAAR----AAQIHDFIESlPDGYDTRVgerglK-LSGGEK 500
|
170 180
....*....|....*....|....*.
gi 505190249 447 NRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALD 526
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
258-472 |
5.60e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 258 EFDR--KLAQEEVWIRQGIKaRRTRNEGRVRALKALRVER---SQRREVMGTAKM---QVEEATRSGKIVFELEDVNYQV 329
Cdd:TIGR00956 691 EFNKgaKQKGEILVFRRGSL-KRAKKAGETSASNKNDIEAgevLGSTDLTDESDDvndEKDMEKESGEDIFHWRNLTYEV 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 330 G----EKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLkaDSGRVHCGTKL------------EVAYFDQHRAD 393
Cdd:TIGR00956 770 KikkeKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRLvngrpldssfqrSIGYVQQQDLH 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 394 LdPERTVMDNL---AEGKQ--EVMVNGRPRHVlGYLQDFLFHPKRA----MTPVKALSGGERNRLLLA-KLFLKPSNLLI 463
Cdd:TIGR00956 848 L-PTSTVRESLrfsAYLRQpkSVSKSEKMEYV-EEVIKLLEMESYAdavvGVPGEGLNVEQRKRLTIGvELVAKPKLLLF 925
|
....*....
gi 505190249 464 LDEPTNDLD 472
Cdd:TIGR00956 926 LDEPTSGLD 934
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
321-500 |
5.76e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 51.27 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVN--YQVGEKVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKL---EVAYFDQHRADL- 394
Cdd:PRK13647 6 EVEDLHfrYKDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnaENEKWVRSKVGLv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 --DPE-----RTVMDNLAEGKQEV-----MVNGRPRHVLGYLQDFLFHPKramtPVKALSGGERNRLLLAKLFLKPSNLL 462
Cdd:PRK13647 85 fqDPDdqvfsSTVWDDVAFGPVNMgldkdEVERRVEEALKAVRMWDFRDK----PPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505190249 463 ILDEPTNDLDVETLELLEELIDGY--QG-TVLLVSHDRQFV 500
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLhnQGkTVIVATHDVDLA 201
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-229 |
6.00e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.09 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 14 SDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQqDPPRNIG-GSVFDFVAEGVA 92
Cdd:TIGR01257 1950 TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS-DVHQNMGyCPQFDAIDDLLT 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 93 EQaEHLKAYHAISHLvesdPSEKnLARMAQimeildhqglWQLDSrisevlLQLGLNGDAELSSLSGGWLRKAALGRALV 172
Cdd:TIGR01257 2029 GR-EHLYLYARLRGV----PAEE-IEKVAN----------WSIQS------LGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505190249 173 SSPRVLLLDEPTNHLDIET--IDW--LEGFLKEfDGSIVFISHDRSFIRNMATRIVDLDRG 229
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQArrMLWntIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-255 |
7.43e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.39 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYeqdlivarlqqdpprniGGSVFDFVAEGVAEQAEHL 98
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILF-----------------DGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 99 KayhaishLVESDPSEKNLArmAQIMEILDHQGLW------QLDSRISEVLLQLGLN--GDAELSSLSGGWLRKAALGRA 170
Cdd:PRK13636 85 G-------MVFQDPDNQLFS--ASVYQDVSFGAVNlklpedEVRKRVDNALKRTGIEhlKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 171 LVSSPRVLLLDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLVSWPGNYDLYlqSKE 246
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF--AEK 233
|
....*....
gi 505190249 247 EALRVEELQ 255
Cdd:PRK13636 234 EMLRKVNLR 242
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
334-473 |
7.54e-07 |
|
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: 51.01 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 334 LVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV-HCGtklEVAYFDQHrADLDPErTVMDNLAEGKQevM 412
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkHSG---RISFSSQF-SWIMPG-TIKENIIFGVS--Y 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 413 VNGRPRHVLGYLQ---DFLFHPKRAMTPVK----ALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03291 125 DEYRYKSVVKACQleeDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-192 |
8.20e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.23 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRViyeqdlivaRLQQDPPRNiggs 82
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI---------QIDGKTATR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 vfdfvaegvAEQAEHLkAYhaISHL--VESDPSE-KNL-------ARMAQIMEildhqglwqldsriSEVLLQLGLNG-- 150
Cdd:PRK13543 78 ---------GDRSRFM-AY--LGHLpgLKADLSTlENLhflcglhGRRAKQMP--------------GSALAIVGLAGye 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505190249 151 DAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETI 192
Cdd:PRK13543 132 DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI 173
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
343-473 |
8.57e-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: 52.09 E-value: 8.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 343 QRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC------------GT------------KLEVAYFDQHrADLDPER 398
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEepswdevlkrfrGTelqdyfkklangEIKVAHKPQY-VDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 399 ---TVMDnLAEGKQEvmvngrpRHVLGYLQDFLfhpkrAMTP-----VKALSGGERNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:COG1245 176 fkgTVRE-LLEKVDE-------RGKLDELAEKL-----GLENildrdISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
...
gi 505190249 471 LDV 473
Cdd:COG1245 243 LDI 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
339-495 |
8.84e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 339 SAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKlEVAyFDQHRADLD-------------PERTVMDNLA 405
Cdd:PRK11288 24 SFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-EMR-FASTTAALAagvaiiyqelhlvPEMTVAENLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 406 EGK---QEVMVNGRP--RHVLGYLQ--DFLFHPKramTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLEL 478
Cdd:PRK11288 102 LGQlphKGGIVNRRLlnYEAREQLEhlGVDIDPD---TPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQ 178
|
170 180
....*....|....*....|
gi 505190249 479 LEELIDGY--QGTVLL-VSH 495
Cdd:PRK11288 179 LFRVIRELraEGRVILyVSH 198
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
318-498 |
9.15e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.55 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 318 IVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLM--LGQLkADSGRVHCgtklEVAYFDQ--HRAD 393
Cdd:PRK14243 9 TVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDL-IPGFRVEG----KVTFHGKnlYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 394 LDP-----------------ERTVMDNLAEGkqevmvngrPRhVLGYLQDFLFHPKRAMT------PVK--------ALS 442
Cdd:PRK14243 84 VDPvevrrrigmvfqkpnpfPKSIYDNIAYG---------AR-INGYKGDMDELVERSLRqaalwdEVKdklkqsglSLS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 443 GGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELID--GYQGTVLLVSHDRQ 498
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHelKEQYTIIIVTHNMQ 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-232 |
1.05e-06 |
|
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: 51.67 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 14 SDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL--------GKeIPLDDgrviyeqdlivARLQQDPPRNIGGSV-- 83
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvgvwpptaGS-VRLDG-----------ADLSQWDREELGRHIgy 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 84 -------FDfvaeG-VAEQaehlkayhaISHLVESDPsEKNL--ARMAQIME-ILdhqglwQL----DSRISEvllqlgl 148
Cdd:COG4618 411 lpqdvelFD----GtIAEN---------IARFGDADP-EKVVaaAKLAGVHEmIL------RLpdgyDTRIGE------- 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 149 NGdaelSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLD-------IETIDwlegFLKEFDGSIVFISHDRSFIrNMAT 221
Cdd:COG4618 464 GG----ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAIR----ALKARGATVVVITHRPSLL-AAVD 534
|
250
....*....|.
gi 505190249 222 RIVDLDRGKLV 232
Cdd:COG4618 535 KLLVLRDGRVQ 545
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
341-500 |
1.10e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 341 QVQRGDKIALVGPNGCGKTTLLKLMLGQLK--ADSGRVHCGTkleVAYFDQHRADLDPerTVMDNLAEG-KQEVMVNGRP 417
Cdd:PLN03232 639 EIPVGSLVAIVGGTGEGKTSLISAMLGELShaETSSVVIRGS---VAYVPQVSWIFNA--TVRENILFGsDFESERYWRA 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 418 RHVLGYLQDFLFHPKRAMTPVKA----LSGGERNRLLLAKLFLKPSNLLILDEPTNDLD--VETLELLEELIDGYQG-TV 490
Cdd:PLN03232 714 IDVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDahVAHQVFDSCMKDELKGkTR 793
|
170
....*....|
gi 505190249 491 LLVSHDRQFV 500
Cdd:PLN03232 794 VLVTNQLHFL 803
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-229 |
1.11e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.47 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRViyeqdlivaRLQQDPPRNIGgs 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI---------TLDGKPVEGPG-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 vfdfvAE-GVAEQAEHLKAYHAISHLVESDPSEKNLARMaqimeildhqglwQLDSRISEVLLQLGLNGDAE--LSSLSG 159
Cdd:PRK11248 70 -----AErGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKM-------------QRLEIAHQMLKKVGLEGAEKryIWQLSG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505190249 160 GWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFL----KEFDGSIVFISHDRSFIRNMATRIVDLDRG 229
Cdd:PRK11248 132 GQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
328-472 |
1.18e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.59 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 328 QVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLM----LGQLKADSGRVHCGTKLEV-------AYFDQHraDLD- 395
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrsPKGVKGSGSVLLNGMPIDAkemraisAYVQQD--DLFi 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 396 PERTVMDNL---AEGK--QEVMVNGRPRHVLGYLQDfLFHPKRAMT------PVKALSGGERNRLLLAKLFLKPSNLLIL 464
Cdd:TIGR00955 112 PTLTVREHLmfqAHLRmpRRVTKKEKRERVDEVLQA-LGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFC 190
|
....*...
gi 505190249 465 DEPTNDLD 472
Cdd:TIGR00955 191 DEPTSGLD 198
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
319-498 |
1.22e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.78 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 319 VFELEDVNYQVGEK----VLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQHRADL 394
Cdd:PRK10584 6 IVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 D--------------PERTVMDN-----LAEGKQEVMVNGRPRHVLGY--LQDFLFHpkramTPVKaLSGGERNRLLLAK 453
Cdd:PRK10584 86 RakhvgfvfqsfmliPTLNALENvelpaLLRGESSRQSRNGAKALLEQlgLGKRLDH-----LPAQ-LSGGEQQRVALAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505190249 454 LFLKPSNLLILDEPTNDLDVETLELLEELI----DGYQGTVLLVSHDRQ 498
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQ 208
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
335-473 |
1.38e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.73 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 335 VRGFSAQVQRGDKIALVGPNGCGKTTLLKLML-------GQLKADSGRVHCGTKLEVA--------YFDQHRADLDPERT 399
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTmietptgGELYYQGQDLLKADPEAQKllrqkiqiVFQNPYGSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 400 VMDNLAE--------GKQE-------VM--VNGRPRHVLGYLQDFlfhpkramtpvkalSGGERNRLLLAK-LFLKPsNL 461
Cdd:PRK11308 111 VGQILEEpllintslSAAErrekalaMMakVGLRPEHYDRYPHMF--------------SGGQRQRIAIARaLMLDP-DV 175
|
170
....*....|..
gi 505190249 462 LILDEPTNDLDV 473
Cdd:PRK11308 176 VVADEPVSALDV 187
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-232 |
1.38e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 50.48 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKeipLDD--------------GRVIYE-QDLIVAR----L 71
Cdd:PRK14271 29 LGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNR---MNDkvsgyrysgdvllgGRSIFNyRDVLEFRrrvgM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 72 QQDPPRNIGGSVFDFVAEGV-AEQAEHLKAYHAISHlvesdpseknlARMAQImeildhqGLWQ-LDSRISEVLLQLgln 149
Cdd:PRK14271 106 LFQRPNPFPMSIMDNVLAGVrAHKLVPRKEFRGVAQ-----------ARLTEV-------GLWDaVKDRLSDSPFRL--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 150 gdaelsslSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDG--SIVFISHDRSFIRNMATRIVDLD 227
Cdd:PRK14271 165 --------SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFF 236
|
....*
gi 505190249 228 RGKLV 232
Cdd:PRK14271 237 DGRLV 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
32-231 |
1.41e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.97 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 32 VCLVGRNGAGKSTLLKILG-KEIPLDDGRVIYEQDLivaRLQQDPPRNIggSVFDfvaegvAEQAEHLKAyhAISHLVES 110
Cdd:PRK10619 34 ISIIGSSGSGKSTFLRCINfLEKPSEGSIVVNGQTI---NLVRDKDGQL--KVAD------KNQLRLLRT--RLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 111 DPSEKNLARMAQIMEI-LDHQGLWQLDSRISEV--LLQLGLNGDAEL---SSLSGGWLRKAALGRALVSSPRVLLLDEPT 184
Cdd:PRK10619 101 FNLWSHMTVLENVMEApIQVLGLSKQEARERAVkyLAKVGIDERAQGkypVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505190249 185 NHLDIETIDWLEGF---LKEFDGSIVFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK10619 181 SALDPELVGEVLRImqqLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-239 |
1.44e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 50.47 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-----------------IYEQDLIVARLQQDPPRNIG- 80
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekeKVLEKLVIQKTRFKKIKKIKe 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 -----GSVFDFVAEGVAEQA-EHLKAYHAISHLVESDPSEKnlaRMAQIMEILDhqglwqLDsrisEVLLQlglngdAEL 154
Cdd:PRK13651 103 irrrvGVVFQFAEYQLFEQTiEKDIIFGPVSMGVSKEEAKK---RAAKYIELVG------LD----ESYLQ------RSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 155 SSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIE-TIDWLEGF--LKEFDGSIVFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFdnLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
....*...
gi 505190249 232 VSWPGNYD 239
Cdd:PRK13651 244 IKDGDTYD 251
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
317-468 |
1.51e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.88 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 317 KIVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLEVAYFDQHRA 392
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkdiTDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 393 DLDPE-------RTVMDNLAEG---KQEVMVNGRPRHVLGYLQDFLfhpKRAMTPVKALSGGERNRLLLAKLFLKPSNLL 462
Cdd:PRK11614 83 AIVPEgrrvfsrMTVEENLAMGgffAERDQFQERIKWVYELFPRLH---ERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
....*.
gi 505190249 463 ILDEPT 468
Cdd:PRK11614 160 LLDEPS 165
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-232 |
1.57e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 50.40 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 26 IEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQD---PPRNIGGSVFDFvaegvaeqAEHlkayh 102
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkPLRKKVGIVFQF--------PEH----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 103 aisHLVEsDPSEKNLARMAQIMEILDHQGLwqldSRISEVLLQLGLNGDAELSS---LSGGWLRKAALGRALVSSPRVLL 179
Cdd:PRK13634 97 ---QLFE-ETVEKDICFGPMNFGVSEEDAK----QKAREMIELVGLPEELLARSpfeLSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 180 LDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13634 169 LDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
342-496 |
1.62e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 342 VQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH------------CGTKLEvAYFDQhradldpertvmdnLAEGKQ 409
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEeepswdevlkrfRGTELQ-NYFKK--------------LYNGEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 410 EV-----MVNGRPRHVLGYLQDFLfhpKRA--------------MTPV-----KALSGGERNRLLLAKLFLKPSNLLILD 465
Cdd:PRK13409 161 KVvhkpqYVDLIPKVFKGKVRELL---KKVdergkldevverlgLENIldrdiSELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|...
gi 505190249 466 EPTNDLDVETLELLEELIDGYQG--TVLLVSHD 496
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAEgkYVLVVEHD 270
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
321-472 |
1.79e-06 |
|
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: 50.96 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLG--QLKADSGRV---------------------- 376
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpskvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 377 --HCGTKLE--------------------VAYFDQHRADLDPERTVMDNLAEGKQEVMVNG-----RPRHVLGYLQdfLF 429
Cdd:TIGR03269 82 cpVCGGTLEpeevdfwnlsdklrrrirkrIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGkeavgRAVDLIEMVQ--LS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505190249 430 HpkRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR03269 160 H--RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD 200
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
326-472 |
2.28e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 49.69 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 326 NYQVGEKVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHcgtklevayfdqhradLDPERTVMDN-- 403
Cdd:PRK13639 10 SYPDGTEAL-KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL----------------IKGEPIKYDKks 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 404 LAEGKQEV-MVNGRPRHVL---GYLQDFLFHP-----------KRAMTPVKA-------------LSGGERNRLLLAKLF 455
Cdd:PRK13639 73 LLEVRKTVgIVFQNPDDQLfapTVEEDVAFGPlnlglskeeveKRVKEALKAvgmegfenkpphhLSGGQKKRVAIAGIL 152
|
170
....*....|....*..
gi 505190249 456 LKPSNLLILDEPTNDLD 472
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLD 169
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-232 |
2.58e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.07 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 13 FSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDD-----------GRVIYEQDLivarlqqDP--PRNI 79
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearvegevrlfGRNIYSPDV-------DPieVRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 80 GGSVFDFvaegvAEQAEHLKAYHAISHLVESDPSEKNLARMAQIME-ILDHQGLWQldsrisEVLLQLglngDAELSSLS 158
Cdd:PRK14267 87 VGMVFQY-----PNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEwALKKAALWD------EVKDRL----NDYPSNLS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505190249 159 GGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-188 |
2.70e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.78 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 17 PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIyeqdlivarlqqdpprnIGG----SVFDFVAEGVA 92
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL-----------------VGGkdieTNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 93 EQAEHLKAYHaisHLVESDpsekNLARMAQIMEILDHQGLWQLDSRISEVLLQLGLNGDAElsSLSGGWLRKAALGRALV 172
Cdd:TIGR01257 1007 MCPQHNILFH---HLTVAE----HILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQ--DLSGGMQRKLSVAIAFV 1077
|
170
....*....|....*.
gi 505190249 173 SSPRVLLLDEPTNHLD 188
Cdd:TIGR01257 1078 GDAKVVVLDEPTSGVD 1093
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
325-473 |
2.78e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.50 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 325 VNYQVGEKVLvRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV--------HCGTKLEVAYFDQHRaDLDP 396
Cdd:PRK15056 14 VTWRNGHTAL-RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrQALQKNLVAYVPQSE-EVDW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 397 ERTVMdnlaegKQEVMVNGRPRHvLGYLQDFLFHPKRAMTPVKA--------------LSGGERNRLLLAKLFLKPSNLL 462
Cdd:PRK15056 92 SFPVL------VEDVVMMGRYGH-MGWLRRAKKRDRQIVTAALArvdmvefrhrqigeLSGGQKKRVFLARAIAQQGQVI 164
|
170
....*....|.
gi 505190249 463 ILDEPTNDLDV 473
Cdd:PRK15056 165 LLDEPFTGVDV 175
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
321-501 |
2.79e-06 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 49.18 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQ--LKADSGRV----HCGTKLEVayfdQHRADL 394
Cdd:TIGR01978 2 KIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsYEVTSGTIlfkgQDLLELEP----DERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 D-----------PERTVMDNL---------AEGKQEV-MVNGRP-----RHVLGYLQDFLfhpKRAMTpvKALSGGERNR 448
Cdd:TIGR01978 78 GlflafqypeeiPGVSNLEFLrsalnarrsARGEEPLdLLDFEKllkekLALLDMDEEFL---NRSVN--EGFSGGEKKR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 449 L-LLAKLFLKPsNLLILDEPTNDLDVETLELLEELIDGYQG---TVLLVSHDRQFVD 501
Cdd:TIGR01978 153 NeILQMALLEP-KLAILDEIDSGLDIDALKIVAEGINRLREpdrSFLIITHYQRLLN 208
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-230 |
3.17e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.83 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKIL-------GKEIPLDDGRVIYEQDLIVARLqqdp 75
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLtgfykptGGTILLRGQHIEGLPGHQIARM---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 76 prnigGSVFDF----------VAEG--VAeQAEHLKAyHAISHLVESdPSEKNLAR--MAQIMEILDHQGLWQLDSRise 141
Cdd:PRK11300 81 -----GVVRTFqhvrlfremtVIENllVA-QHQQLKT-GLFSGLLKT-PAFRRAESeaLDRAATWLERVGLLEHANR--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 142 vllqlglngdaELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLD-IETID---WLEGFLKEFDGSIVFISHDRSFIR 217
Cdd:PRK11300 150 -----------QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNpKETKEldeLIAELRNEHNVTVLLIEHDMKLVM 218
|
250
....*....|...
gi 505190249 218 NMATRIVDLDRGK 230
Cdd:PRK11300 219 GISDRIYVVNQGT 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
345-472 |
3.24e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 48.86 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 345 GDKIALVGPNGCGKTTLLKLM-------LGQLK-AD-----SGRVHCGTKLEV-----AYFDQHraDLDPERTVMDNLAE 406
Cdd:COG4161 28 GETLVLLGPSGAGKSSLLRVLnlletpdSGQLNiAGhqfdfSQKPSEKAIRLLrqkvgMVFQQY--NLWPHLTVMENLIE 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 407 G--------KQEVMvnGRPRHVLGYLQdflFHPKRAMTPVkALSGGERNRLLLAK-LFLKPSNLLiLDEPTNDLD 472
Cdd:COG4161 106 ApckvlglsKEQAR--EKAMKLLARLR---LTDKADRFPL-HLSGGQQQRVAIARaLMMEPQVLL-FDEPTAALD 173
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
318-517 |
3.32e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 49.35 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 318 IVFELEDVNYQVGEKVLVRGF---SAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQHraDL 394
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRALfdiDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQK--EI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 395 DP-----------------ERTVMDNLAEGKQEVMVN--------GRPRHVLGYLQDFLfhpkrAMTPVKaLSGGERNRL 449
Cdd:PRK13643 80 KPvrkkvgvvfqfpesqlfEETVLKDVAFGPQNFGIPkekaekiaAEKLEMVGLADEFW-----EKSPFE-LSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505190249 450 LLAKLFLKPSNLLILDEPTNDLDVETLELLEELIDGYQ---GTVLLVSHDRQFVDNSVTECWIFEGNGVIN 517
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHqsgQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
158-220 |
3.83e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.19 E-value: 3.83e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 158 SGGWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMA 220
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVsvqaQVLNLMMDLQQELGLSYVFISHDLSVVEHIA 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
349-472 |
4.28e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.40 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 349 ALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQHRADLD--PERTVMDNLAEGKQEVM----VNGRPR---- 418
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGmcPQHNILFHHLTVAEHILfyaqLKGRSWeeaq 1039
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 419 -HVLGYLQDFLFHPKRAmTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR01257 1040 lEMEAMLEDTGLHHKRN-EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
310-472 |
4.42e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 48.49 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 310 EEATRSGKIVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMlgqlkadsGRVH-----CGTKLEV 384
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL--------NRMNdlipgARVEGEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 385 AYFDQ--HRADLDPER-----------------TVMDNLAEGkqeVMVNG-RPRHVLGYL-QDFLfhpKRAM-------- 435
Cdd:COG1117 74 LLDGEdiYDPDVDVVElrrrvgmvfqkpnpfpkSIYDNVAYG---LRLHGiKSKSELDEIvEESL---RKAAlwdevkdr 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505190249 436 --TPVKALSGGERNRLLLAK-LFLKPSNLLiLDEPTNDLD 472
Cdd:COG1117 148 lkKSALGLSGGQQQRLCIARaLAVEPEVLL-MDEPTSALD 186
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
30-232 |
4.64e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 30 ERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQ---DLIVARLQQDPPRNIggsvfdfvaegvaeqaehlkayhaisH 106
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqriDTLSPGKLQALRRDI--------------------------Q 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 107 LVESDPSEKNLARMA---QIMEILDHQGLWQLD---SRISEVLLQLGLNGDAELS---SLSGGWLRKAALGRALVSSPRV 177
Cdd:PRK10261 405 FIFQDPYASLDPRQTvgdSIMEPLRVHGLLPGKaaaARVAWLLERVGLLPEHAWRyphEFSGGQRQRICIARALALNPKV 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 178 LLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10261 485 IIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
331-496 |
5.26e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 48.57 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 331 EKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKL--EVAYFDQHRADL---DPER-----T 399
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLteENVWDIRHKIGMvfqNPDNqfvgaT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 400 VMDNLAEGKQ------EVMVNgRPRHVLGY--LQDF-LFHPKRamtpvkaLSGGERNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK13650 99 VEDDVAFGLEnkgiphEEMKE-RVNEALELvgMQDFkEREPAR-------LSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190
....*....|....*....|....*....|
gi 505190249 471 LDVETLELLEELI----DGYQGTVLLVSHD 496
Cdd:PRK13650 171 LDPEGRLELIKTIkgirDDYQMTVISITHD 200
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
324-472 |
5.41e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.49 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 324 DVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADS--------GRVHCGTKLEVAYFDQHRADLD 395
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftgtilanNRKPTKQILKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 396 PERTVMDNLAEGKQEVMVNGRPRHVLGYLQDFLFhPKRAMTP----------VKALSGGERNRLLLA-KLFLKPSnLLIL 464
Cdd:PLN03211 153 PHLTVRETLVFCSLLRLPKSLTKQEKILVAESVI-SELGLTKcentiignsfIRGISGGERKRVSIAhEMLINPS-LLIL 230
|
....*...
gi 505190249 465 DEPTNDLD 472
Cdd:PLN03211 231 DEPTSGLD 238
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-187 |
5.63e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 48.85 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNeRVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRNIGGsVFDFVAEGVAEQAEHL 98
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIEL-TFGSLLSRLLRLLLKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 99 KAYHAISHLVESDPSE--KNLARMAQIMEILDHQGLWQLDSRISEVL-----------LQLGLNGDAELSSLSGG--WLR 163
Cdd:COG3593 92 EDKEELEEALEELNEElkEALKALNELLSEYLKELLDGLDLELELSLdeledllkslsLRIEDGKELPLDRLGSGfqRLI 171
|
170 180
....*....|....*....|....*....
gi 505190249 164 KAALGRALV-----SSPRVLLLDEPTNHL 187
Cdd:COG3593 172 LLALLSALAelkraPANPILLIEEPEAHL 200
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
345-472 |
5.66e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 48.09 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 345 GDKIALVGPNGCGKTTLLKlMLGQLK-ADSGrvhcgtKLEVA--YFD-----------QHRAD---------LDPERTVM 401
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLR-VLNLLEmPRSG------TLNIAgnHFDfsktpsdkairELRRNvgmvfqqynLWPHLTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 402 DNLAE--------GKQEVMvnGRPRHVLGYLQdflFHPKRAMTPVKaLSGGERNRLLLAK-LFLKPSNLLiLDEPTNDLD 472
Cdd:PRK11124 101 QNLIEapcrvlglSKDQAL--ARAEKLLERLR---LKPYADRFPLH-LSGGQQQRVAIARaLMMEPQVLL-FDEPTAALD 173
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
317-473 |
6.14e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.10 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 317 KIVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGqlkadsgrvHCGTKL---EVAYFDQHRAD 393
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG---------HPAYKIlegDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 394 LDPER-------------------TVMDNL-----AEGKQEVMVNGRPRHVLGYLQDFLfhPKRAMTPV-------KALS 442
Cdd:CHL00131 76 LEPEErahlgiflafqypieipgvSNADFLrlaynSKRKFQGLPELDPLEFLEIINEKL--KLVGMDPSflsrnvnEGFS 153
|
170 180 190
....*....|....*....|....*....|.
gi 505190249 443 GGERNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDI 184
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-243 |
6.56e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.56 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 18 LLDNTEIHIEDNERVCLVGRNGAGKSTL--------------LKILG---KEIPLDDGR---VIYEQDLIV----ARLQQ 73
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLtlglfrinesaegeIIIDGlniAKIGLHDLRfkiTIIPQDPVLfsgsLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 74 DPprniggsVFDFVAEGV--AEQAEHLKAYhaishlVESDPSEknlarmaqimeiLDHQglwqldsrISEvllqlglNGD 151
Cdd:TIGR00957 1381 DP-------FSQYSDEEVwwALELAHLKTF------VSALPDK------------LDHE--------CAE-------GGE 1420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 152 aelsSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLK-EFDGSIVF-ISHDRSFIRNMaTRIVDLDRG 229
Cdd:TIGR00957 1421 ----NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRtQFEDCTVLtIAHRLNTIMDY-TRVIVLDKG 1495
|
250
....*....|....
gi 505190249 230 KLVSWPGNYDLYLQ 243
Cdd:TIGR00957 1496 EVAEFGAPSNLLQQ 1509
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-232 |
6.65e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 48.88 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLdnteihIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEqDLIVARLQQDPPRNIGGS 82
Cdd:PRK10070 34 ILEKTGLSLGVKDASLA------IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID-GVDIAKISDAELREVRRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 83 VFDFVaegvaeqaehLKAYHAISHLVESDPSEKNLARMAQIMEILDHQGLwqldsrisEVLLQLGLNGDAE--LSSLSGG 160
Cdd:PRK10070 107 KIAMV----------FQSFALMPHMTVLDNTAFGMELAGINAEERREKAL--------DALRQVGLENYAHsyPDELSGG 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505190249 161 WLRKAALGRALVSSPRVLLLDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK10070 169 MRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
316-473 |
6.94e-06 |
|
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: 47.41 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 316 GKIVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHcgtklevayFDQHRADLD 395
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE---------IDGIDISTI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 396 PERTVMDNLAEGKQE-VMVNGRPRHVLG----YLQDFLFHPKRAMTPVKALSGGERNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:cd03369 76 PLEDLRSSLTIIPQDpTLFSGTIRSNLDpfdeYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
...
gi 505190249 471 LDV 473
Cdd:cd03369 156 IDY 158
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
151-232 |
7.36e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.86 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 151 DAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEfdG-SIVFISHDRSFIRNMATRIVD 225
Cdd:COG1129 389 EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVgakaEIYRLIRELAAE--GkAVIVISSELPELLGLSDRILV 466
|
....*..
gi 505190249 226 LDRGKLV 232
Cdd:COG1129 467 MREGRIV 473
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-188 |
9.09e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 3 LISMSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDdgrviYEQDLIVARLQQ-------DP 75
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQG-----YSNDLTLFGRRRgsgetiwDI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 76 PRNIGgsvfdFVAEGVaeqaeHLKAYHAIShlvesdpseknlARMAQIMEILDHQGLWQLDSRISEVLLQ-----LGLN- 149
Cdd:PRK10938 335 KKHIG-----YVSSSL-----HLDYRVSTS------------VRNVILSGFFDSIGIYQAVSDRQQKLAQqwldiLGIDk 392
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505190249 150 --GDAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLD 188
Cdd:PRK10938 393 rtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
151-232 |
1.06e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.48 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 151 DAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGS-IVFISHDRSFIRNMATRIVDLD 227
Cdd:COG3845 397 DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELrdAGAaVLLISEDLDEILALSDRIAVMY 476
|
....*
gi 505190249 228 RGKLV 232
Cdd:COG3845 477 EGRIV 481
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
319-472 |
1.08e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.49 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 319 VFELEDVNYQV-GEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKL---EVAYFD-- 388
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRgepiTKEnirEVRKFVgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 389 --QHRADLDPERTVMDNLAEGK-----QEVMVNGRPR---HVLGyLQDFlfhpkRAMTPvKALSGGERNRLLLAKLFLKP 458
Cdd:PRK13652 83 vfQNPDDQIFSPTVEQDIAFGPinlglDEETVAHRVSsalHMLG-LEEL-----RDRVP-HHLSGGEKKRVAIAGVIAME 155
|
170
....*....|....
gi 505190249 459 SNLLILDEPTNDLD 472
Cdd:PRK13652 156 PQVLVLDEPTAGLD 169
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
304-495 |
1.26e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.09 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 304 TAKMQVEEATrsGKIVFEleDVN--YQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GT 380
Cdd:PRK11176 330 EGKRVIERAK--GDIEFR--NVTftYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdGH 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 381 KLE----------VAYFDQ--HRADldpeRTVMDNLAEGKQEVMVNGRPRHV--LGYLQDFLFHPKRAMTPV-----KAL 441
Cdd:PRK11176 406 DLRdytlaslrnqVALVSQnvHLFN----DTIANNIAYARTEQYSREQIEEAarMAYAMDFINKMDNGLDTVigengVLL 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505190249 442 SGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELIDGYQG--TVLLVSH 495
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH 537
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-189 |
1.38e-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: 46.98 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 34 LVGRNGAGKSTLLKIL-GKEIPlDDGRVIYEQDLivarlqQDPPRNIGGSVFDFVAEGVAEqaEHLKAYHAISHLVESDP 112
Cdd:cd03236 31 LVGPNGIGKSTALKILaGKLKP-NLGKFDDPPDW------DEILDEFRGSELQNYFTKLLE--GDVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 113 SEKnlARMAQIMEILDHQGlwQLDsrisEVLLQLGLNG--DAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDI 189
Cdd:cd03236 102 AVK--GKVGELLKKKDERG--KLD----ELVDQLELRHvlDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-232 |
1.54e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.43 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 1 MSLISMSGAWLSFSD--APL--LDNTEIHIEDNERVCLVGRNGAGKS-TLLKILGkeipLDD--GRVIYEQ------DLI 67
Cdd:PRK11022 1 MALLNVDKLSVHFGDesAPFraVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMG----LIDypGRVMAEKlefngqDLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 68 vaRLQQDPPRNIGGSVfdfVAEGVAEQAEHLKAYHAISHlvesdpseknlarmaQIMEILD-HQG--LWQLDSRISEVLL 144
Cdd:PRK11022 77 --RISEKERRNLVGAE---VAMIFQDPMTSLNPCYTVGF---------------QIMEAIKvHQGgnKKTRRQRAIDLLN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 145 QLGLNG-----DAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSF 215
Cdd:PRK11022 137 QVGIPDpasrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITHDLAL 216
|
250
....*....|....*..
gi 505190249 216 IRNMATRIVDLDRGKLV 232
Cdd:PRK11022 217 VAEAAHKIIVMYAGQVV 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-188 |
1.56e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 46.69 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 11 LSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLD-----DGRVIYEQDLIVAR--------------L 71
Cdd:PRK14239 13 VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPrtdtvdlrkeigmvF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 72 QQDPPRNIggSVFDFVAEGVAEQAEHLKayHAISHLVEsdpseKNLARMAQIMEILDHQGlwqlDSRISevllqlglngd 151
Cdd:PRK14239 93 QQPNPFPM--SIYENVVYGLRLKGIKDK--QVLDEAVE-----KSLKGASIWDEVKDRLH----DSALG----------- 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 505190249 152 aelssLSGGWLRKAALGRALVSSPRVLLLDEPTNHLD 188
Cdd:PRK14239 149 -----LSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-231 |
1.60e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 39 GAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRNiggsvfdfvaeGVAEQAEHLKAYHAISHL-VESDPSEKNL 117
Cdd:PRK10762 288 GAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN-----------GIVYISEDRKRDGLVLGMsVKENMSLTAL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 118 ARMAQIMEILDHQGLWQLDSRISEVLLQLGLNGDAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETID 193
Cdd:PRK10762 357 RYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVgakkEIYQ 436
|
170 180 190
....*....|....*....|....*....|....*....
gi 505190249 194 WLEGFLKEfdG-SIVFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK10762 437 LINQFKAE--GlSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
341-468 |
1.84e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.71 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 341 QVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKLEVA-------------YfdQHRAdLDPERTVMDNLA- 405
Cdd:COG3845 27 TVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdGKPVRIRsprdaialgigmvH--QHFM-LVPNLTVAENIVl 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 406 --EGKQEVMVNGRP--RHVLGYLQDFLFH--PKRamtPVKALSGGERNRLLLAKLFLKPSNLLILDEPT 468
Cdd:COG3845 104 glEPTKGGRLDRKAarARIRELSERYGLDvdPDA---KVEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-223 |
1.97e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 29 NERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYeqdlivarlqqdpprnIGGSvfdfvaegvaeqaehlkayhaishlv 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY----------------IDGE-------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 109 esdpseknlarmaqimeildhqglwqlDSRISEVLLQLGLNGDAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLD 188
Cdd:smart00382 40 ---------------------------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLD 92
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505190249 189 IET---------IDWLEGFLKEFDGSIVFISHDRSFIRNMATRI 223
Cdd:smart00382 93 AEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-226 |
1.97e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 46.70 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKI---LGKEIP--LDDGRVIYEQDLIVARlQQDPP---RNIG---------- 80
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPgfRVEGKVTFHGKNLYAP-DVDPVevrRRIGmvfqkpnpfp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 GSVFDFVAEGVaeqaeHLKAYHA-ISHLVEsdpseKNLARMAqimeildhqgLWqldsriSEVLLQLGLNGdaelSSLSG 159
Cdd:PRK14243 105 KSIYDNIAYGA-----RINGYKGdMDELVE-----RSLRQAA----------LW------DEVKDKLKQSG----LSLSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505190249 160 GWLRKAALGRALVSSPRVLLLDEPTNHLD-IETIDwLEGFLKEF--DGSIVFISHdrsfirNM--ATRIVDL 226
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDpISTLR-IEELMHELkeQYTIIIVTH------NMqqAARVSDM 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
317-472 |
2.05e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 46.52 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 317 KIVFELEDV--NYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKLEVAYFDQHRAD 393
Cdd:PRK13632 5 SVMIKVENVsfSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 394 L-----DPER-----TVMDNLAEGKQEVMVngrPRHVLGYLQDFLFHpKRAMT------PVKaLSGGERNRLLLAK-LFL 456
Cdd:PRK13632 85 IgiifqNPDNqfigaTVEDDIAFGLENKKV---PPKKMKDIIDDLAK-KVGMEdyldkePQN-LSGGQKQRVAIASvLAL 159
|
170
....*....|....*.
gi 505190249 457 KPSnLLILDEPTNDLD 472
Cdd:PRK13632 160 NPE-IIIFDESTSMLD 174
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
117-231 |
2.06e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.51 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 117 LARMAQIMEILDHQGLWQLDSRISEVLLQLGlNGDAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET---ID 193
Cdd:TIGR02633 365 LKSFCFKMRIDAAAELQIIGSAIQRLKVKTA-SPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIY 443
|
90 100 110
....*....|....*....|....*....|....*...
gi 505190249 194 WLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:TIGR02633 444 KLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-246 |
2.12e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 10 WLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIY-------------------EQDLIVAR 70
Cdd:PTZ00265 1175 YISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVfknehtndmtneqdyqgdeEQNVGMKN 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 71 LQQDPPRNIGGS-----VF----DFVAEGVAEQAEHLKAYHAISHLVESDPSEKNLARMAQIM---------EILDHQGL 132
Cdd:PTZ00265 1255 VNEFSLTKEGGSgedstVFknsgKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfgkedatreDVKRACKF 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 133 WQLDSRISEVLLQLGLNGDAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF----DGSIVF 208
Cdd:PTZ00265 1335 AAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdkaDKTIIT 1414
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 505190249 209 ISHDRSFIRNMATRIV--DLDR-GKLVSWPGNYDLYLQSKE 246
Cdd:PTZ00265 1415 IAHRIASIKRSDKIVVfnNPDRtGSFVQAHGTHEELLSVQD 1455
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
281-376 |
2.35e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 281 NEGRVRALKALRVERSQRREVMGTAKMQVEEATRSGKIVfelEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTT 360
Cdd:PTZ00243 625 DTDYGSPSSASRHIVEGGTGGGHEATPTSERSAKTPKMK---TDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKST 701
|
90
....*....|....*.
gi 505190249 361 LLKLMLGQLKADSGRV 376
Cdd:PTZ00243 702 LLQSLLSQFEISEGRV 717
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
292-472 |
2.38e-05 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 46.48 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 292 RVERSQRREVMGTAKMQVEEATrsgkivfeledvnyqvGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKA 371
Cdd:cd03294 13 NPQKAFKLLAKGKSKEEILKKT----------------GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 372 DSGRVHCGTKlEVAYFD----------------QHRAdLDPERTVMDNLAEGKQevmVNGRPR--------HVL------ 421
Cdd:cd03294 77 TSGKVLIDGQ-DIAAMSrkelrelrrkkismvfQSFA-LLPHRTVLENVAFGLE---VQGVPRaereeraaEALelvgle 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505190249 422 GYLQDFlfhpkramtpVKALSGGERNRLLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:cd03294 152 GWEHKY----------PDELSGGMQQRVGLARaLAVDPD-ILLMDEAFSALD 192
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
321-472 |
2.64e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.76 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDV--NYQVGEKVlVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLEVAYFD-----Q 389
Cdd:PRK11650 5 KLQAVrkSYDGKTQV-IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGgrvvNELEPADRDiamvfQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 390 HRAdLDPERTVMDNLAEG-------KQEvmVNGRPRHVLGYL--QDFLfhpKRamTPvKALSGGERNRLLLA-------K 453
Cdd:PRK11650 84 NYA-LYPHMSVRENMAYGlkirgmpKAE--IEERVAEAARILelEPLL---DR--KP-RELSGGQRQRVAMGraivrepA 154
|
170
....*....|....*....
gi 505190249 454 LFLkpsnlliLDEPTNDLD 472
Cdd:PRK11650 155 VFL-------FDEPLSNLD 166
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-213 |
2.64e-05 |
|
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: 47.60 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 18 LLDNTEIHIEDNERVCLVGRNGAGKSTLLKILgkeiplddgrviyeqdliVARLQQDPPRNIGGSVFDFVAegvaeQAEH 97
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL------------------LRLLSTEGEIQIDGVSWNSVT-----LQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 98 LKAYHAISH--LVESDPSEKNLARMAQ-----IMEILDHQGL----WQLDSRISEVLLQLGLngdaelsSLSGGWLRKAA 166
Cdd:TIGR01271 1291 RKAFGVIPQkvFIFSGTFRKNLDPYEQwsdeeIWKVAEEVGLksviEQFPDKLDFVLVDGGY-------VLSNGHKQLMC 1363
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505190249 167 LGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKE-FDGSIVFISHDR 213
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQsFSNCTVILSEHR 1411
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-376 |
2.88e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 45.88 E-value: 2.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 505190249 321 ELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV 376
Cdd:COG4674 12 YVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSV 67
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
342-473 |
3.08e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 342 VQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG-TKLEVAYFD--QHRADLDPERTVMDNLAEGKQ-------EV 411
Cdd:PRK10938 26 LNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfSHITRLSFEqlQKLVSDEWQRNNTDMLSPGEDdtgrttaEI 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 412 MVNG--RPRHVLGYLQdfLFHPKRAMT-PVKALSGGERNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK10938 106 IQDEvkDPARCEQLAQ--QFGITALLDrRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
316-473 |
3.13e-05 |
|
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: 45.56 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 316 GKIVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKLEVAYFDQH- 390
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDgvdiSKIGLHDLRSRi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 391 --------------RADLDPERTVMD-NLAEGKQEVmvngrprHVLGYLQDflfHPKRAMTPVKA----LSGGERNRLLL 451
Cdd:cd03244 81 siipqdpvlfsgtiRSNLDPFGEYSDeELWQALERV-------GLKEFVES---LPGGLDTVVEEggenLSVGQRQLLCL 150
|
170 180
....*....|....*....|..
gi 505190249 452 AKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDP 172
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
151-189 |
3.36e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 3.36e-05
10 20 30
....*....|....*....|....*....|....*....
gi 505190249 151 DAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDI 189
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-188 |
3.43e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 45.73 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 25 HIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV-IYEQDLIVARLQQDPPrnigGSVFdfvaegvaeQAEHLkayha 103
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtLNGQDHTTTPPSRRPV----SMLF---------QENNL----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 104 ISHL-VES------DPSEK-NLARMAQIMEILDHQGLWQLDSRISevllqlglngdaelSSLSGGWLRKAALGRALVSSP 175
Cdd:PRK10771 83 FSHLtVAQniglglNPGLKlNAAQREKLHAIARQMGIEDLLARLP--------------GQLSGGQRQRVALARCLVREQ 148
|
170
....*....|...
gi 505190249 176 RVLLLDEPTNHLD 188
Cdd:PRK10771 149 PILLLDEPFSALD 161
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-232 |
4.37e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 45.85 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIY-------EQDLIVARLQ-----QDPPRNIggsVFDF 86
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgldtsdEENLWDIRNKagmvfQNPDNQI---VATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 87 VAEGVAEQAEHLKAyhaishlvesDPSEknlarmaqimeildhqglwqLDSRISEVLLQLGLN--GDAELSSLSGGWLRK 164
Cdd:PRK13633 103 VEEDVAFGPENLGI----------PPEE--------------------IRERVDESLKKVGMYeyRRHAPHLLSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505190249 165 AALGRALVSSPRVLLLDEPTNHLD----IETIDWLEGFLKEFDGSIVFISHdrsFIRNM--ATRIVDLDRGKLV 232
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH---YMEEAveADRIIVMDSGKVV 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-232 |
4.61e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 45.59 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRNIG---GSVFDFVAEGVAEQA 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRkkvSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 96 ehlkayhaISHLVESDPseKNLARMAQimeildhqglwQLDSRISEVLLQLGLNGDAELSS---LSGGWLRKAALGRALV 172
Cdd:PRK13641 103 --------VLKDVEFGP--KNFGFSED-----------EAKEKALKWLKKVGLSEDLISKSpfeLSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505190249 173 SSPRVLLLDEPTNHLDIETIDWLEGFLKEFDG---SIVFISHDRSFIRNMATRIVDLDRGKLV 232
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
18-213 |
4.70e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 45.62 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 18 LLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIplddgrviyeqdlivarlqqdpprNIGGsvfDFVAEGVAEQAEH 97
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL------------------------NTEG---DIQIDGVSWNSVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 98 L----KAYHAISH--LVESDPSEKNLarmaqimeilDHQGLWQlDSRISEVLLQLGLN-------GDAELSSLSGGWL-- 162
Cdd:cd03289 72 LqkwrKAFGVIPQkvFIFSGTFRKNL----------DPYGKWS-DEEIWKVAEEVGLKsvieqfpGQLDFVLVDGGCVls 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505190249 163 ----RKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKE-FDGSIVFISHDR 213
Cdd:cd03289 141 hghkQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQaFADCTVILSEHR 196
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-232 |
5.05e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.46 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 14 SDAPLLDNTEIHIEDNERVCLVGRNGAGKS-TLLKILGKEIP---------LDDGRVIYEQDL---IVARLQQDPPrnig 80
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrqtagrvLLDGKPVAPCALrgrKIATIMQNPR---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 81 gSVFDFVaegvaeqaeHLKAYHAIshlvesdpseknlarmaqimEILDHQGLWQLDSRISEVLLQLGLNGDAELSSL--- 157
Cdd:PRK10418 90 -SAFNPL---------HTMHTHAR--------------------ETCLALGKPADDATLTAALEAVGLENAARVLKLypf 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 158 --SGGWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK10418 140 emSGGMLQRMMIALALLCEAPFIIADEPTTDLDVvaqaRILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
.
gi 505190249 232 V 232
Cdd:PRK10418 220 V 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
321-472 |
5.32e-05 |
|
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: 44.88 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVGEK----VLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKL------------- 382
Cdd:cd03258 3 ELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLtllsgkelrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 383 EVAYFDQHRADLDpERTVMDNLA-------EGKQEvmvngRPRHVLGYLQDFLFHPKRAMTPvKALSGGERNRLLLAK-L 454
Cdd:cd03258 83 RIGMIFQHFNLLS-SRTVFENVAlpleiagVPKAE-----IEERVLELLELVGLEDKADAYP-AQLSGGQKQRVGIARaL 155
|
170
....*....|....*...
gi 505190249 455 FLKPSnLLILDEPTNDLD 472
Cdd:cd03258 156 ANNPK-VLLCDEATSALD 172
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
335-503 |
7.12e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.85 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 335 VRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLgqlkADSGRVHCGTKLEvAYFDQHRADLDPERTVMDNlaegkqevmvn 414
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLISFLP-KFSRNKLIFIDQLQFLIDV----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 415 GrprhvLGYLQdflfhPKRAMTpvkALSGGERNRLLLAK-LFLKPSN-LLILDEPTNDLDVETLELLEELIDGY--QG-T 489
Cdd:cd03238 75 G-----LGYLT-----LGQKLS---TLSGGELQRVKLASeLFSEPPGtLFILDEPSTGLHQQDINQLLEVIKGLidLGnT 141
|
170
....*....|....
gi 505190249 490 VLLVSHDRQFVDNS 503
Cdd:cd03238 142 VILIEHNLDVLSSA 155
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-233 |
1.01e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 44.68 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTL--------------LKILGKEIPLDdgrviyEQDLIVARLQ-----QDPPRNI 79
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLflhfngilkptsgeVLIKGEPIKYD------KKSLLEVRKTvgivfQNPDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 80 GGSVfdfVAEGVAEQAEHLKayhaishlvesdpseknlarmaqimeiLDHQglwQLDSRISEVLLQLGLNGDAELSS--L 157
Cdd:PRK13639 92 FAPT---VEEDVAFGPLNLG---------------------------LSKE---EVEKRVKEALKAVGMEGFENKPPhhL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 158 SGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFD--GSIVFIS-HDRSFIRNMATRIVDLDRGKLVS 233
Cdd:PRK13639 139 SGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNkeGITIIIStHDVDLVPVYADKVYVMSDGKIIK 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
130-231 |
1.08e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.04 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 130 QGLWQLDSRISEVL----LQLGL---NGDAELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET---IDWLEGFL 199
Cdd:PRK15439 370 RGFWIKPARENAVLeryrRALNIkfnHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSArndIYQLIRSI 449
|
90 100 110
....*....|....*....|....*....|..
gi 505190249 200 KEFDGSIVFISHDRSFIRNMATRIVDLDRGKL 231
Cdd:PRK15439 450 AAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-472 |
1.19e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 44.13 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 319 VFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLM--LGQLKAD---SGRVHCGT----KLEVAYFdQ 389
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGqdifKMDVIEL-R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 390 HRADL-------DPERTVMDNLAEG-------KQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAKLF 455
Cdd:PRK14247 82 RRVQMvfqipnpIPNLSIFENVALGlklnrlvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170
....*....|....*..
gi 505190249 456 LKPSNLLILDEPTNDLD 472
Cdd:PRK14247 162 AFQPEVLLADEPTANLD 178
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-211 |
1.23e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 43.67 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 10 WLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGKEIP-LDDGRVIYE-QDLIvarlqqdpprniggsvfdf 86
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKtIMGHPKYeVTEGEILFKgEDIT------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 87 vaegvaeqaehlkayhaishlvESDPSEKnlARMAQIMeildhqgLWQLDSRISEVLLQLGLNGDAElsSLSGGWLRKAA 166
Cdd:cd03217 68 ----------------------DLPPEER--ARLGIFL-------AFQYPPEIPGVKNADFLRYVNE--GFSGGEKKRNE 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505190249 167 LGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF---DGSIVFISH 211
Cdd:cd03217 115 ILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreeGKSVLIITH 162
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
337-516 |
1.28e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 44.31 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 337 GFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVhcgtklEVAYFDQH---RADLDPERTVMDNLAEGKQEVM- 412
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI------EWIFKDEKnkkKTKEKEKVLEKLVIQKTRFKKIk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 413 -VNGRPRHVLGYLQ-------------DFLFHP-----------KRAMTPVK--------------ALSGGERNRLLLAK 453
Cdd:PRK13651 99 kIKEIRRRVGVVFQfaeyqlfeqtiekDIIFGPvsmgvskeeakKRAAKYIElvgldesylqrspfELSGGQKRRVALAG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505190249 454 LFLKPSNLLILDEPTNDLD---VETLELLEELIDGYQGTVLLVSHDrqfVDNSV--TECWIFEGNGVI 516
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD---LDNVLewTKRTIFFKDGKI 243
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-229 |
1.42e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 43.85 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 12 SFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLK-----ILGKEIPLDDGRVIYEQDLIVARLQQD--PPRNIGGSVF 84
Cdd:PRK09984 13 TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsglITGDKSAGSHIELLGRTVQREGRLARDirKSRANTGYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 85 dfvaegvaeqaehlkayhaishlvesdpSEKNLARMAQIME-----ILDHQGLW---------QLDSRISEVLLQLGLNG 150
Cdd:PRK09984 93 ----------------------------QQFNLVNRLSVLEnvligALGSTPFWrtcfswftrEQKQRALQALTRVGMVH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 151 DA--ELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF---DGSIVFIS-HDRSFIRNMATRIV 224
Cdd:PRK09984 145 FAhqRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqnDGITVVVTlHQVDYALRYCERIV 224
|
....*
gi 505190249 225 DLDRG 229
Cdd:PRK09984 225 ALRQG 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-195 |
1.66e-04 |
|
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: 43.02 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 13 FSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPlddGRVIYEQDLivarlqqdpprniggsVFDfvaeGVA 92
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVEGDI----------------HYN----GIP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 93 EQAEHLKAYHAISHLVESDPSEKNLArmaqIMEILDhqglwqldsrisevlLQLGLNGDAELSSLSGGWLRKAALGRALV 172
Cdd:cd03233 74 YKEFAEKYPGEIIYVSEEDVHFPTLT----VRETLD---------------FALRCKGNEFVRGISGGERKRVSIAEALV 134
|
170 180
....*....|....*....|....
gi 505190249 173 SSPRVLLLDEPTNHLD-IETIDWL 195
Cdd:cd03233 135 SRASVLCWDNSTRGLDsSTALEIL 158
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
330-473 |
1.76e-04 |
|
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: 44.68 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 330 GEKVLVRGFSAQVQRGDKIALVGPNGCGKT----TLLKLMLGQLKADSGRVH-CGT---KLEVAYFDQHRAD-------- 393
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILfDGQdllGLSERELRRIRGNriamifqe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 394 ----LDPERTVmdnlaeGKQ--EVM-----VNGRP--RHVLGYLQDF-LFHPKRamtPVKA----LSGGERNRLLLA-KL 454
Cdd:COG4172 101 pmtsLNPLHTI------GKQiaEVLrlhrgLSGAAarARALELLERVgIPDPER---RLDAyphqLSGGQRQRVMIAmAL 171
|
170
....*....|....*....
gi 505190249 455 FLKPSnLLILDEPTNDLDV 473
Cdd:COG4172 172 ANEPD-LLIADEPTTALDV 189
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-191 |
1.82e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.41 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 17 PLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPlddgrviYEQDLIVARLQQDP-PRNiggsvfdfvaegvaeqa 95
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK-------GTPVAGCVDVPDNQfGRE----------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 96 ehlkayhaiSHLVESDPSEKNlarMAQIMEILDHQGLwqldsriSEVLLQLglngdAELSSLSGGWLRKAALGRALVSSP 175
Cdd:COG2401 100 ---------ASLIDAIGRKGD---FKDAVELLNAVGL-------SDAVLWL-----RRFKELSTGQKFRFRLALLLAERP 155
|
170
....*....|....*.
gi 505190249 176 RVLLLDEPTNHLDIET 191
Cdd:COG2401 156 KLLVIDEFCSHLDRQT 171
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
318-473 |
2.61e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.93 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 318 IVFELEDVNYQVgekvlVRGFSAQVQRGDKIALVGPNGCGKT-TLLKLMlgQLKADSGRVHCGTKLEVAYFDQHRADLDP 396
Cdd:PRK15134 13 VAFRQQQTVRTV-----VNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSPPVVYPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 397 ERTVMDN-LAEGKQEVMVNGRPRHVL-GYLQDFL-FHpkRAMTPVKA--------------------------LSGGERN 447
Cdd:PRK15134 86 LRGVRGNkIAMIFQEPMVSLNPLHTLeKQLYEVLsLH--RGMRREAArgeilncldrvgirqaakrltdyphqLSGGERQ 163
|
170 180
....*....|....*....|....*.
gi 505190249 448 RLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDV 189
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
143-226 |
2.63e-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: 42.31 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 143 LLQLGLNG---DAELSSLSGGWLRKAALGRALVSSPR--VLLLDEPTNHLDIETIDWLegfLKEFDG------SIVFISH 211
Cdd:cd03238 71 LIDVGLGYltlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL---LEVIKGlidlgnTVILIEH 147
|
90
....*....|....*
gi 505190249 212 DRSFIRNmATRIVDL 226
Cdd:cd03238 148 NLDVLSS-ADWIIDF 161
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
321-376 |
2.88e-04 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 44.02 E-value: 2.88e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505190249 321 ELEDVNYQ---VGEKvlvRGF-----SAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRV 376
Cdd:COG4615 329 ELRGVTYRypgEDGD---EGFtlgpiDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
341-472 |
3.21e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.96 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 341 QVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGrVHCGTKLEVAYFDQHRADLDPerTVMDNLAEGKQ-EVMVNGRPRH 419
Cdd:PLN03130 639 DVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD-ASVVIRGTVAYVPQVSWIFNA--TVRDNILFGSPfDPERYERAID 715
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 420 VLGYLQDFLFHPKRAMTPVKA----LSGGERNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PLN03130 716 VTALQHDLDLLPGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
137-261 |
3.93e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 137 SRISEVLLQLGLNGDA--ELSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETID--WLEGFLKEFDGSIVFISHD 212
Cdd:NF000106 123 ARADELLERFSLTEAAgrAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNevWDEVRSMVRDGATVLLTTQ 202
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 505190249 213 -RSFIRNMATRIVDLDRGKLVSWPGNYDLYLQSKEEALRVEELQNAEFDR 261
Cdd:NF000106 203 yMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAHAAELDR 252
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-219 |
4.03e-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: 42.21 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 34 LVGRNGAGKSTLLkilgkeiplddgrviyeQDLIVARLQQDPPRNIGGsvfDFVAEGVAEQAEHLKAYHAISHlvesdpS 113
Cdd:cd03240 27 IVGQNGAGKTTII-----------------EALKYALTGELPPNSKGG---AHDPKLIREGEVRAQVKLAFEN------A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 114 EKNLARMAQIMEILD-----HQGlwQLDSRISEvllqlglngdaELSSLSGGWLRKA------ALGRALVSSPRVLLLDE 182
Cdd:cd03240 81 NGKKYTITRSLAILEnvifcHQG--ESNWPLLD-----------MRGRCSGGEKVLAsliirlALAETFGSNCGILALDE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505190249 183 PTNHLDIETIDW-----LEGFLKEFDGSIVFISHDRSFIRNM 219
Cdd:cd03240 148 PTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
342-472 |
4.92e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 43.46 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 342 VQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVH-CGTKLEVAYFDQHRA-DLDPERTVMDNLAEGKQEVMVNGRPRH 419
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATvAGKSILTNISDVHQNmGYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505190249 420 V------------LGYLQDFLFHPKRAMTpvkaLSGGERNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR01257 2042 VpaeeiekvanwsIQSLGLSLYADRLAGT----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
335-496 |
5.28e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 42.39 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 335 VRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKLEVAYFDQHRADL-----DPER-----TVMDN 403
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLRRKIgmvfqNPDNqfvgaTVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 404 LAEGKQEvmvNGRPRH-VLGYLQDFLFHPK----RAMTPVKaLSGGERNRLLLAKLFLKPSNLLILDEPTNDLDVETLEL 478
Cdd:PRK13642 103 VAFGMEN---QGIPREeMIKRVDEALLAVNmldfKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180
....*....|....*....|..
gi 505190249 479 LEELI----DGYQGTVLLVSHD 496
Cdd:PRK13642 179 IMRVIheikEKYQLTVLSITHD 200
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-233 |
5.30e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 6 MSGAWLSFSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKeiplddgrvIYEQDlivarlqqdpprniGGSVFd 85
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG---------IYQKD--------------SGSIL- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 86 FVAEGVaeqaEHLKAYHAISHLVESDPSEKNLARMAQIME------------ILDHQGLWQLDSRISEVlLQLGLNGDAE 153
Cdd:PRK10982 57 FQGKEI----DFKSSKEALENGISMVHQELNLVLQRSVMDnmwlgryptkgmFVDQDKMYRDTKAIFDE-LDIDIDPRAK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 154 LSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGF---LKEFDGSIVFISHDRSFIRNMATRIVDLDRGK 230
Cdd:PRK10982 132 VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIirkLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
...
gi 505190249 231 LVS 233
Cdd:PRK10982 212 WIA 214
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-192 |
5.96e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.47 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 13 FSDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQdlivarlqqdppRNIGgsvfdfvaegvA 92
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER------------QSIK-----------K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 93 EQAEHLKAYHAISHLVESDPsekNLA-RMAQIMEILDHQGLWQLDSRISevLLQLGLNGDAELSSLSGGWLRKAALGRAL 171
Cdd:PRK13540 68 DLCTYQKQLCFVGHRSGINP---YLTlRENCLYDIHFSPGAVGITELCR--LFSLEHLIDYPCGLLSSGQKRQVALLRLW 142
|
170 180
....*....|....*....|....
gi 505190249 172 VSSPRVLLLDEPTNHLD---IETI 192
Cdd:PRK13540 143 MSKAKLWLLDEPLVALDelsLLTI 166
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-217 |
7.21e-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: 42.81 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 18 LLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYEQDLIVARLQQDPPRNIGG---------SVFDFVA 88
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTlrdqiiypdSSEDMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 89 EGVAEQaeHLKAYhaishLVEsdpseknlarmAQIMEILDHQGLWQLDSRISEVllqlglngdaelssLSGGWLRKAALG 168
Cdd:TIGR00954 547 RGLSDK--DLEQI-----LDN-----------VQLTHILEREGGWSAVQDWMDV--------------LSGGEKQRIAMA 594
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505190249 169 RALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGSIVFISHDRSFIR 217
Cdd:TIGR00954 595 RLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWK 643
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
335-500 |
8.32e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 41.51 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 335 VRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHC-GTKLE------------VAYFDQHRadLDPERTVM 401
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLrGQHIEglpghqiarmgvVRTFQHVR--LFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 402 DNLaegkqevMVnGRPRHV-LGYLQDFLFHP----------KRAMT-------------PVKALSGGERNRLLLAKLFLK 457
Cdd:PRK11300 99 ENL-------LV-AQHQQLkTGLFSGLLKTPafrraesealDRAATwlervgllehanrQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505190249 458 PSNLLILDEPTNDLDVETLELLEELIDG----YQGTVLLVSHDRQFV 500
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAElrneHNVTVLLIEHDMKLV 217
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
26-188 |
8.33e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.14 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 26 IEDNERVCLVGRNGAGKSTLLK-------ILGKEIPLDDGRViyeQDLivarlqqDPP-RNIGG-----------SVFDF 86
Cdd:PRK11650 27 VADGEFIVLVGPSGCGKSTLLRmvaglerITSGEIWIGGRVV---NEL-------EPAdRDIAMvfqnyalyphmSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 87 VAEGvaeqaehLK----AYHAIshlvesdpsEKNLARMAQIMEIldhQGLwqLDSRISEvllqlglngdaelssLSGGWL 162
Cdd:PRK11650 97 MAYG-------LKirgmPKAEI---------EERVAEAARILEL---EPL--LDRKPRE---------------LSGGQR 140
|
170 180
....*....|....*....|....*.
gi 505190249 163 RKAALGRALVSSPRVLLLDEPTNHLD 188
Cdd:PRK11650 141 QRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-242 |
9.00e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 41.76 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRV----IYEQDLIVARLQQDPP-----------RNIGGSV 83
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPyskkiknfkelRRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 84 FDFvaegvaeqaehlKAYHAISHLVESDPSEKNLArmAQIMEILDHQglwqldsRISEVLLQLGLNGD-AELS--SLSGG 160
Cdd:PRK13631 122 FQF------------PEYQLFKDTIEKDIMFGPVA--LGVKKSEAKK-------LAKFYLNKMGLDDSyLERSpfGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 161 WLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF--DGSIVF-ISHDRSFIRNMATRIVDLDRGKLVSWPGN 237
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkaNNKTVFvITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
....*
gi 505190249 238 YDLYL 242
Cdd:PRK13631 261 YEIFT 265
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
321-496 |
9.26e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 41.74 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 321 ELEDVNYQVG-----EKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGrvhcgtKLEVAyfDQHradLD 395
Cdd:PRK13641 4 KFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSG------TITIA--GYH---IT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 396 PErTVMDNLAEGKQEV-MVNGRPRHVL---GYLQDFLFHPK-----------RAMTPVKA--------------LSGGER 446
Cdd:PRK13641 73 PE-TGNKNLKKLRKKVsLVFQFPEAQLfenTVLKDVEFGPKnfgfsedeakeKALKWLKKvglsedliskspfeLSGGQM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505190249 447 NRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELIDGYQG---TVLLVSHD 496
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHN 204
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
332-473 |
1.06e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 41.35 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 332 KVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGTKLEVAYFDQHRADLDPE-----RTVMDNLAE 406
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNGEPLAAIDAPrlarlRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 407 -----GKQEVMVNGRPRHVLGylQDFLFHPKRAMT---------------PVKALSGGERNRL----LLAKLF-----LK 457
Cdd:PRK13547 94 pafafSAREIVLLGRYPHARR--AGALTHRDGEIAwqalalagatalvgrDVTTLSGGELARVqfarVLAQLWpphdaAQ 171
|
170
....*....|....*.
gi 505190249 458 PSNLLILDEPTNDLDV 473
Cdd:PRK13547 172 PPRYLLLDEPTAALDL 187
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
158-212 |
1.07e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 41.63 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 505190249 158 SGGWLRKAALGRALVSSPRVLLLDEPTNHLDI----ETIDWLEGFLKEFDGSIVFISHD 212
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHD 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
34-230 |
1.12e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 34 LVGRNGAGKSTLLKILGK-------EIPLDDGRVIYEQDLIVAR-----LQQDP-------PRNIGGSVFDFV-AEGVAE 93
Cdd:PTZ00265 416 FVGESGCGKSTILKLIERlydptegDIIINDSHNLKDINLKWWRskigvVSQDPllfsnsiKNNIKYSLYSLKdLEALSN 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 94 QAEHLKAYHAISHLVESDPSEKNLARMAQIMEILDHQGLWQL--------DSRI----SEVLLQ-------------LGL 148
Cdd:PTZ00265 496 YYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMrknyqtikDSEVvdvsKKVLIHdfvsalpdkyetlVGS 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 149 NGdaelSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEFDGS----IVFISHDRSFIRNMATRIV 224
Cdd:PTZ00265 576 NA----SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNenriTIIIAHRLSTIRYANTIFV 651
|
....*.
gi 505190249 225 DLDRGK 230
Cdd:PTZ00265 652 LSNRER 657
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
154-231 |
1.39e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 154 LSSLSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET---IDWLEGFLKEFDGSIVFISHDRSFIRNMATRIVDLDRGK 230
Cdd:PRK10982 389 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAkfeIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGL 468
|
.
gi 505190249 231 L 231
Cdd:PRK10982 469 V 469
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-258 |
1.58e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 41.62 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 14 SDAPLLDNTEIHIEDNERVCLVGRNGAGKSTLLKILGKEIPLDDGRVIYeQDLIVARLQQDPPRN----IGGSVF---DF 86
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF-HDIPLTKLQLDSWRSrlavVSQTPFlfsDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 87 VAEGVAeqaehlkayhaishLVESDPSEKNLARMAQImeildhqglwqldSRISEVLLQLGLNGDAELSS----LSGGWL 162
Cdd:PRK10789 405 VANNIA--------------LGRPDATQQEIEHVARL-------------ASVHDDILRLPQGYDTEVGErgvmLSGGQK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 163 RKAALGRALVSSPRVLLLDEPTNHLDIETIDWLEGFLKEF-DGSIVFISHDRSFIRNMATRIVDLDRG---------KLV 232
Cdd:PRK10789 458 QRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWgEGRTVIISAHRLSALTEASEILVMQHGhiaqrgnhdQLA 537
|
250 260
....*....|....*....|....*...
gi 505190249 233 SWPGNY-DLY-LQSKEEALRVEELQNAE 258
Cdd:PRK10789 538 QQSGWYrDMYrYQQLEAALDDAPEIREE 565
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
18-68 |
1.70e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 41.05 E-value: 1.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 505190249 18 LLDNTEIHIeDNERVCLVGRNGAGKSTLLKIL------GKEIPLDDGRVIYEQDLIV 68
Cdd:pfam13175 13 CLKDTEIDL-DEDLTVLIGKNNSGKSSILEALdiflnnKEKFFEDDFLVLYLKDVIK 68
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-223 |
1.75e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.94 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 14 SDAPL--LDNTEIHIEDNERVCLVGRNGAGKSTLLK-ILGkeIPLDDGRVIYEQ----DLIVARLQQDPPRNIGGsvfdf 86
Cdd:PRK15093 16 SDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKaICG--VTKDNWRVTADRmrfdDIDLLRLSPRERRKLVG----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 87 vaegvaeqaehlkayHAISHLVES-----DPSEKNLARMAQIMEILDHQGLWQL-----DSRISEVLLQLGLNGDAELSS 156
Cdd:PRK15093 89 ---------------HNVSMIFQEpqsclDPSERVGRQLMQNIPGWTYKGRWWQrfgwrKRRAIELLHRVGIKDHKDAMR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505190249 157 -----LSGGWLRKAALGRALVSSPRVLLLDEPTNHLDIET----IDWLEGFLKEFDGSIVFISHDRSFIRNMATRI 223
Cdd:PRK15093 154 sfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqiFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
290-362 |
2.09e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 290 ALRVERSQRREVMGTAKMQVEEAT-------RSGKIVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLL 362
Cdd:PTZ00243 1274 ALERRTGMAADVTGTVVIEPASPTsaaphpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLL 1353
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
437-500 |
3.13e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 3.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505190249 437 PVKALSGGERNRLLLAKLFLKPS---NLLILDEPTNDL---DVETLELLEELIDgYQG-TVLLVSHDRQFV 500
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAYELLAPSkkpTLYVLDEPTTGLhthDIKALIYVLQSLT-HQGhTVVIIEHNMHVV 875
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
566-630 |
3.36e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 566 LLRELEQLPQRLEQLEAEIEALQAQMSDADFFTRPHSETQEVLTALAD-----AEQALEQAFARWEELEA 630
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlslaTEEELQDLAEELEELQQ 206
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-49 |
3.39e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.98 E-value: 3.39e-03
10 20 30
....*....|....*....|....*....|..
gi 505190249 19 LDNTEIHIEDNERV-CLVGRNGAGKSTLLKIL 49
Cdd:COG3950 14 FEDLEIDFDNPPRLtVLVGENGSGKTTLLEAI 45
|
|
| HemX |
COG2959 |
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis ... |
515-621 |
3.45e-03 |
|
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis HemX, COG0755, no evidence of involvement in heme biosynthesis) [General function prediction only];
Pssm-ID: 442199 [Multi-domain] Cd Length: 361 Bit Score: 39.95 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 515 VINAFVGGYYDAHHQ----RATAKPIRQAAPSASKPAAEKKAEQpkKTAAKLSYNLLRELEQLPQRLEQLEAEIEALQAQ 590
Cdd:COG2959 40 ALAAGGGGYYLGWQQlqqqQAELAQLAQQLAALQQQAQELRALA--QQLQELLQQLAARLAQLEQRLAELQQQLAALQQL 117
|
90 100 110
....*....|....*....|....*....|.
gi 505190249 591 MSDAdfftrphSETQEVLTALADAEQALEQA 621
Cdd:COG2959 118 LQSL-------SGSSRDDWLLAEAEYLLRLA 141
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
307-471 |
3.66e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.42 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 307 MQVEEATrsGKIVFELEDVNYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCG----TKL 382
Cdd:PRK15439 1 MQTSDTT--APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgnpcARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 383 EVA-------YFDQHRADLDPERTVMDNLAEGKQEVMVNGRPRHVLgyLQDFLFHPKRAMtPVKALSGGERNRLLLAKLF 455
Cdd:PRK15439 79 TPAkahqlgiYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQL--LAALGCQLDLDS-SAGSLEVADRQIVEILRGL 155
|
170
....*....|....*.
gi 505190249 456 LKPSNLLILDEPTNDL 471
Cdd:PRK15439 156 MRDSRILILDEPTASL 171
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
437-471 |
5.64e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 5.64e-03
10 20 30
....*....|....*....|....*....|....*...
gi 505190249 437 PVKALSGGERNRLLLAKLFLKPSN---LLILDEPTNDL 471
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGL 863
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
347-368 |
5.67e-03 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 37.86 E-value: 5.67e-03
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
349-505 |
6.90e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 37.72 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 349 ALVGPNGCGKTTLLK---LMLGqlkadsGRVHCGTKLEVAYFDQHRADLDPERTVMdnlaegkqevmvngrprhvlgylq 425
Cdd:cd03227 25 IITGPNGSGKSTILDaigLALG------GAQSATRRRSGVKAGCIVAAVSAELIFT------------------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 426 dflfhpkramtpVKALSGGERNRLLLAKLF----LKPSNLLILDEPTNDLDVETLELLEELIDGY---QGTVLLVSHDRQ 498
Cdd:cd03227 75 ------------RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvkGAQVIVITHLPE 142
|
....*..
gi 505190249 499 FVDNSVT 505
Cdd:cd03227 143 LAELADK 149
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
326-472 |
7.35e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 39.31 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 326 NYQVGEKVLVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGrvhcgtklEVAYFDQHRAD--LDPER----- 398
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG--------DIRFHDIPLTKlqLDSWRsrlav 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 399 ----------TVMDNLAEGK-----QEVMVNGRPRHVlgyLQDFLFHPKRAMTPVKA----LSGGERNRLLLAKLFLKPS 459
Cdd:PRK10789 394 vsqtpflfsdTVANNIALGRpdatqQEIEHVARLASV---HDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNA 470
|
170
....*....|...
gi 505190249 460 NLLILDEPTNDLD 472
Cdd:PRK10789 471 EILILDDALSAVD 483
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-49 |
7.37e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.39 E-value: 7.37e-03
10 20 30
....*....|....*....|....*....|.
gi 505190249 19 LDNTEIHIEDNERVCLVGRNGAGKSTLLKIL 49
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVL 47
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
315-472 |
7.61e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 38.84 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 315 SGKIVfeLEDVNYQVGEKV-----LVRGFSAQVQRGDKIALVGPNGCGKTTLLKLMLGQLKADSGRVHCGT--------- 380
Cdd:PRK13645 4 SKDII--LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505190249 381 -------KLEVAYFDQHradldPERTVMD------------NLAEGKQEVMvnGRPRHVLGYLQDFLFHPKRamTPVKaL 441
Cdd:PRK13645 82 ikevkrlRKEIGLVFQF-----PEYQLFQetiekdiafgpvNLGENKQEAY--KKVPELLKLVQLPEDYVKR--SPFE-L 151
|
170 180 190
....*....|....*....|....*....|.
gi 505190249 442 SGGERNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
437-471 |
8.04e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.36 E-value: 8.04e-03
10 20 30
....*....|....*....|....*....|....*...
gi 505190249 437 PVKALSGGERNRLLLAKLFLKPSN---LLILDEPTNDL 471
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGL 203
|
|
| |
