|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-633 |
0e+00 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 1106.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSD 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 81 LTVFDYTAEGLAGVGELLKKYHHISMELAHDPSDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDPDATLDSLSGG 160
Cdd:PRK11147 81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDE 240
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 241 YLQGKEEALRVEELQHAEFDRKLAQEEVWVRQGIKARRTRNEGRVRALEAMRMERSQRRELQGKAKLQMDDVNRSGKLVF 320
Cdd:PRK11147 241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRSGKIVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYRDQLDPEQTV 400
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:PRK11147 401 MDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 481 ELLADYPGTLLLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYADMMATRAqQSTQLAAKAAQVKTPEPVAVASPAASKV 560
Cdd:PRK11147 481 ELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQQQA-QYLALKQPAVKKKEEAAAPKAETVKRSS 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 561 KKLSYKLQLELDNLPARLEQLETELNALQAEVNHPGFFALPSDQTQLKLDALNAAEAALEQAFSRWEELEALK 633
Cdd:PRK11147 560 KKLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLADLADAEQELEVAFERWEELEALK 632
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-528 |
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: 687.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 6 LHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSDLTVFD 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 86 YTAEGLAGVGELLKKYHHISMELAHdpSDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNL---DPDATLDSLSGGWL 162
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAE--PDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFpeeDLDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 163 RKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYL 242
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 243 QGKEEALRVEELQHAEFDRKLAQEEVWVRQ-GIKARR-TRNEGRVRALEAMRMERSQRRElqGKAKLQMDDVNRSGKLVF 320
Cdd:COG0488 239 EQRAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARKaKQAQSRIKALEKLEREEPPRRD--KTVEIRFPPPERLGKKVL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYRDQLDPEQTV 400
Cdd:COG0488 317 ELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEGKQEvmvrGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:COG0488 397 LDELRDGAPG----GTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1411607396 481 ELLADYPGTLLLVSHDRRFIDNTVTGCWLFEgDGRISDYVGGYADMMA 528
Cdd:COG0488 473 EALDDFPGTVLLVSHDRYFLDRVATRILEFE-DGGVREYPGGYDDYLE 519
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-545 |
2.58e-136 |
|
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: 409.71 E-value: 2.58e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelpLD---DGRMVQQQDLKVTRLEQDPPASSDLTVFDYTAEGLAG 93
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDkdfNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 94 VGELLKKYHHISMELAHDPSDAN--IRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDP-DATLDSLSGGWLRKVALARA 170
Cdd:TIGR03719 96 IKDALDRFNEISAKYAEPDADFDklAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPwDADVTKLSGGERRRVALCRL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 171 LACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYLQGKEEALR 250
Cdd:TIGR03719 176 LLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 251 VEELQHAEFDRKLAQEEVWVRQGIKARRTRNEGRVRALEAMRMERSQRRElqGKAKLQMDDVNRSGKLVFETEGLGLDFG 330
Cdd:TIGR03719 256 QEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRN--ETAEIYIPPGPRLGDKVIEAENLTKAFG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYRDQLDPEQTVMDNVGEGKQE 410
Cdd:TIGR03719 334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEEISGGLDI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 411 VMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPGTL 490
Cdd:TIGR03719 414 IKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCA 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 491 LLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYADMMATRAQqstQLAAKAAQVK 545
Cdd:TIGR03719 494 VVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEEDKKR---RLGEDADQPH 545
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-525 |
2.04e-134 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 404.89 E-value: 2.04e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelpLD---DGRMVQQQDLKVTRLEQDPPASSDLTVFDYTAEGLAG 93
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDkefEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 94 VGELLKKYHHISMELAHDP--SDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNL-DPDATLDSLSGGWLRKVALARA 170
Cdd:PRK11819 98 VKAALDRFNEIYAAYAEPDadFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCpPWDAKVTKLSGGERRRVALCRL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 171 LACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYLQGKEEALR 250
Cdd:PRK11819 178 LLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAKRLA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 251 VEELQHAEFDRKLAQEEVWVRQGIKARRTRNEGRVRALEAMRMERSQRRElqGKAKLQMDDVNRSGKLVFETEGLGLDFG 330
Cdd:PRK11819 258 QEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYEELLSEEYQKRN--ETNEIFIPPGPRLGDKVIEAENLSKSFG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYRDQLDPEQTVMDNVGEGKQE 410
Cdd:PRK11819 336 DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKTVWEEISGGLDI 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 411 VMVRGR---SRhilGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYP 487
Cdd:PRK11819 416 IKVGNReipSR---AYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFP 492
|
490 500 510
....*....|....*....|....*....|....*...
gi 1411607396 488 GTLLLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYAD 525
Cdd:PRK11819 493 GCAVVISHDRWFLDRIATHILAFEGDSQVEWFEGNFQE 530
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-531 |
9.38e-91 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 291.03 E-value: 9.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 13 FSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSDLTVFDYTAEGLA 92
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVIMGHT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 93 GVGELLKKYHHISMELahDPSDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDPD---ATLDSLSGGWLRKVALAR 169
Cdd:PRK15064 91 ELWEVKQERDRIYALP--EMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEqhyGLMSEVAPGWKLRVLLAQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 170 ALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYLQGKEEAl 249
Cdd:PRK15064 169 ALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQA- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 250 rvEELQHAEFDRKLAQ-EEVwvrQGIKARRTRNegrvrALEAmRMERSQRRELQgkaKLQMDDVNRSGK----------- 317
Cdd:PRK15064 248 --RERLLADNAKKKAQiAEL---QSFVSRFSAN-----ASKA-KQATSRAKQID---KIKLEEVKPSSRqnpfirfeqdk 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 318 ----LVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQ-YRD 392
Cdd:PRK15064 314 klhrNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdHAY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 QLDPEQTVMDNVGEGKQ----EVMVRGrsrhILGYLqdfLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPT 468
Cdd:PRK15064 394 DFENDLTLFDWMSQWRQegddEQAVRG----TLGRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 469 NDLDVETLELLEELLADYPGTLLLVSHDRRFIDNTVTGCWLFEGDGrISDYVGGYADMMATRA 531
Cdd:PRK15064 467 NHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDG-VVDFSGTYEEYLRSQG 528
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-592 |
3.95e-69 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 236.61 E-value: 3.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASsDLTVFDYTAEGLagvgel 97
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPAL-PQPALEYVIDGD------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 98 lKKYHHISMELAHDPSDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDPDA---TLDSLSGGWLRKVALARALACD 174
Cdd:PRK10636 89 -REYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQlerPVSDFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 175 PDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYLQGKEEALRVEEL 254
Cdd:PRK10636 168 SDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 255 QHAEFDRKLAQEEVWV-RQGIKARRTRN-EGRVRALEamRMERSQRRELQGKAKLQMDDVNRSGKLVFETEGLGLDFGDR 332
Cdd:PRK10636 248 MYESQQERVAHLQSYIdRFRAKATKAKQaQSRIKMLE--RMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSAGYGDR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 333 TLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYrdqldpeQTVMDNVGEGKQEVM 412
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQH-------QLEFLRADESPLQHL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 413 VRGRSRHILGYLQDFL----FEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPG 488
Cdd:PRK10636 399 ARLAPQELEQKLRDYLggfgFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 489 TLLLVSHDRRFIDNTVTGCWL--------FEGDgrISDYVGGYADMMATRAQQS---TQLAAKAAQVKTPEPVAVAspaa 557
Cdd:PRK10636 479 ALVVVSHDRHLLRSTTDDLYLvhdgkvepFDGD--LEDYQQWLSDVQKQENQTDeapKENNANSAQARKDQKRREA---- 552
|
570 580 590
....*....|....*....|....*....|....*
gi 1411607396 558 sKVKKLSYKLQLELDNLPARLEQLETELNALQAEV 592
Cdd:PRK10636 553 -ELRTQTQPLRKEIARLEKEMEKLNAQLAQAEEKL 586
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
18-525 |
2.62e-59 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 211.26 E-value: 2.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIA-----------------GELPLDDGRMVQ---QQDLKVTRLEQDP-- 75
Cdd:PLN03073 192 LIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilhveQEVVGDDTTALQcvlNTDIERTQLLEEEaq 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 76 --PASSDLTVFDYTAEGLAGVGELLKKyhhismelahdpsDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDPDAT 153
Cdd:PLN03073 272 lvAQQRELEFETETGKGKGANKDGVDK-------------DAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 154 L---DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGV 230
Cdd:PLN03073 339 VkatKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 231 ITSWPGNYDEYLQGKEEALRVEELQHAEFDRKLAQEEVWV---RQGIKaRRTRNEGRVRALEAMRMERSQRRELQGKAKL 307
Cdd:PLN03073 419 LVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIdkfRYNAK-RASLVQSRIKALDRLGHVDAVVNDPDYKFEF 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 308 QMDDVNRSGKLV-FETEGLGLDfGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAY 386
Cdd:PLN03073 498 PTPDDRPGPPIIsFSDASFGYP-GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAV 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 387 FDQYR-DQLDPEQT---VMDNVGEGKQEVMVRGrsrhilgYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLL 462
Cdd:PLN03073 577 FSQHHvDGLDLSSNpllYMMRCFPGVPEQKLRA-------HLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIL 649
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 463 ILDEPTNDLDVETLELLEELLADYPGTLLLVSHDRRFIDNTVTGCWLFEgDGRISDYVGGYAD 525
Cdd:PLN03073 650 LLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVS-EGKVTPFHGTFHD 711
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-243 |
4.67e-55 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 195.67 E-value: 4.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPA-SSDL 81
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEElDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 TVFDYtaeglagvgellkkyhhismelahdpsdaniriMSDLQEQLDyqngwqfETRISQVLTLLNLDPDATL---DSLS 158
Cdd:COG0488 395 TVLDE---------------------------------LRDGAPGGT-------EQEVRGYLGRFLFSGDDAFkpvGVLS 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNY 238
Cdd:COG0488 435 GGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGY 514
|
....*
gi 1411607396 239 DEYLQ 243
Cdd:COG0488 515 DDYLE 519
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-542 |
8.20e-54 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 192.20 E-value: 8.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 322 TEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyRDQLDPEQTVM 401
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQ-EPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEGKQEVM-VRGRSRHI-------------LGYLQDFL--------------------FEPKRARTPVKALSGGEKN 447
Cdd:COG0488 80 DTVLDGDAELRaLEAELEELeaklaepdedlerLAELQEEFealggweaearaeeilsglgFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 448 RLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPGTLLLVSHDRRFIDNTVTgcWLFE-GDGRISDYVGGYADM 526
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVAT--RILElDRGKLTLYPGNYSAY 237
|
250
....*....|....*.
gi 1411607396 527 MATRAQQSTQLAAKAA 542
Cdd:COG0488 238 LEQRAERLEQEAAAYA 253
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
323-514 |
2.04e-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: 171.48 E-value: 2.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyrdqldpeqtvmd 402
Cdd:cd03221 4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 403 nvgegkqevmvrgrsrhilgylqdflfepkrartpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEEL 482
Cdd:cd03221 71 --------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEA 112
|
170 180 190
....*....|....*....|....*....|..
gi 1411607396 483 LADYPGTLLLVSHDRRFIDNTVTGCWLFEGDG 514
Cdd:cd03221 113 LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-229 |
8.90e-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: 169.55 E-value: 8.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQdppassdltv 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 fdytaeglagvgellkkyhhismelahdpsdanirimsdlqeqldyqngwqfetrisqvltllnldpdatldsLSGGWLR 163
Cdd:cd03221 71 -------------------------------------------------------------------------LSGGEKM 77
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd03221 78 RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-473 |
1.76e-44 |
|
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: 166.23 E-value: 1.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 2 ALLTLHGACLSF--SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP---------LDDGRMVQQQDLKVTR 70
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrisgevLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 71 LE-----QDPPASSD-LTVFDYTAEGLagvgellkkyhhismeLAHDPSDANIRimsdlqeqldyqngwqfeTRISQVLT 144
Cdd:COG1123 83 RRigmvfQDPMTQLNpVTVGDQIAEAL----------------ENLGLSRAEAR------------------ARVLELLE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 145 LLNLDP--DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHK 218
Cdd:COG1123 129 AVGLERrlDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 219 LATRIIDLDRGVItswpgnydeylqgkeealrVEELQHAEFDRklaqeevwvrqgikarrtrnegRVRALEAMRMERSQR 298
Cdd:COG1123 209 IADRVVVMDDGRI-------------------VEDGPPEEILA----------------------APQALAAVPRLGAAR 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 299 RELQGKAklqmddvnRSGKLVFETEGLGLDF-----GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSR 373
Cdd:COG1123 248 GRAAPAA--------AAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTS 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 374 G--LVKG---GTKLEVAYFDQYRD----------QLDPEQTVMDNVGEGkqeVMVRG------RSRHILGYLQDFLFEPK 432
Cdd:COG1123 320 GsiLFDGkdlTKLSRRSLRELRRRvqmvfqdpysSLNPRMTVGDIIAEP---LRLHGllsraeRRERVAELLERVGLPPD 396
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1411607396 433 RARTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG1123 397 LADRYPHELSGGQRQRVAIARaLALEPK-LLILDEPTSALDV 437
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-231 |
1.75e-37 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 139.79 E-value: 1.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDL----------KVTRL 71
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvLLDGRDLaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 72 EQDPPASSDLTVFDYTAEGLagvgellkkYHHISMELAHDPSDanirimsdlqeqldyqngwqfETRISQVLTLLNLDP- 150
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGR---------YPHLGLFGRPSAED---------------------REAVEEALERTGLEHl 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 -DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIID 225
Cdd:COG1120 131 aDRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVL 210
|
....*.
gi 1411607396 226 LDRGVI 231
Cdd:COG1120 211 LKDGRI 216
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
12-231 |
2.56e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 138.66 E-value: 2.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------VQQQDLKVTR----LEQDPPASSDL 81
Cdd:COG1131 9 RYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedVARDPAEVRRrigyVPQEPALYPDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 TVFDYTaeglagvgELLKKYHHISMELAhdpsdanirimsdlqeqldyqngwqfETRISQVLTLLNLDP--DATLDSLSG 159
Cdd:COG1131 89 TVRENL--------RFFARLYGLPRKEA--------------------------RERIDELLELFGLTDaaDRKVGTLSG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFIS-HDREFIHKLATRIIDLDRGVI 231
Cdd:COG1131 135 GMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVAIIDKGRI 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-257 |
1.19e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.14 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------VQQQDLKVTRLEQD 74
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgkpPRRARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 75 PPASSD--LTVFDYTAEGLAGVGELLKKYHHIsmelahdpsdanirimsdlqeqlDYQngwqfetRISQVLTLLNLDP-- 150
Cdd:COG1121 84 AEVDWDfpITVRDVVLMGRYGRRGLFRRPSRA-----------------------DRE-------AVDEALERVGLEDla 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLD 227
Cdd:COG1121 134 DRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLN 213
|
250 260 270
....*....|....*....|....*....|....*.
gi 1411607396 228 RGVITSwpGNYDEYLQgkEEAL------RVEELQHA 257
Cdd:COG1121 214 RGLVAH--GPPEEVLT--PENLsrayggPVALLAHG 245
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
12-231 |
1.82e-34 |
|
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: 128.67 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmvqqqdlkVTRLEQDPPASsdltvfdytaegl 91
Cdd:cd03230 9 RYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGE--------IKVLGKDIKKE------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 92 agvGELLKKyhhismelahdpsdaNIRIMSDLQEQLDYQNGWQfetrisqvltllNLDpdatldsLSGGWLRKVALARAL 171
Cdd:cd03230 68 ---PEEVKR---------------RIGYLPEEPSLYENLTVRE------------NLK-------LSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 172 ACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-229 |
6.82e-34 |
|
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: 128.35 E-value: 6.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFS----DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTRLE----------QDP 75
Cdd:cd03225 5 LSFSypdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvLVDGKDLTKLSLKelrrkvglvfQNP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 76 passD-----LTVFDYTAEGLAGVGellkkyhhismelaHDPSDAnirimsdlqeqldyqngwqfETRISQVLTLLNLDP 150
Cdd:cd03225 85 ----DdqffgPTVEEEVAFGLENLG--------------LPEEEI--------------------EERVEEALELVGLEG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 --DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIHKLATRIID 225
Cdd:cd03225 127 lrDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRVIV 206
|
....
gi 1411607396 226 LDRG 229
Cdd:cd03225 207 LEDG 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-231 |
8.58e-34 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 129.21 E-value: 8.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD------DGRMVQQQDLKVTR----LEQDPPASSDL 81
Cdd:COG4555 10 KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDsgsiliDGEDVRKEPREARRqigvLPDERGLYDRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 TVFDytaeglagvgellkkyhhismelahdpsdaNIRIMSDLQEQLDYQNgwqfETRISQVLTLLNLDP--DATLDSLSG 159
Cdd:COG4555 90 TVRE------------------------------NIRYFAELYGLFDEEL----KKRIEELIELLGLEEflDRRVGELST 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:COG4555 136 GMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-246 |
1.27e-32 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 132.32 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPA--SSDL 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYdfENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 TVFDYtaeglagvgellkkyhhisMELAHDPSDANIRIMSDLQEQLDYQNgwqfetrisqvltllnlDPDATLDSLSGGW 161
Cdd:PRK15064 400 TLFDW-------------------MSQWRQEGDDEQAVRGTLGRLLFSQD-----------------DIKKSVKVLSGGE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEY 241
Cdd:PRK15064 444 KGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
....*..
gi 1411607396 242 L--QGKE 246
Cdd:PRK15064 524 LrsQGIE 530
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-228 |
1.91e-32 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 124.13 E-value: 1.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtRLEQDPPASSDL 81
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEV---------LWNGEPIRDARE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 TVFDYTAeglagvgellkkYhhismeLAHDPsdaniRIMSDL--QEQLDY----QNGWQFETRISQVLTLLNLDP--DAT 153
Cdd:COG4133 72 DYRRRLA------------Y------LGHAD-----GLKPELtvRENLRFwaalYGLRADREAIDEALEAVGLAGlaDLP 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDREFIhkLATRIIDLDR 228
Cdd:COG4133 129 VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLEL--AAARVLDLGD 204
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-232 |
6.04e-32 |
|
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: 124.15 E-value: 6.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFS----DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------VQQQDLKVTR-- 70
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpVTRRRRKAFRrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 71 ---LEQDPPASSD--LTVFDYTAEGLAGvgellkkyHHISMElahdpsdanirimsdlqeqldyqngwqfETRISQVLTL 145
Cdd:COG1124 81 vqmVFQDPYASLHprHTVDRILAEPLRI--------HGLPDR----------------------------EERIAELLEQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 146 LNLDPDAtLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIH 217
Cdd:COG1124 125 VGLPPSF-LDryphQLSGGQRQRVAIARALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVA 203
|
250
....*....|....*
gi 1411607396 218 KLATRIIDLDRGVIT 232
Cdd:COG1124 204 HLCDRVAVMQNGRIV 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-231 |
1.07e-31 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 122.83 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFS---DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTRLE----------QDP- 75
Cdd:COG1122 6 LSFSypgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlVDGKDITKKNLRelrrkvglvfQNPd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 76 -----PassdlTVFDYTAEGLagvgellkkyhhisMELAHDPSDAnirimsdlqeqldyqngwqfETRISQVLTLLNLDP 150
Cdd:COG1122 86 dqlfaP-----TVEEDVAFGP--------------ENLGLPREEI--------------------RERVEEALELVGLEH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 --DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIHKLATRIID 225
Cdd:COG1122 127 laDRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAELADRVIV 206
|
....*.
gi 1411607396 226 LDRGVI 231
Cdd:COG1122 207 LDDGRI 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-231 |
1.29e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 121.85 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM----VQQQDLKVTRLEQDP---P 76
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMPPPEWRRQVayvP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 77 ASSDLtvFDYTaeglagVGELLKKYHHISmelahdpsdanirimsdlQEQLDyqngwqfETRISQVLTLLNLDP---DAT 153
Cdd:COG4619 81 QEPAL--WGGT------VRDNLPFPFQLR------------------ERKFD-------RERALELLERLGLPPdilDKP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEA----INWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:COG4619 128 VERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
..
gi 1411607396 230 VI 231
Cdd:COG4619 208 RL 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-231 |
5.49e-31 |
|
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: 120.33 E-value: 5.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 6 LHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD------DGRMVQQQDLKVTRLEQDPPASS 79
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTsgsirvFGKPLEKERKRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 80 D--LTVFDYTAEGLAGVGELLKKYHHISMELAhdpsdanirimsdlQEQLDyqngwqfETRISQVLtllnldpDATLDSL 157
Cdd:cd03235 82 DfpISVRDVVLMGLYGHKGLFRRLSKADKAKV--------------DEALE-------RVGLSELA-------DRQIGEL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03235 134 SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-231 |
3.77e-30 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 118.01 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLE---------- 72
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEiLIDGRD--VTGVPperrnigmvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 QDPPASSDLTVFDYTAEGLagvgellkkyhhismelahdpsdaNIRIMSDLQEQldyqngwqfeTRISQVLTLLNLDPDA 152
Cdd:cd03259 79 QDYALFPHLTVAENIAFGL------------------------KLRGVPKAEIR----------ARVRELLELVGLEGLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 153 TL--DSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDL 226
Cdd:cd03259 125 NRypHELSGGQQQRVALARALAREPSLLLLDEPLSALDaklrEELREELKELQRELGITTIYVTHDQEEALALADRIAVM 204
|
....*
gi 1411607396 227 DRGVI 231
Cdd:cd03259 205 NEGRI 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-233 |
1.07e-29 |
|
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: 115.61 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 5 TLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmvqqqdlkvtrleqdppassdLTVF 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE---------------------ILLD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 85 dytaeglagvGELLKKYHHIsmELAhdpsdaniRIMSDLqeqldyqngwqfetriSQVLTLLNLDP--DATLDSLSGGWL 162
Cdd:cd03214 60 ----------GKDLASLSPK--ELA--------RKIAYV----------------PQALELLGLAHlaDRPFNELSGGER 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 163 RKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:cd03214 104 QRVLLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-231 |
1.36e-29 |
|
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: 116.84 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSD----FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM---------VQQQDLKVT 69
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllkLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 70 RLE-----QDPPASSD--LTVFDYTAEGLAGVGELLKKyhhismelahdpsdanirimsdlqeqldyqngWQFETRISQV 142
Cdd:cd03257 81 RKEiqmvfQDPMSSLNprMTIGEQIAEPLRIHGKLSKK--------------------------------EARKEAVLLL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 143 LTLLNLDPDAtLDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDRE 214
Cdd:cd03257 129 LVGVGLPEEV-LNRypheLSGGQRQRVAIARALALNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFITHDLG 207
|
250
....*....|....*..
gi 1411607396 215 FIHKLATRIIDLDRGVI 231
Cdd:cd03257 208 VVAKIADRVAVMYAGKI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-231 |
1.56e-29 |
|
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: 122.70 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSF-----SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTRLE---- 72
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlFDGKDLTKLSRRslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 ---------QDPPASSD--LTVFDYTAEGLagvgellkkyhhismELAHDPSDANIRimsdlqeqldyqngwqfeTRISQ 141
Cdd:COG1123 340 lrrrvqmvfQDPYSSLNprMTVGDIIAEPL---------------RLHGLLSRAERR------------------ERVAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 142 VLTLLNLDPDAtLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDR 213
Cdd:COG1123 387 LLERVGLPPDL-ADryphELSGGQRQRVAIARALALEPKLLILDEPTSALDVsvqaQILNLLRDLQRELGLTYLFISHDL 465
|
250
....*....|....*...
gi 1411607396 214 EFIHKLATRIIDLDRGVI 231
Cdd:COG1123 466 AVVRYIADRVAVMYDGRI 483
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-229 |
1.80e-29 |
|
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: 114.26 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 5 TLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrmvqqqdlKVTRLEQDPPASSDLTVF 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSG--------EILIDGKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 85 DytaeglagvgellkkyhHISMelahdpsdanirimsdlqeqldyqngwqfetrisqvltllnldpdatLDSLSGGWLRK 164
Cdd:cd00267 73 R-----------------RIGY-----------------------------------------------VPQLSGGQRQR 88
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 165 VALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd00267 89 VALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-473 |
1.83e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.43 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVqqqdLKVTRLEQDPPASS- 79
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIL----LDGEPVRFRSPRDAq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 80 ---------------DLTVfdytAEGLAgVGELLKKYHHISMElahdpsdaniRIMSDLQEQLDyqngwqfetRISqvlt 144
Cdd:COG1129 78 aagiaiihqelnlvpNLSV----AENIF-LGREPRRGGLIDWR----------AMRRRARELLA---------RLG---- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 145 lLNLDPDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLAt 221
Cdd:COG1129 130 -LDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAqgvAIIYISHRLDEVFEIA- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 222 riidlDRGVItswpgnydeylqgkeeaLR----VEELQHAEFDRklaqEEVwVRQ--GikarrtrnegrvRALEAMRMER 295
Cdd:COG1129 208 -----DRVTV-----------------LRdgrlVGTGPVAELTE----DEL-VRLmvG------------RELEDLFPKR 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 296 SQrrelqgkaklqmddvnRSGKLVFETEGLGLdfgdRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGL 375
Cdd:COG1129 249 AA----------------APGEVVLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGE 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 376 VK-GGTKLE-----------VAYF--DQYRDQLDPEQTVMDNVGEGKQEVMVRGR-------SRHILGYLQDFLFEPKRA 434
Cdd:COG1129 309 IRlDGKPVRirsprdairagIAYVpeDRKGEGLVLDLSIRENITLASLDRLSRGGlldrrreRALAEEYIKRLRIKTPSP 388
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1411607396 435 RTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG1129 389 EQPVGNLSGGNQQKVVLAKwLATDPK-VLILDEPTRGIDV 427
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
320-501 |
1.62e-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: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLDPEQ- 398
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSG--------EIYLDGKPLSAMPPPEw 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 ----------------TVMDNVGEGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAK-LFLKPSNL 461
Cdd:COG4619 73 rrqvayvpqepalwggTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRaLLLQPDVL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1411607396 462 LiLDEPTNDLDVETLELLEELLADYP----GTLLLVSHDRRFID 501
Cdd:COG4619 153 L-LDEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIE 195
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
335-469 |
3.21e-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: 110.43 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 335 FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-----------GGTKLEVAYFDQYrDQLDPEQTVMDN 403
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderKSLRKEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 404 VGEGKQEVMVRGRSR-----HILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:pfam00005 80 LRLGLLLKGLSKREKdaraeEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-263 |
3.50e-28 |
|
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: 113.64 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPlddgrmvqqqdlkvtrleqdPPASSD 80
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLP--------------------PTYGND 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 81 LTVFDYTAeGLAGVGELLKKYHHISMELAHD-PSDANIR--IMS------DLQEQLDYQNgwqfETRISQVLTLLNLDP- 150
Cdd:COG1119 61 VRLFGERR-GGEDVWELRKRIGLVSPALQLRfPRDETVLdvVLSgffdsiGLYREPTDEQ----RERARELLELLGLAHl 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 -DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEA----INWLEDFLKDFRGAIVFISHDREFIHKLATRIID 225
Cdd:COG1119 136 aDRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLL 215
|
250 260 270
....*....|....*....|....*....|....*....
gi 1411607396 226 LDRGVITSwpgnydeylQG-KEEALRVEELQHAeFDRKL 263
Cdd:COG1119 216 LKDGRVVA---------AGpKEEVLTSENLSEA-FGLPV 244
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-232 |
7.29e-28 |
|
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: 109.83 E-value: 7.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVqqqdlkvtrleqdppassdltv 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 fdytaegLAGvgellKKYHHismelaHDPSDANirimsdlqeqldyQNGWQFetrISQvltllnldpdatldsLSGGWLR 163
Cdd:cd03216 59 -------VDG-----KEVSF------ASPRDAR-------------RAGIAM---VYQ---------------LSVGERQ 89
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:cd03216 90 MVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-248 |
1.04e-27 |
|
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: 112.44 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLeqdPPAS- 78
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRiLFDGRD--ITGL---PPHRi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 79 ---------------SDLTVFDYTAeglagVGELLKKYHHISMELAHDPSDAniRIMSDLQEqldyqngwqfetRISQVL 143
Cdd:COG0411 77 arlgiartfqnprlfPELTVLENVL-----VAAHARLGRGLLAALLRLPRAR--REEREARE------------RAEELL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 144 TLLNLDP--DATLDSLSGGWLRKVALARALACDPDLLLLDEPT---NHLDIEAINWLEDFLKDFRG-AIVFISHDREFIH 217
Cdd:COG0411 138 ERVGLADraDEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVM 217
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1411607396 218 KLATRIIDLDRG-VITSwpGNYDE----------YLqGKEEA 248
Cdd:COG0411 218 GLADRIVVLDFGrVIAE--GTPAEvradprvieaYL-GEEAA 256
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
319-503 |
1.43e-27 |
|
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: 110.26 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKLEVAYFDQ--Y-- 390
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlwngEPIRDAREDYRRRlaYlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 -RDQLDPEQTVMDN---VGEGKQEVMVRGRSRHILGYLQdfLfePKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDE 466
Cdd:COG4133 82 hADGLKPELTVRENlrfWAALYGLRADREAIDEALEAVG--L--AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1411607396 467 PTNDLDVETLELLEELLADYP---GTLLLVSHDRRFIDNT 503
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-518 |
3.31e-27 |
|
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: 116.06 E-value: 3.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 13 FSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG--ELPLDDGRMVQQQDL--KVTRLE-------QDPPASSDL 81
Cdd:TIGR03269 10 FDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVALceKCGYVErpskvgePCPVCGGTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 TVFDYTAEGLA-GVGELLKKYHHI--------------------SMELAHDPSDANIRIMSDLQEQLdyqngwQFETRIS 140
Cdd:TIGR03269 90 EPEEVDFWNLSdKLRRRIRKRIAImlqrtfalygddtvldnvleALEEIGYEGKEAVGRAVDLIEMV------QLSHRIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 141 QVLTllnldpdatldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFL----KDFRGAIVFISHDREFI 216
Cdd:TIGR03269 164 HIAR-----------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeavKASGISMVLTSHWPEVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 217 HKLATRIIDLDRGVITSwPGNYDEYLQgkeealrveelqhaefdrklaqeevwvrqgikarrtrnegrvRALEAMRMERS 296
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKE-EGTPDEVVA------------------------------------------VFMEGVSEVEK 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 297 QRRELQGKAKLQMDDVNRsgklvfetEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV 376
Cdd:TIGR03269 270 ECEVEVGEPIIKVRNVSK--------RYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 377 ------------------KGGTKLEVAYFDQYRDqLDPEQTVMDNVGEG-----KQEVMVRgRSRHILGYLQdflFEPKR 433
Cdd:TIGR03269 342 nvrvgdewvdmtkpgpdgRGRAKRYIGILHQEYD-LYPHRTVLDNLTEAiglelPDELARM-KAVITLKMVG---FDEEK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 434 ARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD----VETLELLEELLADYPGTLLLVSHDRRFIDNTVT 505
Cdd:TIGR03269 417 AEEILDkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCD 496
|
570
....*....|...
gi 1411607396 506 GCWLFEgDGRISD 518
Cdd:TIGR03269 497 RAALMR-DGKIVK 508
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-229 |
4.97e-27 |
|
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: 109.83 E-value: 4.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmVQQQDLKVTRLE----------- 72
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGS-VLFDGEDITGLPpheiarlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 --QDPPASSDLTVFdytaEGLAgVGELLKKYHHISMelahdpsDANIRIMSDLQEqldyqngwqfetRISQVLTLLNLDP 150
Cdd:cd03219 80 tfQIPRLFPELTVL----ENVM-VAAQARTGSGLLL-------ARARREEREARE------------RAEELLERVGLAD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 --DATLDSLSGGWLRKVALARALACDPDLLLLDEPT---NHLDIEAI-NWLEDfLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:cd03219 136 laDRPAGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELaELIRE-LRERGITVLLVEHDMDVVMSLADRVT 214
|
....*
gi 1411607396 225 DLDRG 229
Cdd:cd03219 215 VLDQG 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
330-524 |
5.44e-27 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 115.42 E-value: 5.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyRDQLDPEQTVMDNVGEGKQ 409
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQ-EPQLDPTKTVRENVEEGVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 410 EVmvrgrsRHILGYLQ-------------DFLFEpKRAR------------------------------TPVKALSGGEK 446
Cdd:TIGR03719 95 EI------KDALDRFNeisakyaepdadfDKLAA-EQAElqeiidaadawdldsqleiamdalrcppwdADVTKLSGGER 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 447 NRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPGTLLLVSHDRRFIDNtVTGcWLFEGD-GRISDYVGGYA 524
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDN-VAG-WILELDrGRGIPWEGNYS 244
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-185 |
8.09e-27 |
|
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: 106.19 E-value: 8.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD------DGRMVQQQDLKVTR-----LEQDPPASSDLTVFDyt 87
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTegtillDGQDLTDDERKSLRkeigyVFQDPQLFPRLTVRE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 88 aeglagvgellkkyhhismelahdpsdaNIRIMSDLQEqldYQNGWqFETRISQVLTLLNLD------PDATLDSLSGGW 161
Cdd:pfam00005 79 ----------------------------NLRLGLLLKG---LSKRE-KDARAEEALEKLGLGdladrpVGERPGTLSGGQ 126
|
170 180
....*....|....*....|....
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTN 185
Cdd:pfam00005 127 RQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-504 |
8.35e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 109.41 E-value: 8.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLE-----VAYFDQyRD 392
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlFGKPPRrarrrIGYVPQ-RA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 QLDPEQ--TVMDNVGEG--KQEVMVRGRSRHI----------LGyLQDFlfepkrARTPVKALSGGEKNRLLLAKLFLKP 458
Cdd:COG1121 85 EVDWDFpiTVRDVVLMGryGRRGLFRRPSRADreavdealerVG-LEDL------ADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 459 SNLLILDEPTNDLDVETLELLE---ELLADYPGTLLLVSHD----RRFIDNTV 504
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYellRELRREGKTILVVTHDlgavREYFDRVL 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
15-233 |
1.54e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 107.83 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLkvTRLE---------------QDPPAS 78
Cdd:COG2884 14 GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvLVNGQDL--SRLKrreipylrrrigvvfQDFRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 79 SDLTVFDYTAeglagvgellkkyhhISMELA-HDPSDAnirimsdlqeqldyqngwqfETRISQVLTLLNLD------PD 151
Cdd:COG2884 92 PDRTVYENVA---------------LPLRVTgKSRKEI--------------------RRRVREVLDLVGLSdkakalPH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 152 AtldsLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFI-SHDREFIHKLATRIIDLDR 228
Cdd:COG2884 137 E----LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRMPKRVLELED 212
|
....*
gi 1411607396 229 GVITS 233
Cdd:COG2884 213 GRLVR 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
330-545 |
1.72e-26 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 114.06 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyRDQLDPEQTVMDNVGEGKQ 409
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ-EPQLDPEKTVRENVEEGVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 410 EVM-VRGRSRHI-----------------LGYLQDFL-------FEPK--RA----RTP-----VKALSGGEKNRLLLAK 453
Cdd:PRK11819 97 EVKaALDRFNEIyaayaepdadfdalaaeQGELQEIIdaadawdLDSQleIAmdalRCPpwdakVTKLSGGERRRVALCR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 454 LFLKPSNLLILDEPTNDLDVETLELLEELLADYPGTLLLVSHDRRFIDNtVTGcWLFEGD-GRISDYVGGYadmmatraq 532
Cdd:PRK11819 177 LLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDN-VAG-WILELDrGRGIPWEGNY--------- 245
|
250
....*....|...
gi 1411607396 533 qSTQLAAKAAQVK 545
Cdd:PRK11819 246 -SSWLEQKAKRLA 257
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-231 |
3.17e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 110.19 E-value: 3.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLE------- 72
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRiLLDGRD--VTGLPpekrnvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 ---QDPPASSDLTVFDYTAEGLagvgellkKYHHISmelahdPSDAnirimsdlqeqldyqngwqfETRISQVLTLLNLD 149
Cdd:COG3842 81 mvfQDYALFPHLTVAENVAFGL--------RMRGVP------KAEI--------------------RARVAELLELVGLE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 150 ------PDAtldsLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDRE--FIh 217
Cdd:COG3842 127 gladryPHQ----LSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQEeaLA- 201
|
250
....*....|....
gi 1411607396 218 kLATRIIDLDRGVI 231
Cdd:COG3842 202 -LADRIAVMNDGRI 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-250 |
4.35e-26 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 106.99 E-value: 4.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDL-KVTRLEQDPPAS- 78
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEiLVDGQDItGLSEKELYELRRr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 79 -----------SDLTVFDytaeglaGVGELLKKYHHISMELAHDpsdanirimsdlqeqldyqngwqfetRISQVLTLLN 147
Cdd:COG1127 84 igmlfqggalfDSLTVFE-------NVAFPLREHTDLSEAEIRE--------------------------LVLEKLELVG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 148 LDPDATL--DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA----IVFISHDREFIHKLAT 221
Cdd:COG1127 131 LPGAADKmpSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElgltSVVVTHDLDSAFAIAD 210
|
250 260
....*....|....*....|....*....
gi 1411607396 222 RIIDLDRGVITsWPGNYDEYLQGKEEALR 250
Cdd:COG1127 211 RVAVLADGKII-AEGTPEELLASDDPWVR 238
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-474 |
6.77e-26 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 112.59 E-value: 6.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 34 LVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtrleqDPPASSDlTVFDYTA--------EGLAGvGELlKKYHHIS 105
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIPNLGDY-------------EEEPSWD-EVLKRFRgtelqnyfKKLYN-GEI-KVVHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 106 M-ELAHDPSDANIRimsDLQEQLDyQNGwqfetRISQVLTLLNLDP--DATLDSLSGGWLRKVALARALACDPDLLLLDE 182
Cdd:PRK13409 168 YvDLIPKVFKGKVR---ELLKKVD-ERG-----KLDEVVERLGLENilDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 183 PTNHLDI----EAINWLEDFLKDfrGAIVFISHDrefihkLAtrIIDL--DR-----------GVITSWPGN---YDEYL 242
Cdd:PRK13409 239 PTSYLDIrqrlNVARLIRELAEG--KYVLVVEHD------LA--VLDYlaDNvhiaygepgayGVVSKPKGVrvgINEYL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 243 QG--KEEALRV--EELqhaEFDrklaqeevwvrqgikarrtrnegrvraleamrmERSQRRELQGKAKLQMDDVNRS-GK 317
Cdd:PRK13409 309 KGylPEENMRIrpEPI---EFE---------------------------------ERPPRDESERETLVEYPDLTKKlGD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 318 LVFETEGlGldfgdrtlfqgldlQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKggTKLEVAYFDQYRdQLDPE 397
Cdd:PRK13409 353 FSLEVEG-G--------------EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--PELKISYKPQYI-KPDYD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 398 QTVMD---NVGEG------KQEVMVRgrsrhilgyLQ-DFLFEpkrarTPVKALSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:PRK13409 415 GTVEDllrSITDDlgssyyKSEIIKP---------LQlERLLD-----KNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
....*..
gi 1411607396 468 TNDLDVE 474
Cdd:PRK13409 481 SAHLDVE 487
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-474 |
1.02e-25 |
|
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: 111.80 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 27 ERGERLCLVGRNGAGKSTLMKIIAGEL-P----LDDG-------------------RMVQQQDLKVTRLEQdppassdlt 82
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELkPnlgdYDEEpswdevlkrfrgtelqdyfKKLANGEIKVAHKPQ--------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 83 VFDYTAEGLAG-VGELLKKYhhismelahdpsdanirimsDLQEQLDYqngwqfetrisqVLTLLNLDP--DATLDSLSG 159
Cdd:COG1245 168 YVDLIPKVFKGtVRELLEKV--------------------DERGKLDE------------LAEKLGLENilDRDISELSG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDI-EAIN---WLEDFLKDFRgAIVFISHDrefihkLAtrIIDL--DRGVIT- 232
Cdd:COG1245 216 GELQRVAIAAALLRDADFYFFDEPSSYLDIyQRLNvarLIRELAEEGK-YVLVVEHD------LA--ILDYlaDYVHILy 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 233 SWPGNY-------------DEYLQG--KEEALRV--EELqhaEFDrklaqeevwvrqgikarrtrnegrvraleamrmER 295
Cdd:COG1245 287 GEPGVYgvvskpksvrvgiNQYLDGylPEENVRIrdEPI---EFE---------------------------------VH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 296 SQRRELQGKAKLQMDDVNRS-GKLVFETEGlgldfgdrtlfqGldlQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG 374
Cdd:COG1245 331 APRREKEEETLVEYPDLTKSyGGFSLEVEG------------G---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 375 LVKggTKLEVAYFDQYRDQlDPEQTVMDnvgegkqevMVRGRSRHILG--YLQDFLFEP----KRARTPVKALSGGEKNR 448
Cdd:COG1245 396 EVD--EDLKISYKPQYISP-DYDGTVEE---------FLRSANTDDFGssYYKTEIIKPlgleKLLDKNVKDLSGGELQR 463
|
490 500
....*....|....*....|....*.
gi 1411607396 449 LLLAKLFLKPSNLLILDEPTNDLDVE 474
Cdd:COG1245 464 VAIAACLSRDADLYLLDEPSAHLDVE 489
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-250 |
1.10e-25 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 106.05 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 6 LHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM---------VQQQDLKVTRLE---- 72
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgedisgLSEAELYRLRRRmgml 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 -QDPPASSDLTVFDYTAEGLagvgellkkyhhismelahdpsdaniRIMSDLQEqldyqngWQFETRISQVLTLLNLDPD 151
Cdd:cd03261 83 fQSGALFDSLTVFENVAFPL--------------------------REHTRLSE-------EEIREIVLEKLEAVGLRGA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 152 ATL--DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA----IVFISHDREFIHKLATRIID 225
Cdd:cd03261 130 EDLypAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElgltSIMVTHDLDTAFAIADRIAV 209
|
250 260
....*....|....*....|....*
gi 1411607396 226 LDRGVITsWPGNYDEYLQGKEEALR 250
Cdd:cd03261 210 LYDGKIV-AEGTPEELRASDDPLVR 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
12-231 |
1.19e-25 |
|
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: 104.99 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrmvqqqdlKVTRLEQDppassdltvFDYTAEGL 91
Cdd:cd03268 9 TYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSG--------EITFDGKS---------YQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 92 AGVGELLkKYHHISMEL-AHDpsdaNIRImSDLQEQLDYQngwqfetRISQVLTLLNLD--PDATLDSLSGGWLRKVALA 168
Cdd:cd03268 72 RRIGALI-EAPGFYPNLtARE----NLRL-LARLLGIRKK-------RIDEVLDVVGLKdsAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 169 RALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR--GAIVFI-SHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRdqGITVLIsSHLLSEIQKVADRIGIINKGKL 204
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-236 |
3.67e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 105.17 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSF----SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmVQQQDLKVTRLE---- 72
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGE-VLVDGKPVTGPGpdrg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 ---QDP---PAssdLTVFDYTAEGLAGVGELLKKYHHISMELahdpsdanirimsdlqeqldyqngwqfetrisqvLTLL 146
Cdd:COG1116 84 vvfQEPallPW---LTVLDNVALGLELRGVPKAERRERAREL----------------------------------LELV 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 147 NLDPDATL--DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDieAI------NWLEDFLKDFRGAIVFISHD-REFIH 217
Cdd:COG1116 127 GLAGFEDAypHQLSGGMRQRVAIARALANDPEVLLMDEPFGALD--ALtrerlqDELLRLWQETGKTVLFVTHDvDEAVF 204
|
250
....*....|....*....
gi 1411607396 218 kLATRIIdldrgVITSWPG 236
Cdd:COG1116 205 -LADRVV-----VLSARPG 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
16-231 |
1.03e-24 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 102.57 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 16 FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQD---LKVTRLE-----------QDPPASSD 80
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrVDGTDiskLSEKELAafrrrhigfvfQSFNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 81 LTVFDYTAeglagvgellkkyhhISMELAHDPSDANirimsdlqeqldyqngwqfETRISQVLTLLNLDPDATL--DSLS 158
Cdd:cd03255 97 LTALENVE---------------LPLLLAGVPKKER-------------------RERAEELLERVGLGDRLNHypSELS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEA----INWLEDFLKDFRGAIVFISHDREFIhKLATRIIDLDRGVI 231
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-229 |
1.13e-24 |
|
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: 101.11 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmvqqqdlkvtrLEqdPPASSDLTV 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG-------------------LE--EPDSGSILI 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 FDytaEGLAGVGELLKkyhhismelahdPSDANIRIMsdlqeqldYQNGwqfetrisQVLTLLNLDPDATLdSLSGGWLR 163
Cdd:cd03229 60 DG---EDLTDLEDELP------------PLRRRIGMV--------FQDF--------ALFPHLTVLENIAL-GLSGGQQQ 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd03229 108 RVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqlgiTVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-231 |
1.16e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 105.61 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPlDDGRM----------VQQQDLKVTRLEQDPPASSD 80
Cdd:COG1118 11 RFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETP-DSGRIvlngrdlftnLPPRERRVGFVFQHYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 81 LTVFDYTAEGLAgvgellkkyhhismelAHDPSDANIRimsdlqeqldyqngwqfeTRISQVLTLLNLD------PDAtl 154
Cdd:COG1118 90 MTVAENIAFGLR----------------VRPPSKAEIR------------------ARVEELLELVQLEgladryPSQ-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 155 dsLSGGWLRKVALARALACDPDLLLLDEPTNHLD------IEAinWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDR 228
Cdd:COG1118 134 --LSGGQRQRVALARALAVEPEVLLLDEPFGALDakvrkeLRR--WLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ 209
|
...
gi 1411607396 229 GVI 231
Cdd:COG1118 210 GRI 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-236 |
1.29e-24 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 102.16 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSD----FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD------DGRMVQQQDLKVTRLEQ 73
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTsgevlvDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 74 DP---PAssdLTVFDYTAEGLAGVGellkkyhhismelaHDPSDAnirimsdlqeqldyqngwqfETRISQVLTLLNLDP 150
Cdd:cd03293 81 QDallPW---LTVLDNVALGLELQG--------------VPKAEA--------------------RERAEELLELVGLSG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 --DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHD-REFIHkLATRI 223
Cdd:cd03293 124 feNAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHDiDEAVF-LADRV 202
|
250
....*....|...
gi 1411607396 224 IdldrgVITSWPG 236
Cdd:cd03293 203 V-----VLSARPG 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
321-515 |
2.39e-24 |
|
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: 101.39 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGD--RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL--- 394
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvDGKDLTKLSLKELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 --DPE-QTVMDNVGEgkqEVMV----RGRSRH-----ILGYLQDFLFEPKRARtPVKALSGGEKNRLLLAK-LFLKPsNL 461
Cdd:cd03225 81 fqNPDdQFFGPTVEE---EVAFglenLGLPEEeieerVEEALELVGLEGLRDR-SPFTLSGGQKQRVAIAGvLAMDP-DI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 462 LILDEPTNDLDVETLELLEELLADYPG---TLLLVSHDRRFIDNTVTGCWLFEgDGR 515
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLE-DGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-502 |
3.88e-24 |
|
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: 98.86 E-value: 3.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggtklevaYFDqyrdqldpeqtv 400
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI---------LID------------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 mdnvGEGKQEVMVRGRSRHILgylqdFLFEpkrartpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd00267 60 ----GKDIAKLPLEELRRRIG-----YVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180
....*....|....*....|....*
gi 1411607396 481 ELLADYPG---TLLLVSHDRRFIDN 502
Cdd:cd00267 121 ELLRELAEegrTVIIVTHDPELAEL 145
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
321-496 |
5.76e-24 |
|
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: 100.30 E-value: 5.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK------GGTKLEVAYFDQYRDqL 394
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRS-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 DPEQ--TVMDNVGEGKqevmvRGRSRHILGYLQDflfEPKRART-------------PVKALSGGEKNRLLLAKLFLKPS 459
Cdd:cd03235 80 DRDFpiSVRDVVLMGL-----YGHKGLFRRLSKA---DKAKVDEalervglseladrQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1411607396 460 NLLILDEPTNDLDVETLELLEELLADYPG---TLLLVSHD 496
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHD 191
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
330-495 |
7.25e-24 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 98.61 E-value: 7.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DP---EQTV 400
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILiDGVDLRDLDLESLRKNIayvpqDPflfSGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVgegkqevmvrgrsrhilgylqdflfepkrartpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd03228 93 RENI------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALIL 136
|
170
....*....|....*..
gi 1411607396 481 ELLADYPG--TLLLVSH 495
Cdd:cd03228 137 EALRALAKgkTVIVIAH 153
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
330-496 |
8.11e-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: 8.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DP---EQTV 400
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILiNGVDLSDLDPASWRRQIawvpqNPylfAGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEGKQEVmvrgrSRHIL------GYLQDFLFE-PKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:COG4988 428 RENLRLGRPDA-----SDEELeaaleaAGLDEFVAAlPDGLDTPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
170 180
....*....|....*....|....*....
gi 1411607396 470 DLDVETLELLEELLADYPG--TLLLVSHD 496
Cdd:COG4988 503 HLDAETEAEILQALRRLAKgrTVILITHR 531
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
321-475 |
1.39e-23 |
|
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: 97.85 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQyrdqldpeqtv 400
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSG--------EIKVLGK----------- 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 401 mdNVGEGKQEVmvrgrsRHILGYL--QDFLFEPKRARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03230 63 --DIKKEPEEV------KRRIGYLpeEPSLYENLTVRENLK-LSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
321-496 |
1.42e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 99.75 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLE---------VAYFDQY 390
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVArdpaevrrrIGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 rDQLDPEQTVMDNV-------GEGKQEVMVRgrsrhILGYLQDFLFEPkRARTPVKALSGGEKNRLLLAKLFLKPSNLLI 463
Cdd:COG1131 82 -PALYPDLTVRENLrffarlyGLPRKEARER-----IDELLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1411607396 464 LDEPTNDLDVETLEL---LEELLADYPGTLLLVSHD 496
Cdd:COG1131 155 LDEPTSGLDPEARRElweLLRELAAEGKTVLLSTHY 190
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
17-243 |
1.96e-23 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 105.30 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------VQQQDLKVTR-----LEQDPPASSDlTVFD 85
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidLRQIDPASLRrqigvVLQDVFLFSG-TIRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 86 ytaeglagvgellkkyhHISMElAHDPSDANIR-------IMSDLQEQldyQNGwqFETRISqvltllnldPDATldSLS 158
Cdd:COG2274 568 -----------------NITLG-DPDATDEEIIeaarlagLHDFIEAL---PMG--YDTVVG---------EGGS--NLS 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIE---AINwleDFLKDFRG--AIVFISHDREFIhKLATRIIDLDRGVITS 233
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAEteaIIL---ENLRRLLKgrTVIIIAHRLSTI-RLADRIIVLDKGRIVE 689
|
250
....*....|
gi 1411607396 234 wPGNYDEYLQ 243
Cdd:COG2274 690 -DGTHEELLA 698
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-243 |
1.98e-23 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 104.45 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSD-FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDL----------KVTRL 71
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSiLINGVDLsdldpaswrrQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 72 EQDPpassdlTVFDYT-AEGLAgvgellkkyhhismeLAH-DPSDAnirimsDLQEQLDyqngwqfETRISQVLTLLNLD 149
Cdd:COG4988 417 PQNP------YLFAGTiRENLR---------------LGRpDASDE------ELEAALE-------AAGLDEFVAALPDG 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 150 PDATLDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKD-FRGAIV-FISHDREFIhKLATRI 223
Cdd:COG4988 463 LDTPLGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGRTViLITHRLALL-AQADRI 541
|
250 260
....*....|....*....|
gi 1411607396 224 IDLDRGVITSwPGNYDEYLQ 243
Cdd:COG4988 542 LVLDDGRIVE-QGTHEELLA 560
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-231 |
2.75e-23 |
|
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: 98.25 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDDGRMVQQQDL------KVTRLE-------QDPPASSD 80
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKeELPTSGTIRVNGQDVsdlrgrAIPYLRrkigvvfQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 81 LTVFDYTAeglagvgellkkyhhISMELA-HDPSDANirimsdlqeqldyqngwqfeTRISQVLTLLNLD--PDATLDSL 157
Cdd:cd03292 93 RNVYENVA---------------FALEVTgVPPREIR--------------------KRVPAALELVGLShkHRALPAEL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFIS-HDREFIHKLATRIIDLDRGVI 231
Cdd:cd03292 138 SGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInkAGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
280-497 |
5.42e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 103.14 E-value: 5.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 280 RNEGRVRALEAMRMERSQRRELQGKAKLQMDDvnrSGKLVFEteGLGLDFGDRT-LFQGLDLQVLRGDKIALVGPNGCGK 358
Cdd:TIGR02857 287 RADGVAAAEALFAVLDAAPRPLAGKAPVTAAP---ASSLEFS--GVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 359 STLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQLD--------PEQTVMDNVGEGKQEV---MVRGRSRhiLGYLQD 426
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAvNGVPLADADADSWRDQIAwvpqhpflFAGTIAENIRLARPDAsdaEIREALE--RAGLDE 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 427 FLFE-PKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPG--TLLLVSHDR 497
Cdd:TIGR02857 440 FVAAlPQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL 517
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-496 |
9.00e-23 |
|
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: 95.97 E-value: 9.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEvayfdqyrdQLDPEQt 399
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILlDGKDLA---------SLSPKE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 400 vmdnvgegkqevmvrgRSRHIlGYLQDFL----FEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD--- 472
Cdd:cd03214 71 ----------------LARKI-AYVPQALellgLAHLADR-PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiah 132
|
170 180
....*....|....*....|....*
gi 1411607396 473 -VETLELLEELLADYPGTLLLVSHD 496
Cdd:cd03214 133 qIELLELLRRLARERGKTVVMVLHD 157
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-231 |
1.56e-22 |
|
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: 96.88 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 14 SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmvqqqdlkvtrLEQdpPASSDLTVFDYTAEGLAG 93
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-------------------LER--PTSGSVLVDGTDLTLLSG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 94 vGELLKKYHHISMELAHdpsdANIrimsdLQEQLDYQN--------GWQFETRISQVLTLLNL-----DPDATLDSLSGG 160
Cdd:cd03258 75 -KELRKARRRIGMIFQH----FNL-----LSSRTVFENvalpleiaGVPKAEIEERVLELLELvgledKADAYPAQLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKD----FRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinreLGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
330-516 |
1.60e-22 |
|
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: 96.63 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DPEQ----- 398
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvDGKDITKKNLRELRRKVglvfqNPDDqlfap 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 TVMDNV-------GEGKQEvmVRGRSRHILGY--LQDFlfepkrARTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPT 468
Cdd:COG1122 92 TVEEDVafgpenlGLPREE--IRERVEEALELvgLEHL------ADRPPHELSGGQKQRVAIAGvLAMEPE-VLVLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 469 NDLDVETLELLEELLADYPG---TLLLVSHDRRFIDNTVTGCWLFEgDGRI 516
Cdd:COG1122 163 AGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLD-DGRI 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-231 |
3.39e-22 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 95.87 E-value: 3.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 8 GACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPlDDGRMVQQ---------QDLKVTRLEQDPPA 77
Cdd:cd03296 7 NVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERP-DSGTILFGgedatdvpvQERNVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 78 SSDLTVFDYTAEGLagvgELLKKyhhismelAHDPSDANIRimsdlqeqldyqngwqfeTRISQVLTLLNLD--PDATLD 155
Cdd:cd03296 86 FRHMTVFDNVAFGL----RVKPR--------SERPPEAEIR------------------AKVHELLKLVQLDwlADRYPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03296 136 QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-233 |
3.71e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 95.50 E-value: 3.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 2 ALLTLHGACLSF----SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLeqdpp 76
Cdd:COG1136 3 PLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEvLIDGQD--ISSL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 77 ASSDLTVF--DYtaeglagVGELLKKYHHISmEL-AHDpsdaNIRIMSDLQEQLDYQNgwqfETRISQVLTLLNLDP--D 151
Cdd:COG1136 76 SERELARLrrRH-------IGFVFQFFNLLP-ELtALE----NVALPLLLAGVSRKER----RERARELLERVGLGDrlD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 152 ATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIhKLATRIIDLD 227
Cdd:COG1136 140 HRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLR 218
|
....*.
gi 1411607396 228 RGVITS 233
Cdd:COG1136 219 DGRIVS 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-231 |
5.93e-22 |
|
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: 94.63 E-value: 5.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVqQQDLKVTRLeqdPPASSDL-- 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY-IGGRDVTDL---PPKDRDIam 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 -----------TVFDYTAEGLagvgellkkyhhismELAHDPSDANIRIMSDLQEQLdyqngwqfetRISQvltLLNLDP 150
Cdd:cd03301 77 vfqnyalyphmTVYDNIAFGL---------------KLRKVPKDEIDERVREVAELL----------QIEH---LLDRKP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 DAtldsLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDL 226
Cdd:cd03301 129 KQ----LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM 204
|
....*
gi 1411607396 227 DRGVI 231
Cdd:cd03301 205 NDGQI 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
330-532 |
7.07e-22 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 99.84 E-value: 7.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLE----------VAYFDQ--Y------ 390
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlGGVDLRdldeddlrrrIAVVPQrpHlfdttl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 -------RDQLDPEQ--TVMDNVGegkqevmvrgrsrhilgyLQDFLFE-PKRARTPV----KALSGGEKNRLLLAKLFL 456
Cdd:COG4987 426 renlrlaRPDATDEElwAALERVG------------------LGDWLAAlPDGLDTWLgeggRRLSGGERRRLALARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 457 KPSNLLILDEPTNDLDVETLELLEELLADYPG--TLLLVSHDRRFIDNTVTGCWLfeGDGRISDyVGGYADMMATRAQ 532
Cdd:COG4987 488 RDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLAGLERMDRILVL--EDGRIVE-QGTHEELLAQNGR 562
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-473 |
1.15e-21 |
|
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: 98.99 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSF----SDFPLLDNAELSIERGERLCLVGRNGAGKS----TLMKIIAGELPLDDGRMV-QQQDL----- 66
Cdd:COG4172 4 MPLLSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILfDGQDLlglse 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 67 ---------KVTRLEQDPPASSD--LTVFDYTAEGLAgvgellkkyHHISMelahdpSDANIRimsdlqeqldyqngwqf 135
Cdd:COG4172 84 relrrirgnRIAMIFQEPMTSLNplHTIGKQIAEVLR---------LHRGL------SGAAAR----------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 136 etriSQVLTLLNL----DPDATLDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFLKDFR 203
Cdd:COG4172 132 ----ARALELLERvgipDPERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtVQAqiLDLLKDLQRELG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 204 GAIVFISHDREFIHKLATRIIDLDRGVITswpgnydeylqgkeEALRVEEL----QHAeFDRKLaqeevwvrqgIKArrt 279
Cdd:COG4172 208 MALLLITHDLGVVRRFADRVAVMRQGEIV--------------EQGPTAELfaapQHP-YTRKL----------LAA--- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 280 RNEGRVRALEAmrmersqrrelqgkaklqmddvnrSGKLVFETEGLGLDF-GDRTLFQ----------GLDLQVLRGDKI 348
Cdd:COG4172 260 EPRGDPRPVPP------------------------DAPPLLEARDLKVWFpIKRGLFRrtvghvkavdGVSLTLRRGETL 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 349 ALVGPNGCGKSTLIKLLLGqLEPSRGLVK-GGTKLEVAYFDQ---YRDQ-----------LDPEQTVMDNVGEG----KQ 409
Cdd:COG4172 316 GLVGESGSGKSTLGLALLR-LIPSEGEIRfDGQDLDGLSRRAlrpLRRRmqvvfqdpfgsLSPRMTVGQIIAEGlrvhGP 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 410 EVMVRGRSRHILGYLQDFLFEPK-RARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG4172 395 GLSAAERRARVAEALEEVGLDPAaRHRYP-HEFSGGQRQRIAIARaLILEPK-LLVLDEPTSALDV 458
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-243 |
1.20e-21 |
|
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: 99.07 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 2 ALLTLHGACLSF--SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM---------VQQQDL--KV 68
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdlrdLDEDDLrrRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 69 TRLEQDPPassdltVFDYTaeglagVGELLKkyhhismeLA-HDPSDANIRimsdlqeqldyqngwqfetrisQVLTLLN 147
Cdd:COG4987 412 AVVPQRPH------LFDTT------LRENLR--------LArPDATDEELW----------------------AALERVG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 148 LDPDAT-----LDS--------LSGGWLRKVALARALACDPDLLLLDEPTNHLDIE-AINWLEDFLKDFRG-AIVFISHD 212
Cdd:COG4987 450 LGDWLAalpdgLDTwlgeggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAAtEQALLADLLEALAGrTVLLITHR 529
|
250 260 270
....*....|....*....|....*....|.
gi 1411607396 213 REFIHKlATRIIDLDRGVITSwPGNYDEYLQ 243
Cdd:COG4987 530 LAGLER-MDRILVLEDGRIVE-QGTHEELLA 558
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-496 |
1.27e-21 |
|
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: 94.73 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLE----------VAYF 387
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLlDGRDLAslsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 388 DQyrDQLDPEQ-TVMDNVGegkqevmvRGRSRHilgylQDFLFEPKR------------------ARTPVKALSGGEKNR 448
Cdd:COG1120 81 PQ--EPPAPFGlTVRELVA--------LGRYPH-----LGLFGRPSAedreaveealertglehlADRPVDELSGGERQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 449 LLLAKLFLKPSNLLILDEPTNDLD----VETLELLEELLADYPGTLLLVSHD 496
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARERGRTVVMVLHD 197
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-256 |
1.39e-21 |
|
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: 98.85 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 7 HGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQ-----DPpassDL 81
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQsrdalDP----NK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 TVFDYTAEGLagvgellkkyHHISMELAHDPSDANIrimsdlqEQLDYQNGWQfETRISQvltllnldpdatldsLSGGW 161
Cdd:TIGR03719 402 TVWEEISGGL----------DIIKLGKREIPSRAYV-------GRFNFKGSDQ-QKKVGQ---------------LSGGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLD-RGVITSWPGNYDE 240
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSE 528
|
250 260
....*....|....*....|.
gi 1411607396 241 YLQGK-----EEALRVEELQH 256
Cdd:TIGR03719 529 YEEDKkrrlgEDADQPHRIKY 549
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-473 |
1.71e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.18 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV---QQQDLKvtrleqDPPASS 79
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILidgKPVRIR------SPRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 80 D---------------LTVfdytAEGLAgvgellkkyhhismeLAHDPSDANIRIMSDLQEQLdyqngwqfeTRISQVLT 144
Cdd:COG3845 79 AlgigmvhqhfmlvpnLTV----AENIV---------------LGLEPTKGGRLDRKAARARI---------RELSERYG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 145 lLNLDPDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHD-REfIHKLA 220
Cdd:COG3845 131 -LDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAegkSIIFITHKlRE-VMAIA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 221 TRIIDLDRG-VITSwpgnydeylqgkeeaLRVEELQHAEfdrkLAQEEVwvrqgikarrtrneGRVRALEAMRMERsqrr 299
Cdd:COG3845 209 DRVTVLRRGkVVGT---------------VDTAETSEEE----LAELMV--------------GREVLLRVEKAPA---- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 300 elqgkaklqmddvnRSGKLVFETEGLGL--DFGDRTLfQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK 377
Cdd:COG3845 252 --------------EPGEVVLEVENLSVrdDRGVPAL-KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIR 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 378 -GGTKLE-----------VAYF--DQYRDQLDPEQTVMDNV--GEGKQEVMVRG---RSRHILGYLQDfLFE-----PKR 433
Cdd:COG3845 317 lDGEDITglsprerrrlgVAYIpeDRLGRGLVPDMSVAENLilGRYRRPPFSRGgflDRKAIRAFAEE-LIEefdvrTPG 395
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1411607396 434 ARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:COG3845 396 PDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDV 435
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-231 |
2.95e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 95.53 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDlkVTRLeqdPPASS 79
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIlIGGRD--VTDL---PPKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 80 D-------------LTVFDYTAEGL--AGVgellkkyhhismelahdpSDANIRimsdlqeqldyqngwqfeTRISQVLT 144
Cdd:COG3839 76 NiamvfqsyalyphMTVYENIAFPLklRKV------------------PKAEID------------------RRVREAAE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 145 LLNLDPdaTLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFI 216
Cdd:COG3839 120 LLGLED--LLDrkpkQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHDQVEA 197
|
250
....*....|....*
gi 1411607396 217 HKLATRIIDLDRGVI 231
Cdd:COG3839 198 MTLADRIAVMNDGRI 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-231 |
5.11e-21 |
|
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: 92.75 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 16 FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKvtrlEQDPPassdltvfdytaeglagv 94
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfIDGEDIR----EQDPV------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 95 gELLKKYHHISME---LAHDPSDANIRIMSDLQeqldyqnGW---QFETRISQVLTLLNLDPDATLD----SLSGGWLRK 164
Cdd:cd03295 72 -ELRRKIGYVIQQiglFPHMTVEENIALVPKLL-------KWpkeKIRERADELLALVGLDPAEFADryphELSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 165 VALARALACDPDLLLLDEPTNHLD-IEAINWLEDFLK---DFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDpITRDQLQEEFKRlqqELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-232 |
1.17e-20 |
|
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: 90.39 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 5 TLHGACLSFSDFP-LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-------ELPLDDGRMVQQQDLKVTRL-EQDP 75
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGlikessgSILLNGKPIKAKERRKSIGYvMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 76 passDLTVFDYTAEGlagvgELLkkyhhISMELAHDPsdanirimsdlqeqldyqngwqfETRISQVLTLLNLD--PDAT 153
Cdd:cd03226 81 ----DYQLFTDSVRE-----ELL-----LGLKELDAG-----------------------NEQAETVLKDLDLYalKERH 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGV 230
Cdd:cd03226 124 PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGA 203
|
..
gi 1411607396 231 IT 232
Cdd:cd03226 204 IV 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-229 |
1.21e-20 |
|
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: 89.36 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFS----DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKvtrleqdppassDLTVFD 85
Cdd:cd03228 6 VSFSypgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlIDGVDLR------------DLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 86 YtaeglagvgellkkYHHISMELahdpsdanirimsdlqeqldyQNGWQFETRISQvltllNLdpdatldsLSGGWLRKV 165
Cdd:cd03228 74 L--------------RKNIAYVP---------------------QDPFLFSGTIRE-----NI--------LSGGQRQRI 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 166 ALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISHDREFIhKLATRIIDLDRG 229
Cdd:cd03228 106 AIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAHRLSTI-RDADRIIVLDDG 170
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-224 |
1.36e-20 |
|
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: 93.19 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP---LDDGRMV-QQQDL-KVTRLE-------------QDPPASSD 80
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILfDGEDLlKLSEKElrkirgreiqmifQDPMTSLN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 81 --LTVFDYTAEGLagvgellkKYHHIsmelaHDPSDAnirimsdlqeqldyqngwqfETRISQVLTLLNL-DPDATLDS- 156
Cdd:COG0444 101 pvMTVGDQIAEPL--------RIHGG-----LSKAEA--------------------RERAIELLERVGLpDPERRLDRy 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 157 ---LSGGWLRKVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:COG0444 148 pheLSGGMRQRVMIARALALEPKLLIADEPTTALDvtIQAqiLNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
329-496 |
4.16e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.44 E-value: 4.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyRDQLDPE--QTVMDNVGE 406
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-RSEVPDSlpLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 407 GK-QEvmvRGRSRHI--------------LGyLQDFlfepkrARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:NF040873 81 GRwAR---RGLWRRLtrddraavddalerVG-LADL------AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180
....*....|....*....|....*...
gi 1411607396 472 DVETLELLEELLADYPG---TLLLVSHD 496
Cdd:NF040873 151 DAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-229 |
8.23e-20 |
|
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: 88.02 E-value: 8.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGeRLCLVGRNGAGKSTLMKIIAGELPLDDGrmvqqqdlKVTRLEQDPPASSDltv 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSG--------TIRIDGQDVLKQPQ--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 fdytaeglagvgellKKYHHISMeLAHDPS-DANIRImsdlQEQLDYQnGW-------QFETRISQVLTLLNLDPDAT-- 153
Cdd:cd03264 69 ---------------KLRRRIGY-LPQEFGvYPNFTV----REFLDYI-AWlkgipskEVKARVDEVLELVNLGDRAKkk 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF-RGAIVFIS-HDREFIHKLATRIIDLDRG 229
Cdd:cd03264 128 IGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELgEDRIVILStHIVEDVESLCNQVAVLNKG 205
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
330-542 |
1.11e-19 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 93.31 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQ-------------------Y 390
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQetpalpqpaleyvidgdreY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RdQLDPEQTVMDNVGEGKQEVMVRG----------RSR-----HILGYLQDFLFEPkrartpVKALSGGEKNRLLLAKLF 455
Cdd:PRK10636 92 R-QLEAQLHDANERNDGHAIATIHGkldaidawtiRSRaasllHGLGFSNEQLERP------VSDFSGGWRMRLNLAQAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 456 LKPSNLLILDEPTNDLDVETLELLEELLADYPGTLLLVSHDRRFIDNTVTGCWLFEGDgRISDYVGGYAdmmATRAQQST 535
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQ-SLFEYTGNYS---SFEVQRAT 240
|
....*..
gi 1411607396 536 QLAAKAA 542
Cdd:PRK10636 241 RLAQQQA 247
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-226 |
1.21e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.29 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQ--DPPASSDLTVFDYTAEGLAGV 94
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsEVPDSLPLTVRDLVAMGRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 95 GELLKKYHHismelahdpsdANIRIMSDLQEQLDYQNgwqFETRisqvltllnldpdaTLDSLSGGWLRKVALARALACD 174
Cdd:NF040873 86 RGLWRRLTR-----------DDRAAVDDALERVGLAD---LAGR--------------QLGELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 175 PDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIhKLATRIIDL 226
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELV-RRADPCVLL 191
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
323-496 |
1.93e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.20 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEVAYFD---QYRD-QLDPE 397
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGeLLAGTAPLAEAREDtrlMFQDaRLLPW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 398 QTVMDNVGEGkqevmVRGRSR-HILGYLQDFLFEPKRARTPVkALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD---- 472
Cdd:PRK11247 96 KKVIDNVGLG-----LKGQWRdAALQALAAVGLADRANEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltr 169
|
170 180
....*....|....*....|....
gi 1411607396 473 VETLELLEELLADYPGTLLLVSHD 496
Cdd:PRK11247 170 IEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
330-502 |
2.52e-19 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 92.20 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggtklevaYFDQY-RDQLDPEQ---------- 398
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI---------LIDGIdLRQIDPASlrrqigvvlq 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 -------TVMDNVGEGK-----QEVMvrgRSRHILGyLQDFLFE-PKRARTPV----KALSGGEKNRLLLAKLFLKPSNL 461
Cdd:COG2274 557 dvflfsgTIRENITLGDpdatdEEII---EAARLAG-LHDFIEAlPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1411607396 462 LILDEPTNDLDVETLELLEELLADYPG--TLLLVSHDRRFIDN 502
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL 675
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
321-496 |
2.72e-19 |
|
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: 87.61 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKG--------GTKLEVAYFDQy 390
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGsiLIDGedvrkeprEARRQIGVLPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RDQLDPEQTVMDNV-------GEGKQEVMVRgrsrhILGYLQDFLFEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLI 463
Cdd:COG4555 82 ERGLYDRLTVRENIryfaelyGLFDEELKKR-----IEELIELLGLEEFLDR-RVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1411607396 464 LDEPTNDLDVETLEL---LEELLADYPGTLLLVSHD 496
Cdd:COG4555 156 LDEPTNGLDVMARRLlreILRALKKEGKTVLFSSHI 191
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-235 |
2.93e-19 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 86.85 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD-----------DGRMVQQQDLKVTRLE 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdegevllDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 -------QdPPASSDLTVFDYTAEGLAGVGELLKKyhhismelahdpsdanirimsdlqeqldyqngwQFETRISQVLTL 145
Cdd:cd03260 81 rrvgmvfQ-KPNPFPGSIYDNVAYGLRLHGIKLKE---------------------------------ELDERVEEALRK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 146 LNLDPD----ATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISHDREFIHKL 219
Cdd:cd03260 127 AALWDEvkdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQQAARV 206
|
250
....*....|....*..
gi 1411607396 220 ATRIIDLDRG-VITSWP 235
Cdd:cd03260 207 ADRTAFLLNGrLVEFGP 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-231 |
3.15e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 89.76 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM---------VQQQDLKVTRLEQDPPASSDLT 82
Cdd:PRK10851 11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrfhgtdvsrLHARDRKVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 83 VFDYTAEGLAgvgeLLKKYHHismelahdPSDANIRimsdlqeqldyqngwqfeTRISQVLTLLNLDPDATL--DSLSGG 160
Cdd:PRK10851 91 VFDNIAFGLT----VLPRRER--------PNAAAIK------------------AKVTQLLEMVQLAHLADRypAQLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
320-495 |
4.75e-19 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 84.96 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGD--RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQldp 396
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRlDGADISQWDPNELGDH--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 397 eqtvmdnvgegkqevmvrgrsrhiLGYL-QDF-LFEPKRARTpvkALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03246 78 ------------------------VGYLpQDDeLFSGSIAEN---ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180
....*....|....*....|....
gi 1411607396 475 TLELLEELLADYP---GTLLLVSH 495
Cdd:cd03246 131 GERALNQAIAALKaagATRIVIAH 154
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-225 |
6.76e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD------DGRMVQQQDLK-VTRLEQ 73
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTagtvlvAGDDVEALSARaASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 74 DPPASSDLTvFDYTAEGLAGVGellkKYHHISMELAHDPSDANIrimsdLQEQLDYQNGWQFETRisqvltllnldpdaT 153
Cdd:PRK09536 81 SVPQDTSLS-FEFDVRQVVEMG----RTPHRSRFDTWTETDRAA-----VERAMERTGVAQFADR--------------P 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI-EAINWLE---DFLKDFRGAIVFIsHDREfihkLATRIID 225
Cdd:PRK09536 137 VTSLSGGERQRVLLARALAQATPVLLLDEPTASLDInHQVRTLElvrRLVDDGKTAVAAI-HDLD----LAARYCD 207
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-231 |
8.05e-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: 85.72 E-value: 8.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------VQQQDLKVTR-----LEQDP---------- 75
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdIRQLDPADLRrnigyVPQDVtlfygtlrdn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 76 -----PASSDLTVFDytAEGLAGVGELLKKyHHISMELahdpsdanirimsDLQEQldyqnGwqfetrisqvltllnldp 150
Cdd:cd03245 98 itlgaPLADDERILR--AAELAGVTDFVNK-HPNGLDL-------------QIGER-----G------------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 datlDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISHdREFIHKLATRIIDLDR 228
Cdd:cd03245 139 ----RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDS 213
|
...
gi 1411607396 229 GVI 231
Cdd:cd03245 214 GRI 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
321-501 |
8.13e-19 |
|
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: 86.40 E-value: 8.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFG----DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAY--------- 386
Cdd:COG1124 3 EVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfDGRPVTRRRrkafrrrvq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 387 --FDQYRDQLDPEQTVMDNVGE-----GKQEVMVR-GRSRHILGYLQDFLFepkraRTPvKALSGGEKNRLLLAK-LFLK 457
Cdd:COG1124 83 mvFQDPYASLHPRHTVDRILAEplrihGLPDREERiAELLEQVGLPPSFLD-----RYP-HQLSGGQRQRVAIARaLILE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1411607396 458 PSnLLILDEPTNDLDV----ETLELLEELLADYPGTLLLVSHDRRFID 501
Cdd:COG1124 157 PE-LLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVA 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-473 |
1.11e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.72 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------------VQQQDLKVTR 70
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeiggnpcarltpAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 71 LEQDPPASSDLTVFDYTAEGLAGVGELLKKyhhismelahdpsdaniriMSDLQEQLDYQngwqfetrisqvltllnLDP 150
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPKRQASMQK-------------------MKQLLAALGCQ-----------------LDL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLD 227
Cdd:PRK15439 135 DSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAqgvGIVFISHKLPEIRQLADRISVMR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 228 RGVITswpgnydeyLQGKEEALRVEELQHAefdrklaqeevwVRQGIKARRTRnEGRVRALEamrMERSQRRELQGKAKL 307
Cdd:PRK15439 215 DGTIA---------LSGKTADLSTDDIIQA------------ITPAAREKSLS-ASQKLWLE---LPGNRRQQAAGAPVL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 308 QMDDVnrSGklvfetEGlgldfgdrtlFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqLEPSRGlvkGGTKLEVAYF 387
Cdd:PRK15439 270 TVEDL--TG------EG----------FRNISLEVRAGEILGLAGVVGAGRTELAETLYG-LRPARG---GRIMLNGKEI 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 388 DQY--RDQLD------PEQT------------------VMDNVG---EGKQEVMVRGRSRHILGylqdflFEPKRARTPV 438
Cdd:PRK15439 328 NALstAQRLArglvylPEDRqssglyldaplawnvcalTHNRRGfwiKPARENAVLERYRRALN------IKFNHAEQAA 401
|
490 500 510
....*....|....*....|....*....|....*
gi 1411607396 439 KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK15439 402 RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
302-475 |
1.15e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 85.91 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 302 QGKAKLQMDDVNRSgklvFETEGlgldfGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKG- 378
Cdd:COG1116 3 AAAPALELRGVSKR----FPTGG-----GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGevLVDGk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 379 ---GTKLEVAY-FDQYRdqLDPEQTVMDNV-------GEGKQEvmVRGRSRHIL---GyLQDFlfepkRARTPvKALSGG 444
Cdd:COG1116 74 pvtGPGPDRGVvFQEPA--LLPWLTVLDNValglelrGVPKAE--RRERARELLelvG-LAGF-----EDAYP-HQLSGG 142
|
170 180 190
....*....|....*....|....*....|..
gi 1411607396 445 EKNRLLLAK-LFLKPSnLLILDEPTNDLDVET 475
Cdd:COG1116 143 MRQRVAIARaLANDPE-VLLMDEPFGALDALT 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-223 |
1.25e-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: 84.86 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTRLEqdppASSDLTV---FDYT 87
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTaYINGYSIRTDRKA----ARQSLGYcpqFDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 88 AEGLAGVgELLKKYHhismELAHDPSDANIRIMSDLQEQL---DYQNgwqfeTRISQvltllnldpdatldsLSGGWLRK 164
Cdd:cd03263 87 FDELTVR-EHLRFYA----RLKGLPKSEIKEEVELLLRVLgltDKAN-----KRART---------------LSGGMKRK 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 165 VALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISHDREFIHKLATRI 223
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
4-191 |
1.32e-18 |
|
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: 86.02 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV-----------QQQDLKVTRLE 72
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhglsrRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 QDPPASSDLTVFDYTAeglagvgelLKKYHHISMELAHDPSDANIrimsdlqeqldyqngwqfetrISQVLTLLNLD--P 150
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVA---------LGRIPHRSLWAGDSPHDAAV---------------------VDRALARTELShlA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1411607396 151 DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEA 191
Cdd:TIGR03873 132 DRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRA 172
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-231 |
1.42e-18 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 85.08 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLlDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLeqdPPASSD-- 80
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKiLLNGKD--ITNL---PPEKRDis 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 81 -----------LTVFDYTAEGLAGVGELLKKYHHISMELAhdpSDANIRimsdlqeqldyqngwqfetrisqvlTLLNLD 149
Cdd:cd03299 75 yvpqnyalfphMTVYKNIAYGLKKRKVDKKEIERKVLEIA---EMLGID-------------------------HLLNRK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 150 PDatldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIE----AINWLEDFLKDFRGAIVFISHDREFIHKLATRIID 225
Cdd:cd03299 127 PE----TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRtkekLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAI 202
|
....*.
gi 1411607396 226 LDRGVI 231
Cdd:cd03299 203 MLNGKL 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-229 |
1.81e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 86.32 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrmvqqqdlKVTrLEQDPPASSDLTV 83
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSG--------EVL-WDGEPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 FDYTAE--GL---AGVGELLKkYhhismeLAH----DPSDANIRIMSdlqeqldyqngWqfetrisqvLTLLNLDP--DA 152
Cdd:COG4152 73 IGYLPEerGLypkMKVGEQLV-Y------LARlkglSKAEAKRRADE-----------W---------LERLGLGDraNK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 153 TLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR--GA-IVFISHDREFIHKLATRIIDLDRG 229
Cdd:COG4152 126 KVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAakGTtVIFSSHQMELVEELCDRIVIINKG 205
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
321-500 |
1.91e-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: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRT-LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTK-------LEVAYF--DQY 390
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerRKSIGYvmQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RDQLDpEQTVMDNVGEGKQEV-MVRGRSRHIlgyLQDF-LFEPKRaRTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPT 468
Cdd:cd03226 81 DYQLF-TDSVREELLLGLKELdAGNEQAETV---LKDLdLYALKE-RHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1411607396 469 NDLD---VETLELLEELLADYPGTLLLVSHDRRFI 500
Cdd:cd03226 155 SGLDyknMERVGELIRELAAQGKAVIVITHDYEFL 189
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
321-472 |
2.25e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.40 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK--GGTKLEVAYFDQYR------- 391
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcGEPVPSRARHARQRvgvvpqf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 392 DQLDPEQTVMDNVGE-GKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK13537 89 DNLDPDFTVRENLLVfGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
..
gi 1411607396 471 LD 472
Cdd:PRK13537 169 LD 170
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
336-475 |
2.76e-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: 84.09 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGGTKL--------EVAYFDQYrDQLDPEQTVMDNVg 405
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtaYINGYSIRtdrkaarqSLGYCPQF-DALFDELTVREHL- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 406 egKQEVMVRGRSRH-----ILGYLQDFLFEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03263 97 --RFYARLKGLPKSeikeeVELLLRVLGLTDKANK-RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
336-499 |
3.21e-18 |
|
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: 83.69 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL--------------EVAY-FDQYrdQLDPEQT 399
Cdd:cd03255 21 KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvDGTDIsklsekelaafrrrHIGFvFQSF--NLLPDLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 400 VMDNV-------GEGKQEvmVRGRSRHILGYLQdfLfePKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03255 99 ALENVelplllaGVPKKE--RRERAEELLERVG--L--GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLD 172
|
170 180 190
....*....|....*....|....*....|.
gi 1411607396 473 VETLEL----LEELLADYPGTLLLVSHDRRF 499
Cdd:cd03255 173 SETGKEvmelLRELNKEAGTTIVVVTHDPEL 203
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
329-472 |
3.23e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.42 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggTKLEVAYFDQYR------------DQLDP 396
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI---TVLGVPVPARARlararigvvpqfDNLDL 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 397 EQTVMDN-VGEGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13536 128 EFTVRENlLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
321-496 |
4.26e-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: 83.29 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDR----TLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL-----EVAY-FDQ 389
Cdd:cd03293 2 EVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvDGEPVtgpgpDRGYvFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 390 YRdqLDPEQTVMDNV-------GEGKQEvmVRGRSRHIL---GyLQDFlfepkRARTPvKALSGGEKNRLLLAKLFLKPS 459
Cdd:cd03293 82 DA--LLPWLTVLDNValglelqGVPKAE--ARERAEELLelvG-LSGF-----ENAYP-HQLSGGMRQRVALARALAVDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1411607396 460 NLLILDEPTNDLDVETLELLEELLAD----YPGTLLLVSHD 496
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDiwreTGKTVLLVTHD 191
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-189 |
4.42e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 84.40 E-value: 4.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTRLEQDP------ 75
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEvRLNGRPLAAWSPWELArrravl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 76 PASSDLTvFDYTAEGLAGVGellkkyhhismELAHDPSDAnirimsdlqeqldyqngwQFETRISQVLTLLNLDPDATLD 155
Cdd:COG4559 81 PQHSSLA-FPFTVEEVVALG-----------RAPHGSSAA------------------QDRQIVREALALVGLAHLAGRS 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1411607396 156 --SLSGGWLRKVALARALA-----CDPD--LLLLDEPTNHLDI 189
Cdd:COG4559 131 yqTLSGGEQQRVQLARVLAqlwepVDGGprWLFLDEPTSALDL 173
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-231 |
5.72e-18 |
|
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: 84.09 E-value: 5.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDDGRMVQQQDLKVTRLEQDPPASSDLTVFDYTAEGlagvg 95
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGlEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDSPS----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 96 ellkkyhhismelAHDPSDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDPDaTLD----SLSGGWLRKVALARAL 171
Cdd:TIGR02769 100 -------------AVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSE-DADklprQLSGGQLQRINIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 172 ACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
321-495 |
7.12e-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: 82.65 E-value: 7.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggTKLEVAYFDQYRDQ------- 393
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---TFDGKSYQKNIEALrrigali 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 ----LDPEQTVMDNVGEGKQEVMVRgRSRH--ILGY--LQDflfepkRARTPVKALSGGEKNRLLLAKLFLKPSNLLILD 465
Cdd:cd03268 79 eapgFYPNLTARENLRLLARLLGIR-KKRIdeVLDVvgLKD------SAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190
....*....|....*....|....*....|...
gi 1411607396 466 EPTNDLD---VETLELLEELLADYPGTLLLVSH 495
Cdd:cd03268 152 EPTNGLDpdgIKELRELILSLRDQGITVLISSH 184
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-232 |
7.89e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 83.15 E-value: 7.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 13 FSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmvqqqdlkVTRLEQDPpassdltvFDYTAEGLA 92
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE--------VRVAGLVP--------WKRRKKFLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 93 GVGELLKKYHHISMELAHDPSDANIRIMSDLQEQldyqngwQFETRISQVLTLLNLDP--DATLDSLSGGWLRKVALARA 170
Cdd:cd03267 95 RIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPA-------RFKKRLDELSELLDLEEllDTPVRQLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 171 LACDPDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVFI-SHDREFIHKLATRIIDLDRGVIT 232
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnreRGTTVLLtSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
331-475 |
8.02e-18 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 81.59 E-value: 8.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQYRDQ---LDPE-----QTVMD 402
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLisvLNQRpylfdTTLRN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 403 NVGegkqevmvrgrsrhilgylqdflfepkrartpvKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03247 94 NLG---------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-231 |
8.23e-18 |
|
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: 82.80 E-value: 8.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtrleqdppassdltvfdyTAEGLAGVgell 98
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA--------------------------TVDGFDVV---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 99 kkyhhismelaHDPSDA--NIRIMSD---------LQEQLDY------QNGWQFETRISQVLTLLNLDP--DATLDSLSG 159
Cdd:cd03266 71 -----------KEPAEArrRLGFVSDstglydrltARENLEYfaglygLKGDELTARLEELADRLGMEEllDRRVGGFST 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03266 140 GMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
319-495 |
9.15e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 83.21 E-value: 9.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV-------KGGT-----KLEVAY 386
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgerRGGEdvwelRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 387 F-----DQYRDQLDPEQTVM----DNVGEGKQ--EVMvRGRSRHILGYLQdflFEPKRARtPVKALSGGEKNRLLLAKLF 455
Cdd:COG1119 83 VspalqLRFPRDETVLDVVLsgffDSIGLYREptDEQ-RERARELLELLG---LAHLADR-PFGTLSQGEQRRVLIARAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1411607396 456 LKPSNLLILDEPTNDLDV---ETLELLEELLADYPG-TLLLVSH 495
Cdd:COG1119 158 VKDPELLILDEPTAGLDLgarELLLALLDKLAAEGApTLVLVTH 201
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
12-231 |
9.62e-18 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 82.19 E-value: 9.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVqqqdLKVTRLEQDPPASSDL-----TVFDY 86
Cdd:cd03262 9 SFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTII----IDGLKLTDDKKNINELrqkvgMVFQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 87 -------TAegLAGVGELLKKYHHISMELAhdpsdanirimsdlqeqldyqngwqfETRISQVLTLLNLDP--DATLDSL 157
Cdd:cd03262 85 fnlfphlTV--LENITLAPIKVKGMSKAEA--------------------------EERALELLEKVGLADkaDAYPAQL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RG-AIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03262 137 SGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeEGmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-231 |
1.24e-17 |
|
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: 82.62 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 14 SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM----VQQQDLKVTRLE----------QDPPASS 79
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgTDINKLKGKALRqlrrqigmifQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 80 DLTVFDYTAEGLAGvgellkkYHHIsmelahdpsdanIRIMSDLQEQLDYQngwqfetRISQVLTLLNLDPDATL--DSL 157
Cdd:cd03256 92 RLSVLENVLSGRLG-------RRST------------WRSLFGLFPKEEKQ-------RALAALERVGLLDKAYQraDQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVFIS-HDREFIHKLATRIIDLDRGVI 231
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDLAREYADRIVGLKDGRI 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-229 |
1.32e-17 |
|
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: 82.10 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 5 TLH---GACLsfsdfPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGE-LPlDDGRMVQQQDLKVTRLEQDPP---- 76
Cdd:COG4778 15 TLHlqgGKRL-----PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNyLP-DSGSILVRHDGGWVDLAQASPreil 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 77 ---------ASSDLTV------FDYTAEGLagvgellkkyhhisMELAHDPSDAnirimsdlqeqldyqngwqfETRISQ 141
Cdd:COG4778 89 alrrrtigyVSQFLRViprvsaLDVVAEPL--------------LERGVDREEA--------------------RARARE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 142 VLTLLNLD------PDATLdslSGGWLRKVALARALACDPDLLLLDEPTNHLD-------IEAINWLEDflkdfRG-AIV 207
Cdd:COG4778 135 LLARLNLPerlwdlPPATF---SGGEQQRVNIARGFIADPPLLLLDEPTASLDaanravvVELIEEAKA-----RGtAII 206
|
250 260
....*....|....*....|..
gi 1411607396 208 FISHDREFIHKLATRIIDLDRG 229
Cdd:COG4778 207 GIFHDEEVREAVADRVVDVTPF 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-250 |
1.37e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.11 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLldNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDL--------KVTRLEQD 74
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRiLWNGQDLtalppaerPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 75 PPASSDLTVFDYTAEGLagvgellkkyhhismelahdpsDANIRIMSDLQEQLdyqngwqfETRISQV-LT-LLNLDPDA 152
Cdd:COG3840 80 NNLFPHLTVAQNIGLGL----------------------RPGLKLTAEQRAQV--------EQALERVgLAgLLDRLPGQ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 153 tldsLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDR 228
Cdd:COG3840 130 ----LSGGQRQRVALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVAD 205
|
250 260
....*....|....*....|...
gi 1411607396 229 GVItSWPGNYDEYLQGK-EEALR 250
Cdd:COG3840 206 GRI-AADGPTAALLDGEpPPALA 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-231 |
1.82e-17 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 81.90 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLeqdPPASSD-- 80
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEiLLDGKD--ITNL---PPHKRPvn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 81 -----------LTVFDYTAEGLAgvgelLKKYhhismelahDPSDANIRIMsdlqEQLDyqngwqfetrISQVLTLLNLD 149
Cdd:cd03300 76 tvfqnyalfphLTVFENIAFGLR-----LKKL---------PKAEIKERVA----EALD----------LVQLEGYANRK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 150 PDatldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAI----VFISHDREFIHKLATRIID 225
Cdd:cd03300 128 PS----QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgitfVFVTHDQEEALTMSDRIAV 203
|
....*.
gi 1411607396 226 LDRGVI 231
Cdd:cd03300 204 MNKGKI 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-231 |
2.16e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 82.43 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPldDGRMVQQQDLKVTRLeqdppASSDLTVFDYTaeglagvgel 97
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlESP--SQGNVSWRGEPLAKL-----NRAQRKAFRRD---------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 98 lkkyhhISMELAHDPSDANIR-----IMSDLQEQLDYQNGWQFETRISQVLTLLNLDP---DATLDSLSGGWLRKVALAR 169
Cdd:PRK10419 91 ------IQMVFQDSISAVNPRktvreIIREPLRHLLSLDKAERLARASEMLRAVDLDDsvlDKRPPQLSGGQLQRVCLAR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 170 ALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
315-475 |
2.23e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 85.60 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 315 SGKLVFEteglGLDF---GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL-EVAYfDQ 389
Cdd:COG1132 337 RGEIEFE----NVSFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILiDGVDIrDLTL-ES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 390 YRDQL-----DP---EQTVMDNVGEGKQEVmvrgrSR----------HILGYLQDFlfePKRARTPV----KALSGGEKN 447
Cdd:COG1132 412 LRRQIgvvpqDTflfSGTIRENIRYGRPDA-----TDeeveeaakaaQAHEFIEAL---PDGYDTVVgergVNLSGGQRQ 483
|
170 180
....*....|....*....|....*...
gi 1411607396 448 RLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTET 511
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
321-497 |
2.82e-17 |
|
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: 81.03 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGT--------KLEVAY-FDQY 390
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGeILIDGRdvtgvppeRRNIGMvFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RdqLDPEQTVMDNVG-----EGKQEVMVRGRSRHILGYLQDFLFEPKRARTpvkaLSGGEKNRLLLAK-LFLKPSnLLIL 464
Cdd:cd03259 82 A--LFPHLTVAENIAfglklRGVPKAEIRARVRELLELVGLEGLLNRYPHE----LSGGQQQRVALARaLAREPS-LLLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1411607396 465 DEPTNDLDVETLELLEELLADYPG----TLLLVSHDR 497
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRelgiTTIYVTHDQ 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-501 |
3.04e-17 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 85.07 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmVQQQDLKVTRL--EQDPPAS 78
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE-RQSQFSHITRLsfEQLQKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 79 SDltVFDYTAEGLAGVGEllKKYHHISMELAHDPSDANIRImsdlqEQLDYQNGwqfetrISQVLtllnldpDATLDSLS 158
Cdd:PRK10938 80 SD--EWQRNNTDMLSPGE--DDTGRTTAEIIQDEVKDPARC-----EQLAQQFG------ITALL-------DRRFKYLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGVITswp 235
Cdd:PRK10938 138 TGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDEIPDFVQFAGVLADCTLA--- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 236 gnydeyLQGKEEALR----VEELQHAEfdrklaqeevwvrqgikarrtrnegrvrALEAMRM----ERSQRREL-QGKAK 306
Cdd:PRK10938 215 ------ETGEREEILqqalVAQLAHSE----------------------------QLEGVQLpepdEPSARHALpANEPR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 307 LQMDDVNRSgklvfeteglgldFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQlEPS------------RG 374
Cdd:PRK10938 261 IVLNNGVVS-------------YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQgysndltlfgrrRG 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 375 lvKGGT----KLEVAYFD-----QYRDQLDPEQTVM----DNVGEGKQevmVRGRSRHILGYLQDFLFEPKR-ARTPVKA 440
Cdd:PRK10938 327 --SGETiwdiKKHIGYVSsslhlDYRVSTSVRNVILsgffDSIGIYQA---VSDRQQKLAQQWLDILGIDKRtADAPFHS 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 441 LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDvetlelleelladyPGTLLLVshdRRFID 501
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLD--------------PLNRQLV---RRFVD 445
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-212 |
3.07e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 83.24 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV---------QQQDLKVTRLE-----QDPPASSD--LT 82
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqditglSGRELRPLRRRmqmvfQDPYASLNprMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 83 VFDYTAEGLagvgellkkyhhismeLAHDPSDANIRimsdlqeqldyqngwqfETRISQVLTLLNLDPDAtLDS----LS 158
Cdd:COG4608 114 VGDIIAEPL----------------RIHGLASKAER-----------------RERVAELLELVGLRPEH-ADRypheFS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFLKDFRGAIVFISHD 212
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDvsIQAqvLNLLEDLQDELGLTYLFISHD 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
321-472 |
3.24e-17 |
|
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: 81.39 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLDPEQ-- 398
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSG--------EVLIDGEDISGLSEAEly 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 -------------------TVMDNVG------EGKQEVMVRGRSRHILGYLQdflFEPKRARTPVKaLSGGEKNRLLLAK 453
Cdd:cd03261 74 rlrrrmgmlfqsgalfdslTVFENVAfplrehTRLSEEEIREIVLEKLEAVG---LRGAEDLYPAE-LSGGMKKRVALAR 149
|
170 180
....*....|....*....|
gi 1411607396 454 -LFLKPSnLLILDEPTNDLD 472
Cdd:cd03261 150 aLALDPE-LLLYDEPTAGLD 168
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-229 |
4.31e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 80.42 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 29 GERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV----------QQQDLKVTR-----LEQDPPASSDLTVFDYTAEGLAG 93
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrKKINLPPQQrkiglVFQQYALFPHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 94 vgellkkyhhismelahdPSDANIRImsdlqeqldyqngwqfetRISQVLTLLNLDP--DATLDSLSGGWLRKVALARAL 171
Cdd:cd03297 103 ------------------KRNREDRI------------------SVDELLDLLGLDHllNRYPAQLSGGEKQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 172 ACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd03297 147 AAQPELLLLDEPFSALDralrLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
12-224 |
4.42e-17 |
|
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: 84.84 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 12 SFSDFPLlDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqQQDLKVTRLEQDPPASSDLTVFDYTAEGL 91
Cdd:COG1245 350 SYGGFSL-EVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGTVEEFLRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 92 AGvgellkkyhhismelahdpsdanirimsdlqeqlDYQNGWqFETRISQVLtllNLDP--DATLDSLSGGWLRKVALAR 169
Cdd:COG1245 427 TD----------------------------------DFGSSY-YKTEIIKPL---GLEKllDKNVKDLSGGELQRVAIAA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 170 ALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVF-ISHDREFIHKLATRII 224
Cdd:COG1245 469 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaenRGKTAMvVDHDIYLIDYISDRLM 527
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
323-473 |
5.23e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.93 E-value: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyRDQLDP------ 396
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ-KLYLDTtlpltv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 397 EQTVMDNVGEGKQEVM---VRGRSRHILGYlqdflfepkrartPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK09544 87 NRFLRLRPGTKKEDILpalKRVQAGHLIDA-------------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-500 |
6.22e-17 |
|
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: 78.77 E-value: 6.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKLEVAYFDQYRD--- 392
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlidgEDLTDLEDELPPLRRRigm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 -----QLDPEQTVMDNVGEGkqevmvrgrsrhilgylqdflfepkrartpvkaLSGGEKNRLLLAK-LFLKPsNLLILDE 466
Cdd:cd03229 81 vfqdfALFPHLTVLENIALG---------------------------------LSGGQQQRVALARaLAMDP-DVLLLDE 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 1411607396 467 PTNDLDVETLELLEELLAD----YPGTLLLVSHDRRFI 500
Cdd:cd03229 127 PTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEA 164
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
321-496 |
6.70e-17 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 80.11 E-value: 6.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtKLEVAYFDQYRDQLD----- 395
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG------RATVAGHDVVREPREvrrri 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 ---PEQTVMDNVGEGKQEVMVRGRsrhILGY-----------LQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNL 461
Cdd:cd03265 76 givFQDLSVDDELTGWENLYIHAR---LYGVpgaerrerideLLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1411607396 462 LILDEPTNDLDVETLELL----EELLADYPGTLLLVSHD 496
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVweyiEKLKEEFGMTILLTTHY 191
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
319-475 |
7.35e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK--GGTKLEVAYFDQ-----YR 391
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKldGGDIDDPDVAEAchylgHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 392 DQLDPEQTVMDNVgEGKQEVMvRGRSRHILGYLQDFLFEPKrARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:PRK13539 82 NAMKPALTVAENL-EFWAAFL-GGEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
....
gi 1411607396 472 DVET 475
Cdd:PRK13539 159 DAAA 162
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
321-500 |
7.65e-17 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 80.17 E-value: 7.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTklEVAYFDQYR-------- 391
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfDGE--DITGLPPHEiarlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 392 ----DQLDPEQTVMDNV---------------GEGKQEVMVRGRSRHILgylqDFLFEPKRARTPVKALSGGEKNRLLLA 452
Cdd:cd03219 80 tfqiPRLFPELTVLENVmvaaqartgsglllaRARREEREARERAEELL----ERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 453 K-LFLKPSnLLILDEPT---NDLDVETLELLEELLADYPGTLLLVSHDRRFI 500
Cdd:cd03219 156 RaLATDPK-LLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVV 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
12-231 |
7.73e-17 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 79.72 E-value: 7.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------VQQQDLKVTR----LEQDPPASSDL 81
Cdd:cd03265 9 KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAtvaghdVVREPREVRRrigiVFQDLSVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 TVFD--YTAEGLAGV-GELLKKyhhismelahdpsdaniRImsdlQEQLDYQNGWQFETRIsqvltllnldpdatLDSLS 158
Cdd:cd03265 89 TGWEnlYIHARLYGVpGAERRE-----------------RI----DELLDFVGLLEAADRL--------------VKTYS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEAIN--W--LEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03265 134 GGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-224 |
1.67e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.93 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 26 IERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQqqDLKVTRLEQDPPASSDLTVFDYtaegLAGVGEllkkyhhis 105
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--ELKISYKPQYIKPDYDGTVEDL----LRSITD--------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 106 melahdpsdanirimsdlqeqlDYQNGWqFETRISQVLtllNLDP--DATLDSLSGGWLRKVALARALACDPDLLLLDEP 183
Cdd:PRK13409 427 ----------------------DLGSSY-YKSEIIKPL---QLERllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1411607396 184 TNHLDIE-------AINwleDFLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:PRK13409 481 SAHLDVEqrlavakAIR---RIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-231 |
1.91e-16 |
|
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: 82.81 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKII------AGELPLDDGRMVQ--QQDLKVTRLE-----QDPPASSD--LTV 83
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALlrlipsEGEIRFDGQDLDGlsRRALRPLRRRmqvvfQDPFGSLSprMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 FDYTAEGLAgvgellkkyhhismelAHDPsdanirimsdlqeQLDYQngwQFETRISQVLTLLNLDPDaTLD----SLSG 159
Cdd:COG4172 382 GQIIAEGLR----------------VHGP-------------GLSAA---ERRARVAEALEEVGLDPA-ARHryphEFSG 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDvsVQAqiLDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
330-496 |
2.07e-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: 82.41 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-----------LVKGGTKLEVAYFDQyrdqlDP-- 396
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGevtldgvpvssLDQDEVRRRVSVCAQ-----DAhl 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 397 -EQTVMDNV----GEGKQEVMVRGRSRHILGYLQDFLfePKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:TIGR02868 421 fDTTVRENLrlarPDATDEELWAALERVGLADWLRAL--PDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|.
gi 1411607396 468 TNDLDVETLEL--LEELLADYPGTLLLVSHD 496
Cdd:TIGR02868 499 TEHLDAETADEllEDLLAALSGRTVVLITHH 529
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
337-503 |
2.56e-16 |
|
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: 78.22 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL------EVAYFDQ-----YRD-QLDPEQTVMDN 403
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvNGQDVsdlrgrAIPYLRRkigvvFQDfRLLPDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 404 V-------GEGKQEvmVRGRSRHILgylqDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETL 476
Cdd:cd03292 99 VafalevtGVPPRE--IRKRVPAAL----ELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190
....*....|....*....|....*....|
gi 1411607396 477 ELLEELLADY--PGTLLLVS-HDRRFIDNT 503
Cdd:cd03292 173 WEIMNLLKKInkAGTTVVVAtHAKELVDTT 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
329-570 |
2.64e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 82.25 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyrDQLDPEQ-TVMDNVGEG 407
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQ--DQFAFEEfTVLDTVIMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 408 -------KQE------------------------------VMVRGRSRHIL---GYLQDFLFEPKRARTPvkalsgGEKN 447
Cdd:PRK15064 89 htelwevKQErdriyalpemseedgmkvadlevkfaemdgYTAEARAGELLlgvGIPEEQHYGLMSEVAP------GWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 448 RLLLAK-LFLKPsNLLILDEPTNDLDVETLELLEELLADYPGTLLLVSHDRRFIdNTVtgCW----LFEGDGRIsdYVGG 522
Cdd:PRK15064 163 RVLLAQaLFSNP-DILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFL-NSV--CThmadLDYGELRV--YPGN 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 523 YADMMATRAQQSTQLAA----KAAQVKT-PEPVAVASPAASKVK------KLSYKLQLE 570
Cdd:PRK15064 237 YDEYMTAATQARERLLAdnakKKAQIAElQSFVSRFSANASKAKqatsraKQIDKIKLE 295
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-496 |
2.81e-16 |
|
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: 81.87 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDF--GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqLEPSRGLVKGGTKL-------------- 382
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRISGEVLLdgrdllelsealrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 383 -EVAY-FDQYRDQLDPEqTVMDNVGEGKQEVMVRGRSRH--ILGYLQDFLFEpKRARTPVKALSGGEKNRLLLA-KLFLK 457
Cdd:COG1123 83 rRIGMvFQDPMTQLNPV-TVGDQIAEALENLGLSRAEARarVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAmALALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1411607396 458 PSnLLILDEPTNDLDV----ETLELLEELLADYPGTLLLVSHD 496
Cdd:COG1123 161 PD-LLIADEPTTALDVttqaEILDLLRELQRERGTTVLLITHD 202
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-229 |
3.16e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.16 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDF-PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDP------- 75
Cdd:COG4178 363 LALEDLTLRTPDGrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPylplgtl 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 76 ------PASSDltvfDYTAEGLAgvgELLKKYHhismeLAHdpsdanirimsdLQEQLDYQNGWqfetriSQVLtllnld 149
Cdd:COG4178 443 reallyPATAE----AFSDAELR---EALEAVG-----LGH------------LAERLDEEADW------DQVL------ 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 150 pdatldslSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKD--FRGAIVFISHdREFIHKLATRIIDLD 227
Cdd:COG4178 487 --------SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELT 557
|
..
gi 1411607396 228 RG 229
Cdd:COG4178 558 GD 559
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
321-495 |
3.92e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 77.71 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKG-----GTKLEVAYFDQYRDq 393
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGevLFDGkpldiAARNRIGYLPEERG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 LDPEQTVMDNV-------GEGKQEVmvrgrSRHILGYLQDFLFEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLILDE 466
Cdd:cd03269 81 LYPKMKVIDQLvylaqlkGLKKEEA-----RRRIDEWLERLELSEYANK-RVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190
....*....|....*....|....*....|..
gi 1411607396 467 PTNDLD---VETLELLEELLADYPGTLLLVSH 495
Cdd:cd03269 155 PFSGLDpvnVELLKDVIRELARAGKTVILSTH 186
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-226 |
4.83e-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: 81.18 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDL----------KVTRLEQDPpassdlTVFD 85
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIaVNGVPLadadadswrdQIAWVPQHP------FLFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 86 YT-AEGLAgvgeLLKKyhhismelahDPSDAnirimsDLQEQLDYQNGWQFETRISQVLTLLnLDPDATldSLSGGWLRK 164
Cdd:TIGR02857 410 GTiAENIR----LARP----------DASDA------EIREALERAGLDEFVAALPQGLDTP-IGEGGA--GLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 165 VALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF-RGAIVF-ISHDREFIHkLATRIIDL 226
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaQGRTVLlVTHRLALAA-LADRIVVL 529
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
321-474 |
5.28e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 77.01 E-value: 5.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQY---------R 391
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPhenilylghL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 392 DQLDPEQTVMDNVGegkqevmvrgRSRHILGYLQDFLFEP-------KRARTPVKALSGGEKNRLLLAKLFLKPSNLLIL 464
Cdd:TIGR01189 82 PGLKPELSALENLH----------FWAAIHGGAQRTIEDAlaavgltGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170
....*....|
gi 1411607396 465 DEPTNDLDVE 474
Cdd:TIGR01189 152 DEPTTALDKA 161
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
320-475 |
5.33e-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: 77.99 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGD-RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK----GGTKLEVAYFDQYRDQ- 393
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtDINKLKGKALRQLRRQi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 --------LDPEQTVMDNVGEGKQEVMVRGRS----------RHILGYLQDFLFEPKrARTPVKALSGGEKNRLLLAKLF 455
Cdd:cd03256 81 gmifqqfnLIERLSVLENVLSGRLGRRSTWRSlfglfpkeekQRALAALERVGLLDK-AYQRADQLSGGQQQRVAIARAL 159
|
170 180
....*....|....*....|
gi 1411607396 456 LKPSNLLILDEPTNDLDVET 475
Cdd:cd03256 160 MQQPKLILADEPVASLDPAS 179
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-183 |
5.51e-16 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 77.58 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR------------MVQQQDLKVTRL 71
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKilldgqditklpMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 72 EQDPPASSDLTVfdytAEGLAGVGELLKKyhhismelahdpsdanirimsdlqeqldyqNGWQFETRISQVLTLLNLDP- 150
Cdd:cd03218 81 PQEASIFRKLTV----EENILAVLEIRGL------------------------------SKKEREEKLEELLEEFHITHl 126
|
170 180 190
....*....|....*....|....*....|....
gi 1411607396 151 -DATLDSLSGGWLRKVALARALACDPDLLLLDEP 183
Cdd:cd03218 127 rKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
17-231 |
6.87e-16 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 75.72 E-value: 6.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtRLEqdppassdltvfdytaeglagvGE 96
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV---------RLD----------------------GA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 97 LLKKYHhismelahdpsdaniriMSDLQEQLDY--QNGWQFETRISQvltllNLdpdatldsLSGGWLRKVALARALACD 174
Cdd:cd03246 65 DISQWD-----------------PNELGDHVGYlpQDDELFSGSIAE-----NI--------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 175 PDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIhKLATRIIDLDRGVI 231
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAgatRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
320-472 |
7.02e-16 |
|
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: 77.22 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLL-----LGQLEPSRGlvkggtklEVAYFDQ--YRD 392
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEG--------EVLLDGKdiYDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 QLDPEQ-----------------TVMDNV-------GEGKQEVMvRGRSRHILGylQDFLFEPKRARTPVKALSGGEKNR 448
Cdd:cd03260 73 DVDVLElrrrvgmvfqkpnpfpgSIYDNVayglrlhGIKLKEEL-DERVEEALR--KAALWDEVKDRLHALGLSGGQQQR 149
|
170 180
....*....|....*....|....*
gi 1411607396 449 LLLAK-LFLKPSNLLiLDEPTNDLD 472
Cdd:cd03260 150 LCLARaLANEPEVLL-LDEPTSALD 173
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-243 |
7.28e-16 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 80.98 E-value: 7.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQdppassdlt 82
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ--------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 83 vfdytaeglagvgellkkyHHISMELAHD-PSDANIRIM-SDLQEQL-DYQNGWQFETriSQVltllnldPDATlDSLSG 159
Cdd:PRK10636 383 -------------------HQLEFLRADEsPLQHLARLApQELEQKLrDYLGGFGFQG--DKV-------TEET-RRFSG 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYD 239
Cdd:PRK10636 434 GEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLE 513
|
....
gi 1411607396 240 EYLQ 243
Cdd:PRK10636 514 DYQQ 517
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-227 |
8.21e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 75.27 E-value: 8.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPpassdltvfdYTAEGLagvge 96
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRP----------YLPLGT----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 97 llkkyhhismelahdpsdanirimsdLQEQLDYQngWQfetrisqvltllnldpdatlDSLSGGWLRKVALARALACDPD 176
Cdd:cd03223 80 --------------------------LREQLIYP--WD--------------------DVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 177 LLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHdREFIHKLATRIIDLD 227
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-189 |
8.48e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.43 E-value: 8.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 5 TLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTR----------LEQ 73
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEvLVDGLDVATTPsrelakrlaiLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 74 DPPASSDLTVFDytaegLAGVGellkKYHHISMEL-AHDpsdanirimsdlqeqldyqngwqfETRISQVLTLLNLDP-- 150
Cdd:COG4604 83 ENHINSRLTVRE-----LVAFG----RFPYSKGRLtAED------------------------REIIDEAIAYLDLEDla 129
|
170 180 190
....*....|....*....|....*....|....*....
gi 1411607396 151 DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI 189
Cdd:COG4604 130 DRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
319-500 |
9.25e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 77.39 E-value: 9.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLDPEQ 398
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSG--------RILFDGRDITGLPPHR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 -------------------TVMDNV--------GEG------------KQEVMVRGRSRHILGY--LQDflfepkRARTP 437
Cdd:COG0411 76 iarlgiartfqnprlfpelTVLENVlvaaharlGRGllaallrlprarREEREARERAEELLERvgLAD------RADEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 438 VKALSGGEKNRLLLAK-LFLKPSnLLILDEPT---NDLDVETLELLEELLADYPG-TLLLVSHDRRFI 500
Cdd:COG0411 150 AGNLSYGQQRRLEIARaLATEPK-LLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLV 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-184 |
1.00e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 76.94 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV-QQQDLkvTRLeqdPPAS- 78
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfDGEDI--TGL---PPHRi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 79 ---------------SDLTVfdytAEGLagvgellkkyhhismELAHDPSDANIRIMSDLQEQLDYqngwqF---ETRIS 140
Cdd:COG0410 76 arlgigyvpegrrifPSLTV----EENL---------------LLGAYARRDRAEVRADLERVYEL-----FprlKERRR 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1411607396 141 QvltllnldpDATldSLSGGWLRKVALARALACDPDLLLLDEPT 184
Cdd:COG0410 132 Q---------RAG--TLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
331-475 |
1.02e-15 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 76.89 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQLD--PEQTV------M 401
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILiDGQDIREVTLDSLRRAIGvvPQDTVlfndtiG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEGK-----QEVMVRGRSRHILGYLQDFlfePKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03253 93 YNIRYGRpdatdEEVIEAAKAAQIHDKIMRF---PDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
...
gi 1411607396 473 VET 475
Cdd:cd03253 170 THT 172
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
321-496 |
1.37e-15 |
|
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: 76.39 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLF----QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKLEVAYFDQYRD 392
Cdd:cd03257 3 EVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgKDLLKLSRRLRKIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 Q-----------LDPEQTVMDNVGEG--KQEVMVRGRSRHILGYLQDFLFEPKRA---RTPVkALSGGEKNRLLLAK-LF 455
Cdd:cd03257 83 EiqmvfqdpmssLNPRMTIGEQIAEPlrIHGKLSKKEARKEAVLLLLVGVGLPEEvlnRYPH-ELSGGQRQRVAIARaLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1411607396 456 LKPSnLLILDEPTNDLDVETLELLEELLAD----YPGTLLLVSHD 496
Cdd:cd03257 162 LNPK-LLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHD 205
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-189 |
1.39e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.12 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTRLEQDP----- 75
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrLNGRPLADWSPAELArrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 76 -PASSDLTvFDYTAEglagvgELlkkyhhISMELAHDPSDANirimsdlqeqldyqngwQFETRISQVLTLLNLDPDATL 154
Cdd:PRK13548 81 lPQHSSLS-FPFTVE------EV------VAMGRAPHGLSRA-----------------EDDALVAAALAQVDLAHLAGR 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1411607396 155 D--SLSGGWLRKVALARALA----CDPD--LLLLDEPTNHLDI 189
Cdd:PRK13548 131 DypQLSGGEQQRVQLARVLAqlwePDGPprWLLLDEPTSALDL 173
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-232 |
1.48e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 76.03 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 6 LHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmvqqqdlkVTRLEQDPPA-------S 78
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT--------VTVRGRVSSLlglgggfN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 79 SDLTVFDYTaeglagvgellkkyHHISMELAHDPSDANIRI-----MSDLQEQLDYqngwqfetrisQVLTllnldpdat 153
Cdd:cd03220 97 PELTGRENI--------------YLNGRLLGLSRKEIDEKIdeiieFSELGDFIDL-----------PVKT--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 154 ldsLSGGWLRKVALARALACDPDLLLLDEPT----NHLDIEAINWLEDFLKDFRgAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd03220 143 ---YSSGMKARLAFAIATALEPDILLIDEVLavgdAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKG 218
|
...
gi 1411607396 230 VIT 232
Cdd:cd03220 219 KIR 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
336-501 |
1.78e-15 |
|
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: 75.70 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLevayfdqyrDQLDPeQTVMDNVGEGKQEVM-- 412
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLlDGTDI---------RQLDP-ADLRRNIGYVPQDVTlf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 413 ---VR---------GRSRHIL-----GYLQDFL-FEPKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:cd03245 91 ygtLRdnitlgaplADDERILraaelAGVTDFVnKHPNGLDLQIgergRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190
....*....|....*....|....*....|...
gi 1411607396 471 LDVETLELLEELLADYPG--TLLLVSHDRRFID 501
Cdd:cd03245 171 MDMNSEERLKERLRQLLGdkTLIIITHRPSLLD 203
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
319-475 |
1.81e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.77 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLepSRGLVKGgtklevaYFDQYRDQLDPEQ 398
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL--KGTPVAG-------CVDVPDNQFGREA 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 399 TVMDNVGEgKQEVMVRGRSRHILGYLQDFLFepkraRTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:COG2401 101 SLIDAIGR-KGDFKDAVELLNAVGLSDAVLW-----LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
321-473 |
2.04e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.59 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFD-QYRDQLD--PE 397
Cdd:PRK11231 4 RTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLAllPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 398 QTVmdnVGEG--KQEVMVRGRSRHI-----LGYLQDFLFEPKRART--------PVKALSGGEKNRLLLAKLFLKPSNLL 462
Cdd:PRK11231 84 HHL---TPEGitVRELVAYGRSPWLslwgrLSAEDNARVNQAMEQTrinhladrRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170
....*....|.
gi 1411607396 463 ILDEPTNDLDV 473
Cdd:PRK11231 161 LLDEPTTYLDI 171
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-231 |
2.09e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.15 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIA-------GELPLDDGRM--VQQQDLKVTRL 71
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAgleditsGDLFIGEKRMndVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 72 EQDPPASSDLTVFDYTAEG--LAGVG--ELLKKYHHIS--MELAHdpsdanirimsdlqeqldyqngwqfetrisqvltL 145
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGlkLAGAKkeEINQRVNQVAevLQLAH----------------------------------L 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 146 LNLDPDAtldsLSGGWLRKVALARALACDPDLLLLDEPTNHLD--------IEaINWLEdflKDFRGAIVFISHDREFIH 217
Cdd:PRK11000 127 LDRKPKA----LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmrIE-ISRLH---KRLGRTMIYVTHDQVEAM 198
|
250
....*....|....
gi 1411607396 218 KLATRIIDLDRGVI 231
Cdd:PRK11000 199 TLADKIVVLDAGRV 212
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-231 |
2.59e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 76.62 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTRLEQdppasSDL-----TVFDYTAEGLa 92
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKiIIDGVDITDKKVKL-----SDIrkkvgLVFQYPEYQL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 93 gVGELLKKyhhismELAHDPSDANirimsdLQEQldyqngwQFETRISQVLTLLNLDPDATLD----SLSGGWLRKVALA 168
Cdd:PRK13637 97 -FEETIEK------DIAFGPINLG------LSEE-------EIENRVKRAMNIVGLDYEDYKDkspfELSGGQKRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 169 RALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
321-473 |
3.02e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 75.92 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLDPEQ-- 398
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSG--------EVRLNGRPLAAWSPWEla 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 ----------------TVmdnvgegkQEVmVR-GRSRHILGYLQDflfePKRART-------------PVKALSGGEKNR 448
Cdd:COG4559 75 rrravlpqhsslafpfTV--------EEV-VAlGRAPHGSSAAQD----RQIVREalalvglahlagrSYQTLSGGEQQR 141
|
170 180 190
....*....|....*....|....*....|..
gi 1411607396 449 LLLAKLFL-------KPSNLLILDEPTNDLDV 473
Cdd:COG4559 142 VQLARVLAqlwepvdGGPRWLFLDEPTSALDL 173
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
321-473 |
3.21e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.96 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQLD--PE 397
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvAGDDVEALSARAASRRVAsvPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 398 QTVMDNVGEGKQEVMVrGRSRHI-----LGYLQDFLFEPKRART--------PVKALSGGEKNRLLLAKLFLKPSNLLIL 464
Cdd:PRK09536 85 DTSLSFEFDVRQVVEM-GRTPHRsrfdtWTETDRAAVERAMERTgvaqfadrPVTSLSGGERQRVLLARALAQATPVLLL 163
|
....*....
gi 1411607396 465 DEPTNDLDV 473
Cdd:PRK09536 164 DEPTASLDI 172
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-241 |
3.31e-15 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 79.13 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFSD----FP----LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSDLT 82
Cdd:PLN03073 509 ISFSDasfgYPggplLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLS 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 83 V--FDYTAEGLAGVGELLKKYHHISMELAHDpsdanirimsdlqeqldyqngwqfetrisqvltlLNLDPDATLdslSGG 160
Cdd:PLN03073 589 SnpLLYMMRCFPGVPEQKLRAHLGSFGVTGN----------------------------------LALQPMYTL---SGG 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDE 240
Cdd:PLN03073 632 QKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHD 711
|
.
gi 1411607396 241 Y 241
Cdd:PLN03073 712 Y 712
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
10-233 |
3.61e-15 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 77.46 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 10 CLSFS----DFPLldNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQdlkvtRLEQDPPASSDLTV-- 83
Cdd:TIGR02142 2 SARFSkrlgDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG-----RTLFDSRKGIFLPPek 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 --FDYtaeglagVGELLKKYHHISmelahdpsdanirIMSDLQEQLDYQNGWQFETRISQVLTLLNLDP--DATLDSLSG 159
Cdd:TIGR02142 75 rrIGY-------VFQEARLFPHLS-------------VRGNLRYGMKRARPSERRISFERVIELLGIGHllGRLPGRLSG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:TIGR02142 135 GEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-184 |
4.09e-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: 4.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV-QQQDlkVTRLeqdPPassdlt 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfDGRD--ITGL---PP------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 83 vFDYTAEGLAGVGELLKKYHHIS----MELAhdpsdANIRIMSDLQEQLDyqngWQFE------TRISQvltllnldPDA 152
Cdd:cd03224 70 -HERARAGIGYVPEGRRIFPELTveenLLLG-----AYARRRAKRKARLE----RVYElfprlkERRKQ--------LAG 131
|
170 180 190
....*....|....*....|....*....|..
gi 1411607396 153 TldsLSGGWLRKVALARALACDPDLLLLDEPT 184
Cdd:cd03224 132 T---LSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
323-472 |
4.12e-15 |
|
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: 75.40 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLDPEQ---- 398
Cdd:COG1127 9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSG--------EILVDGQDITGLSEKElyel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 -----------------TVMDNVG------EGKQEVMVRGRSRHIL---GyLQDFlfepkRARTPvKALSGGEKNRLLLA 452
Cdd:COG1127 81 rrrigmlfqggalfdslTVFENVAfplrehTDLSEAEIRELVLEKLelvG-LPGA-----ADKMP-SELSGGMRKRVALA 153
|
170 180
....*....|....*....|.
gi 1411607396 453 K-LFLKPSnLLILDEPTNDLD 472
Cdd:COG1127 154 RaLALDPE-ILLYDEPTAGLD 173
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
24-231 |
4.40e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 75.05 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 24 LSIERGERLCLVGRNGAGKSTLMKIiageLPLddgrmvqqqdlkvtrLEQdpPASSDLTV----FDYTA-----EGLA-- 92
Cdd:PRK11124 23 LDCPQGETLVLLGPSGAGKSSLLRV----LNL---------------LEM--PRSGTLNIagnhFDFSKtpsdkAIRElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 93 -GVGELLKKYH---HisMELAHDPSDANIRIMSdLQEQldyqngwQFETRISQVLTLLNLDP--DATLDSLSGGWLRKVA 166
Cdd:PRK11124 82 rNVGMVFQQYNlwpH--LTVQQNLIEAPCRVLG-LSKD-------QALARAEKLLERLRLKPyaDRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 167 LARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG-AI--VFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGItqVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-231 |
5.30e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 76.66 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPlDDGR-MVQQQDLkvTRLEQDppassdltvfdytaeglagvgE 96
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLlERP-TSGSvLVDGVDL--TALSER---------------------E 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 97 LLKKYHHISMELAHdpsdANIrimsdLQEQLDYQN--------GW---QFETRISQVLTLLNLDP--DATLDSLSGGWLR 163
Cdd:COG1135 77 LRAARRKIGMIFQH----FNL-----LSSRTVAENvalpleiaGVpkaEIRKRVAELLELVGLSDkaDAYPSQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDIE---AInwLeDFLKDFRG----AIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPEttrSI--L-DLLKDINRelglTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
331-475 |
6.34e-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: 77.83 E-value: 6.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEVAYFDQYRDQLDP--------EQTVM 401
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGqILLDGHDLADYTLASLRRQVALvsqdvvlfNDTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEGKQEVMVRGRSRHIL--GYLQDFLFE-PKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVE 474
Cdd:TIGR02203 424 NNIAYGRTEQADRAEIERALaaAYAQDFVDKlPLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALDNE 503
|
.
gi 1411607396 475 T 475
Cdd:TIGR02203 504 S 504
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-231 |
7.43e-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: 73.85 E-value: 7.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrmvqqqdlkVTRLEQDPPASSDLTV 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSG---------EVLFDGKPLDIAARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 FDYTAE--GL---AGVGELLKKYhhismelahdpsdANIRIM--SDLQEQLDYqngWqfetrisqvLTLLNLDP--DATL 154
Cdd:cd03269 72 IGYLPEerGLypkMKVIDQLVYL-------------AQLKGLkkEEARRRIDE---W---------LERLELSEyaNKRV 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 155 DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03269 127 EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgktVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
330-516 |
8.07e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 74.11 E-value: 8.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTK----LEVAYFdqyrdqLDPEQTVMDNV- 404
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsslLGLGGG------FNPELTGRENIy 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 405 ------GEGKQEvmVRGRSRHILGY--LQDFLfepkraRTPVKALSGGEKNRLLLA-KLFLKPsNLLILDEPTNDLDVET 475
Cdd:cd03220 107 lngrllGLSRKE--IDEKIDEIIEFseLGDFI------DLPVKTYSSGMKARLAFAiATALEP-DILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1411607396 476 LELLEELLADY---PGTLLLVSHDRRFIDNTVT-GCWLFegDGRI 516
Cdd:cd03220 178 QEKCQRRLRELlkqGKTVILVSHDPSSIKRLCDrALVLE--KGKI 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
319-472 |
9.06e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.42 E-value: 9.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLDPEQ 398
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSG--------EVRLNGRPLADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 ------------------TVmdnvgegkQEVMVRGRSRHILGYLQD-FLFEPKRART--------PVKALSGGEKNRLLL 451
Cdd:PRK13548 74 larrravlpqhsslsfpfTV--------EEVVAMGRAPHGLSRAEDdALVAAALAQVdlahlagrDYPQLSGGEQQRVQL 145
|
170 180
....*....|....*....|....*..
gi 1411607396 452 AKLFL------KPSNLLILDEPTNDLD 472
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALD 172
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-473 |
9.16e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 72.08 E-value: 9.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklevayfdqyrdqldpeqt 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG------------------------- 55
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 400 vmdnvgegkqEVMVRGRSRHILGylqdflfePKRAR----TPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03216 56 ----------EILVDGKEVSFAS--------PRDARragiAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-229 |
9.22e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 74.04 E-value: 9.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDDGRMVQQQDLkvtrleqDPPASSDLTVF-DYTAEGLAGVGE 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGGVILEGKQI-------TEPGPDRMVVFqNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 97 llkkyhhiSMELAHDpsdaniRIMSDLQEQldyqngwQFETRISQVLTLLNLD--PDATLDSLSGGWLRKVALARALACD 174
Cdd:TIGR01184 74 --------NIALAVD------RVLPDLSKS-------ERRAIVEEHIALVGLTeaADKRPGQLSGGMKQRVAIARALSIR 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 175 PDLLLLDEPTNHLD-IEAINWLEDFLK---DFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:TIGR01184 133 PKVLLLDEPFGALDaLTRGNLQEELMQiweEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-258 |
9.69e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 74.36 E-value: 9.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLD-----DGR-----------MVQQQ-DL- 66
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDglkvnDPKvderlirqeagMVFQQfYLf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 67 -KVTRLE-------QDPPASSDltvfdyTAEGLAGvgELLKKYHhISMELAHDPSDanirimsdlqeqldyqngwqfetr 138
Cdd:PRK09493 90 pHLTALEnvmfgplRVRGASKE------EAEKQAR--ELLAKVG-LAERAHHYPSE------------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 139 isqvltllnldpdatldsLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RG-AIVFISHDREF 215
Cdd:PRK09493 137 ------------------LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLaeEGmTMVIVTHEIGF 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1411607396 216 IHKLATRIIDLDRGVITSwPGNYDEYLQGK-EEALRvEELQHAE 258
Cdd:PRK09493 199 AEKVASRLIFIDKGRIAE-DGDPQVLIKNPpSQRLQ-EFLQHVS 240
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-229 |
9.87e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.41 E-value: 9.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDDGRMVQQQDLKVTRLEQDPpassdl 81
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPTAGQIMLDGVDLSHVPPYQRP------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 tvfdytaeglagVGELLKKYH---HISMElahdpsdANIRIMSDlQEQLDYQngwQFETRISQVLTLLNLDPDATLD--S 156
Cdd:PRK11607 93 ------------INMMFQSYAlfpHMTVE-------QNIAFGLK-QDKLPKA---EIASRVNEMLGLVHMQEFAKRKphQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLE----DFLKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQlevvDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-212 |
1.44e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 76.63 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmVQQQDLKVTRLEQDPPAS------SDLTVFDYTaeg 90
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGE-VTLDGVPVSSLDQDEVRRrvsvcaQDAHLFDTT--- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 91 lagVGELLKkyhhismeLAH-DPSDANI-------RIMSDLQEQLDYQNGWqfetrisqvltllnLDPDATldSLSGGWL 162
Cdd:TIGR02868 425 ---VRENLR--------LARpDATDEELwaalervGLADWLRALPDGLDTV--------------LGEGGA--RLSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 163 RKVALARALACDPDLLLLDEPTNHLDIE-AINWLEDFLKDFRG-AIVFISHD 212
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLAALSGrTVVLITHH 529
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-227 |
1.47e-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: 73.60 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 25 SIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDlKVTRLEQDPPASSDLTVFDYTAEGLAGVGEllkkyhhi 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKADYEGTVRDLLSSITKDFYT-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 105 smelahDPsdanirimsdlqeqldyqngwQFETRISQVLTLLNLdPDATLDSLSGGWLRKVALARALACDPDLLLLDEPT 184
Cdd:cd03237 92 ------HP---------------------YFKTEIAKPLQIEQI-LDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1411607396 185 NHLDIE-------AINWLedFLKDFRGAIVfISHDREFIHKLATRIIDLD 227
Cdd:cd03237 144 AYLDVEqrlmaskVIRRF--AENNEKTAFV-VEHDIIMIDYLADRLIVFE 190
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
329-475 |
1.52e-14 |
|
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: 72.95 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKL------------EVAY-FDQYrdQL 394
Cdd:cd03262 10 FGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtIIIDGLKLtddkkninelrqKVGMvFQQF--NL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 DPEQTVMDNVGEGkqEVMVRGRSR-----HILGYLQDFLFEPKRARTPVKaLSGGEKNRLLLAK-LFLKPSnLLILDEPT 468
Cdd:cd03262 88 FPHLTVLENITLA--PIKVKGMSKaeaeeRALELLEKVGLADKADAYPAQ-LSGGQQQRVAIARaLAMNPK-VMLFDEPT 163
|
....*..
gi 1411607396 469 NDLDVET 475
Cdd:cd03262 164 SALDPEL 170
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-183 |
1.86e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.14 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTR--------- 70
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRiFLDGED--ITHlpmhkrarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 71 ----LEQDPPASSDLTVfdytAEGLAGVGELLKKyhhismelahdpsdanirimsDLQEQldyqngwqfETRISQVLTLL 146
Cdd:COG1137 79 gigyLPQEASIFRKLTV----EDNILAVLELRKL---------------------SKKER---------EERLEELLEEF 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 1411607396 147 NLDP--DATLDSLSGGWLRKVALARALACDPDLLLLDEP 183
Cdd:COG1137 125 GITHlrKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
338-495 |
2.05e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.42 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLePSRGLVK-GGTKLEVAYFDQYRDQLD--------PEQTVMDNVGEGK 408
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKiNGIELRELDPESWRKHLSwvgqnpqlPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 409 QEvMVRGRSRHIL--GYLQDFLFE-PKRARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV--ETLELL 479
Cdd:PRK11174 448 PD-ASDEQLQQALenAWVSEFLPLlPQGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAhsEQLVMQ 526
|
170
....*....|....*.
gi 1411607396 480 EELLADYPGTLLLVSH 495
Cdd:PRK11174 527 ALNAASRRQTTLMVTH 542
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-247 |
2.21e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 73.87 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFS----DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGEL-PLD-----DGRMVQQQDLKVTR-----LEQDP 75
Cdd:PRK13632 13 VSFSypnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQSgeikiDGITISKENLKEIRkkigiIFQNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 76 passD-----LTVFDYTAEGLAGvgellKKYhhismelahDPSDANiRIMSDLQEQLDYQNgwqfetrisqvltLLNLDP 150
Cdd:PRK13632 93 ----DnqfigATVEDDIAFGLEN-----KKV---------PPKKMK-DIIDDLAKKVGMED-------------YLDKEP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 datlDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHDREFIhKLATRIIDL 226
Cdd:PRK13632 141 ----QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrkkTLISITHDMDEA-ILADKVIVF 215
|
250 260
....*....|....*....|..
gi 1411607396 227 DRG-VITSwpGNYDEYLQGKEE 247
Cdd:PRK13632 216 SEGkLIAQ--GKPKEILNNKEI 235
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-231 |
2.29e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 73.12 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 6 LHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLmkiiagelplddgrmvqqqdLKVTRLeQDPPASSDLTV-- 83
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSL--------------------LRVLNL-LETPDSGQLNIag 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 --FDYTAEGLAGVGELLKK--------YH---HISmelahdpsdanirIMSDLQE---QLDYQNGWQFETRISQVLTLLN 147
Cdd:COG4161 64 hqFDFSQKPSEKAIRLLRQkvgmvfqqYNlwpHLT-------------VMENLIEapcKVLGLSKEQAREKAMKLLARLR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 148 LDP--DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG-AI--VFISHDREFIHKLATR 222
Cdd:COG4161 131 LTDkaDRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGItqVIVTHEVEFARKVASQ 210
|
....*....
gi 1411607396 223 IIDLDRGVI 231
Cdd:COG4161 211 VVYMEKGRI 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-231 |
2.69e-14 |
|
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: 73.45 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 21 NAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDDGRMVQQQDLKVTRLEQDPPAS--------SDLTVFD 85
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCInrlieptSGKVLIDGQDIAAMSRKELRELRRKKISMvfqsfallPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 86 YTAEGLagvgellkkyhhismELAHDPsdANIRimsdlqeqldyqngwqfETRISQVLTLLNLDPDAT--LDSLSGGWLR 163
Cdd:cd03294 122 NVAFGL---------------EVQGVP--RAER-----------------EERAAEALELVGLEGWEHkyPDELSGGMQQ 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03294 168 RVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
319-498 |
2.79e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 72.38 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGD----RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL----------- 382
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLiDGQDIsslserelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 383 ---EVAY-FDQYrdQLDPEQTVMDNV-------GEGKQEvmVRGRSRHILGYLQdfLfePKRARTPVKALSGGEKNRLLL 451
Cdd:COG1136 84 rrrHIGFvFQFF--NLLPELTALENValplllaGVSRKE--RRERARELLERVG--L--GDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 452 AK-LFLKPSnLLILDEPTNDLDVETLEL---LEELLADYPG-TLLLVSHDRR 498
Cdd:COG1136 156 ARaLVNRPK-LILADEPTGNLDSKTGEEvleLLRELNRELGtTIVMVTHDPE 206
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-224 |
2.81e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 73.36 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSF----SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtRLEQDPP 76
Cdd:COG4525 1 MSMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI---------TLDGVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 77 ASSD---------------LTVFDYTAEGL--AGVGELlkkyhhismelahdpsdanirimsdlqeqldyqngwQFETRI 139
Cdd:COG4525 72 TGPGadrgvvfqkdallpwLNVLDNVAFGLrlRGVPKA------------------------------------ERRARA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 140 SQVLTLLNLD--PDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDieAIN------WLEDFLKDFRGAIVFISH 211
Cdd:COG4525 116 EELLALVGLAdfARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD--ALTreqmqeLLLDVWQRTGKGVFLITH 193
|
250
....*....|...
gi 1411607396 212 DREFIHKLATRII 224
Cdd:COG4525 194 SVEEALFLATRLV 206
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-473 |
3.20e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.05 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSD----FPLLDNAELSIERGERLCLVGRNGAGKS----TLMKII--AGELPLDDGRMVQQQDLKVTRLE 72
Cdd:PRK10261 12 VLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 QDPPAS------SDLT-VFDYTAEGLA---GVGELLKKYHHISMELAHDPSDANIRIMSDLqeqldyqngwqfeTRISQV 142
Cdd:PRK10261 92 EQSAAQmrhvrgADMAmIFQEPMTSLNpvfTVGEQIAESIRLHQGASREEAMVEAKRMLDQ-------------VRIPEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 143 LTLLNLDPDatldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHK 218
Cdd:PRK10261 159 QTILSRYPH----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaQILQLIKVLQKEMSMGVIFITHDMGVVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 219 LATRIIDLDRGVITswpgnydeylqgkeEALRVEELQHAEfdrklaqEEVWVRQGIKArrtrnegrVRALEAMR------ 292
Cdd:PRK10261 235 IADRVLVMYQGEAV--------------ETGSVEQIFHAP-------QHPYTRALLAA--------VPQLGAMKgldypr 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 293 ------MERSQRRELQ--------GKAKLQMDDV-----------NRSGKLVFETEGLGLDfgdrtlfqgldlqVLRGDK 347
Cdd:PRK10261 286 rfplisLEHPAKQEPPieqdtvvdGEPILQVRNLvtrfplrsgllNRVTREVHAVEKVSFD-------------LWPGET 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 348 IALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEV---------------AYFDQYRdQLDPEQTVMDNVGEG-KQE 410
Cdd:PRK10261 353 LSLVGESGSGKSTTGRALLRLVESQGGeIIFNGQRIDTlspgklqalrrdiqfIFQDPYA-SLDPRQTVGDSIMEPlRVH 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 411 VMVRGRS--RHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAK-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK10261 432 GLLPGKAaaARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARaLALNP-KVIIADEAVSALDV 496
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
338-475 |
3.52e-14 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 72.26 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGgtkLEVAYF--DQYRDQL-----DP---EQTVMDNVG 405
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGriLIDG---HDVRDYtlASLRRQIglvsqDVflfNDTVAENIA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 406 EGKQEVM---VRGRSRhiLGYLQDFLFE-PKRARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03251 98 YGRPGATreeVEEAAR--AANAHEFIMElPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
323-474 |
4.09e-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: 71.84 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGdKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggtklevayfdqYRDQLDpeqtvmd 402
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI-------------RIDGQD------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 403 nVGEGKQEVmvrgrsRHILGYL-QDFLFEPK------------------------------------RARTPVKALSGGE 445
Cdd:cd03264 63 -VLKQPQKL------RRRIGYLpQEFGVYPNftvrefldyiawlkgipskevkarvdevlelvnlgdRAKKKIGSLSGGM 135
|
170 180
....*....|....*....|....*....
gi 1411607396 446 KNRLLLAKLFLKPSNLLILDEPTNDLDVE 474
Cdd:cd03264 136 RRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-231 |
5.47e-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: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDDgrmVQQQDLKVTRLE-QDPPASSDLTVFDY 86
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIprfyepdSGQILLDG---HDLADYTLASLRrQVALVSQDVVLFND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 87 TAEGLAGVGELlkkyhhismelaHDPSDANIR---IMSDLQEQLD-YQNGWQFETRISQVLtllnldpdatldsLSGGWL 162
Cdd:TIGR02203 421 TIANNIAYGRT------------EQADRAEIEralAAAYAQDFVDkLPLGLDTPIGENGVL-------------LSGGQR 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 163 RKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVfISHDREFIHKlATRIIDLDRGVI 231
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLmqgRTTLV-IAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
331-475 |
6.48e-14 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 71.80 E-value: 6.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DP---EQTVM 401
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILlDGVDIRDLNLRWLRSQIglvsqEPvlfDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEGK---QEVMVRGRSRhiLGYLQDFLFE-PKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03249 95 ENIRYGKpdaTDEEVEEAAK--KANIHDFIMSlPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
..
gi 1411607396 474 ET 475
Cdd:cd03249 173 ES 174
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-284 |
7.09e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.80 E-value: 7.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 24 LSIERGERLCLVGRNGAGKSTLMKIIAGELP-----LDDGRMVQQ---QDLKVTR--LEQDPPASSDLTVFDYtaeglag 93
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGLLPgqgeiLLNGRPLSDwsaAELARHRayLSQQQSPPFAMPVFQY------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 94 vgellkkyhhISMELAHDPSDANIrimsdlqeqldyqngwqfETRISQVLTLLNLDP--DATLDSLSGG-WLRkVALARA 170
Cdd:COG4138 90 ----------LALHQPAGASSEAV------------------EQLLAQLAEALGLEDklSRPLTQLSGGeWQR-VRLAAV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 171 L-----ACDPD--LLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDreFIHKL--ATRIIDLDRGVITSwpgny 238
Cdd:COG4138 141 LlqvwpTINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCqqgITVVMSSHD--LNHTLrhADRVWLLKQGKLVA----- 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1411607396 239 deylQGK-EEALRVEELQHAeFdrklaqeevwvrqGIKARRTRNEGR 284
Cdd:COG4138 214 ----SGEtAEVMTPENLSEV-F-------------GVKFRRLEVEGH 242
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-231 |
7.54e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.65 E-value: 7.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmvqqqdlkVTR-------LEQ----DPpassDLTV 83
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR--------VEVngrvsalLELgagfHP----ELTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 FDytaeglagvgellkkyhhismelahdpsdaNIRImsdlqeqldyqNGwqfetrisqvlTLLNL---DPDATLD----- 155
Cdd:COG1134 106 RE------------------------------NIYL-----------NG-----------RLLGLsrkEIDEKFDeivef 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 ------------SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIE----AINWLEDFLKDFRgAIVFISHDREFIHKL 219
Cdd:COG1134 134 aelgdfidqpvkTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRESGR-TVIFVSHSMGAVRRL 212
|
250
....*....|..
gi 1411607396 220 ATRIIDLDRGVI 231
Cdd:COG1134 213 CDRAIWLEKGRL 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
316-475 |
8.57e-14 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 71.10 E-value: 8.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 316 GKLVFETEGLGLDFGDRTLfQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL 394
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVL-KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILiDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 -----DP---EQTVMDNVGEGKQ-----EVMVRGRSRHILgylqDFL-FEPKRARTPV----KALSGGEKNRLLLAKLFL 456
Cdd:cd03254 80 gvvlqDTflfSGTIMENIRLGRPnatdeEVIEAAKEAGAH----DFImKLPNGYDTVLgengGNLSQGERQLLAIARAML 155
|
170
....*....|....*....
gi 1411607396 457 KPSNLLILDEPTNDLDVET 475
Cdd:cd03254 156 RDPKILILDEATSNIDTET 174
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-228 |
8.59e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 70.59 E-value: 8.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP----------LDDGRM--VQQQDLKVTRL 71
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafsasgevlLNGRRLtaLPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 72 EQDPPASSDLTVfdytAEGLAgvgellkkyhhisMELAHDPSDANIRimsdlqeqldyqngwqfeTRISQVLTLLNLDP- 150
Cdd:COG4136 82 FQDDLLFPHLSV----GENLA-------------FALPPTIGRAQRR------------------ARVEQALEEAGLAGf 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 -DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDF----LKDFRGAIVFISHDREFIhKLATRIID 225
Cdd:COG4136 127 aDRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEEDA-PAAGRVLD 205
|
...
gi 1411607396 226 LDR 228
Cdd:COG4136 206 LGN 208
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-231 |
1.00e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 71.18 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV--------QQQDLKVTRLE-- 72
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITvdgedltdSKKDINKLRRKvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 ---QD----PpassDLTVFDYTAEGLAGVgelLKKyhhismelahDPSDANIRIMS-----DLQEQLD-Yqngwqfetri 139
Cdd:COG1126 81 mvfQQfnlfP----HLTVLENVTLAPIKV---KKM----------SKAEAEERAMEllervGLADKADaY---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 140 sqvltllnldPDatldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFI 216
Cdd:COG1126 134 ----------PA----QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgmtMVVVTHEMGFA 199
|
250
....*....|....*
gi 1411607396 217 HKLATRIIDLDRGVI 231
Cdd:COG1126 200 REVADRVVFMDGGRI 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-229 |
1.05e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.97 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKST----LMKIIA--GELPLDDGRMVQ---QQDLKVTR----LEQDPPASSD--LTV 83
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIWFDGQPLHNlnrRQLLPVRHriqvVFQDPNSSLNprLNV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 FDYTAEGLagvgellkKYHHISMELAhdpsdanirimsdlqeqldyqngwQFETRISQVLTLLNLDPDATL---DSLSGG 160
Cdd:PRK15134 382 LQIIEEGL--------RVHQPTLSAA------------------------QREQQVIAVMEEVGLDPETRHrypAEFSGG 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDktVQAqiLALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-232 |
1.19e-13 |
|
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: 69.65 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFS----DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELplddgrmVQQQdlkvtrleqdppassdltvfdy 86
Cdd:cd03247 6 VSFSypeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDL-------KPQQ---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 87 taeglagvGELLKKYHHISmelahdpsdanirimsDLQEQLdyqngwqfetriSQVLTLLNLDP---DATLDS-----LS 158
Cdd:cd03247 57 --------GEITLDGVPVS----------------DLEKAL------------SSLISVLNQRPylfDTTLRNnlgrrFS 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDfrGAIVFISHDREFIHKlATRIIDLDRGVIT 232
Cdd:cd03247 101 GGERQRLALARILLQDAPIVLLDEPTVGLDpiteRQLLSLIFEVLKD--KTLIWITHHLTGIEH-MDKILFLENGKII 175
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
344-520 |
1.23e-13 |
|
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: 70.90 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 344 RGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvKGGTKLE-VAYFDQYRdQLDPEQTVMDNVGEGKQEVMVRGRSR-HIL 421
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEG--DIEIELDtVSYKPQYI-KADYEGTVRDLLSSITKDFYTHPYFKtEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 422 GYLQ-DFLFEPKrartpVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLelleelladypgtLLLVSHDRRFI 500
Cdd:cd03237 101 KPLQiEQILDRE-----VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR-------------LMASKVIRRFA 162
|
170 180
....*....|....*....|
gi 1411607396 501 DNTVTGCWLFEGDGRISDYV 520
Cdd:cd03237 163 ENNEKTAFVVEHDIIMIDYL 182
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
11-229 |
1.49e-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: 72.44 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFSDFPLldNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV----------QQQDLKVTR-----LEQDP 75
Cdd:COG4148 9 LRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsaRGIFLPPHRrrigyVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 76 PASSDLTVfdytaeglagvgellkkyhhismelahdpsdanirimsdlQEQLDY--QNGWQFETRIS--QVLTLLNLDP- 150
Cdd:COG4148 87 RLFPHLSV----------------------------------------RGNLLYgrKRAPRAERRISfdEVVELLGIGHl 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 -DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIID 225
Cdd:COG4148 127 lDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkaEILPYLERLRDELDIPILYVSHSLDEVARLADHVVL 206
|
....
gi 1411607396 226 LDRG 229
Cdd:COG4148 207 LEQG 210
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-231 |
1.54e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.40 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD--------------DGRMVQQQD-LKVTRLEQDPPASSDlT 82
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvtgdvtlNGEPLAAIDaPRLARLRAVLPQAAQ-P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 83 VFDYTAEGLAgvgeLLKKYHHISMELAHDPSDANIrimsdlqeqldyqngwqfetrISQVLTLLNLDPDATLD--SLSGG 160
Cdd:PRK13547 95 AFAFSAREIV----LLGRYPHARRAGALTHRDGEI---------------------AWQALALAGATALVGRDvtTLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 161 WLRKVALARALA---------CDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLD 227
Cdd:PRK13547 150 ELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLahqhRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLA 229
|
....
gi 1411607396 228 RGVI 231
Cdd:PRK13547 230 DGAI 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-211 |
2.56e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.65 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP--------LDDGRMVQQQDLKVTR-- 70
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtyegeiIFEGEELQASNIRDTEra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 71 ----LEQDPPASSDLTVfdytAEglagvgellkkyhhiSMELAHDPSDANIrimsdlqeqLDYQNGWQfetRISQVLTLL 146
Cdd:PRK13549 83 giaiIHQELALVKELSV----LE---------------NIFLGNEITPGGI---------MDYDAMYL---RAQKLLAQL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 147 NLD--PDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISH 211
Cdd:PRK13549 132 KLDinPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAhgiACIYISH 201
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-247 |
2.70e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 70.33 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKI------------IAGELPLDdGRMVQQQDL-- 66
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLD-GQDIFKMDVie 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 67 ---KVTRLEQDPPASSDLTVFDYTAEGLagvgellkKYHHIsmelahdpsdanIRIMSDLQEQLDyqngWQFETriSQVL 143
Cdd:PRK14247 80 lrrRVQMVFQIPNPIPNLSIFENVALGL--------KLNRL------------VKSKKELQERVR----WALEK--AQLW 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 144 TLLNLDPDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISHdrefIHKLAT 221
Cdd:PRK14247 134 DEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH----FPQQAA 209
|
250 260 270
....*....|....*....|....*....|
gi 1411607396 222 RIID----LDRGVITSWPGNYDEYLQGKEE 247
Cdd:PRK14247 210 RISDyvafLYKGQIVEWGPTREVFTNPRHE 239
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-242 |
3.02e-13 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 69.57 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLD--DGRMVQQQDL--KVTRLEQDPPASSDlTVFD 85
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRILIDghDVRDYTLASLrrQIGLVSQDVFLFND-TVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 86 YTAEGLAGVG-----ELLKKYHhismelAHDpsdaniRIMSdLQEQLDyqngwqfeTRISQVLTllnldpdatldSLSGG 160
Cdd:cd03251 95 NIAYGRPGATreeveEAARAAN------AHE------FIME-LPEGYD--------TVIGERGV-----------KLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIE---AI-NWLEDFLKDfRGAIVfISHDREFIhKLATRIIDLDRGVITSwPG 236
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTEserLVqAALERLMKN-RTTFV-IAHRLSTI-ENADRIVVLEDGKIVE-RG 218
|
....*.
gi 1411607396 237 NYDEYL 242
Cdd:cd03251 219 THEELL 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
335-531 |
3.23e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.73 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 335 FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKG--GTKLEV-AYFdqyrdqlDPEQTVMDNV----- 404
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGrvEVNGrvSALLELgAGF-------HPELTGRENIylngr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 405 --GEGKQEvmVRGRSRHILGY--LQDFLfepkraRTPVKALSGGEKNRLLLA-KLFLKPsNLLILDEPT----------- 468
Cdd:COG1134 115 llGLSRKE--IDEKFDEIVEFaeLGDFI------DQPVKTYSSGMRARLAFAvATAVDP-DILLVDEVLavgdaafqkkc 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 469 ----NDLdvetlelleellADYPGTLLLVSHDRRFIDNTVT-GCWLFEG----DGRISDYVGGYADMMATRA 531
Cdd:COG1134 186 lariREL------------RESGRTVIFVSHSMGAVRRLCDrAIWLEKGrlvmDGDPEEVIAAYEALLAGRE 245
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
325-496 |
3.28e-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: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 325 LGLDFGDRTLFQGLDLQ-VLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL--------------EVAY-F 387
Cdd:cd03297 2 LCVDIEKRLPDFTLKIDfDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlNGTVLfdsrkkinlppqqrKIGLvF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 388 DQYrdQLDPEQTVMDNV--GEGKQEVMV-RGRSRHILGYLQ-DFLfepkrARTPVKALSGGEKNRLLLAKLFLKPSNLLI 463
Cdd:cd03297 82 QQY--ALFPHLNVRENLafGLKRKRNREdRISVDELLDLLGlDHL-----LNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1411607396 464 LDEPTNDLDVETLELLEEL----LADYPGTLLLVSHD 496
Cdd:cd03297 155 LDEPFSALDRALRLQLLPElkqiKKNLNIPVIFVTHD 191
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-266 |
3.70e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.11 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLE------------QDPPA--SSDLT 82
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSiLIDGKD--VTKLPeykrakyigrvfQDPMMgtAPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 83 VfdytAEGLAgvgelLKKYHHISMELAHDPSDANIRIMSDLQEQLDyqNGwqFETRIsqvltllnldpDATLDSLSGGWL 162
Cdd:COG1101 99 I----EENLA-----LAYRRGKRRGLRRGLTKKRRELFRELLATLG--LG--LENRL-----------DTKVGLLSGGQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 163 RKVALARALACDPDLLLLDEPTNHLD---IEAINWL-EDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITswpgnY 238
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDpktAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII-----L 229
|
250 260
....*....|....*....|....*....
gi 1411607396 239 DeyLQGKE-EALRVEELQhAEFDRKLAQE 266
Cdd:COG1101 230 D--VSGEEkKKLTVEDLL-ELFEEIRGEE 255
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-230 |
4.07e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.02 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 6 LHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrmvqqqdlKVTRLEQDPPASSDLtvfd 85
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG--------KITVLGVPVPARARL---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 86 ytaeGLAGVGeLLKKYHHISMELAhdpsdanirimsdLQEQL----DY--QNGWQFETRISQVLTLLNLD--PDATLDSL 157
Cdd:PRK13536 112 ----ARARIG-VVPQFDNLDLEFT-------------VRENLlvfgRYfgMSTREIEAVIPSLLEFARLEskADARVSDL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RG-AIVFISHDREFIHKLATRIIDLDRGV 230
Cdd:PRK13536 174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLlaRGkTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
336-500 |
4.40e-13 |
|
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: 69.28 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtKLEVAYFDQY----------------RDQLDPEQT 399
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG------EVRVAGLVPWkrrkkflrrigvvfgqKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 400 VMDNVgegkqEVMVR------GRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03267 112 VIDSF-----YLLAAiydlppARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190
....*....|....*....|....*....|.
gi 1411607396 474 ETLEL----LEELLADYPGTLLLVSHDRRFI 500
Cdd:cd03267 187 VAQENirnfLKEYNRERGTTVLLTSHYMKDI 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-229 |
4.45e-13 |
|
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: 67.84 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmvqqqdlkVTRLEQDPPASSdltVFDYTAEGLAGVGEll 98
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGE--------ITLDGKPVTRRS---PRDAIRAGIAYVPE-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 99 kkyhhismelahDPSDANI-RIMSdlqeqldyqngwqfetrISQVLTLLNLdpdatldsLSGGWLRKVALARALACDPDL 177
Cdd:cd03215 83 ------------DRKREGLvLDLS-----------------VAENIALSSL--------LSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 178 LLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
321-496 |
4.92e-13 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 68.90 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLfQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKL-----EVAYFdqYR 391
Cdd:cd03299 2 KVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngKDITNLppekrDISYV--PQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 392 DQ-LDPEQTVMDNVGEG--KQEVMVRGRSRHILGYLQDFLFEPKRARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEP 467
Cdd:cd03299 79 NYaLFPHMTVYKNIAYGlkKRKVDKKEIERKVLEIAEMLGIDHLLNRKP-ETLSGGEQQRVAIARaLVVNPK-ILLLDEP 156
|
170 180 190
....*....|....*....|....*....|...
gi 1411607396 468 TNDLDVETLELLEELLAD----YPGTLLLVSHD 496
Cdd:cd03299 157 FSALDVRTKEKLREELKKirkeFGVTVLHVTHD 189
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
330-472 |
4.98e-13 |
|
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: 67.83 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV-KGGTKLE------------VAYFDQyrdqlDP 396
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVlIDGEPLDysrkgllerrqrVGLVFQ-----DP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 397 EQTVMD-NVGE---------GKQEVMVRGRSRHILGYLQDFLFEPKrartPVKALSGGEKNRLLLAKLFLKPSNLLILDE 466
Cdd:TIGR01166 78 DDQLFAaDVDQdvafgplnlGLSEAEVERRVREALTAVGASGLRER----PTHCLSGGEKKRVAIAGAVAMRPDVLLLDE 153
|
....*.
gi 1411607396 467 PTNDLD 472
Cdd:TIGR01166 154 PTAGLD 159
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-233 |
5.35e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.04 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQqDLKVtrleqdpPASSDLT--VFDYTAEglA 92
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG-DYAI-------PANLKKIkeVKRLRKE--I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 93 GVGELLKKYHHISMELAHDPSDANIRIMSDLQEQldYQngwqfetRISQVLTLLNLDPDATLDS---LSGGWLRKVALAR 169
Cdd:PRK13645 93 GLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEA--YK-------KVPELLKLVQLPEDYVKRSpfeLSGGQKRRVALAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 170 ALACDPDLLLLDEPTNHLDIEA----INWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-255 |
5.63e-13 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 69.05 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTRLE----QDPPASSDLTVFDYT-AEGL 91
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRvLVDGHDLALADPAwlrrQVGVVLQENVLFNRSiRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 92 AGVGELLKKYHHI---SMELAHDpsdaNIRIMSDLQEQLDYQNGwqfetrisqvltllnldpdatlDSLSGGWLRKVALA 168
Cdd:cd03252 97 ALADPGMSMERVIeaaKLAGAHD----FISELPEGYDTIVGEQG----------------------AGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 169 RALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVfISHDREFIhKLATRIIDLDRGVITSwPGNYDEYLQGK 245
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDIcagRTVII-IAHRLSTV-KNADRIIVMEKGRIVE-QGSHDELLAEN 227
|
250
....*....|
gi 1411607396 246 EEALRVEELQ 255
Cdd:cd03252 228 GLYAYLYQLQ 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-188 |
6.56e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.77 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDlkvtrleqdppassD 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE--------------D 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 81 LTVFDYTAEGLAGVGELLKKYHHISMELAHDPSDANIRIMSDLQEQldyqngwQFETRISQVLTLLNLD--PDATLDSLS 158
Cdd:PRK10895 67 ISLLPLHARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAE-------QREDRANELMEEFHIEhlRDSMGQSLS 139
|
170 180 190
....*....|....*....|....*....|
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK10895 140 GGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-251 |
7.69e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.46 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 24 LSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTrleqdPPAS-------------SDLTVFDYTAE 89
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtLNGQDHTTT-----PPSRrpvsmlfqennlfSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 90 GLagvgellkkyhhismelahdpsDANIRIMSDLQEQLdyqngwqfETRISQV--LTLLNLDPDAtldsLSGGWLRKVAL 167
Cdd:PRK10771 95 GL----------------------NPGLKLNAAQREKL--------HAIARQMgiEDLLARLPGQ----LSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 168 ARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVItSWPGNYDEYLQ 243
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI-AWDGPTDELLS 219
|
....*...
gi 1411607396 244 GKEEALRV 251
Cdd:PRK10771 220 GKASASAL 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
321-474 |
8.02e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.52 E-value: 8.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEvAYFDQYRDQL----- 394
Cdd:PRK13538 3 EARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwQGEPIR-RQRDEYHQDLlylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 ----DPEQTVMDNV-------GEGKQEVMVRGRSRHILGylqdflfepKRARTPVKALSGGEKNRLLLAKLFLKPSNLLI 463
Cdd:PRK13538 82 qpgiKTELTALENLrfyqrlhGPGDDEALWEALAQVGLA---------GFEDVPVRQLSAGQQRRVALARLWLTRAPLWI 152
|
170
....*....|.
gi 1411607396 464 LDEPTNDLDVE 474
Cdd:PRK13538 153 LDEPFTAIDKQ 163
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-233 |
9.40e-13 |
|
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: 68.23 E-value: 9.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 2 ALLTLHGACLSFSD----FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPlDDGR-MVQQQDLkvTRLEQDP 75
Cdd:COG4181 7 PIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGlDRP-TSGTvRLAGQDL--FALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 76 PAssdltvfdytaeGL--AGVGELLKKYHHI-SM----------ELAHDPsDAnirimsdlqeqldyqngwqfETRISQV 142
Cdd:COG4181 84 RA------------RLraRHVGFVFQSFQLLpTLtalenvmlplELAGRR-DA--------------------RARARAL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 143 LTLLNLDP--DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEA----INWLEDFLKDFRGAIVFISHDREfi 216
Cdd:COG4181 131 LERVGLGHrlDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLVTHDPA-- 208
|
250 260
....*....|....*....|
gi 1411607396 217 hkLAT---RIIDLDRGVITS 233
Cdd:COG4181 209 --LAArcdRVLRLRAGRLVE 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-232 |
1.09e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 70.96 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFS---DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKvtrleqdppassdltvfDY 86
Cdd:COG1132 345 VSFSypgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRiLIDGVDIR-----------------DL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 87 TAEGLagvgellkkYHHISMELaHDPS--DANIRimsdlqEQLDYQNGWQFETRISQVLTLLNLD------PDAtLD--- 155
Cdd:COG1132 408 TLESL---------RRQIGVVP-QDTFlfSGTIR------ENIRYGRPDATDEEVEEAAKAAQAHefiealPDG-YDtvv 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 -----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIE---AINW-LEDFLKDfRGAIVfIShdrefiHKLAT----- 221
Cdd:COG1132 471 gergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTEteaLIQEaLERLMKG-RTTIV-IA------HRLSTirnad 542
|
250
....*....|.
gi 1411607396 222 RIIDLDRGVIT 232
Cdd:COG1132 543 RILVLDDGRIV 553
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-231 |
1.22e-12 |
|
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: 67.52 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 24 LSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDDGRMVQQQDLK--------VTRLEQDPPASSDLTVFDYTAEGLAgv 94
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINGVDVTaappadrpVSMLFQENNLFAHLTVEQNVGLGLS-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 95 gellkkyhhismelahdpsdANIRIMSDLQEQLDY---QNGWQ-FETRISqvltllnldpdatlDSLSGGWLRKVALARA 170
Cdd:cd03298 97 --------------------PGLKLTAEDRQAIEValaRVGLAgLEKRLP--------------GELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 171 LACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAetkmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-231 |
1.36e-12 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 67.68 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDD---GR-MVQQQDLKVtrlEQDPPASSDLTVFDYTAEGLAg 93
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQiLFNGQPRKP---DQFQKCVAYVRQDDILLPGLT- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 94 VGELLKKYHHISMelaHDPSDANIRIMSDLQEqldyqngwqfetrisqVLTLLNLDP--DATLDSLSGGWLRKVALARAL 171
Cdd:cd03234 98 VRETLTYTAILRL---PRKSSDAIRKKRVEDV----------------LLRDLALTRigGNLVKGISGGERRRVSIAVQL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 172 ACDPDLLLLDEPTNHLDIEAINWLEDFLKDF----RGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVSTLSQLarrnRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
328-473 |
1.46e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.94 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 328 DFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqLEPSRGLVK-GGTKL------EVAYFDQYRDQLDPEQTV 400
Cdd:COG4138 5 DVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILlNGRPLsdwsaaELARHRAYLSQQQSPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDnVGE--------GKQEVMVRGRSRHILGYLQdflFEPKRARtPVKALSGGEKNRLLLAKLFLK-------PSNLLILD 465
Cdd:COG4138 84 MP-VFQylalhqpaGASSEAVEQLLAQLAEALG---LEDKLSR-PLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLD 158
|
....*...
gi 1411607396 466 EPTNDLDV 473
Cdd:COG4138 159 EPMNSLDV 166
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
321-473 |
1.64e-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: 66.75 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggtKLEVAYFDQYRDQLDPEQTV 400
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV----LLNGGPLDFQRDSIARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEGKQEVMVRGRSRHILGYLQDFLFEPKRART--------PVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03231 78 LGHAPGIKTTLSVLENLRFWHADHSDEQVEEALARVglngfedrPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
.
gi 1411607396 473 V 473
Cdd:cd03231 158 K 158
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
338-472 |
1.96e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.09 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEVA---------YFDQYrdQLDPEQTVMDNVGEG 407
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGqIMLDGVDLSHVppyqrpinmMFQSY--ALFPHMTVEQNIAFG 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 408 -KQEVMVRG----RSRHILG--YLQDFlfepkRARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11607 116 lKQDKLPKAeiasRVNEMLGlvHMQEF-----AKRKP-HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-224 |
1.97e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 68.61 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSD----FPLLDNAELSIERGERLCLVGRNGAGKS----TLM-------KIIAGELPLDdgrmvqQQD 65
Cdd:PRK11022 1 MALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMglidypgRVMAEKLEFN------GQD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 66 LK--------------VTRLEQDPPASSDLTvfdYTaeglagVGellkkyhhismelahdpsdanIRIMsdlqEQLDYQN 131
Cdd:PRK11022 75 LQrisekerrnlvgaeVAMIFQDPMTSLNPC---YT------VG---------------------FQIM----EAIKVHQ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 132 GWQFETRISQVLTLLNL----DPDATLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFL 199
Cdd:PRK11022 121 GGNKKTRRQRAIDLLNQvgipDPASRLDvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtIQAqiIELLLELQ 200
|
250 260
....*....|....*....|....*
gi 1411607396 200 KDFRGAIVFISHDREFIHKLATRII 224
Cdd:PRK11022 201 QKENMALVLITHDLALVAEAAHKII 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
329-472 |
2.10e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.98 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVayfdQYRD--------QLDP 396
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqiFIDGEdvTHRSI----QQRDicmvfqsyALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 397 EQTVMDNVGEG-------KQEvmVRGRSRHILGYLQDFLFEPKRartpVKALSGGEKNRLLLAK-LFLKPSNLLiLDEPT 468
Cdd:PRK11432 92 HMSLGENVGYGlkmlgvpKEE--RKQRVKEALELVDLAGFEDRY----VDQISGGQQQRVALARaLILKPKVLL-FDEPL 164
|
....
gi 1411607396 469 NDLD 472
Cdd:PRK11432 165 SNLD 168
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
309-474 |
2.12e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.80 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 309 MDDVNRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKLEV 384
Cdd:PRK13543 1 MIEPLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgKTATRGDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 385 AYFDQYRDQL---DPEQTVMDNVG-----EGKQEVMVRGRSRHILGyLQDFlfepkrARTPVKALSGGEKNRLLLAKLFL 456
Cdd:PRK13543 81 SRFMAYLGHLpglKADLSTLENLHflcglHGRRAKQMPGSALAIVG-LAGY------EDTLVRQLSAGQKKRLALARLWL 153
|
170
....*....|....*...
gi 1411607396 457 KPSNLLILDEPTNDLDVE 474
Cdd:PRK13543 154 SPAPLWLLDEPYANLDLE 171
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
336-468 |
2.13e-12 |
|
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: 66.69 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGT-----------KLEVAYFDQYRdQLDPEQTVMDN 403
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfDGRditglppheraRAGIGYVPEGR-RIFPELTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 404 --VGEGKQEvmvRGRSRHILgylqDFLFE--PK---RARTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPT 468
Cdd:cd03224 96 llLGAYARR---RAKRKARL----ERVYElfPRlkeRRKQLAGTLSGGEQQMLAIARaLMSRPK-LLLLDEPS 160
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-224 |
2.19e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.58 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 20 DNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV---------QQQDLKVTRLE-----QDPPASSD--LTV 83
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgmKDDEWRAVRSDiqmifQDPLASLNprMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 FDYTAEGLagvgellKKYHHismELAHDPSDANIRIMSdlqeqldyqngwqfeTRISQVLTLLNLDPDatldSLSGGWLR 163
Cdd:PRK15079 118 GEIIAEPL-------RTYHP---KLSRQEVKDRVKAMM---------------LKVGLLPNLINRYPH----EFSGGQCQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:PRK15079 169 RIGIARALILEPKLIICDEPVSALDvsIQAqvVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-473 |
2.19e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.85 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDgrmvqqQDLKVTRLEQDPPASSdlt 82
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGT------WDGEIYWSGSPLKASN--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 83 VFDYTAEGLAGVgellkkyhHISMELAHDPSDA-NIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLD--PDA-TLDSLS 158
Cdd:TIGR02633 72 IRDTERAGIVII--------HQELTLVPELSVAeNIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDadNVTrPVGDYG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGvitswp 235
Cdd:TIGR02633 144 GGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDG------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 236 gnydeylqgkeealrveelQHAefdrklaqeevwvrqGIKARRTRNEGRVRALEAMRMERSqrrelqgkakLQMDDVNRS 315
Cdd:TIGR02633 218 -------------------QHV---------------ATKDMSTMSEDDIITMMVGREITS----------LYPHEPHEI 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 316 GKLVFETEGLGLDFGDRTLFQGLD---LQVLRGDKIALVGPNGCGKSTLIKLLLGQLE------------------PSRG 374
Cdd:TIGR02633 254 GDVILEARNLTCWDVINPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALFGAYPgkfegnvfingkpvdirnPAQA 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 375 LVKGgtkLEVAYFDQYRDQLDPEQTVMDNV---------------GEGKQEVMVRGRSRHILGYLQDFLfepkrartPVK 439
Cdd:TIGR02633 334 IRAG---IAMVPEDRKRHGIVPILGVGKNItlsvlksfcfkmridAAAELQIIGSAIQRLKVKTASPFL--------PIG 402
|
490 500 510
....*....|....*....|....*....|....
gi 1411607396 440 ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
336-472 |
2.30e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 67.73 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DPEQ-----TVMDNV 404
Cdd:PRK13635 24 KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvGGMVLSEETVWDVRRQVgmvfqNPDNqfvgaTVQDDV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 405 GEG------KQEVMVRgRSRHILG--YLQDFL-FEPKRartpvkaLSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13635 104 AFGlenigvPREEMVE-RVDQALRqvGMEDFLnREPHR-------LSGGQKQRVAIAGvLALQPD-IIILDEATSMLD 172
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-192 |
2.54e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.44 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmvqqqdlkVTRLEQDPPASSDLTVFDYtaeglagvge 96
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGT--------IKLDGGDIDDPDVAEACHY---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 97 llkkyhhismeLAHdpSDANIRIMSdLQEQLDYqngW-----QFETRISQVLTLLNLDPDATL--DSLSGGWLRKVALAR 169
Cdd:PRK13539 78 -----------LGH--RNAMKPALT-VAENLEF---WaaflgGEELDIAAALEAVGLAPLAHLpfGYLSAGQKRRVALAR 140
|
170 180
....*....|....*....|...
gi 1411607396 170 ALACDPDLLLLDEPTNHLDIEAI 192
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAAV 163
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
329-496 |
2.64e-12 |
|
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: 66.51 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGG---TKLEVA------YFDQYrdQLDPEQ 398
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGrIYIGGrdvTDLPPKdrdiamVFQNY--ALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 TVMDNV-------GEGKQEVMVRGRSR----HILGYLQdflfepkraRTPvKALSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:cd03301 88 TVYDNIafglklrKVPKDEIDERVREVaellQIEHLLD---------RKP-KQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190
....*....|....*....|....*....|...
gi 1411607396 468 TNDLD----VETLELLEELLADYPGTLLLVSHD 496
Cdd:cd03301 158 LSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
321-472 |
3.02e-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: 66.69 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDF-----GDRTL--FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVK-GGTKLEVAyfdqy 390
Cdd:COG4778 6 EVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsiLVRhDGGWVDLA----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 rdQLDPEQtvmdnvgegkqevMVRGRsRHILGYLQDFL--------------------FEPKRARTPVKAL--------- 441
Cdd:COG4778 81 --QASPRE-------------ILALR-RRTIGYVSQFLrviprvsaldvvaepllergVDREEARARARELlarlnlper 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1411607396 442 ---------SGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:COG4778 145 lwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-257 |
3.40e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 25 SIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRL-----------EQDPPASSdLTVFDYTAeglag 93
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAaelarhraylsQQQTPPFA-MPVFQYLT----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 94 vgellkkyhhismelAHDPSDANIRimsdlqeqldyqngwQFETRISQVLTLLNLDPDAT--LDSLSGG-WLRkVALARA 170
Cdd:PRK03695 92 ---------------LHQPDKTRTE---------------AVASALNEVAEALGLDDKLGrsVNQLSGGeWQR-VRLAAV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 171 -LACDPD------LLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVFISHDREFIHKLATRIIDLDRGVITSwpgnyde 240
Cdd:PRK03695 141 vLQVWPDinpagqLLLLDEPMNSLDVAQQAALDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA------- 213
|
250
....*....|....*...
gi 1411607396 241 ylQGK-EEALRVEELQHA 257
Cdd:PRK03695 214 --SGRrDEVLTPENLAQV 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
322-472 |
3.55e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.34 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 322 TEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAY--FDQYRDQL---- 394
Cdd:PRK13638 4 TSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwQGKPLDYSKrgLLALRQQVatvf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 -DPEQTV------------MDNVGEGKQEVMVRGRSRHILGYLQDFlfepkrARTPVKALSGGEKNRLLLAKLFLKPSNL 461
Cdd:PRK13638 84 qDPEQQIfytdidsdiafsLRNLGVPEAEITRRVDEALTLVDAQHF------RHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170
....*....|.
gi 1411607396 462 LILDEPTNDLD 472
Cdd:PRK13638 158 LLLDEPTAGLD 168
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
224-300 |
4.59e-12 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 62.21 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 224 IDLDRGVITSWPGNYDEYLQGKEEALRVEELQHAEFDRKLAQEEVWV-RQGIKARRTR-NEGRVRALEAM-RMERSQRRE 300
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIdRFRAKASKAKqAQSRIKALEKMeRIEKPERDK 80
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
338-473 |
4.90e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.49 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKL------EVAYFDQYRDQLDPEQTVMD-------NV 404
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLeawsaaELARHRAYLSQQQTPPFAMPvfqyltlHQ 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 405 GEGKQEvmvrGRSRHILGYLQDFL-FEPKRARtPVKALSGGEKNRLLLAKLFLK------P-SNLLILDEPTNDLDV 473
Cdd:PRK03695 95 PDKTRT----EAVASALNEVAEALgLDDKLGR-SVNQLSGGEWQRVRLAAVVLQvwpdinPaGQLLLLDEPMNSLDV 166
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-473 |
4.98e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.66 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrMVQQQDLKVTRLeqDPPASSDLtvfdytaegl 91
Cdd:PRK09700 14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKG-TITINNINYNKL--DHKLAAQL---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 92 aGVGELlkkYHHISM--ELAhdpSDANIRIMSDLQEQLDYQN--GWQFETRISQVLTL---LNLDPDATLDSLSGGWLRK 164
Cdd:PRK09700 81 -GIGII---YQELSVidELT---VLENLYIGRHLTKKVCGVNiiDWREMRVRAAMMLLrvgLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 165 VALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGvitswpgnydey 241
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDRYTVMKDG------------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 242 lqgkeealrveelqhaefdrklaqeeVWVRQGIKARRTrNEGRVRALEAmrmersqrRELQGKAKLQMDDV-NRSGKLVF 320
Cdd:PRK09700 222 --------------------------SSVCSGMVSDVS-NDDIVRLMVG--------RELQNRFNAMKENVsNLAHETVF 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDfgDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLG--------------QLEPSRGL--VKGGtkleV 384
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGvdkraggeirlngkDISPRSPLdaVKKG----M 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 385 AYFDQYRDQ--LDPEQTVMDNVGEGKQevMVRGRSRHILGYLQDF----LFEPKRARTPVKA---------LSGGEKNRL 449
Cdd:PRK09700 341 AYITESRRDngFFPNFSIAQNMAISRS--LKDGGYKGAMGLFHEVdeqrTAENQRELLALKChsvnqniteLSGGNQQKV 418
|
490 500
....*....|....*....|....
gi 1411607396 450 LLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-472 |
5.88e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.58 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFS----DFPLLDNAELSIERGERLCLVGRNGAGKStlmkIIAgelplddgrmvqqqdLKVTRLEQDPP 76
Cdd:PRK15134 3 QPLLAIENLSVAFRqqqtVRTVVNDVSLQIEAGETLALVGESGSGKS----VTA---------------LSILRLLPSPP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 77 A-----------SSDLTVFDYTAEGLAGvgellkkyHHISMELAHDPSDANI--RIMSDLQEQLDYQNGWQFETRISQVL 143
Cdd:PRK15134 64 VvypsgdirfhgESLLHASEQTLRGVRG--------NKIAMIFQEPMVSLNPlhTLEKQLYEVLSLHRGMRREAARGEIL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 144 TLLNL----DPDATLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISH 211
Cdd:PRK15134 136 NCLDRvgirQAAKRLTdyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 212 DREFIHKLATRIIDLDRG----------------------VITSWPGNYDEYLQGKEEA-LRVEELQHAeFDrklaqeev 268
Cdd:PRK15134 216 NLSIVRKLADRVAVMQNGrcveqnraatlfsapthpytqkLLNSEPSGDPVPLPEPASPlLDVEQLQVA-FP-------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 269 wVRQGIKARRTrnegrvraleamrmersqrrelqgkaklqmddvnrsgklvfeteglgldfGDRTLFQGLDLQVLRGDKI 348
Cdd:PRK15134 287 -IRKGILKRTV--------------------------------------------------DHNVVVKNISFTLRPGETL 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 349 ALVGPNGCGKST----LIKLLLGQLE-----------PSRGLVKGGTKLEVAYFDQYrDQLDPEQTVMDNVGEGKQ---- 409
Cdd:PRK15134 316 GLVGESGSGKSTtglaLLRLINSQGEiwfdgqplhnlNRRQLLPVRHRIQVVFQDPN-SSLNPRLNVLQIIEEGLRvhqp 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 410 EVMVRGRSRHILGYLQDFLFEPK-RARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:PRK15134 395 TLSAAQREQQVIAVMEEVGLDPEtRHRYP-AEFSGGQRQRIAIARaLILKPS-LIILDEPTSSLD 457
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
6.68e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 66.36 E-value: 6.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFS-DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP------LDDGRMVQQQDLKVTR--- 70
Cdd:PRK13652 1 MHLIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKptsgsvLIRGEPITKENIREVRkfv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 71 --LEQDPpassDLTVFDYTAEglagvgellkkyhhisMELAHDPSDANirimsdlqeqLDYQNgwqFETRISQVLTLLNL 148
Cdd:PRK13652 81 glVFQNP----DDQIFSPTVE----------------QDIAFGPINLG----------LDEET---VAHRVSSALHMLGL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 149 DP--DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHDREFIHKLATR 222
Cdd:PRK13652 128 EElrDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADY 207
|
250
....*....|.
gi 1411607396 223 IIDLDRGVITS 233
Cdd:PRK13652 208 IYVMDKGRIVA 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
323-472 |
1.01e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 66.64 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GG---TKLE-----VAY-FDQYrd 392
Cdd:COG3839 7 ENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILiGGrdvTDLPpkdrnIAMvFQSY-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 QLDPEQTVMDNV-------GEGKQEvmVRGRSRH---ILGyLQDFLfepkrARTPvKALSGGEKNRLLLA-------KLF 455
Cdd:COG3839 85 ALYPHMTVYENIafplklrKVPKAE--IDRRVREaaeLLG-LEDLL-----DRKP-KQLSGGQRQRVALGralvrepKVF 155
|
170
....*....|....*..
gi 1411607396 456 LkpsnlliLDEPTNDLD 472
Cdd:COG3839 156 L-------LDEPLSNLD 165
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-233 |
1.03e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 65.81 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-----------VQQQDLKVTRLEQDPpassD----- 80
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvggmvlseetVWDVRRQVGMVFQNP----Dnqfvg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 81 LTVFDYTAEGLAGVGEllkkyhhismelahdPSDANIRimsdlqeqldyqngwqfetRISQVLTLLNLDPDATLD--SLS 158
Cdd:PRK13635 97 ATVQDDVAFGLENIGV---------------PREEMVE-------------------RVDQALRQVGMEDFLNREphRLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDfLKDFRGAIVF-ISHDREFIHKlATRIIDLDRGVITS 233
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQ-LKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-231 |
1.04e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 66.26 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-----MV---QQQDLK-----V----TRLEQDPPAssdl 81
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEvrvlgYVpfkRRKEFArrigvVfgqrSQLWWDLPA---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 tvfdytAEGLagvgELLKKYHHISMElahdpsdanirimsdlqeqldyqngwQFETRISQVLTLLNLDPdaTLD----SL 157
Cdd:COG4586 114 ------IDSF----RLLKAIYRIPDA--------------------------EYKKRLDELVELLDLGE--LLDtpvrQL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVFI-SHDREFIHKLATRIIDLDRGVI 231
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnreRGTTILLtSHDMDDIEALCDRVIVIDHGRI 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-473 |
1.12e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.63 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmVQQQDLKVTRLEQDPpassd 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSG---------NYQPDAGSILIDGQE----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 81 lTVFDYTAEGL-AGVG----ELlkkyhHISME--------LAHDPSDANI----RIMSDLQEQLDyqngwqfetRISqvl 143
Cdd:PRK11288 68 -MRFASTTAALaAGVAiiyqEL-----HLVPEmtvaenlyLGQLPHKGGIvnrrLLNYEAREQLE---------HLG--- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 144 tlLNLDPDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLA 220
Cdd:PRK11288 130 --VDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAegrVILYVSHRMEEIFALC 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 221 TRIIDLDRGvitswpgnydEYLQGKEEalrVEELQHAEfdrkLAQEEVwvrqgikarrTRNEGRVRALEAmrmersqrRE 300
Cdd:PRK11288 208 DAITVFKDG----------RYVATFDD---MAQVDRDQ----LVQAMV----------GREIGDIYGYRP--------RP 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 301 LqGKAKLQMDDVnrsgklvfetEGLGLDfgdrtlfQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GG 379
Cdd:PRK11288 253 L-GEVRLRLDGL----------KGPGLR-------EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYlDG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 380 TKLEvayFDQYRDQ------LDPEqtvmdnvgEGKQEVMVRGRS----------RHIL--GYLQDFLFEPKRA------- 434
Cdd:PRK11288 315 KPID---IRSPRDAiragimLCPE--------DRKAEGIIPVHSvadninisarRHHLraGCLINNRWEAENAdrfirsl 383
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1411607396 435 -------RTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11288 384 niktpsrEQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
338-516 |
1.41e-11 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 64.44 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGG---TKLEVA------YFDQyrDQLDPEQTVMDNVGEG 407
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGrVLINGvdvTAAPPAdrpvsmLFQE--NNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 408 -----KQEVMVRGRSRHILGYLQDFLFEPKRARTpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD----VETLEL 478
Cdd:cd03298 95 lspglKLTAEDRQAIEVALARVGLAGLEKRLPGE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1411607396 479 LEELLADYPGTLLLVSH---DRRFIDNTVtgcwLFEGDGRI 516
Cdd:cd03298 171 VLDLHAETKMTVLMVTHqpeDAKRLAQRV----VFLDNGRI 207
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
331-495 |
1.52e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 64.41 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQY-RDQL-----DP---EQTVM 401
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYlHSKVslvgqEPvlfARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEGKQ-----EVMVRGRSRHILGYLQDFlfePKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03248 106 DNIAYGLQscsfeCVKEAAQKAHAHSFISEL---ASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180
....*....|....*....|....*
gi 1411607396 473 VETLELLEELLADYPG--TLLLVSH 495
Cdd:cd03248 183 AESEQQVQQALYDWPErrTVLVIAH 207
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-212 |
1.71e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.75 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKV----TRLEQDPpaS 78
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIgyvpQKLYLDT--T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 79 SDLTVFDYtaeglagvgellkkyhhisMELAhdPSDANIRIMSDLQeqldyqngwqfetRIsQVLTLLnldpDATLDSLS 158
Cdd:PRK09544 82 LPLTVNRF-------------------LRLR--PGTKKEDILPALK-------------RV-QAGHLI----DAPMQKLS 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHD 212
Cdd:PRK09544 123 GGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRReldcAVLMVSHD 180
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
17-242 |
1.81e-11 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 67.07 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDdGRMVQQQDLKVTR-----LEQDPpassdlTVF 84
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLvgffqarSGEILLN-GFSLKDIDRHTLRqfinyLPQEP------YIF 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 85 DYTA-EGLagvgeLLKKYHHISMELAhdpsDANIRIMSDLQEQLDYQNGWQfeTRISQvltllnldpDATldSLSGGWLR 163
Cdd:TIGR01193 561 SGSIlENL-----LLGAKENVSQDEI----WAACEIAEIKDDIENMPLGYQ--TELSE---------EGS--SISGGQKQ 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLD-IEAINWLEDFLKDFRGAIVFISHdREFIHKLATRIIDLDRGVITSwPGNYDEYL 242
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDtITEKKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIE-QGSHDELL 696
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
335-475 |
2.23e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.77 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 335 FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLE-----------------VAYF-DQYRDQL- 394
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlNGQPIAdyseaalrqaisvvsqrVHLFsATLRDNLl 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 --DPEQT------VMDNVGegkqevmvrgrsrhiLGYLQD-------FLFEPKRArtpvkaLSGGEKNRLLLAKLFLKPS 459
Cdd:PRK11160 436 laAPNASdealieVLQQVG---------------LEKLLEddkglnaWLGEGGRQ------LSGGEQRRLGIARALLHDA 494
|
170
....*....|....*.
gi 1411607396 460 NLLILDEPTNDLDVET 475
Cdd:PRK11160 495 PLLLLDEPTEGLDAET 510
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
339-533 |
2.30e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 64.01 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 339 DLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVA------YFDQyrDQLDPEQTVMDNVGEG- 407
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGriLWNGQdlTALPPAerpvsmLFQE--NNLFPHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 408 ----------KQEVmvrgrsRHILGY--LQDFLfepkrARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD--- 472
Cdd:COG3840 97 rpglkltaeqRAQV------EQALERvgLAGLL-----DRLP-GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpal 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 473 -VETLELLEELLADYPGTLLLVSHD----RRFIDNTvtgcwLFEGDGRISdYVGGYADMMATRAQQ 533
Cdd:COG3840 165 rQEMLDLVDELCRERGLTVLMVTHDpedaARIADRV-----LLVADGRIA-ADGPTAALLDGEPPP 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
323-473 |
2.43e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.62 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggtklevaYFDQYRDQLDPEQTVMD 402
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV---------WLDGEHIQHYASKEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 403 NVG--------EGK---QEVMVRGRSRHILGYL------QDFLFEPKR-------ARTPVKALSGGEKNRLLLAKLFLKP 458
Cdd:PRK10253 82 RIGllaqnattPGDitvQELVARGRYPHQPLFTrwrkedEEAVTKAMQatgithlADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170
....*....|....*
gi 1411607396 459 SNLLILDEPTNDLDV 473
Cdd:PRK10253 162 TAIMLLDEPTTWLDI 176
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
416-546 |
2.81e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.42 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 416 RSRHILGYLQdflFEPKRARTPVKALSGGEKNRLLLAK-LFLKPsNLLILDEPTNDLDVETLELLEELLADYPGTLLLVS 494
Cdd:PLN03073 323 RAASILAGLS---FTPEMQVKATKTFSGGWRMRIALARaLFIEP-DLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVS 398
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 495 HDRRFIDNTVTGCWLFEGDgRISDYVGGYADMMATRAQQ-STQLAAKAAQVKT 546
Cdd:PLN03073 399 HAREFLNTVVTDILHLHGQ-KLVTYKGDYDTFERTREEQlKNQQKAFESNERS 450
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-246 |
2.87e-11 |
|
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: 63.71 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDdGRMVQQQDLKVTR-----LEQDPpassdlT 82
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEILLD-GVDIRDLNLRWLRsqiglVSQEP------V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 83 VFDYT-AEGLAgvgelLKKYHHISMELAHDPSDANIR--IMSdLQEQLDYQNGwqfeTRISQvltllnldpdatldsLSG 159
Cdd:cd03249 88 LFDGTiAENIR-----YGKPDATDEEVEEAAKKANIHdfIMS-LPDGYDTLVG----ERGSQ---------------LSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDI--EAI--NWLEDFLKDfRGAIVfISHDREFIHKlATRIIDLDRGVITSwP 235
Cdd:cd03249 143 GQKQRIAIARALLRNPKILLLDEATSALDAesEKLvqEALDRAMKG-RTTIV-IAHRLSTIRN-ADLIAVLQNGQVVE-Q 218
|
250
....*....|.
gi 1411607396 236 GNYDEYLQGKE 246
Cdd:cd03249 219 GTHDELMAQKG 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-231 |
2.99e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.00 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMK------------IIAGELPLDDGRMVQQQDLKV 68
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRcinlleqpeagtIRVGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 69 TRLEQDppassdltvfdytaeglagVGELLKKY----HHISMElahDPSDANIRIMSDLQEQLdyqngwqfETRISQVLT 144
Cdd:PRK11264 81 RQLRQH-------------------VGFVFQNFnlfpHRTVLE---NIIEGPVIVKGEPKEEA--------TARARELLA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 145 LLNLD--PDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINwleDFLKDFRG------AIVFISHDREFI 216
Cdd:PRK11264 131 KVGLAgkETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVG---EVLNTIRQlaqekrTMVIVTHEMSFA 207
|
250
....*....|....*
gi 1411607396 217 HKLATRIIDLDRGVI 231
Cdd:PRK11264 208 RDVADRAIFMDQGRI 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-231 |
3.33e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 65.35 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDlkVTRLeqdPPASSD- 80
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRiMLDGQD--ITHV---PAENRHv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 81 ------------LTVFDYTAEGLAgvgelLKKYhhismelahdPSDanirimsdlqeqldyqngwQFETRISQVLTLLNL 148
Cdd:PRK09452 89 ntvfqsyalfphMTVFENVAFGLR-----MQKT----------PAA-------------------EITPRVMEALRMVQL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 149 DPDAT--LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGAI----VFISHDREFIHKLATR 222
Cdd:PRK09452 135 EEFAQrkPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQEEALTMSDR 214
|
....*....
gi 1411607396 223 IIDLDRGVI 231
Cdd:PRK09452 215 IVVMRDGRI 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
329-472 |
3.38e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 64.37 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQgLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGG---------------TKLEVAYFDQYRDQ 393
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsstskqkeikpVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 LDPEQTVMDNVGEGKQEV--------MVRGRSRHILGYLQDFLfepkrARTPVKaLSGGEKNRLLLAKLFLKPSNLLILD 465
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNFgipkekaeKIAAEKLEMVGLADEFW-----EKSPFE-LSGGQMRRVAIAGILAMEPEVLVLD 169
|
....*..
gi 1411607396 466 EPTNDLD 472
Cdd:PRK13643 170 EPTAGLD 176
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
11-183 |
3.65e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.02 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFS--DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM---------VQQQDL-----KVTRLEQD 74
Cdd:PRK11831 13 VSFTrgNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgenipaMSRSRLytvrkRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 75 PPASSDLTVFDytaeglaGVGELLKKYHHISMELAHdpsdanirimsdlqeqldyqngwqfeTRISQVLTLLNLDPDATL 154
Cdd:PRK11831 93 GALFTDMNVFD-------NVAYPLREHTQLPAPLLH--------------------------STVMMKLEAVGLRGAAKL 139
|
170 180 190
....*....|....*....|....*....|.
gi 1411607396 155 --DSLSGGWLRKVALARALACDPDLLLLDEP 183
Cdd:PRK11831 140 mpSELSGGMARRAALARAIALEPDLIMFDEP 170
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-231 |
3.72e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 63.26 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 14 SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDdGRMVQQQDLK-----VTRLEQDPPASSDl 81
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLenfyqpqGGQVLLD-GKPISQYEHKylhskVSLVGQEPVLFAR- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 TVFDYTAEGLAG-----VGELLKKYHhismelAHDpsdaNIRIMsdlqeqldyQNGWQFET--RISQvltllnldpdatl 154
Cdd:cd03248 103 SLQDNIAYGLQScsfecVKEAAQKAH------AHS----FISEL---------ASGYDTEVgeKGSQ------------- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 155 dsLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFISHDREFIHKlATRIIDLDRGVI 231
Cdd:cd03248 151 --LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-189 |
3.77e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.88 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIA-------GELPLDDGRMVQQQDLKVTR----LE 72
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFArlltpqsGTVFLGDKPISMLSSRQLARrlalLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 QDPPASSDLTVFDYTAEG----LAGVGELLKKYHHI---SMElahdpsdanirimsdlqeqldyqngwqfETRISQVltl 145
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARvnqAME----------------------------QTRINHL--- 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1411607396 146 lnldPDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI 189
Cdd:PRK11231 132 ----ADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
297-475 |
3.80e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 66.14 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 297 QRRELQGKAKLQmddvNRSGKLVFETEGLGLDfGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV 376
Cdd:PRK13657 318 DVRDPPGAIDLG----RVKGAVEFDDVSFSYD-NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 377 K-GGTKLEVAYFDQYRDQL-----DP---EQTVMDNVGEGK----QEVMVRGRSRhilGYLQDFLF-EPKRARTPV---- 438
Cdd:PRK13657 393 LiDGTDIRTVTRASLRRNIavvfqDAglfNRSIEDNIRVGRpdatDEEMRAAAER---AQAHDFIErKPDGYDTVVgerg 469
|
170 180 190
....*....|....*....|....*....|....*..
gi 1411607396 439 KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVET 506
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
141-233 |
3.83e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.90 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 141 QVLTLLNLDPdaTLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHD 212
Cdd:PRK11144 111 KIVALLGIEP--LLDrypgSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHS 188
|
90 100
....*....|....*....|.
gi 1411607396 213 REFIHKLATRIIDLDRGVITS 233
Cdd:PRK11144 189 LDEILRLADRVVVLEQGKVKA 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
321-474 |
3.84e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.62 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGT---------KLEVAYFDQYR 391
Cdd:PRK11264 5 EVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslSQQKGLIRQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 392 DQ---------LDPEQTVMDNVGEG--------KQEVMVRGRSrhilgYLQDFLFEPKRARTPvKALSGGEKNRLLLAKL 454
Cdd:PRK11264 85 QHvgfvfqnfnLFPHRTVLENIIEGpvivkgepKEEATARARE-----LLAKVGLAGKETSYP-RRLSGGQQQRVAIARA 158
|
170 180
....*....|....*....|
gi 1411607396 455 FLKPSNLLILDEPTNDLDVE 474
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPE 178
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
333-498 |
3.90e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.26 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 333 TLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLDPEQTVM---DNVGEGKQ 409
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSG--------EVSLVGQPLHQMDEEARAKlraKHVGFVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 410 EVMV----------------RG----RSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:PRK10584 96 SFMLiptlnalenvelpallRGessrQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190
....*....|....*....|....*....|...
gi 1411607396 470 DLDVETLELLE----ELLADYPGTLLLVSHDRR 498
Cdd:PRK10584 176 NLDRQTGDKIAdllfSLNREHGTTLILVTHDLQ 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-188 |
3.95e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.13 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLD-----DG-----RMVQQQDLKVtrle 72
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKPTEgqifiDGedvthRSIQQRDICM---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 qdppassdltVFDYTAeglagvgellkKYHHISmelahdpsdanirimsdLQEQLDY------QNGWQFETRISQVLTLL 146
Cdd:PRK11432 83 ----------VFQSYA-----------LFPHMS-----------------LGENVGYglkmlgVPKEERKQRVKEALELV 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1411607396 147 NLD--PDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK11432 125 DLAgfEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
313-475 |
5.22e-11 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 65.92 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 313 NRSGKLVFETEGLGLDFGDRTLfQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYR 391
Cdd:TIGR01193 469 NLNGDIVINDVSYSYGYGSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILlNGFSLKDIDRHTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 392 DQLD--PEQ------TVMDNV------GEGKQEVMVRGRSRHI--------LGYLQDFLFEPKrartpvkALSGGEKNRL 449
Cdd:TIGR01193 548 QFINylPQEpyifsgSILENLllgakeNVSQDEIWAACEIAEIkddienmpLGYQTELSEEGS-------SISGGQKQRI 620
|
170 180
....*....|....*....|....*.
gi 1411607396 450 LLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTIT 646
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
321-472 |
5.57e-11 |
|
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: 63.13 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKLEVA------YFDQY 390
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggEDATDVPVQernvgfVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 rdQLDPEQTVMDNVGEG---------KQEVMVRGRSRHILGYLQ-DFLFEpkraRTPVKaLSGGEKNRLLLAKLFLKPSN 460
Cdd:cd03296 84 --ALFRHMTVFDNVAFGlrvkprserPPEAEIRAKVHELLKLVQlDWLAD----RYPAQ-LSGGQRQRVALARALAVEPK 156
|
170
....*....|..
gi 1411607396 461 LLILDEPTNDLD 472
Cdd:cd03296 157 VLLLDEPFGALD 168
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
331-495 |
5.58e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.51 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVAYFDQYRDQLDPE-----QTVM 401
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGqvLLDGVplVQYDHHYLHRQVALVGQEpvlfsGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEG-----KQEVMVRGRSRHILGYLQDFlfePKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR00958 573 ENIAYGltdtpDEEIMAAAKAANAHDFIMEF---PNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180
....*....|....*....|...
gi 1411607396 473 VETLELLEELLADYPGTLLLVSH 495
Cdd:TIGR00958 650 AECEQLLQESRSRASRTVLLIAH 672
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-231 |
7.06e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.04 E-value: 7.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDdGRMVQQQDLKVTRlEQDPPASSDLTVF-DY 86
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLtrfydidEGEILLD-GHDLRDYTLASLR-NQVALVSQNVHLFnDT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 87 TAEGLAGVGEllKKYHHISMELAhdpsdANIRIMSDLQEQLDyqNGwqFETRISQVLTllnldpdatldSLSGGWLRKVA 166
Cdd:PRK11176 433 IANNIAYART--EQYSREQIEEA-----ARMAYAMDFINKMD--NG--LDTVIGENGV-----------LLSGGQRQRIA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 167 LARALACDPDLLLLDEPTNHLDIE---AINWLEDFLKDFRGAIVfISHDREFIHKlATRIIDLDRGVI 231
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTEserAIQAALDELQKNRTSLV-IAHRLSTIEK-ADEILVVEDGEI 556
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
323-475 |
9.00e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 63.96 E-value: 9.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLevayfdqyrDQLDPEQ--- 398
Cdd:COG3842 9 ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILlDGRDV---------TGLPPEKrnv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 -------------TVMDNVGEG-------KQEvmVRGRSRHILGY--LQDFlfepkrARTPVKALSGGEKNRLLLAK-LF 455
Cdd:COG3842 80 gmvfqdyalfphlTVAENVAFGlrmrgvpKAE--IRARVAELLELvgLEGL------ADRYPHQLSGGQQQRVALARaLA 151
|
170 180
....*....|....*....|
gi 1411607396 456 LKPSnLLILDEPTNDLDVET 475
Cdd:COG3842 152 PEPR-VLLLDEPLSALDAKL 170
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
309-473 |
9.83e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 9.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 309 MDDVNRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKL----- 382
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGeILLDAQPLeswss 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 383 -----EVAYFDQyrdQLDPEQtvmdnvGEGKQEVMVRGR-SRHilGYLQDFLFEPKR--------------ARTPVKALS 442
Cdd:PRK10575 81 kafarKVAYLPQ---QLPAAE------GMTVRELVAIGRyPWH--GALGRFGAADREkveeaislvglkplAHRLVDSLS 149
|
170 180 190
....*....|....*....|....*....|.
gi 1411607396 443 GGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-231 |
1.10e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 63.67 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPlDDGR-MVQQQDLkvTRLEQDPPAS---------------SDL 81
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLlERP-TSGRvLVDGQDL--TALSEKELRKarrqigmifqhfnllSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 TVFDYTAeglagvgellkkyhhISMELAHDPSDanirimsdlqeqldyqngwQFETRISQVLTLLNLDP--DATLDSLSG 159
Cdd:PRK11153 98 TVFDNVA---------------LPLELAGTPKA-------------------EIKARVTELLELVGLSDkaDRYPAQLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKD----FRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDinreLGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
562-631 |
1.13e-10 |
|
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: 57.48 E-value: 1.13e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 562 KLSYKLQLELDNLPARLEQLETELNALQAEVNHPGFFALPSDQTQLkLDALNAAEAALEQAFSRWEELEA 631
Cdd:pfam16326 1 KLSYKEQRELEELEAEIEKLEEEIAELEAQLADPELYSDYEKLQEL-SAELEELEAELEELYERWEELEE 69
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-472 |
1.43e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.17 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 317 KLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLL--LGQLEPSrGLVKGGTKL------------ 382
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEE-ARVEGEVRLfgrniyspdvdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 383 -----EVAYFDQYRDQLdPEQTVMDNVGEG-KQEVMVRGRS----RHILGYLQDFLFEPKRARTPVKA--LSGGEKNRLL 450
Cdd:PRK14267 81 ievrrEVGMVFQYPNPF-PHLTIYDNVAIGvKLNGLVKSKKeldeRVEWALKKAALWDEVKDRLNDYPsnLSGGQRQRLV 159
|
170 180
....*....|....*....|...
gi 1411607396 451 LAK-LFLKPsNLLILDEPTNDLD 472
Cdd:PRK14267 160 IARaLAMKP-KILLMDEPTANID 181
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-191 |
1.51e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSdltvFDYTAEGLAGVGE 96
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANG----IVYISEDRKRDGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 97 LLkkyhhiSMELAHDPSDANIRIMSDLQEQLDYQNGWQfetRISQVLTLLNL---DPDATLDSLSGGWLRKVALARALAC 173
Cdd:PRK10762 342 VL------GMSVKENMSLTALRYFSRAGGSLKHADEQQ---AVSDFIRLFNIktpSMEQAIGLLSGGNQQKVAIARGLMT 412
|
170
....*....|....*...
gi 1411607396 174 DPDLLLLDEPTNHLDIEA 191
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGA 430
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
321-473 |
1.53e-10 |
|
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: 61.48 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKlEVAYFDQYRDQ------- 393
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK-DITNLPPHKRPvntvfqn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 --LDPEQTVMDNVG-----EGKQEVMVRGRSRHILGYLQdflFEPKRARTPvKALSGGEKNRLLLAK-LFLKPSnLLILD 465
Cdd:cd03300 81 yaLFPHLTVFENIAfglrlKKLPKAEIKERVAEALDLVQ---LEGYANRKP-SQLSGGQQQRVAIARaLVNEPK-VLLLD 155
|
....*...
gi 1411607396 466 EPTNDLDV 473
Cdd:cd03300 156 EPLGALDL 163
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
337-473 |
1.88e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 62.83 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVAYFDQYRDQ-----------LDPEQTVM 401
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGeiLFDGQdiTGLSGRELRPLRRRmqmvfqdpyasLNPRMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEG--------KQEvmVRGRSRHIL---GYLQDFLfepkrARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTN 469
Cdd:COG4608 116 DIIAEPlrihglasKAE--RRERVAELLelvGLRPEHA-----DRYP-HEFSGGQRQRIGIARaLALNPK-LIVCDEPVS 186
|
....
gi 1411607396 470 DLDV 473
Cdd:COG4608 187 ALDV 190
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-212 |
1.99e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 62.67 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLD-------DGRMVQQQDLKVTRLEQDPPASsdltvf 84
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLtmietptGGELYYQgqdllkaDPEAQKLLRQKIQIVFQNPYGS------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 85 dytaeglagvgelLKKYHHISMELAhDPsdanIRIMSDLQEQldyqngwQFETRISQVLTLLNLDP---DATLDSLSGGW 161
Cdd:PRK11308 105 -------------LNPRKKVGQILE-EP----LLINTSLSAA-------ERREKALAMMAKVGLRPehyDRYPHMFSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLD--IEA--INWLEDFLKDFRGAIVFISHD 212
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDvsVQAqvLNLMMDLQQELGLSYVFISHD 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
284-475 |
2.02e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.67 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 284 RVRAL-EAMRMERSQRRELQGKaklqmdDVNRSGKLVFEteGLGLDFGD-RTLFQGLDLQVLRGDKIALVGPNGCGKSTL 361
Cdd:COG4178 334 RLAGFeEALEAADALPEAASRI------ETSEDGALALE--DLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 362 IKLLLG------------QLE-----PSRGLVKGGTKLEVAYFDQYRDQLDPEQ--TVMDNVGegkqevmvrgrsrhiLG 422
Cdd:COG4178 406 LRAIAGlwpygsgriarpAGArvlflPQRPYLPLGTLREALLYPATAEAFSDAElrEALEAVG---------------LG 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 423 YLQDFLFEPKR-ARTpvkaLSGGEKNRLLLAKLFL-KPSnLLILDEPTNDLDVET 475
Cdd:COG4178 471 HLAERLDEEADwDQV----LSLGEQQRLAFARLLLhKPD-WLFLDEATSALDEEN 520
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-245 |
2.03e-10 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 61.09 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD------DGRMVQQQDLKVTR-----LEQDPPASSDlTVFD 85
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQkgqiliDGIDIRDISRKSLRsmigvVLQDTFLFSG-TIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 86 ytaeglagvgellkkyhhismelahdpsdaNIRIMSDLQEqldyqngwqfETRISQVLTLLNLDP---------DATL-- 154
Cdd:cd03254 96 ------------------------------NIRLGRPNAT----------DEEVIEAAKEAGAHDfimklpngyDTVLge 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 155 --DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAinwlEDFLKDfrgAIVFISHDREFI---HKLAT-----RII 224
Cdd:cd03254 136 ngGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET----EKLIQE---ALEKLMKGRTSIiiaHRLSTiknadKIL 208
|
250 260
....*....|....*....|.
gi 1411607396 225 DLDRGVITSwPGNYDEYLQGK 245
Cdd:cd03254 209 VLDDGKIIE-EGTHDELLAKK 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-243 |
2.06e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 61.64 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmVQQQDLKVtrleqDPPASSDLT 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGS-ITLDGKPV-----EGPGAERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 83 VFDYtaEGLAGVGELLKKYHhISMELAHDPSDANIRIMSDLQEQLDYQNgwqFETR-ISQvltllnldpdatldsLSGGW 161
Cdd:PRK11248 75 VFQN--EGLLPWRNVQDNVA-FGLQLAGVEKMQRLEIAHQMLKKVGLEG---AEKRyIWQ---------------LSGGQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFL----KDFRGAIVFISHDREFIHKLATRIIDLDRGvitswPGN 237
Cdd:PRK11248 134 RQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHDIEEAVFMATELVLLSPG-----PGR 208
|
....*.
gi 1411607396 238 YDEYLQ 243
Cdd:PRK11248 209 VVERLP 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
321-501 |
2.10e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 60.62 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQlePSRGLVKGgtklEVAYFDQYRDQLDPEQTV 400
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVTEG----EILFKGEDITDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEGKQE-VMVRGRSrhilgyLQDFLfepkraRTPVKALSGGEKNRL-LLAKLFLKPSnLLILDEPTNDLDVETLEL 478
Cdd:cd03217 76 RLGIFLAFQYpPEIPGVK------NADFL------RYVNEGFSGGEKKRNeILQLLLLEPD-LAILDEPDSGLDIDALRL 142
|
170 180
....*....|....*....|....*.
gi 1411607396 479 LEELLADY--PGT-LLLVSHDRRFID 501
Cdd:cd03217 143 VAEVINKLreEGKsVLIITHYQRLLD 168
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-233 |
2.20e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.10 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmVQQQDLKVTRLEQD----PPASSDLTVFDYTAEGLAgv 94
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGT-VTVDDITITHKTKDkyirPVRKRIGMVFQFPESQLF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 95 gellkkYHHISMELAHDPSDANIrimsDLQEQLDYQNGWQFETRISQvlTLLNLDPDatldSLSGGWLRKVALARALACD 174
Cdd:PRK13646 100 ------EDTVEREIIFGPKNFKM----NLDEVKNYAHRLLMDLGFSR--DVMSQSPF----QMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 175 PDLLLLDEPTNHLDIEAINWLEDFLKDFR----GAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-473 |
2.22e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQdlKVTRLeQDPPASSDl 81
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG--KEVTF-NGPKSSQE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 tvfdytaeglAGVGELlkkyhHISMELAHDPSDA-NIRImsdlqeqldyqnGWQFETRI------------SQVLTLLNL 148
Cdd:PRK10762 79 ----------AGIGII-----HQELNLIPQLTIAeNIFL------------GREFVNRFgridwkkmyaeaDKLLARLNL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 149 --DPDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHL-DIE------AINwlEdfLKDFRGAIVFISH-------- 211
Cdd:PRK10762 132 rfSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTEteslfrVIR--E--LKSQGRGIVYISHrlkeifei 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 212 --------DREFIHKLATRIIDLDRGVitswpgnydEYLQGkeealrveelqhaefdRKLaqEEVWVRQGIKarrtrneg 283
Cdd:PRK10762 208 cddvtvfrDGQFIAEREVADLTEDSLI---------EMMVG----------------RKL--EDQYPRLDKA-------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 284 rvraleamrmersqrrelQGKAKLQmddvnrsgklVFETEGLGLDFGDRTLFQGLDLQVlrgdkialVGPNGCGKSTLIK 363
Cdd:PRK10762 253 ------------------PGEVRLK----------VDNLSGPGVNDVSFTLRKGEILGV--------SGLMGAGRTELMK 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 364 LLLGQLEPSRGLVK------------GGTKLEVAYF--DQYRDQLDPEQTVMDNVG--------------EGKQEVMVRG 415
Cdd:PRK10762 297 VLYGALPRTSGYVTldghevvtrspqDGLANGIVYIseDRKRDGLVLGMSVKENMSltalryfsraggslKHADEQQAVS 376
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 416 rsrhilgylqDF--LFEPKrarTP-----VKALSGGEKNRLLLAK-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK10762 377 ----------DFirLFNIK---TPsmeqaIGLLSGGNQQKVAIARgLMTRP-KVLILDEPTRGVDV 428
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
345-495 |
2.24e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.99 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 345 GDKIALVGPNGCGKSTLIKLLLGQLEPSRG--------LVKGGTKL-----EVAYFDQYRD-QLDPEQTVMD------NV 404
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKPTSGkiiidgvdITDKKVKLsdirkKVGLVFQYPEyQLFEETIEKDiafgpiNL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 405 GEGKQEVMVR-GRSRHILGylqdFLFEPKRARTPVKaLSGGEKNRLLLAKLF-LKPSnLLILDEPTNDLDV----ETLEL 478
Cdd:PRK13637 113 GLSEEEIENRvKRAMNIVG----LDYEDYKDKSPFE-LSGGQKRRVAIAGVVaMEPK-ILILDEPTAGLDPkgrdEILNK 186
|
170
....*....|....*..
gi 1411607396 479 LEELLADYPGTLLLVSH 495
Cdd:PRK13637 187 IKELHKEYNMTIILVSH 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-231 |
2.27e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.74 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 14 SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDD---------GRMVQQQDL-----KVTRLEQDPPAS- 78
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnskitvdGITLTAKTVwdireKVGIVFQNPDNQf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 79 SDLTVFDYTAEGLAGVGEllkkyhhismelahdPSDANIRIMSDLQEQ---LDYQngwqfetrisqvltllnldpDATLD 155
Cdd:PRK13640 98 VGATVGDDVAFGLENRAV---------------PRPEMIKIVRDVLADvgmLDYI--------------------DSEPA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHDREFIhKLATRIIDLDRGVI 231
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknnlTVISITHDIDEA-NMADQVLVLDDGKL 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
334-495 |
2.33e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.14 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 334 LFQGL----DLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGGT-------KLEVAYFDQyRDQLDPEQTV 400
Cdd:PRK10771 10 LYHHLpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGslTLNGQDhtttppsRRPVSMLFQ-ENNLFSHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEG-----KQEVMVRGRSRHILGY--LQDFLfepkrARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD- 472
Cdd:PRK10771 89 AQNIGLGlnpglKLNAAQREKLHAIARQmgIEDLL-----ARLP-GQLSGGQRQRVALARCLVREQPILLLDEPFSALDp 162
|
170 180
....*....|....*....|....*.
gi 1411607396 473 ---VETLELLEELLADYPGTLLLVSH 495
Cdd:PRK10771 163 alrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-232 |
2.39e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.12 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDlkVTRLeqDPPASSDLTVF----DYTAEGL 91
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIrLDGED--ITGL--SPRERRRLGVAyipeDRLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 92 AG---VGE--LLKKYHH--------ISMELAHDPSDANIRimsdlqeqldyqngwQFETRISqvltllnlDPDATLDSLS 158
Cdd:COG3845 348 VPdmsVAEnlILGRYRRppfsrggfLDRKAIRAFAEELIE---------------EFDVRTP--------GPDTPARSLS 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdagAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
306-472 |
2.56e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 62.66 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 306 KLQMDDVNRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVA 385
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSG--------RIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 386 YFDQYRDQLDPEQ----------------TVMDNVGEG-------KQEV---------MVRgrsrhilgyLQDFlfepkr 433
Cdd:PRK09452 73 LDGQDITHVPAENrhvntvfqsyalfphmTVFENVAFGlrmqktpAAEItprvmealrMVQ---------LEEF------ 137
|
170 180 190
....*....|....*....|....*....|....*....
gi 1411607396 434 ARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK09452 138 AQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
323-473 |
2.76e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.10 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKLEVA------------- 385
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmRDGQLRDLYalseaerrrllrt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 386 ---YFDQY-RDQLDPEQTVMDNVGEGKQEVMVR--GRSRHILG-YLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKP 458
Cdd:PRK11701 90 ewgFVHQHpRDGLRMQVSAGGNIGERLMAVGARhyGDIRATAGdWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTH 169
|
170
....*....|....*
gi 1411607396 459 SNLLILDEPTNDLDV 473
Cdd:PRK11701 170 PRLVFMDEPTGGLDV 184
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
334-475 |
2.80e-10 |
|
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: 60.18 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 334 LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKleVAYFDQYrdqldP---EQTVMDNVGEGKQe 410
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQE-----PwiqNGTIRENILFGKP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 411 vmvrgrsrhilgylqdflFEPKRARTPVKA------------------------LSGGEKNRLLLAKLFLKPSNLLILDE 466
Cdd:cd03250 92 ------------------FDEERYEKVIKAcalepdleilpdgdlteigekginLSGGQKQRISLARAVYSDADIYLLDD 153
|
....*....
gi 1411607396 467 PTNDLDVET 475
Cdd:cd03250 154 PLSAVDAHV 162
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
317-472 |
3.10e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.50 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 317 KLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEVAYFDQYRDQLD 395
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGtLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 -----PE---QTVMDNVGEGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRL-LLAKLFLKPSNLLiLDE 466
Cdd:PRK10247 85 ycaqtPTlfgDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRIsLIRNLQFMPKVLL-LDE 163
|
....*.
gi 1411607396 467 PTNDLD 472
Cdd:PRK10247 164 ITSALD 169
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-231 |
3.16e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.14 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 13 FSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDDGRMVQQQDLKVTRlEQDppasSDLTVFDYTAEGL 91
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFlEKPSEGSIVVNGQTINLVR-DKD----GQLKVADKNQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 92 AGVgELLKKYHHIS----MELAHDPSDANIRIMSdLQEQldyqngwQFETRISQVLTLLNLDPDATLD---SLSGGWLRK 164
Cdd:PRK10619 90 LRT-RLTMVFQHFNlwshMTVLENVMEAPIQVLG-LSKQ-------EARERAVKYLAKVGIDERAQGKypvHLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 165 VALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
336-496 |
3.51e-10 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 60.56 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK---------GGTKLEVayFDQYrdQLDPEQTVMDNVGE 406
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIlegkqitepGPDRMVV--FQNY--SLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 407 GKQEV---MVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLDVETLELLEEL 482
Cdd:TIGR01184 78 AVDRVlpdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARaLSIRPK-VLLLDEPFGALDALTRGNLQEE 156
|
170
....*....|....*...
gi 1411607396 483 L----ADYPGTLLLVSHD 496
Cdd:TIGR01184 157 LmqiwEEHRVTVLMVTHD 174
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-231 |
3.73e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 61.29 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDD-----GRMVQQQDLKVTRLE-----QDPpassDLTVFDYT 87
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiYLPQRGrvkvmGREVNAENEKWVRSKvglvfQDP----DDQVFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 88 AEGLAGVGEllkkyhhISMELAHDpsdaniRIMSDLQEQLDYQNGWQFETRISQvltllnldpdatldSLSGGWLRKVAL 167
Cdd:PRK13647 97 VWDDVAFGP-------VNMGLDKD------EVERRVEEALKAVRMWDFRDKPPY--------------HLSYGQKKRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 168 ARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFIS-HDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhnQGKTVIVAtHDVDLAAEWADQVIVLKEGRV 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
330-528 |
4.10e-10 |
|
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: 63.04 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKggTKLEVAYFdqyrdqldPEQ------TVMDN 403
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH--MKGSVAYV--------PQQawiqndSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 404 VGEGKQevMVRGRSRHIL---GYLQDFLFEPKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETL 476
Cdd:TIGR00957 719 ILFGKA--LNEKYYQQVLeacALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 477 ELLEELLADYPGTL-----LLVSHDRRFIDNtvTGCWLFEGDGRISDyVGGYADMMA 528
Cdd:TIGR00957 797 KHIFEHVIGPEGVLknktrILVTHGISYLPQ--VDVIIVMSGGKISE-MGSYQELLQ 850
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
336-496 |
4.22e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.64 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GG---TKLEVAY-------FDQyRDQL--D------- 395
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGyvpFKRRKEFarrigvvFGQ-RSQLwwDlpaidsf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 ---------PEQTVMDNVGEgkqevMVrgrsrHILGyLQDFLfepkraRTPVKALSGGEKNRL-LLAKLFLKPSnLLILD 465
Cdd:COG4586 118 rllkaiyriPDAEYKKRLDE-----LV-----ELLD-LGELL------DTPVRQLSLGQRMRCeLAAALLHRPK-ILFLD 179
|
170 180 190
....*....|....*....|....*....|....*
gi 1411607396 466 EPTNDLDVETLEL----LEELLADYPGTLLLVSHD 496
Cdd:COG4586 180 EPTIGLDVVSKEAirefLKEYNRERGTTILLTSHD 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-229 |
4.72e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrMVQqqdlkvtrleqdpPASSDL 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLG--------LTH-------------PDAGSI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 TVFDYTAEGLAgvgellkkyHHISMELAHDPS----DANIRIMSDLQEQLDY--QNGWQFETRISQVLTLLNLD--PDAT 153
Cdd:PRK13537 65 SLCGEPVPSRA---------RHARQRVGVVPQfdnlDPDFTVRENLLVFGRYfgLSAAAARALVPPLLEFAKLEnkADAK 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RG-AIVFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK13537 136 VGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLlaRGkTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-242 |
4.91e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.97 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 21 NAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLD--------DGRMVQQQDLKVTRLEQDPPASSDLTVFD 85
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLnrlieptRGQVLIDgvdiakisDAELREVRRKKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 86 YTAEGlagvgellkkyhhisMELAHDPSDANIRIMSDLQEQL---DYQNGWQfetrisqvltllnldpdatlDSLSGGWL 162
Cdd:PRK10070 126 NTAFG---------------MELAGINAEERREKALDALRQVgleNYAHSYP--------------------DELSGGMR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 163 RKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHDREFIHKLATRIIDLDRGVITSwPGNY 238
Cdd:PRK10070 171 QRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAkhqrTIVFISHDLDEAMRIGDRIAIMQNGEVVQ-VGTP 249
|
....
gi 1411607396 239 DEYL 242
Cdd:PRK10070 250 DEIL 253
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
319-472 |
5.25e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.86 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTL-FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGGtklEVAY--------- 386
Cdd:PRK13639 1 ILETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGevLIKGE---PIKYdkksllevr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 387 ------FDQYRDQLDPEQTVMD------NVGEGKQEvmVRGRSRHILGYLQDFLFEPKrartPVKALSGGEKNRLLLAKL 454
Cdd:PRK13639 78 ktvgivFQNPDDQLFAPTVEEDvafgplNLGLSKEE--VEKRVKEALKAVGMEGFENK----PPHHLSGGQKKRVAIAGI 151
|
170
....*....|....*...
gi 1411607396 455 FLKPSNLLILDEPTNDLD 472
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLD 169
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
316-475 |
5.61e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 62.14 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 316 GKLVFEteglGLDFG---DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL-EVAYfDQY 390
Cdd:COG5265 356 GEVRFE----NVSFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILiDGQDIrDVTQ-ASL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RDQLD--PEQTVM------DNVGEGK-----QEVMVRGRSRHILGYLQDFlfePKRARTPV-----KaLSGGEKNRLLLA 452
Cdd:COG5265 431 RAAIGivPQDTVLfndtiaYNIAYGRpdaseEEVEAAARAAQIHDFIESL---PDGYDTRVgerglK-LSGGEKQRVAIA 506
|
170 180
....*....|....*....|...
gi 1411607396 453 KLFLKPSNLLILDEPTNDLDVET 475
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRT 529
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
330-472 |
6.13e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.59 E-value: 6.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVA--------YFDQYRDQLDPE 397
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGsvLIRGEpiTKENIRevrkfvglVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 398 QTVMD------NVGEGKQEVMVRGRSR-HILGylqdflFEPKRARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK13652 95 TVEQDiafgpiNLGLDEETVAHRVSSAlHMLG------LEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
..
gi 1411607396 471 LD 472
Cdd:PRK13652 168 LD 169
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-222 |
6.49e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.79 E-value: 6.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelpLDDGRMVQQQDLKVTRLEQDPPASSDLTVFDytaeglagVGEL 97
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAG---LDDGSSGEVSLVGQPLHQMDEEARAKLRAKH--------VGFV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 98 LKKYHHISMELAHDpsdaNIRIMSDLQEQLDYQNgwqfETRISQVLTLLNLDP--DATLDSLSGGWLRKVALARALACDP 175
Cdd:PRK10584 94 FQSFMLIPTLNALE----NVELPALLRGESSRQS----RNGAKALLEQLGLGKrlDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 176 DLLLLDEPTNHLDIEAINWLEDFL----KDFRGAIVFISHDREfihkLATR 222
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQ----LAAR 212
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
330-472 |
7.30e-10 |
|
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: 58.72 E-value: 7.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSR--GLVK-GGTKLE-------VAYFDQyRDQLDPEQT 399
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLiNGRPLDkrsfrkiIGYVPQ-DDILHPTLT 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 400 VmdnvgegkQEVMvrgrsrhilgylqdfLFEPKrartpVKALSGGEKNRLLLA-KLFLKPSnLLILDEPTNDLD 472
Cdd:cd03213 99 V--------RETL---------------MFAAK-----LRGLSGGERKRVSIAlELVSNPS-LLFLDEPTSGLD 143
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-214 |
7.69e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPlddgrmvqqQDLkvtrleqdppaSSDL 81
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP---------QGY-----------SNDL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 TVFDYTaeglAGVGELL---KKyhHI-----SMELAHDPSdANIR--IMS-------------DLQEQLDYQngWqfetr 138
Cdd:PRK10938 319 TLFGRR----RGSGETIwdiKK--HIgyvssSLHLDYRVS-TSVRnvILSgffdsigiyqavsDRQQKLAQQ--W----- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 139 isqvLTLLNLD---PDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDieAIN------WLEDFLKDFRGAIVFI 209
Cdd:PRK10938 385 ----LDILGIDkrtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD--PLNrqlvrrFVDVLISEGETQLLFV 458
|
....*
gi 1411607396 210 SHDRE 214
Cdd:PRK10938 459 SHHAE 463
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-188 |
7.80e-10 |
|
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: 58.72 E-value: 7.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP--------LDDGRMVQQQDLK--VTRLEQDPPASSD 80
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglgvsgevLINGRPLDKRSFRkiIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 81 LTVfdytaeglagvgellkkyhhismelahdpsdanirimsdlQEQLDYQngwqfetrisqvltllnldpdATLDSLSGG 160
Cdd:cd03213 97 LTV----------------------------------------RETLMFA---------------------AKLRGLSGG 115
|
170 180
....*....|....*....|....*...
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:cd03213 116 ERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
309-472 |
8.26e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 59.67 E-value: 8.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 309 MDDVNRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLL--LGQLEPS-RglVKGgtklEVA 385
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGaR--VEG----EIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 386 YFDQ--YRDQLDPEQ-----------------TVMDNVGEGkqeVMVRG-RSRHILgylqDFLFEP--KRA--------- 434
Cdd:COG1117 75 LDGEdiYDPDVDVVElrrrvgmvfqkpnpfpkSIYDNVAYG---LRLHGiKSKSEL----DEIVEEslRKAalwdevkdr 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1411607396 435 -RTPVKALSGGEKNRLLLAK-LFLKPSNLLiLDEPTNDLD 472
Cdd:COG1117 148 lKKSALGLSGGQQQRLCIARaLAVEPEVLL-MDEPTSALD 186
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
329-474 |
8.94e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 59.34 E-value: 8.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKlLLGQLEPSRG---LVKG----GTKLEV--------AYFDQYrdQ 393
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLR-CINKLEEITSgdlIVDGlkvnDPKVDErlirqeagMVFQQF--Y 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 LDPEQTVMDNVGEGKqeVMVRGRSRHILGYLQDFLFE----PKRARTPVKALSGGEKNRLLLAK-LFLKPsNLLILDEPT 468
Cdd:PRK09493 88 LFPHLTALENVMFGP--LRVRGASKEEAEKQARELLAkvglAERAHHYPSELSGGQQQRVAIARaLAVKP-KLMLFDEPT 164
|
....*.
gi 1411607396 469 NDLDVE 474
Cdd:PRK09493 165 SALDPE 170
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-209 |
9.08e-10 |
|
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: 58.52 E-value: 9.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTRleqDPPASSDLtvfdYT--AEGLAG 93
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrWNGTPLAEQR---DEPHENIL----YLghLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 94 ---VGELLKKYHHIsmelaHDPSDANIrimsdlqeqldyqngwqfetriSQVLTLLNLD--PDATLDSLSGGWLRKVALA 168
Cdd:TIGR01189 87 elsALENLHFWAAI-----HGGAQRTI----------------------EDALAAVGLTgfEDLPAAQLSAGQQRRLALA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1411607396 169 RALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFI 209
Cdd:TIGR01189 140 RLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlaRGGIVLL 182
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
325-497 |
9.48e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 325 LGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV----KGGTKLEVAYFDQ-----YRDQLD 395
Cdd:PRK13540 7 LDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferQSIKKDLCTYQKQlcfvgHRSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 PEQTVMDN------VGEGKQEV--MVRGRSrhiLGYLQDFlfepkrartPVKALSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:PRK13540 87 PYLTLRENclydihFSPGAVGIteLCRLFS---LEHLIDY---------PCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 1411607396 468 TNDLD---VETLELLEELLADYPGTLLLVSHDR 497
Cdd:PRK13540 155 LVALDelsLLTIITKIQEHRAKGGAVLLTSHQD 187
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-233 |
9.65e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.13 E-value: 9.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 14 SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDL-----------KVTRLEQDPPAS-SDL 81
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirhKIGMVFQNPDNQfVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 TVFDYTAEGLAGVGellkkyhhismeLAHDpsdaniRIMSDLQEQLDYQNGWQFETRisqvltllnlDPDatldSLSGGW 161
Cdd:PRK13650 98 TVEDDVAFGLENKG------------IPHE------EMKERVNEALELVGMQDFKER----------EPA----RLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIhKLATRIIDLDRGVITS 233
Cdd:PRK13650 146 KQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVES 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
331-472 |
9.96e-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: 59.21 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQL---------------EPSRGLVKGgtklEVAYFDQYrDQLD 395
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVegggttsgqilfngqPRKPDQFQK----CVAYVRQD-DILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 PEQTVMDNV-------------GEGKQEVMVRGRSRHIlgylqdflfEPKRARTP-VKALSGGEKNRLLLAKLFLKPSNL 461
Cdd:cd03234 94 PGLTVRETLtytailrlprkssDAIRKKRVEDVLLRDL---------ALTRIGGNlVKGISGGERRRVSIAVQLLWDPKV 164
|
170
....*....|.
gi 1411607396 462 LILDEPTNDLD 472
Cdd:cd03234 165 LILDEPTSGLD 175
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-231 |
1.00e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.00 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVqqqdlkVTRLEQ-DP---PASSDLTVFDYTAEGLA 92
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL------VSGIDTgDFsklQGIRKLVGIVFQNPETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 93 GVGELLKKyhhismELAHDPSDANIRIMsdlqeqldyqngwQFETRISQVLTLLNLDP--DATLDSLSGGWLRKVALARA 170
Cdd:PRK13644 90 FVGRTVEE------DLAFGPENLCLPPI-------------EIRKRVDRALAEIGLEKyrHRSPKTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 171 LACDPDLLLLDEPTNHLDIEA-INWLEDFLKDFRGA--IVFISHDREFIHkLATRIIDLDRGVI 231
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGktIVYITHNLEELH-DADRIIVMDRGKI 213
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-253 |
1.03e-09 |
|
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: 59.69 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 29 GERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtrleQDPPASSD-LTVFDYTAeglagVGELLKKYHHISME 107
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKF------------DDPPDWDEiLDEFRGSE-----LQNYFTKLLEGDVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 108 LAHDPS---------DANIRimsDLQEQLDYQNgwQFETRISQvltlLNLDP--DATLDSLSGGWLRKVALARALACDPD 176
Cdd:cd03236 89 VIVKPQyvdlipkavKGKVG---ELLKKKDERG--KLDELVDQ----LELRHvlDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 177 LLLLDEPTNHLDI----EAINWLEDFLKDFRgAIVFISHDREFIHKLATRIIDL-----DRGVITSWPG---NYDEYLQG 244
Cdd:cd03236 160 FYFFDEPSSYLDIkqrlNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLygepgAYGVVTLPKSvreGINEFLDG 238
|
250
....*....|.
gi 1411607396 245 --KEEALRVEE 253
Cdd:cd03236 239 ylPTENMRFRE 249
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
344-473 |
1.32e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 344 RGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKG------------GT------------KLEVAYFDQYRDQLdPEQt 399
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEepswdevlkrfrGTelqnyfkklyngEIKVVHKPQYVDLI-PKV- 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 400 VMDNVGEGKQEVMVRGRSRHILGYLQdflFEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13409 176 FKGKVRELLKKVDERGKLDEVVERLG---LENILDR-DISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
323-475 |
1.33e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.33 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGL-------VKG-GTKLEVAYFDqyrDQL 394
Cdd:PRK11248 5 SHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSitldgkpVEGpGAERGVVFQN---EGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 DPEQTVMDNVGEGKQEVMV-----RGRSRHILGYLQDFLFEPKRartpVKALSGGEKNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:PRK11248 82 LPWRNVQDNVAFGLQLAGVekmqrLEIAHQMLKKVGLEGAEKRY----IWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
....*.
gi 1411607396 470 DLDVET 475
Cdd:PRK11248 158 ALDAFT 163
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
345-474 |
1.35e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.87 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 345 GDKIALVGPNGCGKSTLIKlLLGQLE-PSRGlvkggtKLEVA--YFD----------------------QYrdQLDPEQT 399
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLR-VLNLLEmPRSG------TLNIAgnHFDfsktpsdkairelrrnvgmvfqQY--NLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 400 VMDNV--------GEGKQEVMvrGRSRHILGYLQdflFEPKRARTPVKaLSGGEKNRLLLAK-LFLKPSNLLiLDEPTND 470
Cdd:PRK11124 99 VQQNLieapcrvlGLSKDQAL--ARAEKLLERLR---LKPYADRFPLH-LSGGQQQRVAIARaLMMEPQVLL-FDEPTAA 171
|
....
gi 1411607396 471 LDVE 474
Cdd:PRK11124 172 LDPE 175
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-229 |
1.61e-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: 57.86 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSD-----FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrMVQQQDlKVTRLEQDPPAS 78
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG-SVSVPG-SIAYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 79 SDlTVFDytaeglagvgellkkyhhismelahdpsdaNIRIMSDLQEQldyqngwqfetRISQVLTLLNLDPD-ATLD-- 155
Cdd:cd03250 79 NG-TIRE------------------------------NILFGKPFDEE-----------RYEKVIKACALEPDlEILPdg 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 ----------SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLED-----FLKDFRgAIVFISHDREFIHKlA 220
Cdd:cd03250 117 dlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncilgLLLNNK-TRILVTHQLQLLPH-A 194
|
....*....
gi 1411607396 221 TRIIDLDRG 229
Cdd:cd03250 195 DQIVVLDNG 203
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-231 |
1.80e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 57.92 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmvqQQDLKVTRleqdppassdltvfdytaeglagv 94
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-----------HPKYEVTE------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 95 GELLKKYHHISMELAHDPSDANIRIMsdlqeqldyqngWQFETRISQVLT---LLNLDpdatlDSLSGGWLRKVALARAL 171
Cdd:cd03217 57 GEILFKGEDITDLPPEERARLGIFLA------------FQYPPEIPGVKNadfLRYVN-----EGFSGGEKKRNEILQLL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 172 ACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFI-HKLATRIIDLDRGVI 231
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLLdYIKPDRVHVLYDGRI 183
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-247 |
1.86e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.91 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqQQDLKVTRLEQDppassdltVFDYTAEG 90
Cdd:PRK14246 18 LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKI--KVDGKVLYFGKD--------IFQIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 91 L-AGVGELLKK---YHHISM--ELAHDPSDANIR----IMSDLQEQLDYQNGWQfetrisQVLTLLNldpdATLDSLSGG 160
Cdd:PRK14246 88 LrKEVGMVFQQpnpFPHLSIydNIAYPLKSHGIKekreIKKIVEECLRKVGLWK------EVYDRLN----SPASQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISHDREFIHKLATRIIDLDRGVITSWPGNY 238
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSN 237
|
....*....
gi 1411607396 239 DEYLQGKEE 247
Cdd:PRK14246 238 EIFTSPKNE 246
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
329-472 |
1.92e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.66 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKL-EVA--------YFDQYrdQLDPEQ 398
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGdLFIGEKRMnDVPpaergvgmVFQSY--ALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 TVMDNV-------GEGKQEvmVRGRSRHILGYLQ-DFLFEpkraRTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK11000 91 SVAENMsfglklaGAKKEE--INQRVNQVAEVLQlAHLLD----RKP-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
..
gi 1411607396 471 LD 472
Cdd:PRK11000 164 LD 165
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-231 |
1.95e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.92 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmvqqqdlkvtrLEQdpPASSDLtv 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-------------------LET--PSAGEL-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 fdytaegLAGVGELlkkyhhismelaHDPSDaNIRIMsdLQEQ-------------LDYQNGWQFETRisQVLTLLNLDP 150
Cdd:PRK11247 70 -------LAGTAPL------------AEARE-DTRLM--FQDArllpwkkvidnvgLGLKGQWRDAAL--QALAAVGLAD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 DAT--LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:PRK11247 126 RANewPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVL 205
|
....*..
gi 1411607396 225 DLDRGVI 231
Cdd:PRK11247 206 LIEEGKI 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
337-473 |
2.20e-09 |
|
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: 57.76 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtKLEVAYFDQYRDQLD---------------PEQTVM 401
Cdd:cd03266 23 GVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG------FATVDGFDVVKEPAEarrrlgfvsdstglyDRLTAR 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 402 DNVG-----EGKQEVMVRGRSRHILGYLQdflFEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03266 97 ENLEyfaglYGLKGDELTARLEELADRLG---MEELLDR-RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
331-475 |
2.43e-09 |
|
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: 56.78 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqLEPSR-GLVKGGTKLEVAYFDQ--Yrdqldpeqtvmdnvgeg 407
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWGsGRIGMPEGEDLLFLPQrpY----------------- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 408 kqevMVRGRSRHILGYLQDflfepkrartpvKALSGGEKNRLLLAKLFL-KPSnLLILDEPTNDLDVET 475
Cdd:cd03223 75 ----LPLGTLREQLIYPWD------------DVLSGGEQQRLAFARLLLhKPK-FVFLDEATSALDEES 126
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
320-548 |
2.52e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.54 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRD-----Q 393
Cdd:PRK10419 13 YAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwRGEPLAKLNRAQRKAfrrdiQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 L---------DPEQTVMDNVGEGKQEVMV---RGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNL 461
Cdd:PRK10419 93 MvfqdsisavNPRKTVREIIREPLRHLLSldkAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 462 LILDEPTNDLDVETLELLEELLADYP---GT-LLLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYADMM---ATRAQQS 534
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQqqfGTaCLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFsspAGRVLQN 252
|
250
....*....|....
gi 1411607396 535 TQLAAKAAQVKTPE 548
Cdd:PRK10419 253 AVLPAFPVRRRTTE 266
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
149-232 |
2.66e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 149 DPDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISHDREFIHKLATRIID 225
Cdd:PRK15439 396 HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAqnvAVLFISSDLEEIEQMADRVLV 475
|
....*..
gi 1411607396 226 LDRGVIT 232
Cdd:PRK15439 476 MHQGEIS 482
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
336-468 |
2.80e-09 |
|
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: 58.07 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG----------------LVKGGtkleVAYFDQYRdQLDPEQT 399
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsirfdgeditglpphrIARLG----IGYVPEGR-RIFPSLT 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 400 VMDN--VGegkqevMVRGRSRHILGYLQDFLFE--PK---RARTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPT 468
Cdd:COG0410 95 VEENllLG------AYARRDRAEVRADLERVYElfPRlkeRRRQRAGTLSGGEQQMLAIGRaLMSRPK-LLLLDEPS 164
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-232 |
2.81e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.65 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTrleqDPPASSDLTVF----DYTAEGL 91
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIrLDGKPVRIR----SPRDAIRAGIAyvpeDRKGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 92 AG---VGEllkkyhHISmeLAHDPSDANIRIMSDLQEQldyqngwqfeTRISQVLTLLNL---DPDATLDSLSGGWLRKV 165
Cdd:COG1129 342 VLdlsIRE------NIT--LASLDRLSRGGLLDRRRER----------ALAEEYIKRLRIktpSPEQPVGNLSGGNQQKV 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 166 ALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RG-AIVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:COG1129 404 VLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELaaEGkAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
14-231 |
2.84e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.22 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 14 SDFPL-LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM------VQQQDLKVTRLE-----QDPPASsdl 81
Cdd:PRK13648 19 SDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaITDDNFEKLRKHigivfQNPDNQ--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 tvFdytaeglagVGELLKKYHHISMELAHDPSDANIRIMSDLQEQLDYQNGWQFETRisqvltllnldpdatldSLSGGW 161
Cdd:PRK13648 96 --F---------VGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPN-----------------ALSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG----AIVFISHD-REFIHklATRIIDLDRGVI 231
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHDlSEAME--ADHVIVMNKGTV 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
326-472 |
2.97e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.60 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 326 GLDFGDRTLFqGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKL---------------EVAYFDQY 390
Cdd:PRK13649 15 GTPFEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirkKVGLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RDQLDPEQTVMDNVGEGKQ-------EVMVRGRSRHILGYLQDFLFEpkraRTPVKaLSGGEKNRLLLAKLFLKPSNLLI 463
Cdd:PRK13649 94 PESQLFEETVLKDVAFGPQnfgvsqeEAEALAREKLALVGISESLFE----KNPFE-LSGGQMRRVAIAGILAMEPKILV 168
|
....*....
gi 1411607396 464 LDEPTNDLD 472
Cdd:PRK13649 169 LDEPTAGLD 177
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-189 |
3.04e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.31 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFSDF-----PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQqdlkvTRLEQDPPASSDL--TV 83
Cdd:TIGR01271 429 LFFSNFslyvtPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS-----GRISFSPQTSWIMpgTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 FDYTAEGLAgvgelLKKYHHISMelahdpsdanirimsdlqeqldyQNGWQFETRISQvltLLNLDPDATLD---SLSGG 160
Cdd:TIGR01271 504 KDNIIFGLS-----YDEYRYTSV-----------------------IKACQLEEDIAL---FPEKDKTVLGEggiTLSGG 552
|
170 180
....*....|....*....|....*....
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDI 189
Cdd:TIGR01271 553 QRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-226 |
3.36e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.17 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtRLEQDPPASSDL 81
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI---------QIDGKTATRGDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 TvfdytaeglagvgellkkyHHISMeLAHDPSdanirIMSDLQ--EQLDYQNGWQ---FETRISQVLTLLNLD--PDATL 154
Cdd:PRK13543 81 S-------------------RFMAY-LGHLPG-----LKADLStlENLHFLCGLHgrrAKQMPGSALAIVGLAgyEDTLV 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 155 DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVFISHDREFIHKLATRIIDL 226
Cdd:PRK13543 136 RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
319-472 |
3.84e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 58.32 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRT-LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV-----------KGGTKLEVA- 385
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrKGLMKLRESv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 386 --YFDQYRDQLDPEQTVMD------NVGEGKQEvmVRGRSRHILGYLQdflFEPKRARtPVKALSGGEKNRLLLAKLFLK 457
Cdd:PRK13636 85 gmVFQDPDNQLFSASVYQDvsfgavNLKLPEDE--VRKRVDNALKRTG---IEHLKDK-PTHCLSFGQKKRVAIAGVLVM 158
|
170
....*....|....*
gi 1411607396 458 PSNLLILDEPTNDLD 472
Cdd:PRK13636 159 EPKVLVLDEPTAGLD 173
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-211 |
3.85e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.73 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGElP----LDDGRMVQQQDLkvtrLEQDPPASSDLTV---F 84
Cdd:CHL00131 16 SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PaykiLEGDILFKGESI----LDLEPEERAHLGIflaF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 85 DYTAEgLAGVG--ELLKkyhhismeLAHdpsdaNIRIMSDLQEQLDyqnGWQFETRISQVLTLLNLDPD----ATLDSLS 158
Cdd:CHL00131 91 QYPIE-IPGVSnaDFLR--------LAY-----NSKRKFQGLPELD---PLEFLEIINEKLKLVGMDPSflsrNVNEGFS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISH 211
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTsenSIILITH 209
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-231 |
4.56e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 29 GERLCLVGRNGAGKST----LMKII---AGELPLDDGRMVQQQDLKVTRLE-------QDPPASSD--LTVFDYTAEGLa 92
Cdd:PRK10261 350 GETLSLVGESGSGKSTtgraLLRLVesqGGEIIFNGQRIDTLSPGKLQALRrdiqfifQDPYASLDprQTVGDSIMEPL- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 93 gvgellkkyhhismelahdpsdaniRIMSDLQeqldyqnGWQFETRISQVLTLLNLDPDATL---DSLSGGWLRKVALAR 169
Cdd:PRK10261 429 -------------------------RVHGLLP-------GKAAAARVAWLLERVGLLPEHAWrypHEFSGGQRQRICIAR 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 170 ALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK10261 477 ALALNPKVIIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-189 |
5.02e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.49 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 5 TLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDL----------KVTRLEQ 73
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEiLLDAQPLeswsskafarKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 74 DPPASSDLTVFDYTAEGLAGVGELLKKYhhismelahdpsdanirimsdlqeqldyqnGWQFETRISQVLTLLNLDPDAT 153
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRYPWHGALGRF------------------------------GAADREKVEEAISLVGLKPLAH 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 1411607396 154 --LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI 189
Cdd:PRK10575 143 rlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-467 |
5.76e-09 |
|
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: 56.78 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVayfdQYRDQLD 395
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGkiLLDGQdiTKLPM----HKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 ----PEQ-------TVMDN---VGEGkQEVMVRGRSRHILGYLQDFLFEPKRaRTPVKALSGGEKNRLLLAK-LFLKPSN 460
Cdd:cd03218 77 igylPQEasifrklTVEENilaVLEI-RGLSKKEREEKLEELLEEFHITHLR-KSKASSLSGGERRRVEIARaLATNPKF 154
|
....*..
gi 1411607396 461 LLiLDEP 467
Cdd:cd03218 155 LL-LDEP 160
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-229 |
6.07e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.53 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPlddgrmvqqqdlkvtrleqdpPASSDLTVFDY--TAE-GLAGVG 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLK---------------------PSSGTITIAGYhiTPEtGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 96 ELLKKyhhisMELAHDPSDANI---RIMSDLQ---------EQLDYQNGWQFETRISQVLTLLNLDPDatldSLSGGWLR 163
Cdd:PRK13641 82 KLRKK-----VSLVFQFPEAQLfenTVLKDVEfgpknfgfsEDEAKEKALKWLKKVGLSEDLISKSPF----ELSGGQMR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
330-472 |
6.41e-09 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 56.93 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKlEVAYFDQ--------YRDQ---LDPEQ 398
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE-DIREQDPvelrrkigYVIQqigLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 TVMDNVG-----EGKQEVMVRGRSRHILGYLQdflFEPK--RARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:cd03295 91 TVEENIAlvpklLKWPKEKIRERADELLALVG---LDPAefADRYP-HELSGGQQQRVGVARALAADPPLLLMDEPFGAL 166
|
.
gi 1411607396 472 D 472
Cdd:cd03295 167 D 167
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-226 |
6.48e-09 |
|
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: 56.35 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQdlkvtrleqdppassdltvfdytaeglAGVGEL 97
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG---------------------------GPLDFQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 98 LKKYHHISMELAHDPSdanIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLD--PDATLDSLSGGWLRKVALARALACDP 175
Cdd:cd03231 68 RDSIARGLLYLGHAPG---IKTTLSVLENLRFWHADHSDEQVEEALARVGLNgfEDRPVAQLSAGQQRRVALARLLLSGR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 176 DLLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDREFIHKLATRIIDL 226
Cdd:cd03231 145 PLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTHQDLGLSEAGARELDL 198
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-216 |
6.62e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP-LDDGRMVQQQDLKVTR----LEQDP 75
Cdd:COG2401 28 AIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgTPVAGCVDVPDNQFGReaslIDAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 76 PASSDLTVFDY-TAEGLAGVGELLKKYHHISmelahdpsdanirimsdlqeqldyqNGWQFetrisqvltllnldpdatl 154
Cdd:COG2401 108 RKGDFKDAVELlNAVGLSDAVLWLRRFKELS-------------------------TGQKF------------------- 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 155 dslsggwlrKVALARALACDPDLLLLDEPTNHLD-----IEAINWLEdFLKDFRGAIVFISHDREFI 216
Cdd:COG2401 144 ---------RFRLALLLAERPKLLVIDEFCSHLDrqtakRVARNLQK-LARRAGITLVVATHHYDVI 200
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
329-497 |
6.71e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 57.85 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLE---------VAY-FDQYrdQLDPE 397
Cdd:COG1118 12 FGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVlNGRDLFtnlpprerrVGFvFQHY--ALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 398 QTVMDNVGEGKQevmVRGRSRH-----ILGYLQDFLFEPKRARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDL 471
Cdd:COG1118 90 MTVAENIAFGLR---VRPPSKAeirarVEELLELVQLEGLADRYP-SQLSGGQRQRVALARaLAVEPE-VLLLDEPFGAL 164
|
170 180 190
....*....|....*....|....*....|
gi 1411607396 472 DV----ETLELLEELLADYPGTLLLVSHDR 497
Cdd:COG1118 165 DAkvrkELRRWLRRLHDELGGTTVFVTHDQ 194
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-520 |
7.36e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.84 E-value: 7.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLL--LGQLEPsRGLVKGGT--------KLEVAYFD 388
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYP-EARVSGEVyldgqdifKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 389 QyRDQL-------DPEQTVMDNVGEG-------KQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKL 454
Cdd:PRK14247 82 R-RVQMvfqipnpIPNLSIFENVALGlklnrlvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 455 FLKPSNLLILDEPTNDLDVETLELLEELLADYPG--TLLLVSHdrrfidntvtgcwlFEGD-GRISDYV 520
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH--------------FPQQaARISDYV 215
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
320-516 |
7.49e-09 |
|
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: 57.12 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGG----TKLEVAYFDQYRDQL- 394
Cdd:TIGR02769 12 YRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqdlYQLDRKQRRAFRRDVq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 ----------DPEQTVMDNVGEGKQEVM---VRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAK-LFLKPsN 460
Cdd:TIGR02769 92 lvfqdspsavNPRMTVRQIIGEPLRHLTsldESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARaLAVKP-K 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 461 LLILDEPTNDLDV----ETLELLEELLADYPGTLLLVSHDRRFIDNTVTGCWLFEGdGRI 516
Cdd:TIGR02769 171 LIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK-GQI 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
17-227 |
8.05e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.97 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRmVQQQDLKVTRleQDPPASSDLTVFDYtaegLAGVGE 96
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGE-VLWQGEPIRR--QRDEYHQDLLYLGH----QPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 97 LLKkyhhismelahdpSDANIRIMSDLQEQLDyqngwqfETRISQVLTLLNLD--PDATLDSLSGGWLRKVALARALACD 174
Cdd:PRK13538 88 ELT-------------ALENLRFYQRLHGPGD-------DEALWEALAQVGLAgfEDVPVRQLSAGQQRRVALARLWLTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 175 PDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIV-FISHDREFIHKLATRIIDLD 227
Cdd:PRK13538 148 APLWILDEPFTAIDKQGVARLEALLAQHaeQGGMViLTTHQDLPVASDKVRKLRLG 203
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-188 |
8.47e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.32 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLddgrmvqQQDLKVTRLEQdppasSDLTVFDYTAEg 90
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-------QGSLKINGIEL-----RELDPESWRKH- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 91 LAGVGE---LLKKYHHISMELA-HDPSDAnirimsDLQEQLDYQNGWQFETRISQVLTLLNLDPDATLdslSGGWLRKVA 166
Cdd:PRK11174 425 LSWVGQnpqLPHGTLRDNVLLGnPDASDE------QLQQALENAWVSEFLPLLPQGLDTPIGDQAAGL---SVGQAQRLA 495
|
170 180
....*....|....*....|..
gi 1411607396 167 LARALACDPDLLLLDEPTNHLD 188
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLD 517
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
345-473 |
1.05e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.61 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 345 GDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKG------------GTKLEvAYFD-------------QYRDQLdPEQt 399
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDppdwdeildefrGSELQ-NYFTkllegdvkvivkpQYVDLI-PKA- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 400 VMDNVGegkqEVMVRGRSRHILGYLQDFL-FEPKRARTpVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03236 103 VKGKVG----ELLKKKDERGKLDELVDQLeLRHVLDRN-IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-233 |
1.05e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.53 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIA-------GELPLDDGRMVQQQDLKVTR----LEQDPPASS 79
Cdd:PRK10253 15 LGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahGHVWLDGEHIQHYASKEVARriglLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 80 DLTVFDYTAEGlagvgellkKYhhismelAHDPSDANIRimsdlQEQLDYQNGWQFETRISQVltllnldPDATLDSLSG 159
Cdd:PRK10253 95 DITVQELVARG---------RY-------PHQPLFTRWR-----KEDEEAVTKAMQATGITHL-------ADQSVDTLSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 160 GWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:PRK10253 147 GQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
334-475 |
1.12e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.38 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 334 LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKleVAYFDQYrDQLDPeQTVMDNVGEGKQEVMV 413
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSPQT-SWIMP-GTIKDNIIFGLSYDEY 516
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 414 RGRSrhILGYLQ---DFLFEPKRARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:TIGR01271 517 RYTS--VIKACQleeDIALFPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
316-475 |
1.17e-08 |
|
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: 55.13 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 316 GKLVFETEGLGLdfgdRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGGT----------KLE 383
Cdd:cd03215 1 GEPVLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGeiTLDGKPvtrrsprdaiRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 384 VAYF--DQYRDQLDPEQTVMDNVgegkqevmvrgrsrhILGYLqdflfepkrartpvkaLSGGEKNRLLLAKLFLKPSNL 461
Cdd:cd03215 77 IAYVpeDRKREGLVLDLSVAENI---------------ALSSL----------------LSGGNQQKVVLARWLARDPRV 125
|
170
....*....|....
gi 1411607396 462 LILDEPTNDLDVET 475
Cdd:cd03215 126 LILDEPTRGVDVGA 139
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
329-499 |
1.20e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.52 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV------------KGGtKLEVAYFDQYRD---- 392
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtinlvrdKDG-QLKVADKNQLRLlrtr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 --------QLDPEQTVMDNVGEGKQEVM----VRGRSRHILGYLQDFLFEPKRARTPVKaLSGGEKNRLLLAKLFLKPSN 460
Cdd:PRK10619 94 ltmvfqhfNLWSHMTVLENVMEAPIQVLglskQEARERAVKYLAKVGIDERAQGKYPVH-LSGGQQQRVSIARALAMEPE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1411607396 461 LLILDEPTNDLDVE---TLELLEELLADYPGTLLLVSHDRRF 499
Cdd:PRK10619 173 VLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGF 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
345-474 |
1.25e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 56.17 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 345 GDKIALVGPNGCGKSTLIKLL-------LGQLE--------PSRGLVKGGTKL--EVAY-FDQYrdQLDPEQTVMDNV-- 404
Cdd:COG4161 28 GETLVLLGPSGAGKSSLLRVLnlletpdSGQLNiaghqfdfSQKPSEKAIRLLrqKVGMvFQQY--NLWPHLTVMENLie 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 405 ------GEGKQEVmvRGRSRHILGYLQdflFEPKRARTPVkALSGGEKNRLLLAK-LFLKPSNLLiLDEPTNDLDVE 474
Cdd:COG4161 106 apckvlGLSKEQA--REKAMKLLARLR---LTDKADRFPL-HLSGGQQQRVAIARaLMMEPQVLL-FDEPTAALDPE 175
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
334-475 |
1.47e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 56.40 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 334 LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKleVAYFDQYrDQLDPeQTVMDNVGEGKQEVMV 413
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSSQF-SWIMP-GTIKENIIFGVSYDEY 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 414 RGRSRHILGYL-QDFLFEPKRARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03291 128 RYKSVVKACQLeEDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
337-473 |
1.50e-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: 56.60 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqLEPSRGLVKG-----G---TKLEVAYFDQYRDQ------------LDP 396
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGITSGeilfdGedlLKLSEKELRKIRGReiqmifqdpmtsLNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 397 EQTVMDNVGE--------GKQEVmvRGRSRHILG---------YLQDFLFEpkrartpvkaLSGGEKNRLLLAK-LFLKP 458
Cdd:COG0444 102 VMTVGDQIAEplrihgglSKAEA--RERAIELLErvglpdperRLDRYPHE----------LSGGMRQRVMIARaLALEP 169
|
170
....*....|....*
gi 1411607396 459 SnLLILDEPTNDLDV 473
Cdd:COG0444 170 K-LLIADEPTTALDV 183
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
321-471 |
1.58e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.49 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVkggTKLEVAYfdqyrDQLDPEQTV 400
Cdd:PRK09700 7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI---TINNINY-----NKLDHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEGKQEVMV-------------RGRSRHILGY-LQDFLFEPKRAR-------------TPVKALSGGEKNRLLLAK 453
Cdd:PRK09700 79 QLGIGIIYQELSVideltvlenlyigRHLTKKVCGVnIIDWREMRVRAAmmllrvglkvdldEKVANLSISHKQMLEIAK 158
|
170
....*....|....*...
gi 1411607396 454 LFLKPSNLLILDEPTNDL 471
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSL 176
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
329-500 |
1.66e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.27 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGG----TKL---EVAYFDQ-----YRD-QLD 395
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghdiTRLknrEVPFLRRqigmiFQDhHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 PEQTVMDNVGegkQEVMVRGRS-----RHILGYLQDFLFEPKRARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK10908 92 MDRTVYDNVA---IPLIIAGASgddirRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190
....*....|....*....|....*....|...
gi 1411607396 471 LDVETLELLEELLADYPG---TLLLVSHDRRFI 500
Cdd:PRK10908 168 LDDALSEGILRLFEEFNRvgvTVLMATHDIGLI 200
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
344-503 |
1.71e-08 |
|
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: 53.92 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 344 RGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKggtklevaYFDqyrdqldpeqtvmdnvGEGKQEVMVRGRSRHILGy 423
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI--------YID----------------GEDILEEVLDQLLLIIVG- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 424 lqdflfepkrarTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPGTLLLVSHDRRFIDNT 503
Cdd:smart00382 56 ------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTT 123
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-243 |
1.92e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.14 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 2 ALLTLHGACLSFSD--FPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIA-------GELPLDDgrmvqqQDLKvtrle 72
Cdd:PRK11160 337 VSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrawdpqqGEILLNG------QPIA----- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 qdppassdltvfDYTAEGL-AGVGELLKKYHHISMEL-------AHDPSDAnirimsdlqeqldyqngwQFETRISQV-L 143
Cdd:PRK11160 406 ------------DYSEAALrQAISVVSQRVHLFSATLrdnlllaAPNASDE------------------ALIEVLQQVgL 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 144 TLLnLDPDATLDS--------LSGGWLRKVALARALACDPDLLLLDEPTNHLDIEA---InwLEDFLKDFRG-AIVFISH 211
Cdd:PRK11160 456 EKL-LEDDKGLNAwlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqI--LELLAEHAQNkTVLMITH 532
|
250 260 270
....*....|....*....|....*....|...
gi 1411607396 212 DREFIHKLaTRIIDLDRG-VITSwpGNYDEYLQ 243
Cdd:PRK11160 533 RLTGLEQF-DRICVMDNGqIIEQ--GTHQELLA 562
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-231 |
1.98e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.48 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 4 LTLHGACLSfSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP----------LDDGRMVQQQDL---KVTR 70
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrqtagrvLLDGKPVAPCALrgrKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 71 LEQDPPASSD--LTVFDYTAEGLAGVGELlkkyhhismelahdPSDAnirimsdlqeqldyqngwqfetRISQVLTLLNL 148
Cdd:PRK10418 84 IMQNPRSAFNplHTMHTHARETCLALGKP--------------ADDA----------------------TLTAALEAVGL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 149 -DPDATLDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLDIEA----INWLEDFLKDFRGAIVFISHDREFIHKL 219
Cdd:PRK10418 128 eNAARVLKLypfeMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAqariLDLLESIVQKRALGMLLVTHDMGVVARL 207
|
250
....*....|..
gi 1411607396 220 ATRIIDLDRGVI 231
Cdd:PRK10418 208 ADDVAVMSHGRI 219
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-232 |
2.24e-08 |
|
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: 57.07 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP-------LDD-----------GRMV----QQQDL-------K 67
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPptagsvrLDGadlsqwdreelGRHIgylpQDVELfdgtiaeN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 68 VTRLEQDPPASsdltVFDytAEGLAGVGELlkkyhhismelahdpsdanirIMSdlqeqldYQNGwqFETRIsqvltlln 147
Cdd:COG4618 426 IARFGDADPEK----VVA--AAKLAGVHEM---------------------ILR-------LPDG--YDTRI-------- 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 148 ldpDATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD-------IEAInwleDFLKDFRGAIVFISHDREFIhKLA 220
Cdd:COG4618 462 ---GEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAI----RALKARGATVVVITHRPSLL-AAV 533
|
250
....*....|..
gi 1411607396 221 TRIIDLDRGVIT 232
Cdd:COG4618 534 DKLLVLRDGRVQ 545
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-226 |
2.50e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.11 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 2 ALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV-QQQDL----------KVTR 70
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLfEGEDIstlkpeiyrqQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 71 LEQDPPASSDlTVFDytaeglagvgELLKKYhhismELAHDPSDANiRIMSDLQeqldyqngwQFETrisqvltllnldP 150
Cdd:PRK10247 86 CAQTPTLFGD-TVYD----------NLIFPW-----QIRNQQPDPA-IFLDDLE---------RFAL------------P 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 DATLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIhKLATR 222
Cdd:PRK10247 128 DTILTkniaELSGGEKQRISLIRNLQFMPKVLLLDEITSALDesnkHNVNEIIHRYVREQNIAVLWVTHDKDEI-NHADK 206
|
....
gi 1411607396 223 IIDL 226
Cdd:PRK10247 207 VITL 210
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-229 |
2.63e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.40 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 12 SFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDD---------GRMVQQQ-----DLKVTRLE----- 72
Cdd:PRK09984 13 TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREgrlarDIRKSRANtgyif 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 QDPPASSDLTVFDYTAEGLAGVGELLKkyhhismelahdpsdANIRIMSDLQEQldyqngwqfetRISQVLTLLNLDPDA 152
Cdd:PRK09984 93 QQFNLVNRLSVLENVLIGALGSTPFWR---------------TCFSWFTREQKQ-----------RALQALTRVGMVHFA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 153 --TLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFIS-HDREFIHKLATRIIDL 226
Cdd:PRK09984 147 hqRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqndGITVVVTlHQVDYALRYCERIVAL 226
|
...
gi 1411607396 227 DRG 229
Cdd:PRK09984 227 RQG 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-229 |
2.67e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.33 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSDLTVFDYTAEGLAGvge 96
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTG--- 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 97 llKKYHHISMELAHDPSdanirimsdlqEQLDYQNGWQFETrisqvlTLLNLDPDATLDSLSGGWLRKVALARALACDPD 176
Cdd:TIGR01257 2030 --REHLYLYARLRGVPA-----------EEIEKVANWSIQS------LGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 177 LLLLDEPTNHLDIEA----INWLEDFLKDFRgAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQArrmlWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-237 |
2.68e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.04 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 2 ALLTLHGACLSF----SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIaGEL--PLDDGRMVQQQDlkVTRLEQDP 75
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLdkPTSGTYRVAGQD--VATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 76 PASSDLTVFdytaeglagvGELLKKYHHismeLAHDPSDANIRI---MSDLQEQldyqngwQFETRISQVLTLLNLDP-- 150
Cdd:PRK10535 80 LAQLRREHF----------GFIFQRYHL----LSHLTAAQNVEVpavYAGLERK-------QRLLRAQELLQRLGLEDrv 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 151 DATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDfLKDfRGAIVFI-SHDREfIHKLATRIID 225
Cdd:PRK10535 139 EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDshsgEEVMAILHQ-LRD-RGHTVIIvTHDPQ-VAAQAERVIE 215
|
250
....*....|..
gi 1411607396 226 LDRGVITSWPGN 237
Cdd:PRK10535 216 IRDGEIVRNPPA 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
311-521 |
2.84e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.44 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 311 DVNRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKleVAYFDQY 390
Cdd:PRK14246 2 EAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK--VLYFGKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RDQLD------------------PEQTVMDNVGEGKQEVMVRGRsRHILGYLQDFLFEP-------KRARTPVKALSGGE 445
Cdd:PRK14246 80 IFQIDaiklrkevgmvfqqpnpfPHLSIYDNIAYPLKSHGIKEK-REIKKIVEECLRKVglwkevyDRLNSPASQLSGGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 446 KNRLLLAK-LFLKPSnLLILDEPTNDLDVETLELLEELLADYPG--TLLLVSHDRRFIdntvtgcwlfegdGRISDYVG 521
Cdd:PRK14246 159 QQRLTIARaLALKPK-VLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQV-------------ARVADYVA 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-231 |
2.88e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 55.48 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTRLEQDPPASSDLtVFDYTAEGLagVGEL 97
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyVDGLDTSDEENLWDIRNKAGM-VFQNPDNQI--VATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 98 LKKyhhismELAHDPSDANI---RIMSDLQEQLDYQNGWQFETRISQVLtllnldpdatldslSGGWLRKVALARALACD 174
Cdd:PRK13633 103 VEE------DVAFGPENLGIppeEIRERVDESLKKVGMYEYRRHAPHLL--------------SGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 175 PDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKlATRIIDLDRGVI 231
Cdd:PRK13633 163 PECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-472 |
3.71e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 55.11 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLD----- 395
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSG--------EVLWDGEPLDPEDrrrig 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 396 --PE-------QTVMDNV-------GEGKQEVMVRGrsrhilgylqDFLFE----PKRARTPVKALSGGEKNRL-LLAKL 454
Cdd:COG4152 75 ylPEerglypkMKVGEQLvylarlkGLSKAEAKRRA----------DEWLErlglGDRANKKVEELSKGNQQKVqLIAAL 144
|
170
....*....|....*...
gi 1411607396 455 FLKPSnLLILDEPTNDLD 472
Cdd:COG4152 145 LHDPE-LLILDEPFSGLD 161
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-223 |
3.74e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.58 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSF--SDFPL--LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmVQQQDLKVT--RLEQD 74
Cdd:PRK15093 1 MPLLDIRNLTIEFktSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG---------VTKDNWRVTadRMRFD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 75 ppassDLTVFDYTA-EGLAGVGellkkyHHISMELAH-----DPSDaniRIMSDLQEQL---DYQNGW--QFETRISQVL 143
Cdd:PRK15093 72 -----DIDLLRLSPrERRKLVG------HNVSMIFQEpqsclDPSE---RVGRQLMQNIpgwTYKGRWwqRFGWRKRRAI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 144 TLLNL----DPDATLDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISH 211
Cdd:PRK15093 138 ELLHRvgikDHKDAMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEpttqAQIFRLLTRLNQNNNTTILLISH 217
|
250
....*....|..
gi 1411607396 212 DREFIHKLATRI 223
Cdd:PRK15093 218 DLQMLSQWADKI 229
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
281-495 |
3.98e-08 |
|
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: 56.30 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 281 NEGRVRALEAMRMERSQRRELQGKAKLQMDDvNRsgkLVFETEGLGLDFGDrTLFQGLDLQVLRGDKIALVGPNGCGKST 360
Cdd:TIGR00954 419 KRPRVEEIESGREGGRNSNLVPGRGIVEYQD-NG---IKFENIPLVTPNGD-VLIESLSFEVPSGNNLLICGPNGCGKSS 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 361 LIKLLlGQLEPSR-GLVKGGTKLEVAYFDQ--------YRDQL----DPEQTVMDNVGEGK-QEVMVRGRSRHIL----G 422
Cdd:TIGR00954 494 LFRIL-GELWPVYgGRLTKPAKGKLFYVPQrpymtlgtLRDQIiypdSSEDMKRRGLSDKDlEQILDNVQLTHILeregG 572
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 423 Y--LQDFLFEpkrartpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADYPGTLLLVSH 495
Cdd:TIGR00954 573 WsaVQDWMDV----------LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
11-211 |
4.59e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 54.30 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFS--DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG--ELPLDDGRM-VQQQDLkvTRLE------------- 72
Cdd:COG0396 6 LHVSveGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSIlLDGEDI--LELSpderaragiflaf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 QDPPASSDLTVFDytaeglagvgeLLKkyhhismeLAhdpsdanirIMSDLQEQLDYQngwQFETRISQVLTLLNLDPDA 152
Cdd:COG0396 84 QYPVEIPGVSVSN-----------FLR--------TA---------LNARRGEELSAR---EFLKLLKEKMKELGLDEDF 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 153 tLD-----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG---AIVFISH 211
Cdd:COG0396 133 -LDryvneGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpdrGILIITH 198
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-216 |
4.83e-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: 53.87 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 14 SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSDLTVfDYTAEglag 93
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSV-AYAAQ---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 94 vgellKKYhhismeLAHDPSDANIRIMSDLQEQldyqngwqfetRISQVLTLLNLDPDATL-------------DSLSGG 160
Cdd:cd03290 87 -----KPW------LLNATVEENITFGSPFNKQ-----------RYKAVTDACSLQPDIDLlpfgdqteigergINLSGG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLE-----DFLKDFRGAIVFISHDREFI 216
Cdd:cd03290 145 QRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqegilKFLQDDKRTLVLVTHKLQYL 205
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-223 |
4.95e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 55.30 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmVQQQDLKVTrleqdppasSDLTVFDytaeglaGVgELL 98
Cdd:COG4170 23 VDRVSLTLNEGEIRGLVGESGSGKSLIAKAICG---------ITKDNWHVT---------ADRFRWN-------GI-DLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 99 KKY---------HHISMeLAHDPS---DANIRIMSDLQEQLDYQNG----WQ-FETRISQVLTLLNL----DPDATLDS- 156
Cdd:COG4170 77 KLSprerrkiigREIAM-IFQEPSsclDPSAKIGDQLIEAIPSWTFkgkwWQrFKWRKKRAIELLHRvgikDHKDIMNSy 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 157 ---LSGGWLRKVALARALACDPDLLLLDEPTNHLdiEAINWLEDF-----LKDFRG-AIVFISHDREFIHKLATRI 223
Cdd:COG4170 156 pheLTEGECQKVMIAMAIANQPRLLIADEPTNAM--ESTTQAQIFrllarLNQLQGtSILLISHDLESISQWADTI 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
323-472 |
5.11e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 53.64 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEP---SRGLVkggtklevaYFDQYR-DQLDPEQ 398
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEV---------LLNGRRlTALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 ----------------TVMDNVGEGKQEVMVRG-RSRHILGYLQDFLFEPKRARTPvKALSGGEKNRL-LLAKLFLKPSN 460
Cdd:COG4136 76 rrigilfqddllfphlSVGENLAFALPPTIGRAqRRARVEQALEEAGLAGFADRDP-ATLSGGQRARVaLLRALLAEPRA 154
|
170
....*....|..
gi 1411607396 461 LLiLDEPTNDLD 472
Cdd:COG4136 155 LL-LDEPFSKLD 165
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
332-472 |
5.52e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 54.32 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 332 RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTklEVAYFDQYR----------DQLD---PE 397
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILiDGK--DVTKLPEYKrakyigrvfqDPMMgtaPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 398 QTVMDNV----GEGKQevmvRGRSRHILGYLQDFLFE---------PKRARTPVKALSGGEknR----LLLAKLflKPSN 460
Cdd:COG1101 97 MTIEENLalayRRGKR----RGLRRGLTKKRRELFREllatlglglENRLDTKVGLLSGGQ--RqalsLLMATL--TKPK 168
|
170
....*....|..
gi 1411607396 461 LLILDEPTNDLD 472
Cdd:COG1101 169 LLLLDEHTAALD 180
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-203 |
6.48e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.50 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-----MVQQQDLKVTRLEQDPPASSDLTVFDYTAEGLAG 93
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKisilgQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 94 VGellkKYHHisMELAHDPSDANIRIMSDLQEQLDYQngwqfETRISQVltllnldpdatlDSLSGGWLRKVALARALAC 173
Cdd:PRK15056 103 MG----RYGH--MGWLRRAKKRDRQIVTAALARVDMV-----EFRHRQI------------GELSGGQKKRVFLARAIAQ 159
|
170 180 190
....*....|....*....|....*....|
gi 1411607396 174 DPDLLLLDEPTNHLDIEAINWLEDFLKDFR 203
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELR 189
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
319-496 |
6.49e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.94 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDfGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLE-------------VA 385
Cdd:PRK10418 4 QIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDgkpvapcalrgrkIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 386 YFDQY-RDQLDPEQTVMDNVGEGKQEVMVRGRSRHILGYLQDF-LFEPKRA--RTPVKaLSGGEKNRLLLAKLFLKPSNL 461
Cdd:PRK10418 83 TIMQNpRSAFNPLHTMHTHARETCLALGKPADDATLTAALEAVgLENAARVlkLYPFE-MSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1411607396 462 LILDEPTNDLDVETLELLEELLADY-----PGtLLLVSHD 496
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIvqkraLG-MLLVTHD 200
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-229 |
7.06e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDG----RMVQQQDLKVTRL------- 71
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGevhyRMRDGQLRDLYALseaerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 72 ---------EQDPpassdltvfdytAEGL-------AGVGEllkkyhhismelahdpsdaniRIMSdlqeqldyqNGWQF 135
Cdd:PRK11701 86 llrtewgfvHQHP------------RDGLrmqvsagGNIGE---------------------RLMA---------VGARH 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 136 ETRI----SQVLTLLNLDPDATLD---SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLK----DFRG 204
Cdd:PRK11701 124 YGDIrataGDWLERVEIDAARIDDlptTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRglvrELGL 203
|
250 260
....*....|....*....|....*
gi 1411607396 205 AIVFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK11701 204 AVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
318-472 |
7.84e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.97 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 318 LVFETEGLGLDFGDRT-LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL- 394
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvMGREVNAENEKWVRSKVg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 ----DPEQ-----TVMD-------NVGEGKQEVMVRGRSRHILGYLQDFlfepkRARTPVKaLSGGEKNRLLLAKLFLKP 458
Cdd:PRK13647 83 lvfqDPDDqvfssTVWDdvafgpvNMGLDKDEVERRVEEALKAVRMWDF-----RDKPPYH-LSYGQKKRVAIAGVLAMD 156
|
170
....*....|....
gi 1411607396 459 SNLLILDEPTNDLD 472
Cdd:PRK13647 157 PDVIVLDEPMAYLD 170
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
11-189 |
8.49e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 54.09 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFSDF-----PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQqdlkvTRLEQDPPASSDL--TV 83
Cdd:cd03291 40 LFFSNLclvgaPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS-----GRISFSSQFSWIMpgTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 FDYTAEGLAgvgelLKKYHHISMELAhdpsdanirimSDLQEQLDyqngwQFETRISQVLTLLNLdpdatldSLSGGWLR 163
Cdd:cd03291 115 KENIIFGVS-----YDEYRYKSVVKA-----------CQLEEDIT-----KFPEKDNTVLGEGGI-------TLSGGQRA 166
|
170 180
....*....|....*....|....*.
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDI 189
Cdd:cd03291 167 RISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
321-374 |
9.69e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 53.62 E-value: 9.69e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG 374
Cdd:PRK11831 9 DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHG 62
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
157-231 |
1.06e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.09 E-value: 1.06e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR--GAIVF-ISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKanNKTVFvITHTMEHVLEVADEVIVMDKGKI 254
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-188 |
1.11e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 55.05 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP---------LDDGRMVQQQDLKV--TRLEQDppassDLTVFDY 86
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvkgsgsvLLNGMPIDAKEMRAisAYVQQD-----DLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 87 TAEglagvgELLKKYHHISMElahdpsdaniRIMSDLQEQLdyqngwqfetRISQVLTLLNLDPDA--------TLDSLS 158
Cdd:TIGR00955 115 TVR------EHLMFQAHLRMP----------RRVTKKEKRE----------RVDEVLQALGLRKCAntrigvpgRVKGLS 168
|
170 180 190
....*....|....*....|....*....|
gi 1411607396 159 GGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:TIGR00955 169 GGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-212 |
1.18e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.96 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFS----DFPLLDNAELSIERGERLCLVGRNGAGKS----TLMKIIA-----GELPLDDGRMV---QQQ 64
Cdd:PRK09473 10 DALLDVKDLRVTFStpdgDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAangriGGSATFNGREIlnlPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 65 DLKVTRLE------QDPPASsdLTVFDYTAEGLAgvgELLKKYHHISMELAHDPSdanIRImsdlqeqLDyqngwqfETR 138
Cdd:PRK09473 90 ELNKLRAEqismifQDPMTS--LNPYMRVGEQLM---EVLMLHKGMSKAEAFEES---VRM-------LD-------AVK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 139 ISQVLTLLNLDPDatldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----EAINWLEDFLKDFRGAIVFISHD 212
Cdd:PRK09473 148 MPEARKRMKMYPH----EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHD 221
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-224 |
1.21e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.22 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 28 RGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVqqqdlkvtrleqdppassdltvfdytaeglagvgellkkyhhisme 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------------- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 108 lAHDPSDANIRIMSDLQEQLDYQNGWQFEtRISQVltllnldpdatldslsggwlrKVALARALACDPDLLLLDEPTNHL 187
Cdd:smart00382 35 -YIDGEDILEEVLDQLLLIIVGGKKASGS-GELRL---------------------RLALALARKLKPDVLILDEITSLL 91
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1411607396 188 DIEA---------INWLEDFLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:smart00382 92 DAEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR 137
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-223 |
1.21e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELP--------LDDGRMVQQQDLKvtrleqdppassdltvfDYTAEG 90
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgsyegeiLFDGEVCRFKDIR-----------------DSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 91 LAgvgellkkyhHISMELAHDP--SDA-NIRIMSdlqEQLdyQNG---WQfETRISQVLTL----LNLDPDATLDSLSGG 160
Cdd:NF040905 80 IV----------IIHQELALIPylSIAeNIFLGN---ERA--KRGvidWN-ETNRRARELLakvgLDESPDTLVTDIGVG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPT---NHLDIEAinwLEDFLKDFRG---AIVFISHDREFIHKLATRI 223
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTaalNEEDSAA---LLDLLLELKAqgiTSIIISHKLNEIRRVADSI 209
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-233 |
1.47e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.58 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 13 FSDFPLLDnAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrMVQQQDLKVT----RLEQDPPASSDLTVFDYTA 88
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEG-KVTVGDIVVSstskQKEIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 89 EGLagVGELLKKyhhismELAHDPSdaNIRIMSDLQEQLdyqngwqfetrISQVLTLLNLDPDATLDS---LSGGWLRKV 165
Cdd:PRK13643 95 SQL--FEETVLK------DVAFGPQ--NFGIPKEKAEKI-----------AAEKLEMVGLADEFWEKSpfeLSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 166 ALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRgAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
321-475 |
1.71e-07 |
|
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: 52.58 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDR----TLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKL------------- 382
Cdd:cd03258 3 ELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvDGTDLtllsgkelrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 383 EVAY-FDQYrdQLDPEQTVMDNV-------GEGKQEvmVRGRSRHILgylqDFL-FEPKRARTPvKALSGGEKNRLLLAK 453
Cdd:cd03258 83 RIGMiFQHF--NLLSSRTVFENValpleiaGVPKAE--IEERVLELL----ELVgLEDKADAYP-AQLSGGQKQRVGIAR 153
|
170 180
....*....|....*....|...
gi 1411607396 454 -LFLKPSnLLILDEPTNDLDVET 475
Cdd:cd03258 154 aLANNPK-VLLCDEATSALDPET 175
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
319-496 |
1.75e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.17 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDF---GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL 394
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKiDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 -----DPEQ-----TVMDNVGEGKQ------EVMVRGRSRHILGY-LQDFlfepkRARTPVKaLSGGEKNRLLLAKLFLK 457
Cdd:PRK13642 84 gmvfqNPDNqfvgaTVEDDVAFGMEnqgiprEEMIKRVDEALLAVnMLDF-----KTREPAR-LSGGQKQRVAVAGIIAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1411607396 458 PSNLLILDEPTNDLD----VETLELLEELLADYPGTLLLVSHD 496
Cdd:PRK13642 158 RPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
156-267 |
1.96e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.20 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAinwlEDFLKDfrgAIVFISHDR-EFI--HKLAT-----RIIDLD 227
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVET----EAKVKA---ALDELMKGRtTFIiaHRLSTvrnadRILVFD 543
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1411607396 228 RG-VITSwpGNYDEYLQGKEealRVEELQHAEFdrkLAQEE 267
Cdd:PRK13657 544 NGrVVES--GSFDELVARGG---RFAALLRAQG---MLQED 576
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
157-231 |
2.09e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.17 E-value: 2.09e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRgAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
332-475 |
2.36e-07 |
|
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: 52.10 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 332 RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEVAYFDQYRDQLDP--------EQTVMD 402
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrVLVDGHDLALADPAWLRRQVGVvlqenvlfNRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 403 NVGEGKqEVMVRGRSRHI--LGYLQDFLFE-PKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03252 95 NIALAD-PGMSMERVIEAakLAGAHDFISElPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
337-473 |
2.52e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 53.17 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKG-GTKLEVAYFDQYRD--------------QLDPEQTVM 401
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlGKDLLGMKDDEWRAvrsdiqmifqdplaSLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGE---------GKQEVMVRGRSRHI-LGYLQDFLfepkrARTPvKALSGGEKNRLLLAK-LFLKPsNLLILDEPTND 470
Cdd:PRK15079 119 EIIAEplrtyhpklSRQEVKDRVKAMMLkVGLLPNLI-----NRYP-HEFSGGQCQRIGIARaLILEP-KLIICDEPVSA 191
|
...
gi 1411607396 471 LDV 473
Cdd:PRK15079 192 LDV 194
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-190 |
2.78e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 53.57 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 12 SFS-----DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDDGRMVQQQ----DLKVTRLEQDP 75
Cdd:TIGR00958 485 SFSypnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLqnlyqptGGQVLLDGVPLVQYDhhylHRQVALVGQEP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 76 PASSDlTVFDYTAEGLAgvgellkkyhhismelahDPSDANIRIMSDLQEQLDYqngwqfetrISQVLTLLNLDPDATLD 155
Cdd:TIGR00958 565 VLFSG-SVRENIAYGLT------------------DTPDEEIMAAAKAANAHDF---------IMEFPNGYDTEVGEKGS 616
|
170 180 190
....*....|....*....|....*....|....*
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIE 190
Cdd:TIGR00958 617 QLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
315-472 |
2.87e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.49 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 315 SGKLVFETEGLGLDfgDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLE----PSRGLVKGG---------TK 381
Cdd:cd03233 5 SWRNISFTTGKGRS--KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvsVEGDIHYNGipykefaekYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 382 LEVAYFDQyRDQLDPEQTV---MDNVGEGKQEVMVRGrsrhilgylqdflfepkrartpvkaLSGGEKNRLLLAKLFLKP 458
Cdd:cd03233 83 GEIIYVSE-EDVHFPTLTVretLDFALRCKGNEFVRG-------------------------ISGGERKRVSIAEALVSR 136
|
170
....*....|....
gi 1411607396 459 SNLLILDEPTNDLD 472
Cdd:cd03233 137 ASVLCWDNSTRGLD 150
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
349-501 |
3.10e-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: 51.45 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 349 ALVGPNGCGKSTLIKLLL----GQLEPSRGLVKGGTKL-----EVAYFD-QYRDQLDPEQTVMDNVGEGKQEVMVRGrsr 418
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltGELPPNSKGGAHDPKLiregeVRAQVKlAFENANGKKYTITRSLAILENVIFCHQ--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 419 hilGYLQDFLFEPkrartpVKALSGGEKN------RLLLAKLFLKPSNLLILDEPTNDLDVETLELL-----EELLADYP 487
Cdd:cd03240 103 ---GESNWPLLDM------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESlaeiiEERKSQKN 173
|
170
....*....|....
gi 1411607396 488 GTLLLVSHDRRFID 501
Cdd:cd03240 174 FQLIVITHDEELVD 187
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-188 |
3.26e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.92 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFS-DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-------ELPLDDGRmvqqqdlkVTRLE 72
Cdd:PRK11650 1 MAGLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGleritsgEIWIGGRV--------VNELE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 qdpPASSD-------------LTVFDYTAEGL--AGVGEllkkyHHIsmelahdpsdanirimsdlqeqldyqngwqfET 137
Cdd:PRK11650 73 ---PADRDiamvfqnyalyphMSVRENMAYGLkiRGMPK-----AEI-------------------------------EE 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 138 RISQVLTLLNLDPdaTLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK11650 114 RVAEAARILELEP--LLDrkprELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-468 |
3.56e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.59 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGElplddgRMVQQqdlkvtrleqdppasSDLTVFD------------- 85
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGA------RKIQQ---------------GRVEVLGgdmadarhrravc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 86 ----YTAEGLagvGELLkkYHHISMElahdpsdanirimsdlqEQLDY------QNGWQFETRISQVLTLLNLDP--DAT 153
Cdd:NF033858 76 priaYMPQGL---GKNL--YPTLSVF-----------------ENLDFfgrlfgQDAAERRRRIDELLRATGLAPfaDRP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----------IEAInwledflkdfRGA------IVfishdrefih 217
Cdd:NF033858 134 AGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplsrrqfwelIDRI----------RAErpgmsvLV---------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 218 klATriidldrgvitswpgnydEYLqgkEEALRveelqhaeFDRKLAQeevwvrqgikarrtrNEGRVRALEAMR--MER 295
Cdd:NF033858 194 --AT------------------AYM---EEAER--------FDWLVAM---------------DAGRVLATGTPAelLAR 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 296 SQRREL-------------QGKAKLQMD--DVNRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKST 360
Cdd:NF033858 228 TGADTLeaafiallpeekrRGHQPVVIPprPADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKST 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 361 LIKLLLGQLEPSRG-------LVKGG---TKLEVAYFDQ----YRdqldpEQTVMDN---------VGEGKQEVMVRgrs 417
Cdd:NF033858 308 TMKMLTGLLPASEGeawlfgqPVDAGdiaTRRRVGYMSQafslYG-----ELTVRQNlelharlfhLPAAEIAARVA--- 379
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 418 rhilGYLQDFLFEPKRARTPvKALSGGEKNRLLLAKLFL-KPSnLLILDEPT 468
Cdd:NF033858 380 ----EMLERFDLADVADALP-DSLPLGIRQRLSLAVAVIhKPE-LLILDEPT 425
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
319-471 |
3.68e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqLEPSrGLVKG-----GTKLEvayFDQYRDQ 393
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPH-GTYEGeiifeGEELQ---ASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 394 -------------LDPEQTVMDNVGEGkQEVMVRGRSRHILGYL--QDFLFEPKRA---RTPVKALSGGEKNRLLLAKLF 455
Cdd:PRK13549 80 eragiaiihqelaLVKELSVLENIFLG-NEITPGGIMDYDAMYLraQKLLAQLKLDinpATPVGNLGLGQQQLVEIAKAL 158
|
170
....*....|....*.
gi 1411607396 456 LKPSNLLILDEPTNDL 471
Cdd:PRK13549 159 NKQARLLILDEPTASL 174
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
349-472 |
3.93e-07 |
|
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: 52.42 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 349 ALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGT--------------KLEVAY-FDQYRdqLDPEQTVMDNVGEGKQEVM 412
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGeIVLNGRtlfdsrkgiflppeKRRIGYvFQEAR--LFPHLSVRGNLRYGMKRAR 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 413 VRGRSRHILGYLQDFLFEPKRARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR02142 105 PSERRISFERVIELLGIGHLLGRLPGR-LSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-184 |
4.16e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.42 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 1 MALLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV-------QQQDLKVTRleq 73
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVfdgkditDWQTAKIMR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 74 dppassdltvfdytaEGLAGVGELLKKYHHISMElahdpsdANIRIMSDLQEQLDYQngwqfeTRISQVLTL---LNLDP 150
Cdd:PRK11614 80 ---------------EAVAIVPEGRRVFSRMTVE-------ENLAMGGFFAERDQFQ------ERIKWVYELfprLHERR 131
|
170 180 190
....*....|....*....|....*....|....
gi 1411607396 151 DATLDSLSGGWLRKVALARALACDPDLLLLDEPT 184
Cdd:PRK11614 132 IQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-191 |
4.21e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.90 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPlddGRMVQQQDLKVTRLEQDPPASSdltvfdyTAEGLAGVGELL 98
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP---GKFEGNVFINGKPVDIRNPAQA-------IRAGIAMVPEDR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 99 KKYHHIS-MELAHDPSDANIRIMSDLQeQLDYQNGWQFETRISQVLTLLNLDPDATLDSLSGGWLRKVALARALACDPDL 177
Cdd:TIGR02633 346 KRHGIVPiLGVGKNITLSVLKSFCFKM-RIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRV 424
|
170
....*....|....
gi 1411607396 178 LLLDEPTNHLDIEA 191
Cdd:TIGR02633 425 LILDEPTRGVDVGA 438
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
317-474 |
4.22e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.57 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 317 KLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQlePSRGLVKGgtklEVAYFDQYRDQLDP 396
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAYKILEG----DILFKGESILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 397 EQTVMDNVGEGKQ-EVMVRGRSRhilgylQDFL---------FEPKRARTPVKAL------------------------- 441
Cdd:CHL00131 79 EERAHLGIFLAFQyPIEIPGVSN------ADFLrlaynskrkFQGLPELDPLEFLeiineklklvgmdpsflsrnvnegf 152
|
170 180 190
....*....|....*....|....*....|...
gi 1411607396 442 SGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVE 474
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDID 185
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
136-231 |
4.40e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 51.94 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 136 ETRISQVLTLLNLDPDATLDS---LSGGWLRKVALARALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVF 208
Cdd:PRK13634 122 KQKAREMIELVGLPEELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVL 201
|
90 100
....*....|....*....|...
gi 1411607396 209 ISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13634 202 VTHSMEDAARYADQIVVMHKGTV 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-243 |
5.17e-07 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLD--DGRMVQQQDL--KVTRLEQDPPASSDlTV 83
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvsSGSILIDgqDIREVTLDSLrrAIGVVPQDTVLFND-TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 84 FDYTAEGLAGVGEllkkyhhISMELAHDPSDANIRIMSdLQEQLDYQNGwqfETRIsqvltllnldpdatldSLSGGWLR 163
Cdd:cd03253 92 GYNIRYGRPDATD-------EEVIEAAKAAQIHDKIMR-FPDGYDTIVG---ERGL----------------KLSGGEKQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISHD-REFIHklATRIIDLDRGVITSwPGNYDE 240
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAHRlSTIVN--ADKIIVLKDGRIVE-RGTHEE 221
|
...
gi 1411607396 241 YLQ 243
Cdd:cd03253 222 LLA 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
321-512 |
6.00e-07 |
|
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: 52.50 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLG--QLEPSRGLV---------------------- 376
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpskvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 377 --KGGTKLE--------------------VAYFDQYRDQLDPEQTVMDNVGEGKQEVMVRGRSRhiLGYLQDFLFEPK-- 432
Cdd:TIGR03269 82 cpVCGGTLEpeevdfwnlsdklrrrirkrIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEA--VGRAVDLIEMVQls 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 433 -RARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETL----ELLEELLADYPGTLLLVSHDRRFIDNTVT-G 506
Cdd:TIGR03269 160 hRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDkA 239
|
....*.
gi 1411607396 507 CWLFEG 512
Cdd:TIGR03269 240 IWLENG 245
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
338-472 |
6.02e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSR--GLVKGGTkleVAYFDQYRDQLDpeQTVMDNVGEG-KQEVMVR 414
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtsSVVIRGS---VAYVPQVSWIFN--ATVRENILFGsDFESERY 710
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 415 GRSRHILGYLQDFLFEPKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PLN03232 711 WRAIDVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
330-501 |
6.40e-07 |
|
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: 51.11 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQlePSRGLVKGgtklEVAYFDQYRDQLDPEQtvmdnvgegkq 409
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH--PSYEVTSG----TILFKGQDLLELEPDE----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 410 evmvRGRSRHILGY----------LQDFLFEPKRAR------TPVKAL----------------------------SGGE 445
Cdd:TIGR01978 74 ----RARAGLFLAFqypeeipgvsNLEFLRSALNARrsargeEPLDLLdfekllkeklalldmdeeflnrsvnegfSGGE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 446 KNRL-LLAKLFLKPsNLLILDEPTNDLDVETLELLEELLADY--PGT-LLLVSHDRRFID 501
Cdd:TIGR01978 150 KKRNeILQMALLEP-KLAILDEIDSGLDIDALKIVAEGINRLrePDRsFLIITHYQRLLN 208
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
344-475 |
6.92e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.58 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 344 RGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV--KGGT--KLEVAYFDQYRDQ----------LDPEQTVMDNVGE--- 406
Cdd:PRK11629 34 EGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifNGQPmsKLSSAAKAELRNQklgfiyqfhhLLPDFTALENVAMpll 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 407 --GKQEVMVRGRSRHILGYLQdflfEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:PRK11629 114 igKKKPAEINSRALEMLAAVG----LEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-228 |
7.58e-07 |
|
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: 50.57 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTRLE----------QDPpassdlTVFD 85
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSiLIDGVDISKIGLHdlrsrisiipQDP------VLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 86 YTaeglagvgellkkyhhISMELahDP----SDAnirimsDLQEQLDYQNGWQFetrISQVLTLLNLDPDATLDSLSGGW 161
Cdd:cd03244 92 GT----------------IRSNL--DPfgeySDE------ELWQALERVGLKEF---VESLPGGLDTVVEEGGENLSVGQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKD-FRGAIVF-IShdrefiHKLATrIIDLDR 228
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREaFKDCTVLtIA------HRLDT-IIDSDR 206
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-246 |
8.10e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.00 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMvqqqdlkvtrLEQDPPassdltvFDYTAEGL----AGV 94
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI----------LFDGKP-------IDYSRKGLmklrESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 95 GELLKKYHH--ISMELAHDPS--DANIRIMSDlqeqldyqngwQFETRISQVLTLLNLDP--DATLDSLSGGWLRKVALA 168
Cdd:PRK13636 85 GMVFQDPDNqlFSASVYQDVSfgAVNLKLPED-----------EVRKRVDNALKRTGIEHlkDKPTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 169 RALACDPDLLLLDEPTNHLD----IEAINWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITsWPGNYDEYLQG 244
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGNPKEVFAE 232
|
..
gi 1411607396 245 KE 246
Cdd:PRK13636 233 KE 234
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
23-219 |
8.44e-07 |
|
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: 51.54 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 23 ELSIERGERL-CLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLEQDPPASSDLTvFDYTAEGLAGVGELLKKY 101
Cdd:COG3593 16 DLSIELSDDLtVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELT-FGSLLSRLLRLLLKEEDK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 102 HHISMELAHDPSDANIRImSDLQEQLD-YQNGWQFETRIS---------QVLTLLNL----DPDATLDSLSGG--WLRKV 165
Cdd:COG3593 95 EELEEALEELNEELKEAL-KALNELLSeYLKELLDGLDLElelsldeleDLLKSLSLriedGKELPLDRLGSGfqRLILL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411607396 166 ALARALA-----CDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFIS-HDREFIHKL 219
Cdd:COG3593 174 ALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELseKPNQVIITtHSPHLLSEV 235
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
340-475 |
9.10e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 50.65 E-value: 9.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 340 LQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV--------KGGTKLEVAYFDQyRDQLDPEQTVMdnvgegKQEV 411
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrQALQKNLVAYVPQ-SEEVDWSFPVL------VEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 412 MVRGRSRHiLGYLQdflfEPK-RARTPVKA-----------------LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK15056 101 VMMGRYGH-MGWLR----RAKkRDRQIVTAalarvdmvefrhrqigeLSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
..
gi 1411607396 474 ET 475
Cdd:PRK15056 176 KT 177
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
319-472 |
9.53e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.55 E-value: 9.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLL--LGQLEPSrGLVKGgtklEVAYFDQ--YRDQL 394
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPG-FRVEG----KVTFHGKnlYAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 395 DP-----------------EQTVMDNVGEGKQevmvrgrsrhILGYLQDF--LFEP--KRA----------RTPVKALSG 443
Cdd:PRK14243 85 DPvevrrrigmvfqkpnpfPKSIYDNIAYGAR----------INGYKGDMdeLVERslRQAalwdevkdklKQSGLSLSG 154
|
170 180
....*....|....*....|....*....
gi 1411607396 444 GEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-231 |
1.02e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 50.85 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLK------------VTRLEQDPpassDLTVFD 85
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEvLIKGEPIKydkksllevrktVGIVFQNP----DDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 86 YTAEGLAGVGELlkkyhhiSMELAHDpsdanirimsdlqeqldyqngwQFETRISQVLTLLNLD--PDATLDSLSGGWLR 163
Cdd:PRK13639 94 PTVEEDVAFGPL-------NLGLSKE----------------------EVEKRVKEALKAVGMEgfENKPPHHLSGGQKK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 164 KVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFIS-HDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGITIIIStHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
344-513 |
1.14e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.11 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 344 RGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKgGTKLEVAYFDQYRDqldpeqtvmdnvgegkqevmvrgrsrhilgy 423
Cdd:cd03222 24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE-WDGITPVYKPQYID------------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 424 lqdflfepkrartpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLADY----PGTLLLVSHDRRF 499
Cdd:cd03222 72 -----------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAV 134
|
170
....*....|....
gi 1411607396 500 IDNTVTGCWLFEGD 513
Cdd:cd03222 135 LDYLSDRIHVFEGE 148
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
338-472 |
1.31e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 50.37 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DPEQ-----TVMDNVGE 406
Cdd:PRK13632 28 VSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKiDGITISKENLKEIRKKIgiifqNPDNqfigaTVEDDIAF 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 407 GKQEVMV-RGRSRHILGYL------QDFL-FEPKRartpvkaLSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13632 108 GLENKKVpPKKMKDIIDDLakkvgmEDYLdKEPQN-------LSGGQKQRVAIASvLALNPE-IIIFDESTSMLD 174
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-229 |
1.52e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.49 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTLMKIIAG-ELPLDDGRMVQQQDlkVTRLE---------------QDPPASSDLT 82
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGiERPSAGKIWFSGHD--ITRLKnrevpflrrqigmifQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 83 VFDYTAEGLAGVGellkkyhhismelahdPSDANIRimsdlqeqldyqngwqfeTRISQVLTLLNLdpdatLD------- 155
Cdd:PRK10908 96 VYDNVAIPLIIAG----------------ASGDDIR------------------RRVSAALDKVGL-----LDkaknfpi 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDiEAINwlEDFLKDFR-----GAIVFI-SHDREFIHKLATRIIDLDRG 229
Cdd:PRK10908 137 QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD-DALS--EGILRLFEefnrvGVTVLMaTHDIGLISRRSYRMLTLSDG 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
156-211 |
1.84e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 49.65 E-value: 1.84e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISH 211
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKdyTIVIVTH 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-236 |
2.14e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 49.62 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDlkvtrleqdppassdlt 82
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 83 VFDYTAEGLAGVGELLKKyhhismeLAHDPsDANI---RIMSDLQEQLDYQNGWQFET--RISQVLTLLNLD--PDATLD 155
Cdd:PRK13638 64 PLDYSKRGLLALRQQVAT-------VFQDP-EQQIfytDIDSDIAFSLRNLGVPEAEItrRVDEALTLVDAQhfRHQPIQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:PRK13638 136 CLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
....*.
gi 1411607396 233 SW--PG 236
Cdd:PRK13638 216 THgaPG 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-232 |
2.18e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.74 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDDGRMVQQ---QDLKVTR----LEQDPPASS--D 80
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLnglhvptQGSVRVDDTLITSTsknKDIKQIRkkvgLVFQFPESQlfE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 81 LTVFDYTAEGLAGVGellkkyhhISMELAHDPSDANIRIMSdLQEQLDYQNgwQFEtrisqvltllnldpdatldsLSGG 160
Cdd:PRK13649 101 ETVLKDVAFGPQNFG--------VSQEEAEALAREKLALVG-ISESLFEKN--PFE--------------------LSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgmtIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
335-475 |
2.18e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 49.60 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 335 FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGGTKLEVAYFDQYRDQL-----DPE-----QTVMD 402
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGkvLVSGIDTGDFSKLQGIRKLVgivfqNPEtqfvgRTVEE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 403 NVGEGKQE-----VMVRGRSRHILGYLQdflFEPKRARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:PRK13644 98 DLAFGPENlclppIEIRKRVDRALAEIG---LEKYRHRSP-KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-213 |
2.23e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 13 FSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKvtrleqdppasSDLTVFDytaEGL 91
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlFERQSIK-----------KDLCTYQ---KQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 92 AGVGellkkyHHISMelahdpsDANIRIMSDLQEQLDYQNGwqfETRISQVLTLLNLDP--DATLDSLSGGWLRKVALAR 169
Cdd:PRK13540 77 CFVG------HRSGI-------NPYLTLRENCLYDIHFSPG---AVGITELCRLFSLEHliDYPCGLLSSGQKRQVALLR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1411607396 170 ALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR---GAIVFISHDR 213
Cdd:PRK13540 141 LWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-232 |
2.38e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.29 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 22 AELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR-MVQQQDLKVTRLEQDPPASSDLTVFDYTAEG---LAGVGEL 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQvYLDGKPIDIRSPRDAIRAGIMLCPEDRKAEGiipVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 98 LkkyhHISMELAHDPSDANIRimsdlqeqldyqNGWQFETRISQVlTLLNL---DPDATLDSLSGGWLRKVALARALACD 174
Cdd:PRK11288 352 I----NISARRHHLRAGCLIN------------NRWEAENADRFI-RSLNIktpSREQLIMNLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 175 PDLLLLDEPTNHLDIEAINWLEDFLKDF--RG-AIVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELaaQGvAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
337-475 |
2.41e-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: 48.56 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKggtklevayFDQYRDQLDPEQTVMDNVGEGKQE-VMVRG 415
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE---------IDGIDISTIPLEDLRSSLTIIPQDpTLFSG 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 416 RSRHILG----YLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03369 97 TIRSNLDpfdeYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-237 |
2.93e-06 |
|
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: 50.18 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 24 LSIERGERLCLVGRNGAGKSTLMKII-------AGELPLdDGRMVQQQDLkvtrleqdppAS---------SDLTVFD-- 85
Cdd:COG4615 353 LTIRRGELVFIVGGNGSGKSTLAKLLtglyrpeSGEILL-DGQPVTADNR----------EAyrqlfsavfSDFHLFDrl 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 86 YTAEGLAG---VGELLKKyhhisMELAHdpsdanirimsdlqeQLDYQNGwqfetRISqvltllnldpdaTLDsLSGGWL 162
Cdd:COG4615 422 LGLDGEADparARELLER-----LELDH---------------KVSVEDG-----RFS------------TTD-LSQGQR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 163 RKVALARALACDPDLLLLDEptnhldieainWLED--------F-------LKDfRG-AIVFISHDREFIHkLATRIIDL 226
Cdd:COG4615 464 KRLALLVALLEDRPILVFDE-----------WAADqdpefrrvFytellpeLKA-RGkTVIAISHDDRYFD-LADRVLKM 530
|
250
....*....|.
gi 1411607396 227 DRGVITSWPGN 237
Cdd:COG4615 531 DYGKLVELTGP 541
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
339-496 |
2.95e-06 |
|
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: 49.18 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 339 DLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVAYFDQYRDQ----------LDPEQTVMDNV 404
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGkvLIDGQdiAAMSRKELRELRRKkismvfqsfaLLPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 405 -------GEGKQEvmvrgRSRHILGYLQDFLFEPKRARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD---- 472
Cdd:cd03294 124 afglevqGVPRAE-----REERAAEALELVGLEGWEHKYP-DELSGGMQQRVGLARaLAVDPD-ILLMDEAFSALDplir 196
|
170 180
....*....|....*....|....
gi 1411607396 473 VETLELLEELLADYPGTLLLVSHD 496
Cdd:cd03294 197 REMQDELLRLQAELQKTIVFITHD 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
315-496 |
3.09e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 50.03 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 315 SGKLVFETEGLGLDFGDRTLfqgldlQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGG--TKLEVAYFDQY 390
Cdd:PRK10070 30 SKEQILEKTGLSLGVKDASL------AIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGqvLIDGVdiAKISDAELREV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 RDQ----------LDPEQTVMDNVGEGKQ--EVMVRGRSRHILGYLQDFLFEPKRARTPvKALSGGEKNRLLLAKLFLKP 458
Cdd:PRK10070 104 RRKkiamvfqsfaLMPHMTVLDNTAFGMElaGINAEERREKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAIN 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1411607396 459 SNLLILDEPTNDLD----VETLELLEELLADYPGTLLLVSHD 496
Cdd:PRK10070 183 PDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
319-475 |
3.12e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 49.24 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKL----------------LLGQLEPSRGLVKGGTKL 382
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHlsglitgdksagshieLLGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 383 EVAY----FDQYrdQLDPEQTVMDNVGEG-------------------KQEVMvRGRSRHILGYLqdflfepkrARTPVK 439
Cdd:PRK09984 84 SRANtgyiFQQF--NLVNRLSVLENVLIGalgstpfwrtcfswftreqKQRAL-QALTRVGMVHF---------AHQRVS 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1411607396 440 ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPES 187
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
338-393 |
3.55e-06 |
|
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: 50.18 E-value: 3.55e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQ 393
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILlDGQPVTADNREAYRQL 407
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-241 |
3.67e-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: 48.18 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRM-VQQQDLKVTRLEQdppASSDLTVfdytaeglagvg 95
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeIDGIDISTIPLED---LRSSLTI------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 96 ellkkyhhismeLAHDPsdanIRIMSDLQEQLDYQNGWQFEtrisQVLTLLNLDPDAtlDSLSGGWLRKVALARALACDP 175
Cdd:cd03369 87 ------------IPQDP----TLFSGTIRSNLDPFDEYSDE----EIYGALRVSEGG--LNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 176 DLLLLDEPTNHLDIEAINWLEDFL-KDFRGAIVFIshdreFIHKLATrIIDLDRGVITSwPGNYDEY 241
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIrEEFTNSTILT-----IAHRLRT-IIDYDKILVMD-AGEVKEY 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-253 |
3.77e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV-----QQQDLKVTRLEQDPPASS----DL 81
Cdd:PTZ00265 1176 ISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkneHTNDMTNEQDYQGDEEQNvgmkNV 1255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 82 TVFDYTAEGLAGVGELLKKYHHISMELAHDPSDANIRIMSDL-----QEQL-----DYQN---GWQFETR---------- 138
Cdd:PTZ00265 1256 NEFSLTKEGGSGEDSTVFKNSGKILLDGVDICDYNLKDLRNLfsivsQEPMlfnmsIYENikfGKEDATRedvkrackfa 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 139 -ISQVLTLLNLDPDATL----DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGaivfiSHDR 213
Cdd:PTZ00265 1336 aIDEFIESLPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD-----KADK 1410
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1411607396 214 EFI---HKLATrIIDLDRGVITSWPGNYDEYLQGK---EEALRVEE 253
Cdd:PTZ00265 1411 TIItiaHRIAS-IKRSDKIVVFNNPDRTGSFVQAHgthEELLSVQD 1455
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-219 |
4.48e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 48.27 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 18 LLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmvqqqdlkvtrleQDPPASSD-------LTVFDYTAEG 90
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGG---------------------LDTPTSGDvifngqpMSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 91 LAGVGEL--LKKYHHismeLAHDPSDANIRIMSDLqeqLDYQNGWQFETRISQVLTLLNLDPDATLDS--LSGGWLRKVA 166
Cdd:PRK11629 83 ELRNQKLgfIYQFHH----LLPDFTALENVAMPLL---IGKKKPAEINSRALEMLAAVGLEHRANHRPseLSGGERQRVA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 167 LARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR----GAIVFISHDREFIHKL 219
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHDLQLAKRM 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
349-472 |
4.53e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.01 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 349 ALVGPNGCGKSTLIKLLLGQLEPSRGLV-KGGTKLEVAyFDQYRDQLD--PEQTVMDNVGEGKQEVM----VRGRSR--- 418
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVlVGGKDIETN-LDAVRQSLGmcPQHNILFHHLTVAEHILfyaqLKGRSWeea 1038
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 419 --HILGYLQDFLFEPKRaRTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR01257 1039 qlEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
341-496 |
4.74e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 48.57 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 341 QVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEVAYFDQYRDQL-----DPEQ-----TVMDNVG---- 405
Cdd:PRK13650 29 HVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGqIIIDGDLLTEENVWDIRHKIgmvfqNPDNqfvgaTVEDDVAfgle 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 406 -EGKQEVMVRGRSRHILGY--LQDFlfepkRARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD----VETLEL 478
Cdd:PRK13650 109 nKGIPHEEMKERVNEALELvgMQDF-----KEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKT 182
|
170
....*....|....*...
gi 1411607396 479 LEELLADYPGTLLLVSHD 496
Cdd:PRK13650 183 IKGIRDDYQMTVISITHD 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
323-468 |
5.24e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqlepSRGLVKGgtKLEV------------------ 384
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG----ARKIQQG--RVEVlggdmadarhrravcpri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 385 AYFDQ------YrdqldPEQTVMDNV-------GEGKQEvmvrgRSRHILGYLQDFLFEPKRARtPVKALSGGEKNRL-L 450
Cdd:NF033858 79 AYMPQglgknlY-----PTLSVFENLdffgrlfGQDAAE-----RRRRIDELLRATGLAPFADR-PAGKLSGGMKQKLgL 147
|
170
....*....|....*...
gi 1411607396 451 LAKLFLKPsNLLILDEPT 468
Cdd:NF033858 148 CCALIHDP-DLLILDEPT 164
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-216 |
5.44e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.60 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 34 LVGRNGAGKSTLMKIIA----GELPLD-DGRmvqQQDLKVTRlEQDPPASSDLTVfdYTAEGlagvgellKKYHhISMEL 108
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltGELPPNsKGG---AHDPKLIR-EGEVRAQVKLAF--ENANG--------KKYT-ITRSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 109 AHDPSDANIRimsdlQEQLDyqngwqfetrisqvlTLLnLDPdatLDSLSGGW-------LRkVALARALACDPDLLLLD 181
Cdd:cd03240 92 AILENVIFCH-----QGESN---------------WPL-LDM---RGRCSGGEkvlasliIR-LALAETFGSNCGILALD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1411607396 182 EPTNHLDIEAINW-LEDFLKDFRGAIVF----ISHDREFI 216
Cdd:cd03240 147 EPTTNLDEENIEEsLAEIIEERKSQKNFqlivITHDEELV 186
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-210 |
5.48e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 20 DNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPlddGR-----MVQQQDLKVTRleqdpPAssdltvfDYTAEGLAGV 94
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP---GRwegeiFIDGKPVKIRN-----PQ-------QAIAQGIAMV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 95 GELLKKYHHIS-MELAHDPSDANIRIMS-----DLQEQLDYqngwqfetrISQVLTLLNL---DPDATLDSLSGGWLRKV 165
Cdd:PRK13549 344 PEDRKRDGIVPvMGVGKNITLAALDRFTggsriDDAAELKT---------ILESIQRLKVktaSPELAIARLSGGNQQKA 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 166 ALARALACDPDLLLLDEPTNHLDIEA-------INWLEDflkdfRG-AIVFIS 210
Cdd:PRK13549 415 VLAKCLLLNPKILILDEPTRGIDVGAkyeiyklINQLVQ-----QGvAIIVIS 462
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-229 |
5.83e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 8 GACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMV---QQQDLK---------VTRLEQDP 75
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILfqgKEIDFKsskealengISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 76 PASSDLTVFDytaeglagvGELLKKYHHISMELAHDPS-DANIRIMSDLQeqldyqngwqfetrisqvltlLNLDPDATL 154
Cdd:PRK10982 83 NLVLQRSVMD---------NMWLGRYPTKGMFVDQDKMyRDTKAIFDELD---------------------IDIDPRAKV 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 155 DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDF---LKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK10982 133 ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIirkLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
336-501 |
7.04e-06 |
|
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: 46.93 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRgLVKGGTKlevaYFDQYRDQLDPEQTVMDnVGegkqevmvrg 415
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKAR-LISFLPK----FSRNKLIFIDQLQFLID-VG---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 416 rsrhiLGYLqdflfepkRARTPVKALSGGEKNRLLLAK-LFLKPSN-LLILDEPTNDL---DVETLELLEELLADYPGTL 490
Cdd:cd03238 76 -----LGYL--------TLGQKLSTLSGGELQRVKLASeLFSEPPGtLFILDEPSTGLhqqDINQLLEVIKGLIDLGNTV 142
|
170
....*....|.
gi 1411607396 491 LLVSHDRRFID 501
Cdd:cd03238 143 ILIEHNLDVLS 153
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
157-222 |
7.49e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.17 E-value: 7.49e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFISHDREFIHKLATR 222
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHNLAQAARISDR 231
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
156-245 |
8.21e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.80 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIE----AINWLEDFLKDFRGAIVFISHDREFIHKLATRIIdldrgVI 231
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH-----VF 145
|
90
....*....|....
gi 1411607396 232 TSWPGNYDEYLQGK 245
Cdd:cd03222 146 EGEPGVYGIASQPK 159
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-211 |
9.00e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.53 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 13 FSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDD-----------GRMVQQQDL-------KVTRLEQD 74
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearvegevrlfGRNIYSPDVdpievrrEVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 75 PPASSDLTVFDYTAEGLAgVGELLKKyhhismelahdpsdanirimsdlQEQLDYQNGWQFE--TRISQVLTLLNLDPDa 152
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVK-LNGLVKS-----------------------KKELDERVEWALKkaALWDEVKDRLNDYPS- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 153 tldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRG--AIVFISH 211
Cdd:PRK14267 149 ---NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-232 |
9.75e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 9.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 24 LSIERGERLCLVGRNGAGKSTLMKII-------AGELPLdDGRMVQQQDLKVTRlEQDPPASSDLTVFDYT--AEGLAGV 94
Cdd:PRK10522 344 LTIKRGELLFLIGGNGSGKSTLAMLLtglyqpqSGEILL-DGKPVTAEQPEDYR-KLFSAVFTDFHLFDQLlgPEGKPAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 95 GELLKKYhhismeLAHdpsdanirimSDLQEQLDYQNGwqfetrisqvlTLLNLDpdatldsLSGGWLRKVALARALACD 174
Cdd:PRK10522 422 PALVEKW------LER----------LKMAHKLELEDG-----------RISNLK-------LSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 175 PDLLLLDEptnhldieainWLEDFLKDFR--------------GAIVF-ISHDRE-FIHklATRIIDLDRGVIT 232
Cdd:PRK10522 468 RDILLLDE-----------WAADQDPHFRrefyqvllpllqemGKTIFaISHDDHyFIH--ADRLLEMRNGQLS 528
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
337-475 |
9.92e-06 |
|
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: 47.10 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DP---EQTVMDNV--- 404
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILiDGVDISKIGLHDLRSRIsiipqDPvlfSGTIRSNLdpf 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 405 GEGKQEVMVRGRSR-HILGYLQDFlfePKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:cd03244 102 GEYSDEELWQALERvGLKEFVESL---PGGLDTVVEEggenLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
321-474 |
1.21e-05 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 46.98 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLG--QLEPSRG--LVKGG--TKLEV---------- 384
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGsiLLDGEdiLELSPderaragifl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 385 AYfdQY---------RDQLdpeQTVMDNVGEGKQEVM-----VRGRSRhILGYLQDFLfepKRartPVKA-LSGGEKNRL 449
Cdd:COG0396 82 AF--QYpveipgvsvSNFL---RTALNARRGEELSAReflklLKEKMK-ELGLDEDFL---DR---YVNEgFSGGEKKRN 149
|
170 180
....*....|....*....|....*.
gi 1411607396 450 -LLAKLFLKPSnLLILDEPTNDLDVE 474
Cdd:COG0396 150 eILQMLLLEPK-LAILDETDSGLDID 174
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
338-500 |
1.30e-05 |
|
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: 46.56 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLE---------------VAYFDQYRDQLDPeqTVMD 402
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKPWLLNA--TVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 403 NVGEGKQEVMVRGRSRHILGYLQ-DFLFEPKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLE 477
Cdd:cd03290 98 NITFGSPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 177
|
170 180
....*....|....*....|....*...
gi 1411607396 478 LLEEL-----LADYPGTLLLVSHDRRFI 500
Cdd:cd03290 178 HLMQEgilkfLQDDKRTLVLVTHKLQYL 205
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
337-516 |
1.41e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.39 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLV-----------KGGTKLEVAY------------------- 386
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkKTKEKEKVLEklviqktrfkkikkikeir 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 387 --------FDQYrdQLDpEQTVMDNV-------GEGKQEVMVRGRSR-HILGYLQDFLfepkrARTPVkALSGGEKNRLL 450
Cdd:PRK13651 105 rrvgvvfqFAEY--QLF-EQTIEKDIifgpvsmGVSKEEAKKRAAKYiELVGLDESYL-----QRSPF-ELSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 451 LAKLFLKPSNLLILDEPTNDLD---VETLELLEELLADYPGTLLLVSHDrrfIDNTV--TGCWLFEGDGRI 516
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD---LDNVLewTKRTIFFKDGKI 243
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
5-195 |
1.45e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 46.49 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 5 TLHGACLSF------SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPlddgrmvqqQDLKVTRleqdppas 78
Cdd:cd03233 3 TLSWRNISFttgkgrSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---------GNVSVEG-------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 79 sDLTVFDYTAEglagvgELLKKYHH-ISMELAHDPSDANIRImsdlQEQLDYQngwqfetrisqvltlLNLDPDATLDSL 157
Cdd:cd03233 66 -DIHYNGIPYK------EFAEKYPGeIIYVSEEDVHFPTLTV----RETLDFA---------------LRCKGNEFVRGI 119
|
170 180 190
....*....|....*....|....*....|....*....
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLD-IEAINWL 195
Cdd:cd03233 120 SGGERKRVSIAEALVSRASVLCWDNSTRGLDsSTALEIL 158
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
138-226 |
1.51e-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: 45.78 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 138 RISQVLTLLN-----LDPDATLDSLSGGWLRKVALARALACDPD--LLLLDEPTNHLDIEAINWLEDFLKDFRG---AIV 207
Cdd:cd03238 64 FIDQLQFLIDvglgyLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDlgnTVI 143
|
90
....*....|....*....
gi 1411607396 208 FISHDREFIhKLATRIIDL 226
Cdd:cd03238 144 LIEHNLDVL-SSADWIIDF 161
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-226 |
1.53e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.95 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 18 LLDNAELSIERGERLCLVGRNGAGKSTLMKII------AGELPLDD-----GRMVQQQDLKVTRLEQD------PPASSD 80
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmnelESEVRVEGrveffNQNIYERRVNLNRLRRQvsmvhpKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 81 LTVFDYTAEGLAGVGellkkyHHISMELaHDPSDANIRiMSDLQEQLdyqngwqfETRISQvltllnldpdATLDsLSGG 160
Cdd:PRK14258 102 MSVYDNVAYGVKIVG------WRPKLEI-DDIVESALK-DADLWDEI--------KHKIHK----------SALD-LSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 161 WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDFR----GAIVFISHDrefIHKLaTRIIDL 226
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN---LHQV-SRLSDF 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
339-472 |
1.55e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.31 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 339 DLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKL---------------EVAYFDQYRD-QLDPEQTVM 401
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIpanlkkikevkrlrkEIGLVFQFPEyQLFQETIEK 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 402 D------NVGEGKQEVMVRgrsrhiLGYLQDFLFEPKR--ARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13645 111 DiafgpvNLGENKQEAYKK------VPELLKLVQLPEDyvKRSPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-240 |
1.94e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVqqqdLKVTRLEQDPPassdltvFDYTAEGLAGV 94
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR----LNGKDISPRSP-------LDAVKKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 95 GELLKK---YHHISMElahdpsdANIRIMSDLQEQlDYQNGWQF-----ETRISQ----VLTLLNLDPDATLDSLSGGWL 162
Cdd:PRK09700 344 TESRRDngfFPNFSIA-------QNMAISRSLKDG-GYKGAMGLfhevdEQRTAEnqreLLALKCHSVNQNITELSGGNQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 163 RKVALARALACDPDLLLLDEPTNHLDIEA---INWLEDFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYD 239
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAkaeIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
.
gi 1411607396 240 E 240
Cdd:PRK09700 496 D 496
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
336-472 |
2.13e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.15 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGqLEPsrglVKGG---------TKLEVA------YFDQYrdQLDPEQTV 400
Cdd:PRK11650 21 KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG-LER----ITSGeiwiggrvvNELEPAdrdiamVFQNY--ALYPHMSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGEG-------KQEVMVR-GRSRHILGyLQDFLfepkrARTPvKALSGGEKNRLLLA-------KLFLkpsnlliLD 465
Cdd:PRK11650 94 RENMAYGlkirgmpKAEIEERvAEAARILE-LEPLL-----DRKP-RELSGGQRQRVAMGraivrepAVFL-------FD 159
|
....*..
gi 1411607396 466 EPTNDLD 472
Cdd:PRK11650 160 EPLSNLD 166
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-229 |
2.50e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.14 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 3 LLTLHGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKII-------AGELPLDDGRMVQQQDLKVTRLE--- 72
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLtgfykptGGTILLRGQHIEGLPGHQIARMGvvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 73 --QDPPASSDLTVFdytaEGLagvgeLLKKYHHIsmelahdpsdaNIRIMSDL----------QEQLDYQNGWqfetris 140
Cdd:PRK11300 85 tfQHVRLFREMTVI----ENL-----LVAQHQQL-----------KTGLFSGLlktpafrraeSEALDRAATW------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 141 qvLTLLNLDPDATLDS--LSGGWLRKVALARALACDPDLLLLDEPT---NHLDIEAINWLEDFLKD-FRGAIVFISHDRE 214
Cdd:PRK11300 138 --LERVGLLEHANRQAgnLAYGQQRRLEIARCMVTQPEILMLDEPAaglNPKETKELDELIAELRNeHNVTVLLIEHDMK 215
|
250
....*....|....*
gi 1411607396 215 FIHKLATRIIDLDRG 229
Cdd:PRK11300 216 LVMGISDRIYVVNQG 230
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-188 |
2.74e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.02 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFS---DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLD------DGRMVQQQDLKVTR-----LEQDPP 76
Cdd:PRK10790 346 VSFAyrdDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTegeirlDGRPLSSLSHSVLRqgvamVQQDPV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 77 ASSDlTVFdytaeglagvgellkkyhhismelahdpsdANIRIMSDLQEqldyQNGWQ-FETriSQVLTLLNLDPDA--T 153
Cdd:PRK10790 426 VLAD-TFL------------------------------ANVTLGRDISE----EQVWQaLET--VQLAELARSLPDGlyT 468
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1411607396 154 L-----DSLSGGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK10790 469 PlgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
321-472 |
2.95e-05 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 45.84 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGgtkLEVAYFDQyRD------ 392
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGevLVDG---LDVATTPS-RElakrla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 393 ------QLDPEQTVMDNVGEGkqevmvR-----GR-----SRHI--------LGYLQD-FLFEpkrartpvkaLSGGEKN 447
Cdd:COG4604 79 ilrqenHINSRLTVRELVAFG------RfpyskGRltaedREIIdeaiayldLEDLADrYLDE----------LSGGQRQ 142
|
170 180
....*....|....*....|....*
gi 1411607396 448 RLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLD 167
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
348-473 |
3.32e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 45.94 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 348 IALVGPNGCGKSTLIKLLLGQLEPSRG-LVKGGTKLEVAYFdQYRDQ------------LDPEQTV---MDNVGEGKQEV 411
Cdd:PRK15112 42 LAIIGENGSGKSTLAKMLAGMIEPTSGeLLIDDHPLHFGDY-SYRSQrirmifqdpstsLNPRQRIsqiLDFPLRLNTDL 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 412 MVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAK-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK15112 121 EPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARaLILRP-KVIIADEALASLDM 182
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
338-472 |
4.78e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 45.56 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEP-----SRGLVKGGTKLEVAYFDqYRDQL-----DPEQ-----TVMD 402
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnSKITVDGITLTAKTVWD-IREKVgivfqNPDNqfvgaTVGD 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 403 NVGEGKQEvmvRGRSR-HILGYLQDFLFE---PKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13640 105 DVAFGLEN---RAVPRpEMIKIVRDVLADvgmLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
156-188 |
5.48e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 45.15 E-value: 5.48e-05
10 20 30
....*....|....*....|....*....|...
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK14239 148 GLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-210 |
5.83e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 19 LDNAELSIERGERLCLVGRNGAGKSTL-MKI--------IAGELpLDDGRMVqqqDLKvtrleqdppassdlTVFDYTAE 89
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSVfgrsygrnISGTV-FKDGKEV---DVS--------------TVSDAIDA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 90 GLAGVGELLKKYHHISME-LAHDPSDANIRIMS-----DLQEQLDYQNGWQFETRI--SQVltllnldpDATLDSLSGGW 161
Cdd:NF040905 338 GLAYVTEDRKGYGLNLIDdIKRNITLANLGKVSrrgviDENEEIKVAEEYRKKMNIktPSV--------FQKVGNLSGGN 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1411607396 162 LRKVALARALACDPDLLLLDEPTNHLDIEA-------INWLEDFLKdfrgAIVFIS 210
Cdd:NF040905 410 QQKVVLSKWLFTDPDVLILDEPTRGIDVGAkyeiytiINELAAEGK----GVIVIS 461
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
335-467 |
5.87e-05 |
|
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: 45.86 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 335 FQGLDLQV---LRGDKI-ALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLevayFDQYRDQ---------------- 393
Cdd:COG4148 11 RGGFTLDVdftLPGRGVtALFGPSGSGKTTLLRAIAGLERPDSGRIRlGGEVL----QDSARGIflpphrrrigyvfqea 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 394 -LDPEQTVMDNVGEGkQEVMVRGRSRHILGYLQDFL-FEPKRARTPVkALSGGEKNRLLLAK-LFLKPSnLLILDEP 467
Cdd:COG4148 87 rLFPHLSVRGNLLYG-RKRAPRAERRISFDEVVELLgIGHLLDRRPA-TLSGGERQRVAIGRaLLSSPR-LLLMDEP 160
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-191 |
7.25e-05 |
|
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: 44.16 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 17 PLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGelplddgrmvqqqdlkvtrleqdppassdltvfdytaEGLAGV-- 94
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG-------------------------------------RKTAGVit 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 95 GELLkkyhhismeLAHDPSDANIRIMSDLQEQLDYQNGwqfETRISQVLTLlnldpDATLDSLSGGWLRKVALARALACD 174
Cdd:cd03232 64 GEIL---------INGRPLDKNFQRSTGYVEQQDVHSP---NLTVREALRF-----SALLRGLSVEQRKRLTIGVELAAK 126
|
170
....*....|....*..
gi 1411607396 175 PDLLLLDEPTNHLDIEA 191
Cdd:cd03232 127 PSILFLDEPTSGLDSQA 143
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
329-472 |
7.47e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.03 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPS----RGLVKGG--TK--LEVAYFDQYRDQLDPEQTV 400
Cdd:PLN03211 78 IQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnftgTILANNRkpTKqiLKRTGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNV----------GEGKQEVMVRGRS-----------RHILGylqdflfepkraRTPVKALSGGEKNRLLLA-KLFLKP 458
Cdd:PLN03211 158 RETLvfcsllrlpkSLTKQEKILVAESviselgltkceNTIIG------------NSFIRGISGGERKRVSIAhEMLINP 225
|
170
....*....|....
gi 1411607396 459 SnLLILDEPTNDLD 472
Cdd:PLN03211 226 S-LLILDEPTSGLD 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
345-472 |
7.98e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.81 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 345 GDKIALVGPNGCGKSTLIKLLLGQLEPsrGLVKGGTKL------------EVAYFDQYRDQLDPEQTV-----------M 401
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLlngmpidakemrAISAYVQQDDLFIPTLTVrehlmfqahlrM 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 402 DNVGEGKQEvmvRGRSRHILGYL-----QDFLF-EPKRartpVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR00955 129 PRRVTKKEK---RERVDEVLQALglrkcANTRIgVPGR----VKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
25-189 |
8.70e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 44.78 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 25 SIERGERLCLVGRNGAGKSTLMKIIAGelplddgrMVqqqdlkvtrleqdPPASSDLTVFDYTAEglagVGELLKKYHHI 104
Cdd:PRK15112 35 TLREGQTLAIIGENGSGKSTLAKMLAG--------MI-------------EPTSGELLIDDHPLH----FGDYSYRSQRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 105 SMeLAHDPS-------------DANIRIMSDLQEQldyqngwQFETRISQVLTLLNLDPDATL---DSLSGGWLRKVALA 168
Cdd:PRK15112 90 RM-IFQDPStslnprqrisqilDFPLRLNTDLEPE-------QREKQIIETLRQVGLLPDHASyypHMLAPGQKQRLGLA 161
|
170 180
....*....|....*....|.
gi 1411607396 169 RALACDPDLLLLDEPTNHLDI 189
Cdd:PRK15112 162 RALILRPKVIIADEALASLDM 182
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
337-473 |
1.12e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.57 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLL-------------LGQ--LEPSRGLVKG-GTKLEVAYFDQYrDQLDPEQTV 400
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLtmietptggelyyQGQdlLKADPEAQKLlRQKIQIVFQNPY-GSLNPRKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 401 MDNVGE--------GKQEvmvrgRSRHILGYLQDFLFEPKRA-RTPvKALSGGEKNRLLLAK-LFLKPsNLLILDEPTND 470
Cdd:PRK11308 112 GQILEEpllintslSAAE-----RREKALAMMAKVGLRPEHYdRYP-HMFSGGQRQRIAIARaLMLDP-DVVVADEPVSA 184
|
...
gi 1411607396 471 LDV 473
Cdd:PRK11308 185 LDV 187
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-59 |
1.40e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 1.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 7 HGACLSFSDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGR 59
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE 322
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
331-474 |
1.61e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.63 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSrglVKGGtklEVAYFDQYRDQLDPEqtvmDNVGEG--- 407
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYE---VTGG---TVEFKGKDLLELSPE----DRAGEGifm 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 408 --KQEVMVRGRSRHIL---------GY----------LQDFLFEPKR---------ARTPVKALSGGEKNRLLLAKLFLK 457
Cdd:PRK09580 83 afQYPVEIPGVSNQFFlqtalnavrSYrgqepldrfdFQDLMEEKIAllkmpedllTRSVNVGFSGGEKKRNDILQMAVL 162
|
170
....*....|....*..
gi 1411607396 458 PSNLLILDEPTNDLDVE 474
Cdd:PRK09580 163 EPELCILDESDSGLDID 179
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
156-212 |
1.72e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 43.62 E-value: 1.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFISHD 212
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTHN 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
344-472 |
2.49e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 43.20 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 344 RGDKIALVGPNGCGKSTLIKLLLGQLEPSRGlvkggtklEVAYFDQYRDQLD--------------PEQ-----TVMDNV 404
Cdd:PRK13648 34 KGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--------EIFYNNQAITDDNfeklrkhigivfqnPDNqfvgsIVKYDV 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411607396 405 GEGKQEVMVRGRSRH--ILGYLQDFLFEPKRARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13648 106 AFGLENHAVPYDEMHrrVSEALKQVDMLERADYEP-NALSGGQKQRVAIAGvLALNPS-VIILDEATSMLD 174
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
331-475 |
3.11e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 43.93 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLEVAYFDQYRDQL-----DP---EQTVM 401
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfHDIPLTKLQLDSWRSRLavvsqTPflfSDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 402 DNVGEGKQ-------EVMVRGRSRHilgylQDFLFEPKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK10789 407 NNIALGRPdatqqeiEHVARLASVH-----DDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSA 481
|
....*
gi 1411607396 471 LDVET 475
Cdd:PRK10789 482 VDGRT 486
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
332-473 |
3.19e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.89 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 332 RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLepSRGLVKGGTKL--EVAYFDQYRDQLDPEQ-----TVMDNV 404
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL--TGGGAPRGARVtgDVTLNGEPLAAIDAPRlarlrAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 405 GE-----GKQEVMVRGRSRHIL---------GYLQDFLFEPKRA----RTPVKALSGGEKNRL----LLAKLF-----LK 457
Cdd:PRK13547 92 AQpafafSAREIVLLGRYPHARragalthrdGEIAWQALALAGAtalvGRDVTTLSGGELARVqfarVLAQLWpphdaAQ 171
|
170
....*....|....*.
gi 1411607396 458 PSNLLILDEPTNDLDV 473
Cdd:PRK13547 172 PPRYLLLDEPTAALDL 187
|
|
| RNA_helicase |
pfam00910 |
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ... |
350-413 |
3.34e-04 |
|
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.
Pssm-ID: 459992 Cd Length: 102 Bit Score: 40.28 E-value: 3.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 350 LVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKL---EVAYFDQYRDQldpEQTVMDNVGEGKQEVMV 413
Cdd:pfam00910 3 LYGPPGCGKSTLAKYLARALLKKLGLPKDSVYSrnpDDDFWDGYTGQ---PVVIIDDFGQNPDGPDE 66
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
319-472 |
4.83e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 42.46 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLL--LGQLEPS---RGLVK-GGTKLEVAYFD--QY 390
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVyNGHNIYSPRTDtvDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 391 R-------DQLDP-EQTVMDNV-------GEGKQEVM-------VRGRSrhILGYLQDFLFEPkrartpVKALSGGEKNR 448
Cdd:PRK14239 85 RkeigmvfQQPNPfPMSIYENVvyglrlkGIKDKQVLdeaveksLKGAS--IWDEVKDRLHDS------ALGLSGGQQQR 156
|
170 180
....*....|....*....|....
gi 1411607396 449 LLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALD 180
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
307-475 |
5.10e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.08 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 307 LQMDDVNRSGKLVFETEGLGLDFGDRTL-FQGLDLQVLR--------GDKIALVGPNGCGKSTLIKLLLGQLEPSRG-LV 376
Cdd:PRK11176 322 LDLEQEKDEGKRVIERAKGDIEFRNVTFtYPGKEVPALRninfkipaGKTVALVGRSGSGKSTIANLLTRFYDIDEGeIL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 377 KGGTKLEVAYFDQYRDQ--LDPEQ------TVMDNVGEGKQEVMVRGRSRHI--LGYLQDFLFEPKRARTPV-----KAL 441
Cdd:PRK11176 402 LDGHDLRDYTLASLRNQvaLVSQNvhlfndTIANNIAYARTEQYSREQIEEAarMAYAMDFINKMDNGLDTVigengVLL 481
|
170 180 190
....*....|....*....|....*....|....
gi 1411607396 442 SGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVET 475
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
330-472 |
6.21e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.19 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRG--LVKGGTkleVAYFDQYRDQLDpeQTVMDNVGEG 407
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDasVVIRGT---VAYVPQVSWIFN--ATVRDNILFG 702
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 408 KQEVMVR-GRSRHILGYLQDFLFEPKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PLN03130 703 SPFDPERyERAIDVTALQHDLDLLPGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-229 |
6.31e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 135 FETRISQV--LTLLNLDPDATLDSLSGGWLRKVALARALACDPD--LLLLDEPTNHLDIEAINWLEDFLKDFR---GAIV 207
Cdd:PRK00635 453 LKSRLSILidLGLPYLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRdqgNTVL 532
|
90 100
....*....|....*....|..
gi 1411607396 208 FISHDREFIhKLATRIIDLDRG 229
Cdd:PRK00635 533 LVEHDEQMI-SLADRIIDIGPG 553
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
15-278 |
7.77e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 15 DFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGRMVQQQDLKVTRLeqDPPASSDLTVFDYTAEGLAGV 94
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAI--SAGLSGQLTGIENIEFKMLCM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 95 GELLKKYHHISMELAHdpsdaniriMSDLQEQLdYQngwqfetrisqvltllnldpdaTLDSLSGGWLRKVALARALACD 174
Cdd:PRK13546 114 GFKRKEIKAMTPKIIE---------FSELGEFI-YQ----------------------PVKKYSSGMRAKLGFSINITVN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 175 PDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIHKLATRIIDLDRGVITSWpGNYDEYLQGKEEALRv 251
Cdd:PRK13546 162 PDILVIDEALSVGDQTFAQKCLDKIYEFKEQnktIFFVSHNLGQVRQFCTKIAWIEGGKLKDY-GELDDVLPKYEAFLN- 239
|
250 260
....*....|....*....|....*..
gi 1411607396 252 eelqhaEFDRKLAQEEVWVRQGIKARR 278
Cdd:PRK13546 240 ------DFKKKSKAEQKEFRNKLDESR 260
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
154-214 |
7.88e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 7.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 154 LDSLSGG------WLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDF----LKDFRG--AIVFISHDRE 214
Cdd:PRK01156 799 IDSLSGGektavaFALRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIieysLKDSSDipQVIMISHHRE 871
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-227 |
8.86e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.01 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 36 GRNGAGKSTLMKIIAGELPLDDGRMVQQ-------QDLKVTRLEQDPPASSDLTVFDYtaeglagvgelLKKYHHISMEL 108
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKncninniAKPYCTYIGHNLGLKLEMTVFEN-----------LKFWSEIYNSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 109 AHDPSDANIRIMSDLQEQLDYqngwqfetrisqvltllnldpdatldSLSGGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK13541 102 ETLYAAIHYFKLHDLLDEKCY--------------------------SLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1411607396 189 IEAINWLEDF--LKDFRGAIVFISHDREFIHKLAtRIIDLD 227
Cdd:PRK13541 156 KENRDLLNNLivMKANSGGIVLLSSHLESSIKSA-QILQLD 195
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
321-377 |
9.39e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 41.51 E-value: 9.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK 377
Cdd:PRK11300 7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIL 63
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
11-187 |
2.11e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 11 LSFSDFPLLDNAELSIERGERL-CLVGRNGAGKSTLMKIIA---------------GELPLDDGRMVQQQDL----KVTR 70
Cdd:COG3950 6 LTIENFRGFEDLEIDFDNPPRLtVLVGENGSGKTTLLEAIAlalsgllsrlddvkfRKLLIRNGEFGDSAKLilyyGTSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 71 LEQDPPASSDLTVFDYTAEGLAGVGELLKkyhhismelahdpSDANIR----IMSDLQEQLDYQNGWQFETRISQVLTLL 146
Cdd:COG3950 86 LLLDGPLKKLERLKEEYFSRLDGYDSLLD-------------EDSNLRefleWLREYLEDLENKLSDELDEKLEAVREAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411607396 147 N-LDPDA----------------------TLDSLSGG------W----LRKVALARALACDPD----LLLLDEPTNHL 187
Cdd:COG3950 153 NkLLPDFkdiridrdpgrlvildkngeelPLNQLSDGersllaLvgdlARRLAELNPALENPLegegIVLIDEIDLHL 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
158-261 |
2.19e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.87 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIEAINWLEDFLKDF--RGAIVFISHD-REFIHKLATRIIDLDRGVITSw 234
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvrDGATVLLTTQyMEEAEQLAHELTVIDRGRVIA- 224
|
90 100
....*....|....*....|....*....
gi 1411607396 235 PGNYDEyLQGK--EEALRVEELQHAEFDR 261
Cdd:NF000106 225 DGKVDE-LKTKvgGRTLQIRPAHAAELDR 252
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
309-377 |
2.23e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.80 E-value: 2.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 309 MDDVNRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVK 377
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLE 69
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
331-473 |
2.42e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.84 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKS----TLIKLL--------------LGQ--LEPSRGLVKG--GTKLEVAyFD 388
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypsgdirfHGEslLHASEQTLRGvrGNKIAMI-FQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 389 QYRDQLDPEQTVMdnvgegKQ--EVMV--RGRSR-----HILGYLQDFLFE--PKRARTPVKALSGGEKNRLLLAKLFLK 457
Cdd:PRK15134 100 EPMVSLNPLHTLE------KQlyEVLSlhRGMRReaargEILNCLDRVGIRqaAKRLTDYPHQLSGGERQRVMIAMALLT 173
|
170
....*....|....*.
gi 1411607396 458 PSNLLILDEPTNDLDV 473
Cdd:PRK15134 174 RPELLIADEPTTALDV 189
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
33-268 |
2.94e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 33 CLVGRNGAGKSTLMKII---------AGELPLDDGRMVQQQDLKVTRLEQDPPASSDLTVFDYTAEGLAGVGELLKKYHH 103
Cdd:pfam13304 3 VLIGPNGSGKSNLLEALrfladfdalVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLERED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 104 ISMELAHDPSDANIRIMSDLQEQLDYQNGWQFETRISQVLTLLNLDPDAtldslsggwlrkVALARALACDPDLLLLDEP 183
Cdd:pfam13304 83 VEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELS------------LSELSDLISGLLLLSIISP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 184 TNHLDIEAINWLEDFLKDFRGA--IVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYLQGKEEALRVEELQHAEFDR 261
Cdd:pfam13304 151 LSFLLLLDEGLLLEDWAVLDLAadLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGG 230
|
....*..
gi 1411607396 262 KLAQEEV 268
Cdd:pfam13304 231 ELPAFEL 237
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
156-226 |
3.42e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 3.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411607396 156 SLSGGWLRKVALARAL---ACDPDLLLLDEPTNHLDIEAINWLEDFLKDFRGA---IVFISHDREFIhKLATRIIDL 226
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgntVVVIEHNLDVI-KTADYIIDL 904
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
349-471 |
3.46e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 349 ALVGPNGCGKSTLIKLLLGQLEPSRG--LVKG------GTK--LE--VAYFDQYRDQLDpEQTVMDNVGEGK-------- 408
Cdd:PRK10982 28 ALMGENGAGKSTLLKCLFGIYQKDSGsiLFQGkeidfkSSKeaLEngISMVHQELNLVL-QRSVMDNMWLGRyptkgmfv 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411607396 409 -QEVMVRgRSRHILGYLqDFLFEPkraRTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:PRK10982 107 dQDKMYR-DTKAIFDEL-DIDIDP---RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
325-475 |
3.63e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 39.69 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 325 LGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGL-VKGGTKLEVAYFDQYRDQLDPEQ----- 398
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrYSGDVLLGGRSIFNYRDVLEFRRrvgml 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 399 ---------TVMDNVGEGKQEVMVRGRsRHILGYLQDFLFE--------PKRARTPVKaLSGGEKNRLLLAKLFLKPSNL 461
Cdd:PRK14271 107 fqrpnpfpmSIMDNVLAGVRAHKLVPR-KEFRGVAQARLTEvglwdavkDRLSDSPFR-LSGGQQQLLCLARTLAVNPEV 184
|
170
....*....|....
gi 1411607396 462 LILDEPTNDLDVET 475
Cdd:PRK14271 185 LLLDEPTSALDPTT 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
152-191 |
4.01e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.10 E-value: 4.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1411607396 152 ATLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIEA 191
Cdd:PRK10982 387 TQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGA 426
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
437-471 |
4.61e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 4.61e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1411607396 437 PVKALSGGEKNRLLLAKLFLKPSN---LLILDEPTNDL 471
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGL 863
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
439-472 |
4.74e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 4.74e-03
10 20 30
....*....|....*....|....*....|....
gi 1411607396 439 KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
338-504 |
4.86e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 39.38 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGG-----TKLEVAYFDQYRDQLD-----PE-QTVMDNVge 406
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDdititHKTKDKYIRPVRKRIGmvfqfPEsQLFEDTV-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 407 gKQEVM------------VRGRSRHIL---GYLQDFLfepkrARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:PRK13646 104 -EREIIfgpknfkmnldeVKNYAHRLLmdlGFSRDVM-----SQSPFQ-MSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1411607396 472 D----VETLELLEELLADYPGTLLLVSHDR----RFIDNTV 504
Cdd:PRK13646 177 DpqskRQVMRLLKSLQTDENKTIILVSHDMnevaRYADEVI 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
157-231 |
4.87e-03 |
|
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: 39.80 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIEAinwlEdflKDFRGAIVFISHDREFI---HKLAT-----RIIDLDR 228
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT----E---RAIQAALREVARGRTTLviaHRLSTivdadEILVLEA 567
|
...
gi 1411607396 229 GVI 231
Cdd:COG5265 568 GRI 570
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
336-466 |
5.79e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLLGQLEPSRGLVKGGTKLEVAYFDQyrdQLDPEQTVMDNVgEGKQEVM--- 412
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISA---GLSGQLTGIENI-EFKMLCMgfk 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1411607396 413 ---VRGRSRHILGY--LQDFLFEpkrartPVKALSGGEKNRLLLAKLFLKPSNLLILDE 466
Cdd:PRK13546 117 rkeIKAMTPKIIEFseLGEFIYQ------PVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
349-473 |
5.85e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 39.47 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 349 ALVGPNGCGKSTLIKLLLGQLEPSRGLVK-GGTKLevayFDQYRD-QLDPEQ----------------TVMDNVGEGKQE 410
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVlNGRVL----FDAEKGiCLPPEKrrigyvfqdarlfphyKVRGNLRYGMAK 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411607396 411 VMvRGRSRHILGYLQdflFEPKRARTPVkALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11144 104 SM-VAQFDKIVALLG---IEPLLDRYPG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-188 |
7.32e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 39.31 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 14 SDFPLLDNAELSIERGERLCLVGRNGAGKSTLMKIIAGELPLDDGrMVQQQDLKVTRLEQDP----PASSDLTVF---DY 86
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG-DIRFHDIPLTKLQLDSwrsrLAVVSQTPFlfsDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 87 TAEGLAgvgelLKKYHHISMELAHDPSDANIRimsdlQEQLDYQNGWQFETRISQVLtllnldpdatldsLSGGWLRKVA 166
Cdd:PRK10789 405 VANNIA-----LGRPDATQQEIEHVARLASVH-----DDILRLPQGYDTEVGERGVM-------------LSGGQKQRIS 461
|
170 180
....*....|....*....|..
gi 1411607396 167 LARALACDPDLLLLDEPTNHLD 188
Cdd:PRK10789 462 IARALLLNAEILILDDALSAVD 483
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
437-471 |
7.72e-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: 38.75 E-value: 7.72e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1411607396 437 PVKALSGGEKNRLLLAKLFLKPSN---LLILDEPTNDL 471
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGL 203
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
153-216 |
8.63e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.52 E-value: 8.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411607396 153 TLDSLSGGWLRKVALARALACD---PDLLLLDEPTNHLDIEAINWLEDFLKDF---RGAIVFISHDREFI 216
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLSAlpkGGLLLIDEPESGLHPKLLRRLLELLKELsrnGAQLILTTHSPLLL 302
|
|
|