|
Name |
Accession |
Description |
Interval |
E-value |
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-686 |
9.49e-142 |
|
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: 431.18 E-value: 9.49e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 3 RKKIKFIPQMTSFDCGPSCLAMIMHYYGSAVQASEIRNSKIINKKSAwSLLDIKKVSKSYGLSATAYRIEnITDLQRIQK 82
Cdd:COG2274 1 RRKVPFVLQMEAADCGLACLAMIARYYGRPVSLEELREALGVSRDGL-SLLGLLRAARRLGLRARGVRLD-LEELAELPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 83 PMIAFWGFNHFVIIERVKANKFYIVDPKAGPMIIDIRSFEEMFCDYILVIENKKDIQP-NTKRREKHILLRYIDHFvsPS 161
Cdd:COG2274 79 PAILHWDGNHFVVLEGVDGDKVTIADPATGRRKLSLEEFAESWTGVALLLEPTPEFDKrGEKPFGLRWFLRLLRRY--RR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 162 QIVLLALLALLAQISILAFPFILKKFMD--ILNASKEVdvryLLIILGSLIVVIGIKSITSIIK----VNFQKEIDRKST 235
Cdd:COG2274 157 LLLQVLLASLLINLLALATPLFTQVVIDrvLPNQDLST----LWVLAIGLLLALLFEGLLRLLRsyllLRLGQRIDLRLS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 236 TKVFEHMFNIPIEKITSRHAGDLNVRIMSLESIRGYILEDLIEMIISIVVIIPLLMYLLYTETFYTLILMFFIASSLFIN 315
Cdd:COG2274 233 SRFFRHLLRLPLSFFESRSVGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 316 ISLGKFIYNANLVETYYLGEHRGKINESLKAMYYVKATGIFSKIKSVWKKDYNKYLDTVHKRVLKQNALESFNSSLSTIF 395
Cdd:COG2274 313 LLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 396 IIIMLAVGFYNFSKGE---GDLsnIFFFIAISSIIfSPVSTIIGSILNWNSVKPLLLRTLDILEEELEKDGSDTKVNI-- 470
Cdd:COG2274 393 TVALLWLGAYLVIDGQltlGQL--IAFNILSGRFL-APVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLpr 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 471 LRGSIEFNNISFSF--DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRK 548
Cdd:COG2274 470 LKGDIELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 549 NVGLMTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQ-----FQSIndilISEGGTNFSGGQRQRLAMLRL 623
Cdd:COG2274 550 QIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEalpmgYDTV----VGEGGSNLSGGQRQRLAIARA 625
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 624 FMKEYPILILDEPTNHLDRETANAVIENIFAM--PSTKIIITHDENILERVDRVYELTDKKLKQR 686
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
178-664 |
5.55e-90 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 292.07 E-value: 5.55e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 178 LAFPFILKKFMDILNASKevDVRYLLIILGSLIVVIGIKSITSIIKVNFQKEIDRKST----TKVFEHMFNIPIEKITSR 253
Cdd:COG1132 38 LLLPLLLGRIIDALLAGG--DLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVadlrRDLFEHLLRLPLSFFDRR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 254 HAGDLNVRIMS-LESIRGYILEDLIEMIISIVVIIPLLMYLLYTETFYTLILMFFIASSLFINISLGKFIYNANLVETYY 332
Cdd:COG1132 116 RTGDLLSRLTNdVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 333 LGEHRGKINESLKAMYYVKATGIFSKIKSVWKKDYNKYLDTVHKRVLKQNALESFNSSLSTIFIIIMLAVGFYNFSKGEG 412
Cdd:COG1132 196 LAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 413 DLSNIFFFIAISSIIFSPVSTIIGSILNWNSVKPLLLRTLDILEEELE-KDGSDTK-VNILRGSIEFNNISFSFD-DKKI 489
Cdd:COG1132 276 TVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEiPDPPGAVpLPPVRGEIEFENVSFSYPgDRPV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 490 IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMTQDGVLFRGSLSENLS 569
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIR 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 570 YFDINYDPSKIQESIDKLNLSNYIQ-----FQSIndilISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRET 644
Cdd:COG1132 436 YGRPDATDEEVEEAAKAAQAHEFIEalpdgYDTV----VGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTET 511
|
490 500
....*....|....*....|..
gi 1261268082 645 ANAVIENIFAMPS--TKIIITH 664
Cdd:COG1132 512 EALIQEALERLMKgrTTIVIAH 533
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
11-687 |
1.45e-87 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 289.54 E-value: 1.45e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 11 QMTSFDCGPSCLAMIMHYYGSAVQASEIRN----SKiiNKKSAWSLLdikKVSKSYGLSATAYRIEnITDLQRIQKPMIA 86
Cdd:TIGR03796 7 QMEAVECGAASLAMILAYYGRYVPLEELREecgvSR--DGSKASNLL---KAARSYGLEAKGFRKE-LDALAELPLPYIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 87 FWGFNHFVIIERVKANKFYIVDPKAGPMIIDIRSFEEMFCDYILVIENKKDIQPNTKRRE-KHILLRYIDHfvSPSQIVL 165
Cdd:TIGR03796 81 FWNFNHFVVVEGFRGGRVYLNDPALGPRTVSLEEFDESFTGVVLTFEPGPEFQKGGRKPSlLRALWRRLRG--SRGALLY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 166 LALLALLAQISILAFPFILKKFMD-ILNASKEVDVRYLLIILGSLIVVIGIKS-ITSIIKVNFQKEIDRKSTTKVFEHMF 243
Cdd:TIGR03796 159 LLLAGLLLVLPGLVIPAFSQIFVDeILVQGRQDWLRPLLLGMGLTALLQGVLTwLQLYYLRRLEIKLAVGMSARFLWHIL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 244 NIPIEKITSRHAGDLNVRIMSLESIRGYILEDLIEMIISIVVII--PLLMYLlytetfYTLILMFFIASSLFINISLGKF 321
Cdd:TIGR03796 239 RLPVRFFAQRHAGDIASRVQLNDQVAEFLSGQLATTALDAVMLVfyALLMLL------YDPVLTLIGIAFAAINVLALQL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 322 IYNANLVETYYLGEHRGKINES----LKAMYYVKATGIFSKIKSVWKKDYNKYLDTVHKRVLKQNALESFNSSLSTIFII 397
Cdd:TIGR03796 313 VSRRRVDANRRLQQDAGKLTGVaisgLQSIETLKASGLESDFFSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLNSA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 398 IMLAVGFYNFSkgEGDLSnIFFFIAISSIIFS---PVSTIIGSILNWNSVKPLLLRTLDILE-------EELEKDGSDT- 466
Cdd:TIGR03796 393 LILVVGGLRVM--EGQLT-IGMLVAFQSLMSSflePVNNLVGFGGTLQELEGDLNRLDDVLRnpvdpllEEPEGSAATSe 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 467 KVNILRGSIEFNNISFSFD--DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSE 544
Cdd:TIGR03796 470 PPRRLSGYVELRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPRE 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 545 ELRKNVGLMTQDGVLFRGSLSENLSYFDinydpskiqESIDKLNLSNYIQFQSINDIL----------ISEGGTNFSGGQ 614
Cdd:TIGR03796 550 VLANSVAMVDQDIFLFEGTVRDNLTLWD---------PTIPDADLVRACKDAAIHDVItsrpggydaeLAEGGANLSGGQ 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 615 RQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTKIIITH--------DENI-LERVDRVYELTDKKLKQ 685
Cdd:TIGR03796 621 RQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRRGCTCIIVAHrlstirdcDEIIvLERGKVVQRGTHEELWA 700
|
..
gi 1261268082 686 RE 687
Cdd:TIGR03796 701 VG 702
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
380-686 |
1.73e-64 |
|
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: 223.87 E-value: 1.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 380 KQNALESFNSSLST----IFIIIMLAVGFYNFskGEGDLSNI----FFFIAISSiiFSPVSTIIGSILNWNSVKPLLLRT 451
Cdd:COG4987 234 RLARLSALAQALLQlaagLAVVAVLWLAAPLV--AAGALSGPllalLVLAALAL--FEALAPLPAAAQHLGRVRAAARRL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 452 LDILEEELE-KDGSDTKVNILRGSIEFNNISFSFDD--KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDK 528
Cdd:COG4987 310 NELLDAPPAvTEPAEPAPAPGGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQS 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 529 GNILIDDRDIKDWNSEELRKNVGLMTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQfQSIN--DILISEG 606
Cdd:COG4987 390 GSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLA-ALPDglDTWLGEG 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 607 GTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIF-AMP-STKIIITHDENILERVDRVYELTDKKLK 684
Cdd:COG4987 469 GRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLeALAgRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
..
gi 1261268082 685 QR 686
Cdd:COG4987 549 EQ 550
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
383-686 |
3.35e-62 |
|
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: 217.32 E-value: 3.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 383 ALESFnSSLSTIFIIIMLAVGFYNfskGEGDLSNIFFFIAISSIIFSPvstiigsilnwnsvkpllLRTL---------- 452
Cdd:COG4988 247 VLEFF-ASLSIALVAVYIGFRLLG---GSLTLFAALFVLLLAPEFFLP------------------LRDLgsfyharang 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 453 --------DILEEELEKDGSDTKVNILRG--SIEFNNISFSFDD-KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLL 521
Cdd:COG4988 305 iaaaekifALLDAPEPAAPAGTAPLPAAGppSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 522 KLHTPDKGNILIDDRDIKDWNSEELRKNVGLMTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIqfQSINDI 601
Cdd:COG4988 385 GFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFV--AALPDG 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 602 L---ISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTK--IIITHDENILERVDRVY 676
Cdd:COG4988 463 LdtpLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRtvILITHRLALLAQADRIL 542
|
330
....*....|
gi 1261268082 677 ELTDKKLKQR 686
Cdd:COG4988 543 VLDDGRIVEQ 552
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
228-675 |
4.68e-57 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 205.87 E-value: 4.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 228 KEIDRKSTTKVFEHMFNIPIEKitsRHA--GDLNVRIMSLESIRGYI-------LEDL---------IEMIISIVVIIPL 289
Cdd:TIGR03375 216 KKADLILSAKLFERVLGLRMEA---RPAsvGSFANQLREFESVRDFFtsatltaLIDLpfallfllvIAIIGGPLVWVPL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 290 LMYLLytetfytlILMFfiasSLFINISLGKFIyNANLVETYylgEHRGKINESLKAMYYVKATGIFSKIKSVWKKdYNK 369
Cdd:TIGR03375 293 VAIPL--------ILLP----GLLLQRPLSRLA-EESMRESA---QRNAVLVESLSGLETIKALNAEGRFQRRWEQ-TVA 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 370 YLDTV--HKRVLKQNA--LESFNSSLSTIFIIImlaVGFYNFSKGE---GDLsnifffIA---ISSIIFSPVSTIIGSIL 439
Cdd:TIGR03375 356 ALARSglKSRFLSNLAtnFAQFIQQLVSVAIVV---VGVYLISDGEltmGGL------IAcvmLSGRALAPLGQLAGLLT 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 440 NWNSVKPLLLRTLDILEEELEKDGSDTKVN--ILRGSIEFNNISFSF--DDKKIIENLSLNIKNNESIAIVGESGSGKST 515
Cdd:TIGR03375 427 RYQQAKTALQSLDELMQLPVERPEGTRFLHrpRLQGEIEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKST 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 516 LANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQ- 594
Cdd:TIGR03375 507 LLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRr 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 595 ----FqsinDILISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS--TKIIITHDENI 668
Cdd:TIGR03375 587 hpdgL----DMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAgkTLVLVTHRTSL 662
|
....*..
gi 1261268082 669 LERVDRV 675
Cdd:TIGR03375 663 LDLVDRI 669
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
475-682 |
3.19e-56 |
|
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: 189.13 E-value: 3.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDD--KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGL 552
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLFRGSLSENLsyfdinydpskiqesidklnlsnyiqfqsindiliseggtnFSGGQRQRLAMLRLFMKEYPILI 632
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 633 LDEPTNHLDRETANAVIENIFAMP--STKIIITHDENILERVDRVYELTDKK 682
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAkgKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
473-675 |
7.33e-56 |
|
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: 189.72 E-value: 7.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 473 GSIEFNNISFSFDDKKI--IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNV 550
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQFQSIN-DILISEGGTNFSGGQRQRLAMLRLFMKEYP 629
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGlDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1261268082 630 ILILDEPTNHLDRETANAVIENIFAMPSTK--IIITHDENILERVDRV 675
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKtlIIITHRPSLLDLVDRI 208
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
18-683 |
6.33e-50 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 185.72 E-value: 6.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 18 GPSCLAMIMHYYGSAVQASEIRNSKIINKKSAwSLLDIKKVSKSYGLSATAYRIeNITDLQRIQKPMIAFWGFNHFVIIe 97
Cdd:TIGR01846 1 GLEALSLLAQVHNIAVTPSQLRHMLGHAGASL-DDLEILLAAKQLGLKAKAVKV-SIGRLNKLPLPALIDGEGGWFVLG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 98 RVKANKFYIVDP-KAGPMIIDIRSFEEMFCDYILVIENKkdiQPNTKRrEKHILLRYIDHFV-SPSQIVLLALLALLAQI 175
Cdd:TIGR01846 78 KLTANGVTIYDPpGDAPEVLSREVLEALWSGTVILLATR---SVAGKA-LKFGFSWFIPAIIrYRKQFREVLLISLALQL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 176 SILAFPFILKKFMDILNASKEVDVryLLIILGSLIVV----IGIKSITSIIKVNFQKEIDRKSTTKVFEHMFNIPIEKIT 251
Cdd:TIGR01846 154 FALVTPLLFQVVIDKVLVHRGLST--LSVLALAMLAVaifePALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 252 SRHAGDLNVRIMSLESIRGYILEDLIEMIISIVVIIPLLMYLLYTETFYTLI----LMFFIASSLFINISLGKFI---YN 324
Cdd:TIGR01846 232 SRRVGDTVARVRELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVvigsLVCYALLSVFVGPILRKRVedkFE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 325 ANLVETYYLgehrgkiNESLKAMYYVKATGIFSKIKSVWKKDYNKYLDTVHKRVLKQNALESFNSSLSTIFIIIMLAVGF 404
Cdd:TIGR01846 312 RSAAATSFL-------VESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 405 YNFSKGEGDLSNIFFFIAISSIIFSPVSTIIGSILNWNSVKPLLLRTLDILEEELEkDGSDTKVNI--LRGSIEFNNISF 482
Cdd:TIGR01846 385 HLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTE-PRSAGLAALpeLRGAITFENIRF 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 483 SF--DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMTQDGVLF 560
Cdd:TIGR01846 464 RYapDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLF 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 561 RGSLSENLSYFDINYDPSKIQESIDKLNLSNYI--QFQSINDIlISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTN 638
Cdd:TIGR01846 544 SRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFIseLPQGYNTE-VGEKGANLSGGQRQRIAIARALVGNPRILIFDEATS 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1261268082 639 HLDRETANAVIENIFAMPS--TKIIITHDENILERVDRVYELTDKKL 683
Cdd:TIGR01846 623 ALDYESEALIMRNMREICRgrTVIIIAHRLSTVRACDRIIVLEKGQI 669
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
181-686 |
5.50e-49 |
|
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: 181.07 E-value: 5.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 181 PFILKKFMDILN-----ASKEVDVRYLLIILGsLIVVIGIKSITS---IIKVNfqKEIDRKSTTKVFEHMFNIPIEKITS 252
Cdd:TIGR02203 31 STLAALLKPLLDdgfggRDRSVLWWVPLVVIG-LAVLRGICSFVStylLSWVS--NKVVRDIRVRMFEKLLGLPVSFFDR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 253 RHAGDLNVRIMSL-ESIRGYILEDLIEMIISIVVIIPLLMYLLYTETFYTLIL---------MFFIASSLFINISlgKFI 322
Cdd:TIGR02203 108 QPTGTLLSRITFDsEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVvvmlpvlsiLMRRVSKRLRRIS--KEI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 323 YNANlvetyylGEHRGKINESLKAMYYVKATGIfskiKSVWKKDYNKYLDTVHKRVLKQNALESFNSSLSTIFIIIMLAV 402
Cdd:TIGR02203 186 QNSM-------GQVTTVAEETLQGYRVVKLFGG----QAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 403 GFY--NFSKGEGDLS--NIFFFIAISSIIFSPvstiIGSILNWNSVKPLLL----RTLDILEEELEKDGSDTKVNILRGS 474
Cdd:TIGR02203 255 VLFiaLFQAQAGSLTagDFTAFITAMIALIRP----LKSLTNVNAPMQRGLaaaeSLFTLLDSPPEKDTGTRAIERARGD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF--DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGL 552
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLFRGSLSENLSYFDI-NYDPSKIQESIDKLNLSNYIQfQSIN--DILISEGGTNFSGGQRQRLAMLRLFMKEYP 629
Cdd:TIGR02203 411 VSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVD-KLPLglDTPIGENGVLLSGGQRQRLAIARALLKDAP 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261268082 630 ILILDEPTNHLDRETANAV---IENIfaMPS-TKIIITHDENILERVDRVYELTDKKLKQR 686
Cdd:TIGR02203 490 ILILDEATSALDNESERLVqaaLERL--MQGrTTLVIAHRLSTIEKADRIVVMDDGRIVER 548
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
238-686 |
7.46e-49 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 182.46 E-value: 7.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 238 VFEHMFNIPIEKITSRHAGDLNVRIMSLESIRgyiledlieMIISIVVIIPLLMYLLyteTFYTLILMFF------IASS 311
Cdd:TIGR03797 215 VWDRLLRLPVSFFRQYSTGDLASRAMGISQIR---------RILSGSTLTTLLSGIF---ALLNLGLMFYyswklaLVAV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 312 LFINISLGKFIYnANLVETYYLG---EHRGKINeslkAMYYVKATGIfSKIK---------SVWKKDYNKYLDTVHKRVL 379
Cdd:TIGR03797 283 ALALVAIAVTLV-LGLLQVRKERrllELSGKIS----GLTVQLINGI-SKLRvagaenrafARWAKLFSRQRKLELSAQR 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 380 KQNALESFNSSLSTIF--IIIMLAVGFYnfskGEGDLSN---IFFFIAISSIIFSpVSTIIGSILNWNSVKPLLLRTLDI 454
Cdd:TIGR03797 357 IENLLTVFNAVLPVLTsaALFAAAISLL----GGAGLSLgsfLAFNTAFGSFSGA-VTQLSNTLISILAVIPLWERAKPI 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 455 LEEELEKDGSDTKVNILRGSIEFNNISFSFDDK--KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNIL 532
Cdd:TIGR03797 432 LEALPEVDEAKTDPGKLSGAIEVDRVTFRYRPDgpLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVF 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 533 IDDRDIKDWNSEELRKNVGLMTQDGVLFRGSLSENLsyfdINYDPSKIQESIDKLNLSNYIQfqsinDI---------LI 603
Cdd:TIGR03797 512 YDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI----AGGAPLTLDEAWEAARMAGLAE-----DIrampmgmhtVI 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 604 SEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTKIIITHDENILERVDRVYELTDKKL 683
Cdd:TIGR03797 583 SEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRV 662
|
...
gi 1261268082 684 KQR 686
Cdd:TIGR03797 663 VQQ 665
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
473-685 |
8.99e-48 |
|
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: 168.17 E-value: 8.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 473 GSIEFNNISFSFDDKK-IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVG 551
Cdd:cd03254 1 GEIEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 552 LMTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQFqSIN--DILISEGGTNFSGGQRQRLAMLRLFMKEYP 629
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMK-LPNgyDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261268082 630 ILILDEPTNHLDRETANAVIENIFAM--PSTKIIITHDENILERVDRVYELTDKKLKQ 685
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
475-683 |
1.70e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 163.83 E-value: 1.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMT 554
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLFRGSLSENL----SYFDINYDPSKIQESIDKLNLSNYIQFQSINDIliseggtnfSGGQRQRLAMLRLFMKEYPI 630
Cdd:COG4619 81 QEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKPVERL---------SGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261268082 631 LILDEPTNHLDRETANAVIENIFAMPSTK----IIITHDENILERV-DRVYELTDKKL 683
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEgravLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
475-686 |
5.68e-46 |
|
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: 163.56 E-value: 5.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF--DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGL 552
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYI-QFQSINDILISEGGTNFSGGQRQRLAMLRLFMKEYPIL 631
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFImELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1261268082 632 ILDEPTNHLDRETANAVIENI--FAMPSTKIIITHDENILERVDRVYELTDKKLKQR 686
Cdd:cd03251 161 ILDEATSALDTESERLVQAALerLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVER 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
474-675 |
2.18e-44 |
|
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: 167.08 E-value: 2.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDK-KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGL 552
Cdd:TIGR02857 321 SLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQF--QSInDILISEGGTNFSGGQRQRLAMLRLFMKEYPI 630
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAAlpQGL-DTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1261268082 631 LILDEPTNHLDRETANAVIENI--FAMPSTKIIITHDENILERVDRV 675
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALraLAQGRTVLLVTHRLALAALADRI 526
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
475-676 |
1.79e-43 |
|
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: 156.55 E-value: 1.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFD---DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVG 551
Cdd:cd03249 1 IEFKNVSFRYPsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 552 LMTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQ-FQSINDILISEGGTNFSGGQRQRLAMLRLFMKEYPI 630
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMsLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1261268082 631 LILDEPTNHLDRETANAVIENI--FAMPSTKIIITHDENILERVDRVY 676
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALdrAMKGRTTIVIAHRLSTIRNADLIA 208
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
475-664 |
2.71e-42 |
|
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: 153.15 E-value: 2.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDD-KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLM 553
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYI-QFQSINDILISEGGTNFSGGQRQRLAMLRLFMKEYPILI 632
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKImRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190
....*....|....*....|....*....|....
gi 1261268082 633 LDEPTNHLDRETANAVIENIFAMPS--TKIIITH 664
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKgrTTIVIAH 194
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
11-683 |
5.61e-42 |
|
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: 162.60 E-value: 5.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 11 QMTSFDCGPSCLAMIMHYYGSAVQASEIRNSKIINKKSAwSLLDIKKVSKSYGLSATAYRI-ENITDLQRIQKPMIAF-- 87
Cdd:TIGR01193 1 QVDEKDCGIAALSMILKKYGTEYSLAKLRQLAKTDLEGT-TVLGLVKAAEYLNFEAKAIQAdMSLFEDKNLPLPFIAHvi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 88 --WGFNHFVIIERVKANKFYIVDPKAGPMIIDI--RSFEEMFCDYILVIENKKDIQPNTKRRekHILLRYIDHFVSPSQI 163
Cdd:TIGR01193 80 knGKLPHYYVVYGVTKNHLIIADPDPTVGITKIskEDFYEEWTGIAIFISPTPEYKPIKEKE--NSLLKFIPLITRQKKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 164 VLLALL--ALLAQISILAfPFILKKFMDILNASKEVDVryLLIILGSLIVVIGIKSITSIIKVNFQKEIDRKSTTKV--- 238
Cdd:TIGR01193 158 IVNIVIaaIIVTLISIAG-SYYLQKIIDTYIPHKMMGT--LGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIils 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 239 -FEHMFNIPIEKITSRHAGDLNVRIMSLESIRGYILEDLIEMIISIVVIIPLLMYLLYTETFYTLILMFFIASSLFINIS 317
Cdd:TIGR01193 235 yIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIIL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 318 LGKFIYNANLVETYYLGEHRGKINESLKAMYYVKATGI----FSKIKSVWKKDYNKYLdTVHKRVLKQNALESfnsSLST 393
Cdd:TIGR01193 315 FKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSeaerYSKIDSEFGDYLNKSF-KYQKADQGQQAIKA---VTKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 394 IFIIIMLAVGFYNFSKGEGDLSNIFFFIAISSIIFSPVSTIIG--SILNWNSVKPLLLRTLDILEEELEKDGSDTKVNIL 471
Cdd:TIGR01193 391 ILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINlqPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 472 RGSIEFNNISFSFD-DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNV 550
Cdd:TIGR01193 471 NGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFI 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDGVLFRGSLSENLSyfdINYDPSKIQESIDKLNLSNYI-----QFQSINDILISEGGTNFSGGQRQRLAMLRLFM 625
Cdd:TIGR01193 551 NYLPQEPYIFSGSILENLL---LGAKENVSQDEIWAACEIAEIkddieNMPLGYQTELSEEGSSISGGQKQRIALARALL 627
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1261268082 626 KEYPILILDEPTNHLDRETANAVIENIFAMPSTKII-ITHDENILERVDRVYELTDKKL 683
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTIIfVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
475-683 |
8.16e-42 |
|
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: 149.67 E-value: 8.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKK--IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGL 552
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLFRGSLSENLsyfdinydpskiqesidklnlsnyiqfqsindiliseggtnFSGGQRQRLAMLRLFMKEYPILI 632
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1261268082 633 LDEPTNHLDRETANAVIENIFAMP---STKIIITHDENILERVDRVYELTDKKL 683
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKaagATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
175-684 |
1.79e-41 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 159.05 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 175 ISILAF--PFILKKFMDILNASKEVD--VRYLLIILGSLIVVIGIKSITSIIKVNFQKEIDRKSTTKVFEHMFNIPIEki 250
Cdd:TIGR01842 18 INILMLapPLYMLQVYDRVLTSGSVPtlLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGALNQPIFAASFSATLR-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 251 tsRHAGDLNVRIMSLESIRGYI-------LEDLIEMIISIVVIIPLLMYLLYTETFYTLILMffiASSLFINISLGKFIY 323
Cdd:TIGR01842 96 --RGSGDGLQALRDLDQLRQFLtgpglfaFFDAPWMPIYLLVCFLLHPWIGILALGGAVVLV---GLALLNNRATKKPLK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 324 NANLvetyYLGEHRGKINESLKAMYYVKATGIFSKIKSVWKKDYNKYLDTVHKRVLKQNALESFNSSLSTIFIIIMLAVG 403
Cdd:TIGR01842 171 EATE----ASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 404 FYNFSKGEGDLSNIfffIAiSSII----FSPVSTIIGSILNWNSVKPLLLRTLDILEEELEKDGSdTKVNILRGSIEFNN 479
Cdd:TIGR01842 247 AYLAIDGEITPGMM---IA-GSILvgraLAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPA-MPLPEPEGHLSVEN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 480 ISF--SFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMTQDG 557
Cdd:TIGR01842 322 VTIvpPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 558 VLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQ-FQSINDILISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEP 636
Cdd:TIGR01842 402 ELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILrLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEP 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1261268082 637 TNHLDRETANAVIENIFAMPS---TKIIITHDENILERVDRVYELTDKKLK 684
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKArgiTVVVITHRPSLLGCVDKILVLQDGRIA 532
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
450-683 |
5.55e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 158.06 E-value: 5.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 450 RTLDILEEELE-KDGSDTKVNILRGSIEFNNISFSFDDK--KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTP 526
Cdd:PRK11160 313 RINEITEQKPEvTFPTTSTAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 527 DKGNILIDDRDIKDWNSEELRKNVGLMTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQFQSINDILISEG 606
Cdd:PRK11160 393 QQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLEDDKGLNAWLGEG 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261268082 607 GTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTK--IIITHDENILERVDRVYELTDKKL 683
Cdd:PRK11160 473 GRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKtvLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
236-675 |
6.42e-41 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 158.20 E-value: 6.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 236 TKVFEHMFNIPIEKITSRHAGD-LNVRIMSLESIRGYILEDLIE---MIISIVVIIPLLMYLLYTETFYTLILMffIASS 311
Cdd:PRK13657 93 TEYFERIIQLPLAWHSQRGSGRaLHTLLRGTDALFGLWLEFMREhlaTLVALVVLLPLALFMNWRLSLVLVVLG--IVYT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 312 LFINISLGKFIYNANLVETYY--LGEHrgkINESLKAMYYVKAtgiFSKIKSVWK--KDYNKYLDTVHKRVLKQNALES- 386
Cdd:PRK13657 171 LITTLVMRKTKDGQAAVEEHYhdLFAH---VSDAIGNVSVVQS---YNRIEAETQalRDIADNLLAAQMPVLSWWALASv 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 387 FNSSLSTIFIIIMLAVGFYNFSKGEGDLSNIFFFIAISSIIFSPVSTIIGSILNWNSVKPLLLRTLDILEE--ELEKDGS 464
Cdd:PRK13657 245 LNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAvpDVRDPPG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 465 DTKVNILRGSIEFNNISFSFDDKK-IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNS 543
Cdd:PRK13657 325 AIDLGRVKGAVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 544 EELRKNVGLMTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQFQSIN-DILISEGGTNFSGGQRQRLAMLR 622
Cdd:PRK13657 405 ASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGyDTVVGERGRQLSGGERQRLAIAR 484
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1261268082 623 LFMKEYPILILDEPTNHLDRET---ANAVIENIfaMPS-TKIIITHDENILERVDRV 675
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETeakVKAALDEL--MKGrTTFIIAHRLSTVRNADRI 539
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
473-664 |
1.11e-40 |
|
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: 148.41 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 473 GSIEFNNISFSF--DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNV 550
Cdd:cd03244 1 GDIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDGVLFRGSLSENLSYFDInYDPSKIQESIDKLNLSNYIQFQSI-NDILISEGGTNFSGGQRQRLAMLRLFMKEYP 629
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGE-YSDEELWQALERVGLKEFVESLPGgLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1261268082 630 ILILDEPTNHLDRETAN---AVIENIFAmPSTKIIITH 664
Cdd:cd03244 160 ILVLDEATASVDPETDAliqKTIREAFK-DCTVLTIAH 196
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
475-694 |
4.45e-39 |
|
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: 144.01 E-value: 4.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF-DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLM 553
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQ--DGVLFRGSLSENLSYFDIN--YDPSKI----QESIDKLNLSNYIQfQSINDIliseggtnfSGGQRQRLAMLR-LF 624
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGPENlgLPREEIrervEEALELVGLEHLAD-RPPHEL---------SGGQKQRVAIAGvLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261268082 625 MKeyP-ILILDEPTNHLDRETANAVIENIFAMPS---TKIIITHD-ENILERVDRVYELTDKKL----KQREIFSKSKL 694
Cdd:COG1122 151 ME--PeVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDlDLVAELADRVIVLDDGRIvadgTPREVFSDYEL 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
471-675 |
6.41e-39 |
|
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: 143.38 E-value: 6.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 471 LRGSIEFNNISFSF---DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELR 547
Cdd:cd03248 8 LKGIVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 548 KNVGLMTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQ-FQSINDILISEGGTNFSGGQRQRLAMLRLFMK 626
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISeLASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1261268082 627 EYPILILDEPTNHLDRETANAVIENIFAMPS--TKIIITHDENILERVDRV 675
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAHRLSTVERADQI 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
475-675 |
2.22e-38 |
|
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: 142.24 E-value: 2.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF--DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGL 552
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYI-QFQSINDILISEGGTNFSGGQRQRLAMLRLFMKEYPIL 631
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFIsELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1261268082 632 ILDEPTNHLDRETANAVIENIFAMPS--TKIIITHDENILERVDRV 675
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAgrTVIIIAHRLSTVKNADRI 206
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
471-685 |
6.36e-38 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 150.64 E-value: 6.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 471 LRGSIEFNNISFSF---DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELR 547
Cdd:TIGR00958 475 LEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 548 KNVGLMTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQ-FQSINDILISEGGTNFSGGQRQRLAMLRLFMK 626
Cdd:TIGR00958 555 RQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMeFPNGYDTEVGEKGSQLSGGQKQRIAIARALVR 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1261268082 627 EYPILILDEPTNHLDRETANAVIENIFAMPSTKIIITHDENILERVDRVYELTDKKLKQ 685
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
475-687 |
1.60e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 139.41 E-value: 1.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKK----IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL---- 546
Cdd:COG1136 5 LELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 547 RKNVGLMTQDGVLFrGSLS--EN------LSYFDINYDPSKIQESIDKLNLSNYIQFqsindiLISEggtnFSGGQRQRL 618
Cdd:COG1136 85 RRHIGFVFQFFNLL-PELTalENvalpllLAGVSRKERRERARELLERVGLGDRLDH------RPSQ----LSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 619 AMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMP----STKIIITHDENILERVDRVYELTDKKLKQRE 687
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrelgTTIVMVTHDPELAARADRVIRLRDGRIVSDE 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
475-684 |
2.59e-37 |
|
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: 137.44 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFD--DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWnSEELRKNVGL 552
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLFRGSLSENLsyfdinydpskiqesidklnlsnyiqfqsindilisegGTNFSGGQRQRLAMLRLFMKEYPILI 632
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1261268082 633 LDEPTNHLDRETANAVIENIFAMPSTK--IIITHDENILERVDRVYELTDKKLK 684
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKtlIWITHHLTGIEHMDKILFLENGKII 175
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
476-682 |
5.73e-37 |
|
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: 137.60 E-value: 5.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 476 EFNNISFSFDD--KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLM 553
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQ--DGVLFRGSLSEnlsyfDINYDP-----------SKIQESIDKLNLSNYiQFQSINDiliseggtnFSGGQRQRLAM 620
Cdd:cd03225 81 FQnpDDQFFGPTVEE-----EVAFGLenlglpeeeieERVEEALELVGLEGL-RDRSPFT---------LSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 621 LRLFMKEYPILILDEPTNHLDRETANAVIE---NIFAMPSTKIIITHD-ENILERVDRVYELTDKK 682
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLEllkKLKAEGKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
203-675 |
1.17e-36 |
|
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: 145.28 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 203 LIILGSLIVVIGIKSITSIIKVNFQKEIDRKSTTKVFEHMFNIPIEKITSRHAGDLNvrimSLESIRGYI-------LED 275
Cdd:COG4618 64 LLALGLYAVMGLLDAVRSRILVRVGARLDRRLGPRVFDAAFRAALRGGGGAAAQALR----DLDTLRQFLtgpglfaLFD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 276 LIEMIISIVVII---PLLMYLlyteTFYTLILMFFIA--SSLFINISLGKFiyNANLVETYYLGEH--RGKinESLKAMy 348
Cdd:COG4618 140 LPWAPIFLAVLFlfhPLLGLL----ALVGALVLVALAllNERLTRKPLKEA--NEAAIRANAFAEAalRNA--EVIEAM- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 349 yvkatGIFSKIKSVWKKDYNKYLDTvhkrvlkQNALESFNSSLSTI--FI-----IIMLAVGFYNFSKGE---GDLsnif 418
Cdd:COG4618 211 -----GMLPALRRRWQRANARALAL-------QARASDRAGGFSALskFLrlllqSAVLGLGAYLVIQGEitpGAM---- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 419 ffIAiSSIIFS----PVSTIIGSILNWNSVKpLLLRTLDILEEELEKDGSDTKVNILRGSIEFNNISFSF--DDKKIIEN 492
Cdd:COG4618 275 --IA-ASILMGralaPIEQAIGGWKQFVSAR-QAYRRLNELLAAVPAEPERMPLPRPKGRLSVENLTVVPpgSKRPILRG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 493 LSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMTQDGVLFRGSLSENLSYFD 572
Cdd:COG4618 351 VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 573 iNYDPSKIQES---------IDKLNLSnYiqfqsinDILISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDR- 642
Cdd:COG4618 431 -DADPEKVVAAaklagvhemILRLPDG-Y-------DTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDe 501
|
490 500 510
....*....|....*....|....*....|....*
gi 1261268082 643 -ETA-NAVIENIFAMPSTKIIITHDENILERVDRV 675
Cdd:COG4618 502 gEAAlAAAIRALKARGATVVVITHRPSLLAAVDKL 536
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
428-666 |
2.39e-36 |
|
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: 143.66 E-value: 2.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 428 FSPVSTIIGSILNWNSVKPLLLRTLDILEEEL---------EKDGSDTKVnilrgSIEFNNISFSFDDKKII-ENLSLNI 497
Cdd:TIGR02868 284 FEAFAALPAAAQQLTRVRAAAERIVEVLDAAGpvaegsapaAGAVGLGKP-----TLELRDLSAGYPGAPPVlDGVSLDL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 498 KNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMTQDGVLFRGSLSENLSYFDINYDP 577
Cdd:TIGR02868 359 PPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 578 SKIQESIDKLNLSNYIQ-FQSINDILISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMP 656
Cdd:TIGR02868 439 EELWAALERVGLADWLRaLPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL 518
|
250
....*....|..
gi 1261268082 657 S--TKIIITHDE 666
Cdd:TIGR02868 519 SgrTVVLITHHL 530
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
490-638 |
2.92e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 133.54 E-value: 2.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 490 IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMTQDGVLFRG-SLSENL 568
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 569 SYFDINYDPSK------IQESIDKLNLSNyiqfqsINDILISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTN 638
Cdd:pfam00005 81 RLGLLLKGLSKrekdarAEEALEKLGLGD------LADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
476-682 |
5.46e-36 |
|
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: 132.75 E-value: 5.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 476 EFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMTQ 555
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 556 dgvlfrgslsenlsyfdinydpskiqesidklnlsnyiqfqsindiliseggtnFSGGQRQRLAMLRLFMKEYPILILDE 635
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1261268082 636 PTNHLDRETANAVIENIFAMPSTK---IIITHDENILERV-DRVYELTDKK 682
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGrtvIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
451-686 |
1.40e-35 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 142.47 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 451 TL-DILEEELEKDGSDTKVNILRGSIEFNNISFSFDDKKI--IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPD 527
Cdd:PRK11176 317 TLfAILDLEQEKDEGKRVIERAKGDIEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 528 KGNILIDDRDIKDWNSEELRKNVGLMTQDGVLFRGSLSENLSY-FDINYDPSKIQESIDKLNLSNYI-QFQSINDILISE 605
Cdd:PRK11176 397 EGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYaRTEQYSREQIEEAARMAYAMDFInKMDNGLDTVIGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 606 GGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS--TKIIITHDENILERVDRVYELTDKKL 683
Cdd:PRK11176 477 NGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAHRLSTIEKADEILVVEDGEI 556
|
...
gi 1261268082 684 KQR 686
Cdd:PRK11176 557 VER 559
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
475-683 |
2.42e-35 |
|
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: 133.00 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKK----IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL---- 546
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 547 RKNVGLMTQDGVLFRG-SLSENLSY-FDINYDPS-----KIQESIDKLNLSNYIqfqsinDILISEggtnFSGGQRQRLA 619
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELpLLLAGVPKkerreRAEELLERVGLGDRL------NHYPSE----LSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1261268082 620 MLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS----TKIIITHDENILERVDRVYELTDKKL 683
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeagtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
475-683 |
1.19e-34 |
|
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: 131.86 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL---RKNVG 551
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 552 LMTQDGVLFrGSLS--ENLSYF---DINYDPSKIQESI-DKLNLSNYIQFQsinDILISEggtnFSGGQRQRLAMLRLFM 625
Cdd:cd03261 81 MLFQSGALF-DSLTvfENVAFPlreHTRLSEEEIREIVlEKLEAVGLRGAE---DLYPAE----LSGGMKKRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 626 KEYPILILDEPTNHLDRETANAVIENIF----AMPSTKIIITHDEN-ILERVDRVYELTDKKL 683
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRslkkELGLTSIMVTHDLDtAFAIADRIAVLYDGKI 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
475-684 |
1.55e-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: 131.52 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDwNSEELRKNVGLMT 554
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLF-RGSLSENLSYF------DINYDPSKIQESIDKLNLSNYIqfqsinDILISEggtnFSGGQRQRLAMLRLFMKE 627
Cdd:COG4555 81 DERGLYdRLTVRENIRYFaelyglFDEELKKRIEELIELLGLEEFL------DRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261268082 628 YPILILDEPTNHLDRETANAVIENIFAM---PSTKIIITHDENILERV-DRVYELTDKKLK 684
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALcDRVVILHKGKVV 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
475-675 |
2.38e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 130.95 E-value: 2.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDwNSEELRKNVGLMT 554
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLFRG-SLSENLSYF------DINYDPSKIQESIDKLNLSNYIqfqsinDILISeggtNFSGGQRQRLAMLRLFMKE 627
Cdd:COG1131 80 QEPALYPDlTVRENLRFFarlyglPRKEARERIDELLELFGLTDAA------DRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 628 YPILILDEPTNHLDRETANAV---IENIFAMPSTKIIITHDENILERV-DRV 675
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELwelLRELAAEGKTVLLSTHYLEEAERLcDRV 201
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
472-664 |
5.72e-34 |
|
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: 137.64 E-value: 5.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 472 RGSIEFNNISFSFD-DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNV 550
Cdd:COG5265 355 GGEVRFENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQ-----FQSindiLISEGGTNFSGGQRQRLAMLRLFM 625
Cdd:COG5265 435 GIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIEslpdgYDT----RVGERGLKLSGGEKQRVAIARTLL 510
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1261268082 626 KEYPILILDEPTNHLDRETANAVIENIFAMPS--TKIIITH 664
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARgrTTLVIAH 551
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
475-641 |
7.91e-34 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 130.16 E-value: 7.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMT 554
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDgvlfrGSLSENLSYFDI----------------NYDPSKIQESIDKLNLSNYIQfQSINDIliseggtnfSGGQRQRL 618
Cdd:COG1120 82 QE-----PPAPFGLTVRELvalgryphlglfgrpsAEDREAVEEALERTGLEHLAD-RPVDEL---------SGGERQRV 146
|
170 180
....*....|....*....|...
gi 1261268082 619 AMLRLFMKEYPILILDEPTNHLD 641
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLD 169
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
475-676 |
1.82e-33 |
|
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: 126.53 E-value: 1.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDI--KDWNSEELRKNVGL 552
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLFRG-SLSENLSYfdinydpskiqesidklnlsnyiqfqsindiliseggtNFSGGQRQRLAMLRLFMKEYPIL 631
Cdd:cd03229 81 VFQDFALFPHlTVLENIAL--------------------------------------GLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1261268082 632 ILDEPTNHLDRETAN---AVIENIFAMPS-TKIIITHDENILERV-DRVY 676
Cdd:cd03229 123 LLDEPTSALDPITRRevrALLKSLQAQLGiTVVLVTHDLDEAARLaDRVV 172
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
475-683 |
2.48e-33 |
|
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: 128.17 E-value: 2.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL---RKNVG 551
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 552 LMTQDGVLFrGSLS--ENLSYFDI---NYDPSKIQESID-KLNLSNyiqFQSINDILISEggtnFSGGQRQRLAMLRLFM 625
Cdd:COG1127 86 MLFQGGALF-DSLTvfENVAFPLRehtDLSEAEIRELVLeKLELVG---LPGAADKMPSE----LSGGMRKRVALARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 626 KEYPILILDEPTNHLDRETANAVIENIF----AMPSTKIIITHDENILERV-DRVYELTDKKL 683
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRelrdELGLTSVVVTHDLDSAFAIaDRVAVLADGKI 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
475-683 |
5.68e-33 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 124.82 E-value: 5.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDwNSEELRKNVGLMT 554
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLFRG-SLSENLSYfdinydpskiqesidklnlsnyiqfqsindiliseggtnfSGGQRQRLAMLRLFMKEYPILIL 633
Cdd:cd03230 80 EEPSLYENlTVRENLKL----------------------------------------SGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1261268082 634 DEPTNHLDRETANAVIENIFAMPS---TKIIITHDENILERV-DRVYELTDKKL 683
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKegkTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
475-684 |
1.45e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 132.50 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNIliddrdikdwnseELRKNV--GL 552
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-------------KLGETVkiGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDgvlfRGSLSENLSYFDI--NYDPSKIQESI----DKLNLSNYIQFQSINDiliseggtnFSGGQRQRLAMLRLFMK 626
Cdd:COG0488 383 FDQH----QEELDPDKTVLDElrDGAPGGTEQEVrgylGRFLFSGDDAFKPVGV---------LSGGEKARLALAKLLLS 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1261268082 627 EYPILILDEPTNHLDRETANAVIENIFAMPSTKIIITHDENILERV-DRVYELTDKKLK 684
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVaTRILEFEDGGVR 508
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
475-665 |
1.50e-32 |
|
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: 125.37 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLH-----TPDKGNILIDDRDIKDWNS--EELR 547
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVdvLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 548 KNVGLMTQDGVLFRGSLSENLSYfdinydPSKIQESIDKLNLSNYIQ--------FQSINDILiseGGTNFSGGQRQRLA 619
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAY------GLRLHGIKLKEELDERVEealrkaalWDEVKDRL---HALGLSGGQQQRLC 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1261268082 620 MLRLFMKEYPILILDEPTNHLDReTANAVIENI---FAMPSTKIIITHD 665
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDP-ISTAKIEELiaeLKKEYTIVIVTHN 199
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
475-678 |
2.30e-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: 125.69 E-value: 2.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF----DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNV 550
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQD--GVL-----FRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQFQSINDIliseggtnfSGGQRQRLAMLRL 623
Cdd:COG1124 82 QMVFQDpyASLhprhtVDRILAEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQL---------SGGQRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 624 FMKEYPILILDEPTNHLD----RETANAVIENIFAMPSTKIIITHDENILERV-DRVYEL 678
Cdd:COG1124 153 LILEPELLLLDEPTSALDvsvqAEILNLLKDLREERGLTYLFVSHDLAVVAHLcDRVAVM 212
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
473-685 |
7.66e-32 |
|
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: 122.91 E-value: 7.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 473 GSIEFNNISFSF--DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNV 550
Cdd:cd03369 5 GEIEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDGVLFRGSLSENLSYFDiNYDPSKIQESIDklnlsnyiqfqsindilISEGGTNFSGGQRQRLAMLRLFMKEYPI 630
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLDPFD-EYSDEEIYGALR-----------------VSEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261268082 631 LILDEPTNHLDRETANAVIENI---FAmPSTKIIITHDENILERVDRVYELTDKKLKQ 685
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIreeFT-NSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
476-683 |
2.07e-31 |
|
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: 120.62 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 476 EFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMTQ 555
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 556 dgvlfrgslsenlsyfdinydpskiqeSIDKLNLSNYIQfQSINDIliseggtnfSGGQRQRLAMLRLFMKEYPILILDE 635
Cdd:cd03214 81 ---------------------------ALELLGLAHLAD-RPFNEL---------SGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 636 PTNHLDRETANAVIENIFAMPSTK----IIITHDENILERV-DRVYELTDKKL 683
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERgktvVMVLHDLNLAARYaDRVILLKDGRI 176
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
475-682 |
7.08e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 119.89 E-value: 7.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDwNSEELRKNVGLMT 554
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLFRG-SLSENLSYF----DINYDPSKIQESIDKLNLSNYIqfqsinDILISeggtNFSGGQRQRLAMLRLFMKEYP 629
Cdd:COG4133 82 HADGLKPElTVRENLRFWaalyGLRADREAIDEALEAVGLAGLA------DLPVR----QLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1261268082 630 ILILDEPTNHLDREtANAVIENIFAMPSTK----IIITHDEnILERVDRVYELTDKK 682
Cdd:COG4133 152 LWLLDEPFTALDAA-GVALLAELIAAHLARggavLLTTHQP-LELAAARVLDLGDFK 206
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
474-690 |
2.36e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 126.50 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNIS-FSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLhTPDKGNILIDDRDIKDWNSEELRKNVGL 552
Cdd:PRK11174 349 TIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQFQSIN-DILISEGGTNFSGGQRQRLAMLRLFMKEYPIL 631
Cdd:PRK11174 428 VGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGlDTPIGDQAAGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261268082 632 ILDEPTNHLDRETANAVIENIF-AMPS-TKIIITHDENILERVDRVYELTDKKLKQREIFS 690
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNaASRRqTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYA 568
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
475-685 |
9.07e-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: 117.24 E-value: 9.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEelRKNVGLMT 554
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLFRgSLS--ENLSY-FDINYDPS-----KIQESIDKLNLSNYIqfqsinDILISEggtnFSGGQRQRLAMLRLFMK 626
Cdd:cd03259 79 QDYALFP-HLTvaENIAFgLKLRGVPKaeiraRVRELLELVGLEGLL------NRYPHE----LSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261268082 627 EYPILILDEPTNHLD---RETANAVIENIF-AMPSTKIIITHD-ENILERVDRVYELTDKKLKQ 685
Cdd:cd03259 148 EPSLLLLDEPLSALDaklREELREELKELQrELGITTIYVTHDqEEALALADRIAVMNEGRIVQ 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
475-682 |
2.46e-29 |
|
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: 113.31 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRdikdwnseelrknvglmt 554
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 qdgvlfrgslsENLSYFDinydpskiqesidklnlsnyiqfqsindiliseggtNFSGGQRQRLAMLRLFMKEYPILILD 634
Cdd:cd03221 63 -----------VKIGYFE------------------------------------QLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1261268082 635 EPTNHLDRETANAVIENIFAMPSTKIIITHDENILERV-DRVYELTDKK 682
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
475-676 |
2.55e-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: 116.45 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDK----KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL---R 547
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 548 KNVGLMTQDGvlfRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQFQSINDILISEGGTN-----FSGGQRQRLAMLR 622
Cdd:cd03257 82 KEIQMVFQDP---MSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrypheLSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 623 LFMKEYPILILDEPTNHLDRETANAVI--------ENIFAMpstkIIITHDENILERV-DRVY 676
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILdllkklqeELGLTL----LFITHDLGVVAKIaDRVA 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
475-683 |
3.48e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 115.92 E-value: 3.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF-DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRD---IKDWNSEELRKNV 550
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDgvlFRgsLSENLSYFD--------INYDPSKIQ----ESIDKLNLSNYIqfqsinDILISEggtnFSGGQRQRL 618
Cdd:COG2884 82 GVVFQD---FR--LLPDRTVYEnvalplrvTGKSRKEIRrrvrEVLDLVGLSDKA------KALPHE----LSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 619 AMLRLFMKEYPILILDEPTNHLDRETANAVIEnIF----AMPSTKIIITHDENILERVD-RVYELTDKKL 683
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIME-LLeeinRRGTTVLIATHDLELVDRMPkRVLELEDGRL 215
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
475-697 |
1.02e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.19 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIK--------------- 539
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRrarrrigyvpqraev 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 540 DWNS----EELrknV--GLMTQDGVLFRGSLSenlsyfdinyDPSKIQESIDKLNLSNYIqfqsinDILISEggtnFSGG 613
Cdd:COG1121 87 DWDFpitvRDV---VlmGRYGRRGLFRRPSRA----------DREAVDEALERVGLEDLA------DRPIGE----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 614 QRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS---TKIIITHD-ENILERVDRVYELTDKKLKQ---R 686
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDlGAVREYFDRVLLLNRGLVAHgppE 223
|
250
....*....|.
gi 1261268082 687 EIFSKSKLQTL 697
Cdd:COG1121 224 EVLTPENLSRA 234
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
450-664 |
1.37e-28 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 121.36 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 450 RTLDILEEELEKDGSDTKVnILRGSIEFNNISFSF-DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDK 528
Cdd:PRK10790 317 RVFELMDGPRQQYGNDDRP-LQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 529 GNILIDDRDIKDWNSEELRKNVGLMTQDGVLFRGSLSENLSyFDINYDPSKIQESIDKLNLSNYIQFQS--INDILiSEG 606
Cdd:PRK10790 396 GEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVT-LGRDISEEQVWQALETVQLAELARSLPdgLYTPL-GEQ 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 607 GTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAM--PSTKIIITH 664
Cdd:PRK10790 474 GNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAH 533
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
476-678 |
6.01e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 111.86 E-value: 6.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 476 EFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIkdwnsEELRKNVGLMTQ 555
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 556 dgvlfRGSLSEN--LSYFDI----------------NYDPSKIQESIDKLNLSNYIQFQsindilISEggtnFSGGQRQR 617
Cdd:cd03235 76 -----RRSIDRDfpISVRDVvlmglyghkglfrrlsKADKAKVDEALERVGLSELADRQ------IGE----LSGGQQQR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 618 LAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS---TKIIITHDENILER-VDRVYEL 678
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEyFDRVLLL 205
|
|
| Peptidase_C39 |
pfam03412 |
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ... |
5-137 |
7.80e-28 |
|
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as precursor peptides containing N-terminal extensions (leader peptides) which are cleaved off during maturation. Most non-lantibiotics and also some lantibiotics have leader peptides of the so-called double-glycine type. These leader peptides share consensus sequences and also a common processing site with two conserved glycine residues in positions -1 and -2. The double- glycine-type leader peptides are unrelated to the N-terminal signal sequences which direct proteins across the cytoplasmic membrane via the sec pathway. Their processing sites are also different from typical signal peptidase cleavage sites, suggesting that a different processing enzyme is involved. Peptide bacteriocins are exported across the cytoplasmic membrane by a dedicated ATP-binding cassette (ABC) transporter. The ABC transporter is the maturation protease and its proteolytic domain resides in the N-terminal part of the protein. This peptidase domain is found in a wide range of ABC transporters, however the presumed catalytic cysteine and histidine are not conserved in all members of this family.
Pssm-ID: 367483 [Multi-domain] Cd Length: 133 Bit Score: 108.85 E-value: 7.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 5 KIKFIPQMTSFDCGPSCLAMIMHYYGSAVQASEIRNsKIINKKSAWSLLDIKKVSKSYGLSATAYRIEnITDLQRIQKPM 84
Cdd:pfam03412 1 KYKIVLQVDENDCGLACLAMILKYYGSNVSLEELRE-LAGTPAEGTSLLGLKKAAEKLGFKAKAIKAD-LSELKELPLPF 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 85 IAFWGFN--HFVIIERVKANKFYIVDPKAGPMIIDIRSFEEMFCDYILVIENKKD 137
Cdd:pfam03412 79 IAHWDGNggHFVVVYGIKKNKVLIADPAVGKIKLSREEFEKEWTGVALLVAPKPS 133
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
475-675 |
8.79e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 118.08 E-value: 8.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF-----DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSE---EL 546
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrEL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 547 RKNVGLMTQD--GVLF-----RGSLSENLSYFDInYDPS----KIQESIDKLNLSnyiqfQSINDILISEggtnFSGGQR 615
Cdd:COG1123 341 RRRVQMVFQDpySSLNprmtvGDIIAEPLRLHGL-LSRAerreRVAELLERVGLP-----PDLADRYPHE----LSGGQR 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261268082 616 QRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENI--------FAMpstkIIITHDENILERV-DRV 675
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLrdlqrelgLTY----LFISHDLAVVRYIaDRV 475
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
475-698 |
9.08e-28 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 112.91 E-value: 9.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDD--KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKD----WnseELRK 548
Cdd:TIGR04520 1 IEVENVSFSYPEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDeenlW---EIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 549 NVGLMTQ------------DGVLFrgSLsENLsyfdiNYDPSKI----QESIDKLNLSNYIQFQSindiliseggTNFSG 612
Cdd:TIGR04520 78 KVGMVFQnpdnqfvgatveDDVAF--GL-ENL-----GVPREEMrkrvDEALKLVGMEDFRDREP----------HLLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 613 GQRQR------LAMLrlfmkeyP-ILILDEPTNHLDRETANAVIENI------FAMpsTKIIITHDENILERVDRVYELT 679
Cdd:TIGR04520 140 GQKQRvaiagvLAMR-------PdIIILDEATSMLDPKGRKEVLETIrklnkeEGI--TVISITHDMEEAVLADRVIVMN 210
|
250 260
....*....|....*....|....
gi 1261268082 680 D-KKLKQ---REIFSK-SKLQTLG 698
Cdd:TIGR04520 211 KgKIVAEgtpREIFSQvELLKEIG 234
|
|
| Peptidase_C39F |
cd02425 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
6-132 |
2.58e-27 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239105 [Multi-domain] Cd Length: 126 Bit Score: 106.96 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 6 IKFIPQMTSFDCGPSCLAMIMHYYGSAVQASEIRnSKIINKKSAWSLLDIKKVSKSYGLSATAYRIENITDLQRIQKPMI 85
Cdd:cd02425 1 VKPILQNNQTECGLACYAMILNYFGYKVSLNELR-EKYELGRDGLSLSYLKQLLEEYGFKCKVYKISFKKNLYPLKLPVI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1261268082 86 AFWGFNHFVIIERVKANKFYIVDPKAGPMIIDIRSFEEMFCDYILVI 132
Cdd:cd02425 80 IFWNNNHFVVLEKIKKNKVTIVDPAIGRIKISIDEFLENFSGYILTF 126
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
474-685 |
3.00e-27 |
|
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: 110.89 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEElrKNVGLM 553
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLFRG-SLSENLSyFDINYDPSKIQESIDKL-----NLSNYIQFQSINDILISEggtnFSGGQRQRLAMLRLFMKE 627
Cdd:cd03296 80 FQHYALFRHmTVFDNVA-FGLRVKPRSERPPEAEIrakvhELLKLVQLDWLADRYPAQ----LSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 628 YPILILDEPTNHLD----RETANAVIENIFAMPSTKIIITHD-ENILERVDRVYELTDKKLKQ 685
Cdd:cd03296 155 PKVLLLDEPFGALDakvrKELRRWLRRLHDELHVTTVFVTHDqEEALEVADRVVVMNKGRIEQ 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
473-675 |
8.70e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 117.15 E-value: 8.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 473 GSIEFNNISFSF--DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNV 550
Cdd:PLN03130 1236 GSIKFEDVVLRYrpELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDGVLFRGSLSENLSYFDINYDpSKIQESIDKLNLSNYIQFQSIN-DILISEGGTNFSGGQRQRLAMLRLFMKEYP 629
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLDPFNEHND-ADLWESLERAHLKDVIRRNSLGlDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1261268082 630 ILILDEPTNHLDRETaNAVIENIFA---MPSTKIIITHDENILERVDRV 675
Cdd:PLN03130 1395 ILVLDEATAAVDVRT-DALIQKTIReefKSCTMLIIAHRLNTIIDCDRI 1442
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
475-679 |
1.43e-26 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 108.33 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDK----KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKdwnseELRKNV 550
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDGVLF--RgSLSENLSY-FDINYDPSK-----IQESIDKLNLSNYIQ---FQsindiliseggtnFSGGQRQRLA 619
Cdd:cd03293 76 GYVFQQDALLpwL-TVLDNVALgLELQGVPKAearerAEELLELVGLSGFENaypHQ-------------LSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261268082 620 MLRLFMKEYPILILDEPTNHLD---RETANAVIENIFA-MPSTKIIITHDenILERV---DRVYELT 679
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDaltREQLQEELLDIWReTGKTVLLVTHD--IDEAVflaDRVVVLS 206
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
479-684 |
1.91e-26 |
|
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: 107.34 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 479 NISFSF-DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWnseELRKNVGLMTQD- 556
Cdd:cd03226 4 NISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERRKSIGYVMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 557 -GVLFRGSLSENLSYFDINYD--PSKIQESIDKLNLSnyiqfqsindILISEGGTNFSGGQRQRLAMLRLFMKEYPILIL 633
Cdd:cd03226 81 dYQLFTDSVREELLLGLKELDagNEQAETVLKDLDLY----------ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 634 DEPTNHLDRETANAV---IENIFAMPSTKIIITHDENILERV-DRVYELTDKKLK 684
Cdd:cd03226 151 DEPTSGLDYKNMERVgelIRELAAQGKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
174-450 |
2.69e-26 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 109.52 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 174 QISILAFPFILKKFMDilNASKEVDVRYLLIILGSLIVVIGIKSITSIIK----VNFQKEIDRKSTTKVFEHMFNIPIEK 249
Cdd:cd18555 15 QLLTLLIPILTQYVID--NVIVPGNLNLLNVLGIGILILFLLYGLFSFLRgyiiIKLQTKLDKSLMSDFFEHLLKLPYSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 250 ITSRHAGDLNVRIMSLESIRGYILEDLIEMIISIVVIIPLLMYLLYTETFYTLILMFFIASSLFINISLGKFIYNANLVE 329
Cdd:cd18555 93 FENRSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 330 TYYLGEHRGKINESLKAMYYVKATGIFSKIKSVWKKDYNKYLDTVHKRVLKQNALESFNSSLSTIFIIIMLAVGFYNFSK 409
Cdd:cd18555 173 IVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVIN 252
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1261268082 410 GEGDLSNIFFFIAISSIIFSPVSTIIGSILNWNSVKPLLLR 450
Cdd:cd18555 253 GELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLER 293
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
475-685 |
7.25e-26 |
|
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: 106.62 E-value: 7.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF-DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLM 553
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLF-RGSLSENLSYFD--INYDPSKIQESIDKLnLSnyiqfqsindiLISEGGTNF--------SGGQRQRLAMLR 622
Cdd:cd03295 81 IQQIGLFpHMTVEENIALVPklLKWPKEKIRERADEL-LA-----------LVGLDPAEFadryphelSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 623 LFMKEYPILILDEPTNHLDRETANAVIENIFAMPS----TKIIITHDenILERV---DRVYELTDKKLKQ 685
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelgkTIVFVTHD--IDEAFrlaDRIAIMKNGEIVQ 216
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
479-684 |
7.70e-26 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 106.28 E-value: 7.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 479 NISFSFDDKK----IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE---LR-KNV 550
Cdd:TIGR02211 6 NLGKRYQEGKldtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNErakLRnKKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 G-------LMTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQFQSindiliSEggtnFSGGQRQRLAMLRL 623
Cdd:TIGR02211 86 GfiyqfhhLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRP------SE----LSGGERQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 624 FMKEYPILILDEPTNHLDRETANAVIENIFAMPSTK----IIITHDENILERVDRVYELTDKKLK 684
Cdd:TIGR02211 156 LVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELntsfLVVTHDLELAKKLDRVLEMKDGQLF 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
477-684 |
3.19e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.15 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 477 FNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDdRDIKdwnseelrknVGLMTQD 556
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR----------IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 557 GVLFRGS----------------------LSENLSYFDINYD-----------------PSKIQESIDKLNLSNYIQFQS 597
Cdd:COG0488 70 PPLDDDLtvldtvldgdaelraleaeleeLEAKLAEPDEDLErlaelqeefealggweaEARAEEILSGLGFPEEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 598 INDiliseggtnFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDretANAVI--ENIFA-MPSTKIIITHDENILERV-D 673
Cdd:COG0488 150 VSE---------LSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEwlEEFLKnYPGTVLVVSHDRYFLDRVaT 217
|
250
....*....|.
gi 1261268082 674 RVYELTDKKLK 684
Cdd:COG0488 218 RILELDRGKLT 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
475-675 |
5.99e-25 |
|
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: 109.22 E-value: 5.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF--DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPD---KGNILIDDRDIKDWNSEELRKN 549
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 550 VGLMTQD------GVLFRGSLSENLSYFDInyDPSKIQESIdkLNLSNYIQFQSINDILISEggtnFSGGQRQRLAMLRL 623
Cdd:COG1123 85 IGMVFQDpmtqlnPVTVGDQIAEALENLGL--SRAEARARV--LELLEAVGLERRLDRYPHQ----LSGGQRQRVAIAMA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1261268082 624 FMKEYPILILDEPTNHLDRETANAVIENIFAMPS----TKIIITHD-ENILERVDRV 675
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRergtTVLLITHDlGVVAEIADRV 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
474-665 |
6.19e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 106.72 E-value: 6.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEelRKNVGLM 553
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLFrGSLS--ENLSYF---------DINydpSKIQESIDKLNLSNYIqfqsinDILISEggtnFSGGQRQRLAMLR 622
Cdd:COG3842 83 FQDYALF-PHLTvaENVAFGlrmrgvpkaEIR---ARVAELLELVGLEGLA------DRYPHQ----LSGGQQQRVALAR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1261268082 623 LFMKEYPILILDEPTNHLDRETANAVIENIFAM----PSTKIIITHD 665
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLqrelGITFIYVTHD 195
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
489-685 |
6.52e-25 |
|
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: 103.67 E-value: 6.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 489 IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL----RKNVGLMTQDgvlFR--G 562
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARHVGFVFQS---FQllP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 563 SLS--EN----LSYFDINYDPSKIQESIDKLNLSNYIQF---QsindiliseggtnFSGGQRQRLAMLRLFMKEYPILIL 633
Cdd:COG4181 104 TLTalENvmlpLELAGRRDARARARALLERVGLGHRLDHypaQ-------------LSGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 634 DEPTNHLDRETANAVIENIFAMP----STKIIITHDENILERVDRVYELTDKKLKQ 685
Cdd:COG4181 171 DEPTGNLDAATGEQIIDLLFELNrergTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
475-698 |
6.98e-25 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 104.84 E-value: 6.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFD-----DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDI---KDWNSEEL 546
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 547 RKNVGLMTQ--DGVLFrgslsENLSYFDINYDPS-----------KIQESIDKLNLSNYIQFQSINDIliseggtnfSGG 613
Cdd:TIGR04521 81 RKKVGLVFQfpEHQLF-----EETVYKDIAFGPKnlglseeeaeeRVKEALELVGLDEEYLERSPFEL---------SGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 614 QRQRLAMLR-LFMKeyP-ILILDEPTNHLD---RETANAVIENIFAMPSTKII-ITHD-ENILERVDRVYELTDKKL--- 683
Cdd:TIGR04521 147 QMRRVAIAGvLAME--PeVLILDEPTAGLDpkgRKEILDLFKRLHKEKGLTVIlVTHSmEDVAEYADRVIVMHKGKIvld 224
|
250
....*....|....*..
gi 1261268082 684 -KQREIFSKSK-LQTLG 698
Cdd:TIGR04521 225 gTPREVFSDVDeLEKIG 241
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
475-641 |
8.23e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 104.01 E-value: 8.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMT 554
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDG-----------VLF------RGSLSENlsyfdinyDPSKIQESIDKLNLsnyiqfQSINDILISEggtnFSGGQRQR 617
Cdd:COG4604 82 QENhinsrltvrelVAFgrfpysKGRLTAE--------DREIIDEAIAYLDL------EDLADRYLDE----LSGGQRQR 143
|
170 180
....*....|....*....|....*.
gi 1261268082 618 --LAMlrLFMKEYPILILDEPTNHLD 641
Cdd:COG4604 144 afIAM--VLAQDTDYVLLDEPLNNLD 167
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
475-678 |
9.16e-25 |
|
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: 102.55 E-value: 9.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKK-----IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNIliddrdikdwnseELRKN 549
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 550 VGLMTQDGVLFRGSLSENLsYFDINYDPSKIQESIDKLNLSNYIqfqsinDIL-------ISEGGTNFSGGQRQRLAMLR 622
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENI-LFGKPFDEERYEKVIKACALEPDL------EILpdgdlteIGEKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 623 LFMKEYPILILDEPTNHLDRETANAVIENIF----AMPSTKIIITHDENILERVDRVYEL 678
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIFENCIlgllLNNKTRILVTHQLQLLPHADQIVVL 200
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
475-679 |
9.71e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.87 E-value: 9.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMT 554
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLFRGSLSENLSY-FDINY---DPSKIQESIDKLNLSNYIQFQSINDIliseggtnfSGGQRQRLAMLR--LFMKEy 628
Cdd:PRK10247 88 QTPTLFGDTVYDNLIFpWQIRNqqpDPAIFLDDLERFALPDTILTKNIAEL---------SGGEKQRISLIRnlQFMPK- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 629 pILILDEPTNHLDRETANAVIENIFAMPSTKII----ITHDENILERVDRVYELT 679
Cdd:PRK10247 158 -VLLLDEITSALDESNKHNVNEIIHRYVREQNIavlwVTHDKDEINHADKVITLQ 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
475-676 |
4.84e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 102.09 E-value: 4.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKK----IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIkdwnsEELRKNV 550
Cdd:COG1116 8 LELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDGVLF--RgSLSENLSY------FDINYDPSKIQESIDKLNLSNYIQ---FQsindiLiseggtnfSGGQRQRLA 619
Cdd:COG1116 83 GVVFQEPALLpwL-TVLDNVALglelrgVPKAERRERARELLELVGLAGFEDaypHQ-----L--------SGGMRQRVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261268082 620 MLRLFMKEYPILILDEPTNHLD---RETANAVIENIFA-MPSTKIIITHDenILERV---DRVY 676
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDaltRERLQDELLRLWQeTGKTVLFVTHD--VDEAVflaDRVV 210
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
471-679 |
5.49e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 108.14 E-value: 5.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 471 LRGSIEFNNISFSFDDK--KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRK 548
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGlpPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 549 NVGLMTQDGVLFRGSLSENLSYFDINYDpSKIQESIDKLNLSNYIQFQSIN-DILISEGGTNFSGGQRQRLAMLRLFMKE 627
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFNIDPFSEHND-ADLWEALERAHIKDVIDRNPFGlDAEVSEGGENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1261268082 628 YPILILDEPTNHLDRETANAVIENIFA--MPSTKIIITHDENILERVDRVYELT 679
Cdd:PLN03232 1390 SKILVLDEATASVDVRTDSLIQRTIREefKSCTMLVIAHRLNTIIDCDKILVLS 1443
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
475-699 |
9.00e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.61 E-value: 9.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF--DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGL 552
Cdd:PRK13632 8 IKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQD-GVLFRGSLSENLSYF---DINYDPSKIQESID----KLNLSNYIQFQSindiliseggTNFSGGQRQRLAMLRLF 624
Cdd:PRK13632 88 IFQNpDNQFIGATVEDDIAFgleNKKVPPKKMKDIIDdlakKVGMEDYLDKEP----------QNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261268082 625 MKEYPILILDEPTNHLDRETANAVIENIFAMPSTK----IIITHDENILERVDRVYeltdkklkqreIFSKSKLQTLGK 699
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkktlISITHDMDEAILADKVI-----------VFSEGKLIAQGK 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
472-689 |
9.65e-24 |
|
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: 107.34 E-value: 9.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 472 RGSIEFNNISFSF--DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKN 549
Cdd:TIGR00957 1282 RGRVEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 550 VGLMTQDGVLFRGSLSENLSYFDiNYDPSKIQESIDKLNLSNYIQFQSIN-DILISEGGTNFSGGQRQRLAMLRLFMKEY 628
Cdd:TIGR00957 1362 ITIIPQDPVLFSGSLRMNLDPFS-QYSDEEVWWALELAHLKTFVSALPDKlDHECAEGGENLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261268082 629 PILILDEPTNHLDRETANAVIENIFAM--PSTKIIITHDENILERVDRVYELtDKK-----------LKQREIF 689
Cdd:TIGR00957 1441 KILVLDEATAAVDLETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVL-DKGevaefgapsnlLQQRGIF 1513
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
475-666 |
1.57e-23 |
|
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: 99.25 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEElrKNVGLMT 554
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLF-RGSLSENLSYfdinydPSKI----QESIDKlnlsnyiQFQSINDIL-ISE----GGTNFSGGQRQRLAMLRLF 624
Cdd:cd03301 79 QNYALYpHMTVYDNIAF------GLKLrkvpKDEIDE-------RVREVAELLqIEHlldrKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1261268082 625 MKEYPILILDEPTNHLD---RETANAVIENIFA-MPSTKIIITHDE 666
Cdd:cd03301 146 VREPKVFLMDEPLSNLDaklRVQMRAELKRLQQrLGTTTIYVTHDQ 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
475-650 |
2.17e-23 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 99.56 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF-DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL---RKNV 550
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDGVLF-RGSLSEN-----LSYFDI------NYDPSKIQ---ESIDKLNLSNYIqFQSINdiliseggtNFSGGQR 615
Cdd:cd03256 81 GMIFQQFNLIeRLSVLENvlsgrLGRRSTwrslfgLFPKEEKQralAALERVGLLDKA-YQRAD---------QLSGGQQ 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1261268082 616 QRLAMLRLFMKEYPILILDEPTNHLDRETANAVIE 650
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMD 185
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
475-680 |
3.71e-23 |
|
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: 99.00 E-value: 3.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGN-ILIDDRDIKDWNSEELRKNVGLM 553
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVL-FRGSLS-EN--LS-YFDI-----NYDP---SKIQESIDKLNLSNYIQ--FQSIndiliseggtnfSGGQRQRL 618
Cdd:COG1119 84 SPALQLrFPRDETvLDvvLSgFFDSiglyrEPTDeqrERARELLELLGLAHLADrpFGTL------------SQGEQRRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261268082 619 AMLRLFMKEYPILILDEPTNHLD---RETANAVIENIFAMPSTKII-ITHD-ENILERVDRVYELTD 680
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDlgaRELLLALLDKLAAEGAPTLVlVTHHvEEIPPGITHVLLLKD 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
414-683 |
5.48e-23 |
|
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: 103.34 E-value: 5.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 414 LSNIFFFIAISSIIF------------------------SPVSTIIGSIlnwnsvkPLL------LRTLDILEEELEKDG 463
Cdd:COG4615 238 WGNLLFFALIGLILFllpalgwadpavlsgfvlvllflrGPLSQLVGAL-------PTLsranvaLRKIEELELALAAAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 464 SDTKVNILRG------SIEFNNISFSFDDKKIIEN-----LSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNIL 532
Cdd:COG4615 311 PAAADAAAPPapadfqTLELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEIL 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 533 IDDRDIKDWNSEELRKnvgLMT---QDGVLFrgslsENLSYFDINYDPSKIQESIDKLNLSNYIQFQsiNDILISeggTN 609
Cdd:COG4615 391 LDGQPVTADNREAYRQ---LFSavfSDFHLF-----DRLLGLDGEADPARARELLERLELDHKVSVE--DGRFST---TD 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 610 FSGGQRQRLAMLRLFMKEYPILILDE------PTNhldREtanavienIF---------AMPSTKIIITHDENILERVDR 674
Cdd:COG4615 458 LSQGQRKRLALLVALLEDRPILVFDEwaadqdPEF---RR--------VFytellpelkARGKTVIAISHDDRYFDLADR 526
|
....*....
gi 1261268082 675 VYELTDKKL 683
Cdd:COG4615 527 VLKMDYGKL 535
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
475-683 |
7.45e-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: 97.09 E-value: 7.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF-DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE---LRKNV 550
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDG-VLFRGSLSENLSY-FDINYDPSK-----IQESIDKLNLSNYIqfqsinDILISEggtnFSGGQRQRLAMLRL 623
Cdd:cd03292 81 GVVFQDFrLLPDRNVYENVAFaLEVTGVPPReirkrVPAALELVGLSHKH------RALPAE----LSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261268082 624 FMKEYPILILDEPTNHLDRETANAVI---ENIFAMPSTKIIITHDENILERVD-RVYELTDKKL 683
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMnllKKINKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
473-665 |
1.10e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 100.15 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 473 GSIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEElRkNVGL 552
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-R-NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLFRgSLS--ENLSY---------FDINydpSKIQESIDKLNLSNYIqfqsinDILISEggtnFSGGQRQRLAML 621
Cdd:COG3839 80 VFQSYALYP-HMTvyENIAFplklrkvpkAEID---RRVREAAELLGLEDLL------DRKPKQ----LSGGQRQRVALG 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1261268082 622 RLFMKEYPILILDEPTNHLD---RETANAVIENIFA-MPSTKIIITHD 665
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDaklRVEMRAEIKRLHRrLGTTTIYVTHD 193
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
475-693 |
1.37e-22 |
|
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: 96.92 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKdwNSEELRKNVGLMT 554
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLF-RGSLSENLSY------FDINYDPSKIQESIDKLNLSNYIQfQSINDIliseggtnfSGGQRQRLAMLRLFMKE 627
Cdd:cd03300 79 QNYALFpHLTVFENIAFglrlkkLPKAEIKERVAEALDLVQLEGYAN-RKPSQL---------SGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 628 YPILILDEPTNHLD---RETANAVIENIFAM-PSTKIIITHD-ENILERVDRVYELTDKKLKQ----REIFSKSK 693
Cdd:cd03300 149 PKVLLLDEPLGALDlklRKDMQLELKRLQKElGITFVFVTHDqEEALTMSDRIAVMNKGKIQQigtpEEIYEEPA 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
475-675 |
2.95e-22 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 95.67 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDI--KDWNSEELRKNVGL 552
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLFrgslsENLSYFD-INYDPSKIQ------------ESIDKLNLSNYIqfqsinDILISEggtnFSGGQRQRLA 619
Cdd:cd03262 81 VFQQFNLF-----PHLTVLEnITLAPIKVKgmskaeaeeralELLEKVGLADKA------DAYPAQ----LSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 620 MLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS---TKIIITHDENILERV-DRV 675
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVaDRV 205
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
376-682 |
2.97e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 102.80 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 376 KRVLKQNALESFNSSLSTIFIIIMLAVGFY---------------NFSKGEGDLSNIFFFIAIS----SIIFSPVSTIIG 436
Cdd:PTZ00265 271 KYILKANFMESLHIGMINGFILASYAFGFWygtriiisdlsnqqpNNDFHGGSVISILLGVLISmfmlTIILPNITEYMK 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 437 SILNWNSVKPLLLRTLDIleeELEKDGSDTKvNILRgsIEFNNISFSFDDKKIIE---NLSLNIKNNESIAIVGESGSGK 513
Cdd:PTZ00265 351 SLEATNSLYEIINRKPLV---ENNDDGKKLK-DIKK--IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGK 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 514 STLANLLLKLHTPDKGNILIDD-RDIKDWNSEELRKNVGLMTQDGVLFRGSLSENLSYF------------DINYDPSKI 580
Cdd:PTZ00265 425 STILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnYYNEDGNDS 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 581 QESIDKLN---------LSNYIQ-------------FQSIND------------------------ILISEGGTNFSGGQ 614
Cdd:PTZ00265 505 QENKNKRNscrakcagdLNDMSNttdsneliemrknYQTIKDsevvdvskkvlihdfvsalpdkyeTLVGSNASKLSGGQ 584
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 615 RQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTK----IIITHDENILERVDRVYELTDKK 682
Cdd:PTZ00265 585 KQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnritIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
475-650 |
5.73e-22 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 95.44 E-value: 5.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF-DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRK---NV 550
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDGVLF-RGSLSENLSYFDINYDPS--------------KIQESIDKLNLSNYIQFQSindiliseggTNFSGGQR 615
Cdd:TIGR02315 82 GMIFQHYNLIeRLTVLENVLHGRLGYKPTwrsllgrfseedkeRALSALERVGLADKAYQRA----------DQLSGGQQ 151
|
170 180 190
....*....|....*....|....*....|....*
gi 1261268082 616 QRLAMLRLFMKEYPILILDEPTNHLDRETANAVIE 650
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMD 186
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
475-686 |
5.81e-22 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 94.57 E-value: 5.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNeSIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDwNSEELRKNVGLMT 554
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QD-GVLFRGSLSENLSYFDINYD------PSKIQESIDKLNLSNYiqfqsiNDILISEggtnFSGGQRQRLAMLRLFMKE 627
Cdd:cd03264 79 QEfGVYPNFTVREFLDYIAWLKGipskevKARVDEVLELVNLGDR------AKKKIGS----LSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 628 YPILILDEPTNHLDRETANAVIENIFAMPSTKIII--THD-ENILERVDRVYELTDKKLKQR 686
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVIlsTHIvEDVESLCNQVAVLNKGKLVFE 210
|
|
| C39G |
COG3271 |
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ... |
4-136 |
8.04e-22 |
|
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442502 [Multi-domain] Cd Length: 179 Bit Score: 93.13 E-value: 8.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 4 KKIKF---IPQMTSFDCGPSCLAMIM-HYYGSAV---QASEIRNSKIINKKSAWSLLDIKKVSKSYGLSATAYRIEnITD 76
Cdd:COG3271 38 KELRFrnvVRQQYDYSCGAAALATLLnYHYGRPVseaEVLEGMLTHGDQRRRGFSLLDMKRYLEALGLRADGYRLT-LDD 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 77 LQRIQKPMIAF---WGFNHFVIIERVKANKFYIVDPKAGPMIIDIRSFEEMFCDYILVIENKK 136
Cdd:COG3271 117 LAQLGIPAIVLinlGGYKHFVVVKGVDDGRVLLADPALGNRSLSREEFEKMWDGNVLFVVPPK 179
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
475-698 |
3.04e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.28 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF-DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNS-EELRKNVGL 552
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQD-GVLFRG-SLSENLSYFDIN--YDPSKIQESIDK----LNLSNYiQFQSindilisegGTNFSGGQRQRLAMLRLF 624
Cdd:PRK13644 82 VFQNpETQFVGrTVEEDLAFGPENlcLPPIEIRKRVDRalaeIGLEKY-RHRS---------PKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 625 MKEYPILILDEPTNHLDRETANAVIENIFAM---PSTKIIITHDENILERVDRVYELTDKKL----KQREIFSKSKLQTL 697
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLhekGKTIVYITHNLEELHDADRIIVMDRGKIvlegEPENVLSDVSLQTL 231
|
.
gi 1261268082 698 G 698
Cdd:PRK13644 232 G 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
475-693 |
3.50e-21 |
|
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: 93.03 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDK----KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL---R 547
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 548 KNVGLMTQD-GVLFRGSLSENLSY------FDINYDPSKIQESIDKLNLSNYIQFQSindiliseggTNFSGGQRQRLAM 620
Cdd:cd03258 82 RRIGMIFQHfNLLSSRTVFENVALpleiagVPKAEIEERVLELLELVGLEDKADAYP----------AQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 621 LRLFMKEYPILILDEPTNHLDRETANAVIE---------NIfampsTKIIITHDENILERV-DRVYELTDKKLKQ----R 686
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILAllrdinrelGL-----TIVLITHEMEVVKRIcDRVAVMEKGEVVEegtvE 226
|
....*..
gi 1261268082 687 EIFSKSK 693
Cdd:cd03258 227 EVFANPQ 233
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
475-650 |
3.51e-21 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 93.20 E-value: 3.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF-DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRK---NV 550
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDGVLFrGSLS--EN---------------LSYF---DINydpsKIQESIDKLNLSNYIqFQSInDILiseggtnf 610
Cdd:COG3638 83 GMIFQQFNLV-PRLSvlTNvlagrlgrtstwrslLGLFppeDRE----RALEALERVGLADKA-YQRA-DQL-------- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1261268082 611 SGGQRQRLAMLRLFMKEyPILIL-DEPTNHLDRETANAVIE 650
Cdd:COG3638 148 SGGQQQRVAIARALVQE-PKLILaDEPVASLDPKTARQVMD 187
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
474-641 |
5.27e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.15 E-value: 5.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLM 553
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQ-----DGVLFR--------------GSLSENlsyfdinyDPSKIQESIDKLNLsnyiqfqsinDILISEGGTNFSGGQ 614
Cdd:PRK11231 82 PQhhltpEGITVRelvaygrspwlslwGRLSAE--------DNARVNQAMEQTRI----------NHLADRRLTDLSGGQ 143
|
170 180
....*....|....*....|....*....
gi 1261268082 615 RQR--LAMlrLFMKEYPILILDEPTNHLD 641
Cdd:PRK11231 144 RQRafLAM--VLAQDTPVVLLDEPTTYLD 170
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
230-699 |
5.29e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 98.51 E-value: 5.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 230 IDRKSTTKVFEHMFNIPIEKITSRHAGDLNVRIMSLESIRGyiledliemIISIVVIIPLLMYLLYTE-----TFYTLIL 304
Cdd:PLN03232 380 IFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHG---------LWSAPFRIIVSMVLLYQQlgvasLFGSLIL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 305 MFFIASSLFINISLGKFIYNAnlveTYYLGEHRGKINESLKAMYYVKATGifskiksvWKKDYNKYLDTVHKRVL----K 380
Cdd:PLN03232 451 FLLIPLQTLIVRKMRKLTKEG----LQWTDKRVGIINEILASMDTVKCYA--------WEKSFESRIQGIRNEELswfrK 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 381 QNALESFNSSLSTIFIIIMLAVGFYNFSKGEGDLSNIFFFIAIS--SIIFSPVSTI---IGSILNWNsVKPLLLRTLDIL 455
Cdd:PLN03232 519 AQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSlfAVLRSPLNMLpnlLSQVVNAN-VSLQRIEELLLS 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 456 EEELEKDGSDTKVNILRGSIEfnNISFSFD---DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPdkgnil 532
Cdd:PLN03232 598 EERILAQNPPLQPGAPAISIK--NGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH------ 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 533 iddrdiKDWNSEELRKNVGLMTQDGVLFRGSLSENLsYFDINYDPSKIQESIDKLNLSNYIQFQSINDIL-ISEGGTNFS 611
Cdd:PLN03232 670 ------AETSSVVIRGSVAYVPQVSWIFNATVRENI-LFGSDFESERYWRAIDVTALQHDLDLLPGRDLTeIGERGVNIS 742
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 612 GGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFA---MPSTKIIITHDENILERVDRVYELTDKKLKQREI 688
Cdd:PLN03232 743 GGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKdelKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGT 822
|
490
....*....|..
gi 1261268082 689 FSK-SKLQTLGK 699
Cdd:PLN03232 823 FAElSKSGSLFK 834
|
|
| Peptidase_C39B |
cd02418 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
7-133 |
6.70e-21 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239099 [Multi-domain] Cd Length: 136 Bit Score: 89.19 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 7 KFIPQMTSFDCGPSCLAMIMHYYGSAVQASEIRNSKIINKKSAwSLLDIKKVSKSYGLSATAYRI-ENITDLQRIQKPMI 85
Cdd:cd02418 2 PYVLQVDEMDCGAACLAMIAKYYGKNYSLAKLRELAGTDREGT-SLLGLVKAAEKLGFETRAVKAdMDLFELKDIPLPFI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 86 AF----WGFNHFVIIERVKANKFYIVDPKAGPMIIDIRSFEEMFCDYILVIE 133
Cdd:cd02418 81 AHvikeWKLNHYVVVYKIKKKKILIADPAVGITKISKEEFEKEWTGVALFLE 132
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
476-676 |
6.93e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.44 E-value: 6.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 476 EFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLL--KLHTPDKGNILIDDRDIKDWNSEE-LRKNVGL 552
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSPDErARAGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLFRG-SLSE--NLSYFDINYDPSKIQESIDKLNlsNYIQFQSINDILIS----EGgtnFSGGQRQRLAMLRLFM 625
Cdd:COG0396 82 AFQYPVEIPGvSVSNflRTALNARRGEELSAREFLKLLK--EKMKELGLDEDFLDryvnEG---FSGGEKKRNEILQMLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 626 KEYPILILDEPTNHLDRETANAVIENIFAMPSTK---IIITHDENILERV--DRVY 676
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDrgiLIITHYQRILDYIkpDFVH 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
474-665 |
9.79e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.00 E-value: 9.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDD------RDIKDWNSEELR 547
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 548 KNVGLMTQDGVLF-RGSLSENLsyfdinydpskIQESIDKLNLSNYIQFQSINDILISEGGTNF--------SGGQRQRL 618
Cdd:COG4161 82 QKVGMVFQQYNLWpHLTVMENL-----------IEAPCKVLGLSKEQAREKAMKLLARLRLTDKadrfplhlSGGQQQRV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1261268082 619 AMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTKI---IITHD 665
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHE 200
|
|
| Peptidase_C39D |
cd02420 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
11-131 |
1.10e-20 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239101 [Multi-domain] Cd Length: 125 Bit Score: 88.26 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 11 QMTSFDCGPSCLAMIMHYYGSAVQASEIRNSKIINK--KSAWSLLdikKVSKSYGLSATAYRIeNITDLQRIQKPMIAFW 88
Cdd:cd02420 6 QMEATECGAASLAIILAYYGRYVPLSELRIACGVSRdgSNASNLL---KAAREYGLTAKGYKK-DLEALREVSLPAIVFW 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1261268082 89 GFNHFVIIERVKANKFYIVDPKAGPMIIDIRSFEEMFCDYILV 131
Cdd:cd02420 82 NFNHFLVVEGFDKRKVFLNDPATGRRTVSLEEFDQSFTGVVLT 124
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
474-675 |
1.78e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 93.29 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRkNVGLM 553
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRER-RVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLFRgslseNLSYFD--------INYDPSKIQESIDK-LNLsnyIQFQSINDILISEggtnFSGGQRQRLAMLRLF 624
Cdd:COG1118 81 FQHYALFP-----HMTVAEniafglrvRPPSKAEIRARVEElLEL---VQLEGLADRYPSQ----LSGGQRQRVALARAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 625 MKEYPILILDEPTNHLDRETANAVIENIF----AMPSTKIIITHD-ENILERVDRV 675
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRrlhdELGGTTVFVTHDqEEALELADRV 204
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
463-664 |
1.79e-20 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain] Cd Length: 257 Bit Score: 91.51 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 463 GSDTKVNILRGSIEFNNISFSFDD--KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKD 540
Cdd:cd03288 8 SSNSGLVGLGGEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 541 WNSEELRKNVGLMTQDGVLFRGSLSENLsyfdinyDP------SKIQESIDKLNLSNYIQ-FQSINDILISEGGTNFSGG 613
Cdd:cd03288 88 LPLHTLRSRLSIILQDPILFSGSIRFNL-------DPeckctdDRLWEALEIAQLKNMVKsLPGGLDAVVTEGGENFSVG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1261268082 614 QRQRLAMLRLFMKEYPILILDEPTNHLDRETAN---AVIENIFAmPSTKIIITH 664
Cdd:cd03288 161 QRQLFCLARAFVRKSSILIMDEATASIDMATENilqKVVMTAFA-DRTVVTIAH 213
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
475-672 |
3.01e-20 |
|
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: 95.00 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDrdikdwnseelrknvglmt 554
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE------------------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 qdgvlfrgslSENLSYFDI---NYDPSK-----IQESIDKLNLSNYiQFQSINDIliseGGTNF------------SGGQ 614
Cdd:TIGR03719 384 ----------TVKLAYVDQsrdALDPNKtvweeISGGLDIIKLGKR-EIPSRAYV----GRFNFkgsdqqkkvgqlSGGE 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261268082 615 RQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTKIIITHDENILERV 672
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRI 506
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
494-641 |
4.87e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 91.72 E-value: 4.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 494 SLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL---RKNVGLMTQDGvlfRGSLSENLSY 570
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP---YASLNPRMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 571 FDINYDPSKIQESIDKLNLSNYIQFqsindiLISEGGTN----------FSGGQRQRLAMLRLFMKEYPILILDEPTNHL 640
Cdd:COG4608 115 GDIIAEPLRIHGLASKAERRERVAE------LLELVGLRpehadrypheFSGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
.
gi 1261268082 641 D 641
Cdd:COG4608 189 D 189
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
475-693 |
7.84e-20 |
|
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: 88.93 E-value: 7.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIiENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEelRKNVGLMT 554
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLF-RGSLSENLSYFDINYDPSKIQESIDKLNLSnyiQFQSINDILISEGGTnFSGGQRQRLAMLRLFMKEYPILIL 633
Cdd:cd03299 78 QNYALFpHMTVYKNIAYGLKKRKVDKKEIERKVLEIA---EMLGIDHLLNRKPET-LSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261268082 634 DEPTNHLDRETANAVIENIFAMPS----TKIIITHD-ENILERVDRVYELTDKKL----KQREIFSKSK 693
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKefgvTVLHVTHDfEEAWALADKVAIMLNGKLiqvgKPEEVFKKPK 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
475-698 |
8.41e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 90.07 E-value: 8.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDD--KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGL 552
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQ------------DGVLFrgSLsENlsyfdiNYDP-----SKIQESIDKLNLSNYIQFQSindiliseggTNFSGGQR 615
Cdd:PRK13635 86 VFQnpdnqfvgatvqDDVAF--GL-EN------IGVPreemvERVDQALRQVGMEDFLNREP----------HRLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 616 QRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS----TKIIITHDENILERVDRVYELTDKKLKQ----RE 687
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkgiTVLSITHDLDEAAQADRVIVMNKGEILEegtpEE 226
|
250
....*....|..
gi 1261268082 688 IFSKS-KLQTLG 698
Cdd:PRK13635 227 IFKSGhMLQEIG 238
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
475-636 |
8.57e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 89.04 E-value: 8.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIieNLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEElRKnVGLMT 554
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP-VSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLFrGSLS--ENLSyfdINYDPSkiqesidkLNLSNyIQFQSINDILISEGGTNF--------SGGQRQRLAMLRLF 624
Cdd:COG3840 78 QENNLF-PHLTvaQNIG---LGLRPG--------LKLTA-EQRAQVEQALERVGLAGLldrlpgqlSGGQRQRVALARCL 144
|
170
....*....|..
gi 1261268082 625 MKEYPILILDEP 636
Cdd:COG3840 145 VRKRPILLLDEP 156
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
483-686 |
9.18e-20 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 88.51 E-value: 9.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 483 SFDDKKIIENLSLNIK---NNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDikdWNSEEL-------RKNVGL 552
Cdd:cd03297 3 CVDIEKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV---LFDSRKkinlppqQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLF-RGSLSENLSYFDINYDPSKIQESIDKLnlSNYIQFQSINDILISEggtnFSGGQRQRLAMLRLFMKEYPIL 631
Cdd:cd03297 80 VFQQYALFpHLNVRENLAFGLKRKRNREDRISVDEL--LDLLGLDHLLNRYPAQ----LSGGEKQRVALARALAAQPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 632 ILDEPTNHLDRETANAV------IENIFAMPStkIIITHDENILERV-DRVYELTDKKLKQR 686
Cdd:cd03297 154 LLDEPFSALDRALRLQLlpelkqIKKNLNIPV--IFVTHDLSEAEYLaDRIVVMEDGRLQYI 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
475-674 |
2.70e-19 |
|
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: 86.78 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIieNLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKdwNSEELRKNVGLMT 554
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLFRG-SLSENLsyfDINYDPSkiqesidkLNLsNYIQFQSINDILISEGGTNF--------SGGQRQRLAMLRLFM 625
Cdd:cd03298 77 QENNLFAHlTVEQNV---GLGLSPG--------LKL-TAEDRQAIEVALARVGLAGLekrlpgelSGGERQRVALARVLV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 626 KEYPILILDEPTNHLD---RETANAVIENIFAMPS-TKIIITHDENILERVDR 674
Cdd:cd03298 145 RDKPVLLLDEPFAALDpalRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQ 197
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
475-683 |
2.86e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 91.96 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKI-IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLM 553
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLFRGSL-SENLSyfdinYDPSKIQESIDKLNLSNYIQFQSiNDILisegGTNFSGGQRQRLAMLRLFMKEYPILI 632
Cdd:PRK10522 403 FTDFHLFDQLLgPEGKP-----ANPALVEKWLERLKMAHKLELED-GRIS----NLKLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1261268082 633 LDE------PtnHLDRETANAVIENIFAMPSTKIIITHDENILERVDRVYELTDKKL 683
Cdd:PRK10522 473 LDEwaadqdP--HFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
474-675 |
3.24e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 89.76 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEElrKNVGLM 553
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLFRG-SLSENLSyFDINYDPSKIQESIDKLN-----LSNYIQFQSINDILISEggtnFSGGQRQRLAMLRLFMKE 627
Cdd:PRK10851 80 FQHYALFRHmTVFDNIA-FGLTVLPRRERPNAAAIKakvtqLLEMVQLAHLADRYPAQ----LSGGQKQRVALARALAVE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 628 YPILILDEPTNHLD---RETANAVIENIFA-MPSTKIIITHD-ENILERVDRV 675
Cdd:PRK10851 155 PQILLLDEPFGALDaqvRKELRRWLRQLHEeLKFTSVFVTHDqEEAMEVADRV 207
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
475-675 |
3.53e-19 |
|
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: 86.65 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKK----IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDwNSEELRKNV 550
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMT-QDGVLFRGSLSENLSYFDINY--DPSKIQESIDKLnlsnyIQFQSINDILISEGGtNFSGGQRQRLAMLRLFMKE 627
Cdd:cd03266 81 GFVSdSTGLYDRLTARENLEYFAGLYglKGDELTARLEEL-----ADRLGMEELLDRRVG-GFSTGMRQKVAIARALVHD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1261268082 628 YPILILDEPTNHLDRETANAVIENIFAMPSTKIIITHDENILERVDRV 675
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERL 202
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
475-685 |
3.53e-19 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 86.45 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFsfDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKdwNSEELRKNVGLMT 554
Cdd:TIGR01277 1 LALDKVRY--EYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHT--GLAPYQRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLFRG-SLSENLSyfdINYDPSkiqesidkLNLsNYIQFQSINDILISEGGTNF--------SGGQRQRLAMLRLFM 625
Cdd:TIGR01277 77 QENNLFAHlTVRQNIG---LGLHPG--------LKL-NAEQQEKVVDAAQQVGIADYldrlpeqlSGGQRQRVALARCLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 626 KEYPILILDEPTNHLD---RETANAVIENIFAMPS-TKIIITHD-ENILERVDRVYELTDKKLKQ 685
Cdd:TIGR01277 145 RPNPILLLDEPFSALDpllREEMLALVKQLCSERQrTLLMVTHHlSDARAIASQIAVVSQGKIKV 209
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
474-700 |
3.72e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.18 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFD-----DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDI--KDWNSEEL 546
Cdd:PRK13637 2 SIKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 547 RKNVGLMTQ--DGVLFrgslsENLSYFDINYDPSKIQESIDKLNLSNYIQFQSIN---DILISEGGTNFSGGQRQRLAML 621
Cdd:PRK13637 82 RKKVGLVFQypEYQLF-----EETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGldyEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 622 RLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS----TKIIITHD-ENILERVDRVYELTDKKL----KQREIFSK- 691
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeynmTIILVSHSmEDVAKLADRIIVMNKGKCelqgTPREVFKEv 236
|
....*....
gi 1261268082 692 SKLQTLGKG 700
Cdd:PRK13637 237 ETLESIGLA 245
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
489-685 |
4.35e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 86.76 E-value: 4.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 489 IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSE---ELR-KNVGLMTQDGVL----- 559
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLiptln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 560 ----------FRGSlSENLSYfdinydpSKIQESIDKLNLSNYIQFQSindiliseggTNFSGGQRQRLAMLRLFMKEYP 629
Cdd:PRK10584 105 alenvelpalLRGE-SSRQSR-------NGAKALLEQLGLGKRLDHLP----------AQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 630 ILILDEPTNHLDRETANAVIENIFAM----PSTKIIITHDENILERVDRVYELTDKKLKQ 685
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLnrehGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
475-683 |
4.95e-19 |
|
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: 85.66 E-value: 4.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLH--TPDKGNILIDDRDIKDWNSEE-LRKNVG 551
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEErARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 552 LMTQDGVLFRGslsenlsyfdinydpskiqesidkLNLSNYIQFqsindilISEGgtnFSGGQRQRLAMLRLFMKEYPIL 631
Cdd:cd03217 81 LAFQYPPEIPG------------------------VKNADFLRY-------VNEG---FSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261268082 632 ILDEPTNHLD----RETANaVIENIFAMPSTKIIITHDENILERV--DRVYELTDKKL 683
Cdd:cd03217 127 ILDEPDSGLDidalRLVAE-VINKLREEGKSVLIITHYQRLLDYIkpDRVHVLYDGRI 183
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
475-698 |
7.02e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.11 E-value: 7.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF--DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGL 552
Cdd:PRK13648 8 IVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQD------GVLFRGSLSENLSYFDINYDP--SKIQESIDKLNLSNYIQFQSindiliseggTNFSGGQRQRLAMLRLF 624
Cdd:PRK13648 88 VFQNpdnqfvGSIVKYDVAFGLENHAVPYDEmhRRVSEALKQVDMLERADYEP----------NALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 625 MKEYPILILDEPTNHLDRETANAVIENIFAMPSTK----IIITHDENILERVDRVYELTDKKLKQ----REIFSKSK-LQ 695
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHnitiISITHDLSEAMEADHVIVMNKGTVYKegtpTEIFDHAEeLT 237
|
...
gi 1261268082 696 TLG 698
Cdd:PRK13648 238 RIG 240
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
475-641 |
9.09e-19 |
|
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: 85.35 E-value: 9.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDwnSEELRKNVGLMT 554
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 qDGVLFRGSLS--ENLSYFDINYDPSK--IQESIDKLNLSNYiqfqsiNDILISeggtNFSGGQRQRLAMLRLFMKEYPI 630
Cdd:cd03268 79 -EAPGFYPNLTarENLRLLARLLGIRKkrIDEVLDVVGLKDS------AKKKVK----GFSLGMKQRLGIALALLGNPDL 147
|
170
....*....|.
gi 1261268082 631 LILDEPTNHLD 641
Cdd:cd03268 148 LILDEPTNGLD 158
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
489-679 |
9.59e-19 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 85.52 E-value: 9.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 489 IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRD-------IKDWNSEELRK-NVGLMTQD-GVL 559
Cdd:TIGR02324 23 VLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEGawvdlaqASPREVLEVRRkTIGYVSQFlRVI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 560 FRGS----LSENLSYFDINYDPS--KIQESIDKLNlsnyiqfqsINDILISEGGTNFSGGQRQRLAMLRLFMKEYPILIL 633
Cdd:TIGR02324 103 PRVSalevVAEPLLERGVPREAAraRARELLARLN---------IPERLWHLPPATFSGGEQQRVNIARGFIADYPILLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1261268082 634 DEPTNHLDRETANAVIE---NIFAMPSTKIIITHDENILERV-DRVYELT 679
Cdd:TIGR02324 174 DEPTASLDAANRQVVVEliaEAKARGAALIGIFHDEEVRELVaDRVMDVT 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
475-681 |
1.20e-18 |
|
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: 83.63 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE-LRKNVGLM 553
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQdgvlfrgslsenlsyfdinydpskiqesidklnlsnyiqfqsindiliseggtnFSGGQRQRLAMLRLFMKEYPILIL 633
Cdd:cd03216 81 YQ------------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1261268082 634 DEPTNHL-DRETAN--AVIENIFAMPSTKIIITHdenileRVDRVYELTDK 681
Cdd:cd03216 107 DEPTAALtPAEVERlfKVIRRLRAQGVAVIFISH------RLDEVFEIADR 151
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
474-693 |
1.36e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.81 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFD-----DKKIIENLSLNIKNNESIAIVGESGSGKSTLA---NLLLKlhtPDKGNILIDDRDIK----DW 541
Cdd:PRK13641 2 SIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLK---PSSGTITIAGYHITpetgNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 542 NSEELRKNVGLMTQ--DGVLFRGSLSENLSYFDINYDPSKIQESIDKLnlsNYIQFQSINDILISEGGTNFSGGQRQRLA 619
Cdd:PRK13641 79 NLKKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKAL---KWLKKVGLSEDLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 620 MLRLFMKEYPILILDEPTNHLD---RETANAVIENIFAMPSTKIIITHD-ENILERVDRVYELTDKKL----KQREIFSK 691
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDpegRKEMMQLFKDYQKAGHTVILVTHNmDDVAEYADDVLVLEHGKLikhaSPKEIFSD 235
|
..
gi 1261268082 692 SK 693
Cdd:PRK13641 236 KE 237
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
178-431 |
2.13e-18 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 85.77 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 178 LAFPFILKKFMDILNASKEVDVRYLLIILGSLIVVIGIKSITSIIKVNFQKE----IDRKSTTKVFEHMFNIPIEKITSR 253
Cdd:pfam00664 16 PAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHtgerLSRRLRRKLFKKILRQPMSFFDTN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 254 HAGDLNVRIMS-LESIRGYILEDLIEMIISIVVIIPLLMYLLYTETFYTLILMFFIASSLFINISLGKFIYNANLVETYY 332
Cdd:pfam00664 96 SVGELLSRLTNdTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 333 LGEHRGKINESLKAMYYVKATGIfskiKSVWKKDYNKYLDTVHKRVLK----QNALESFNSSLSTIFIIIMLAVGFYNFS 408
Cdd:pfam00664 176 VAKASSVAEESLSGIRTVKAFGR----EEYELEKYDKALEEALKAGIKkavaNGLSFGITQFIGYLSYALALWFGAYLVI 251
|
250 260
....*....|....*....|...
gi 1261268082 409 KGEGDLSNIFFFIAISSIIFSPV 431
Cdd:pfam00664 252 SGELSVGDLVAFLSLFAQLFGPL 274
|
|
| Peptidase_C39C |
cd02419 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
17-113 |
2.56e-18 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239100 [Multi-domain] Cd Length: 127 Bit Score: 81.53 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 17 CGPSCLAMIMHYYGSAVQASEIRNSKIINKKSAwSLLDIKKVSKSYGLSATAYRIEnITDLQRIQKPMIAFWGFNHFVII 96
Cdd:cd02419 12 CGLACLAMIASYHGHHVDLASLRQRFPVSLKGA-TLADLIDIAQQLGLSTRALRLD-LEELGQLKLPCILHWDMNHFVVL 89
|
90
....*....|....*..
gi 1261268082 97 ERVKANKFYIVDPKAGP 113
Cdd:cd02419 90 KKVSRRRIVIHDPALGK 106
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
475-684 |
3.12e-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: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNIS--FSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDwNSEELRKNVGL 552
Cdd:cd03263 1 LQIRNLTktYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLFRG-SLSENLSYFDI------NYDPSKIQESIDKLNLSNYIqfqsinDILISeggtNFSGGQRQRLAMLRLFM 625
Cdd:cd03263 80 CPQFDALFDElTVREHLRFYARlkglpkSEIKEEVELLLRVLGLTDKA------NKRAR----TLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 626 KEYPILILDEPTNHLDRETANAVIENIFAMPSTKIII--THDENILERV-DRVYELTDKKLK 684
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIIltTHSMDEAEALcDRIAIMSDGKLR 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
475-680 |
3.46e-18 |
|
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: 84.02 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF-----DDKKI--IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILI------------DD 535
Cdd:COG4778 5 LEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdggwvdlaqaSP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 536 RDIKdwnseELRKN-VGLMTQ-----------DGV---LFRGSLSENLSYfdinydpSKIQESIDKLNL-----SNYiqf 595
Cdd:COG4778 85 REIL-----ALRRRtIGYVSQflrviprvsalDVVaepLLERGVDREEAR-------ARARELLARLNLperlwDLP--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 596 qsindilisegGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIF---AMPSTKIIITHDENILERV 672
Cdd:COG4778 150 -----------PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEeakARGTAIIGIFHDEEVREAV 218
|
....*....
gi 1261268082 673 -DRVYELTD 680
Cdd:COG4778 219 aDRVVDVTP 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
474-675 |
3.69e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.42 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDwNSEELRKNVGLM 553
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQ-DGVLFRGSLSENL----SYFDINydPSKIQESIDklNLSNYIQFQSINDILISEggtnFSGGQRQRLAMLRLFMKEY 628
Cdd:PRK13536 120 PQfDNLDLEFTVRENLlvfgRYFGMS--TREIEAVIP--SLLEFARLESKADARVSD----LSGGMKRRLTLARALINDP 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1261268082 629 PILILDEPTNHLDRETANAVIE---NIFAMPSTKIIITHdenILERVDRV 675
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWErlrSLLARGKTILLTTH---FMEEAERL 238
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
475-672 |
4.12e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 84.37 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE--LRKNVGL 552
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLF-RGSLSENLSYFDINYDPSKIQES-------IDKLNLSNYIQFQSindiliSEggtnFSGGQRQRLAMLR-L 623
Cdd:PRK09493 82 VFQQFYLFpHLTALENVMFGPLRVRGASKEEAekqarelLAKVGLAERAHHYP------SE----LSGGQQQRVAIARaL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 624 FMKeyPILIL-DEPTNHLDRETANAVIEnifAMPS------TKIIITHDENILERV 672
Cdd:PRK09493 152 AVK--PKLMLfDEPTSALDPELRHEVLK---VMQDlaeegmTMVIVTHEIGFAEKV 202
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
364-680 |
6.50e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.56 E-value: 6.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 364 KKDYNKYLDTVHKRVLKQNALESFNSS---LSTIFIIIMLAVGFynFSkGE---GDLSNI---FFFI--AISSIIFSpvs 432
Cdd:COG4178 248 RRRFDAVIANWRRLIRRQRNLTFFTTGygqLAVIFPILVAAPRY--FA-GEitlGGLMQAasaFGQVqgALSWFVDN--- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 433 tiIGSILNWNSVkplLLRtLDILEEELEK--DGSDTKVNILR---GSIEFNNISFSF-DDKKIIENLSLNIKNNESIAIV 506
Cdd:COG4178 322 --YQSLAEWRAT---VDR-LAGFEEALEAadALPEAASRIETsedGALALEDLTLRTpDGRPLLEDLSLSLKPGERLLIT 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 507 GESGSGKSTlanlLLK------------LHTPDKGNILiddrdikdwnseelrknvgLMTQDGVLFRGSLSENLSY--FD 572
Cdd:COG4178 396 GPSGSGKST----LLRaiaglwpygsgrIARPAGARVL-------------------FLPQRPYLPLGTLREALLYpaTA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 573 INYDPSKIQESIDKLNLSNYI----QFQSINDILiseggtnfSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAV 648
Cdd:COG4178 453 EAFSDAELREALEAVGLGHLAerldEEADWDQVL--------SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL 524
|
330 340 350
....*....|....*....|....*....|....
gi 1261268082 649 IENIFA-MPSTKII-ITHDENILERVDRVYELTD 680
Cdd:COG4178 525 YQLLREeLPGTTVIsVGHRSTLAAFHDRVLELTG 558
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
475-689 |
7.90e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 85.77 E-value: 7.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEelRKNVGLMT 554
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLF-RGSLSENLSY---------FDINydpSKIQESIDKLNLSNYIQFQSindiliseggTNFSGGQRQRLAMLRLF 624
Cdd:PRK09452 93 QSYALFpHMTVFENVAFglrmqktpaAEIT---PRVMEALRMVQLEEFAQRKP----------HQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 625 MKEYPILILDEPTNHLD---REtanavienifAMPS-----------TKIIITHD-ENILERVDRVYELTDKKLKQ---- 685
Cdd:PRK09452 160 VNKPKVLLLDESLSALDyklRK----------QMQNelkalqrklgiTFVFVTHDqEEALTMSDRIVVMRDGRIEQdgtp 229
|
....
gi 1261268082 686 REIF 689
Cdd:PRK09452 230 REIY 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
475-680 |
9.92e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.02 E-value: 9.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF-DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLM 553
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQ--DGVLFRGSLSENLSYFDIN--YDPSKIQESI-DKLNLSNYIQFQsindiliSEGGTNFSGGQRQRLAMLRLFMKEY 628
Cdd:PRK13647 85 FQdpDDQVFSSTVWDDVAFGPVNmgLDKDEVERRVeEALKAVRMWDFR-------DKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 629 PILILDEPTNHLD---RETANAVIENIFAMPSTKIIITHDENI-LERVDRVYELTD 680
Cdd:PRK13647 158 DVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKE 213
|
|
| Peptidase_C39_like |
cd02259 |
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ... |
11-125 |
1.42e-17 |
|
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in all sub-families.
Pssm-ID: 239073 [Multi-domain] Cd Length: 122 Bit Score: 79.35 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 11 QMTSFDCGPSCLAMIMHYYGSAVQASEIRNSKIINKKSAwSLLDIKKVSKSYGLSATAYRIeNITDLQRIQKPMIAFWGF 90
Cdd:cd02259 1 GGGPLDCGLACLQMLLRYFGIPVRRDVLLNAQQRRQQGL-SLADLVSLANKLGLTAQGVKL-PLAALSRLQLPALLLWKQ 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 1261268082 91 NHFVIIERVKANKFYIVDP-KAGPMIIDIRSFEEMF 125
Cdd:cd02259 79 GHFVILYGADKGQVLIADPlEEGPVTLSESELEERW 114
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
475-694 |
1.74e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 83.20 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF-DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSE--ELRKNVG 551
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 552 LMTQ--DGVLFRGSLSENLSYFDINYDPSK------IQESIDKLNLSNYIqfqsindiliSEGGTNFSGGQRQRLAMLRL 623
Cdd:PRK13639 82 IVFQnpDDQLFAPTVEEDVAFGPLNLGLSKeevekrVKEALKAVGMEGFE----------NKPPHHLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261268082 624 FMKEYPILILDEPTNHLDRETANAVIENIFAMPS---TKIIITHDENILER-VDRVYELTDKKLKQ----REIFSKSKL 694
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHDVDLVPVyADKVYVMSDGKIIKegtpKEVFSDIET 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
475-653 |
2.09e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.23 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMT 554
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDG--VLFRGSLSENLSYFDINYDPSKIQESIDKLnlsnYIQFQSINDILISEGGTnFSGGQRQRLAMLRLFMKEYPILI 632
Cdd:PRK11614 86 PEGrrVFSRMTVEENLAMGGFFAERDQFQERIKWV----YELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLL 160
|
170 180
....*....|....*....|.
gi 1261268082 633 LDEPTNHLdretANAVIENIF 653
Cdd:PRK11614 161 LDEPSLGL----APIIIQQIF 177
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
479-643 |
2.48e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 80.87 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 479 NISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMTQDGV 558
Cdd:TIGR01189 5 NLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 559 LFRGSLSENLSYF--DINYDPSKIQESIDKLNLSNYiqfqsiNDILISEggtnFSGGQRQRLAMLRLFMKEYPILILDEP 636
Cdd:TIGR01189 85 KPELSALENLHFWaaIHGGAQRTIEDALAAVGLTGF------EDLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEP 154
|
....*..
gi 1261268082 637 TNHLDRE 643
Cdd:TIGR01189 155 TTALDKA 161
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
474-672 |
2.49e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.98 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILI-----------DDRDIKdwn 542
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktpSDKAIR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 543 seELRKNVGLMTQDGVLF-RGSLSENLsyfdinydpskIQESIDKLNLSNYIQFQSINDILISEGGTNF--------SGG 613
Cdd:PRK11124 79 --ELRRNVGMVFQQYNLWpHLTVQQNL-----------IEAPCRVLGLSKDQALARAEKLLERLRLKPYadrfplhlSGG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 614 QRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTKI---IITHDENILERV 672
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVEVARKT 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
489-655 |
2.78e-17 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 81.33 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 489 IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE-LRKNVGLMTQDGVLFrGSLS-- 565
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIF-PELTve 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 566 ENLSYFDINYDPSKIQESIDKLnlsnYIQFQSINDILISEGGTnFSGGQRQRLAMLRLFMKEYPILILDEPTNHLdretA 645
Cdd:cd03224 94 ENLLLGAYARRRAKRKARLERV----YELFPRLKERRKQLAGT-LSGGEQQMLAIARALMSRPKLLLLDEPSEGL----A 164
|
170
....*....|
gi 1261268082 646 NAVIENIFAM 655
Cdd:cd03224 165 PKIVEEIFEA 174
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
475-698 |
2.89e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.47 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFD---DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVG 551
Cdd:PRK13650 5 IEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 552 LMTQ------------DGVLFrGSLSENLSYFDINydpSKIQESIDKLNLSNYIQFQSindiliseggTNFSGGQRQRLA 619
Cdd:PRK13650 85 MVFQnpdnqfvgatveDDVAF-GLENKGIPHEEMK---ERVNEALELVGMQDFKEREP----------ARLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 620 MLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS----TKIIITHDENILERVDRVYELTDKKLKQ----REIFSK 691
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyqmTVISITHDLDEVALSDRVLVMKNGQVEStstpRELFSR 230
|
....*...
gi 1261268082 692 -SKLQTLG 698
Cdd:PRK13650 231 gNDLLQLG 238
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
474-691 |
3.08e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.48 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDKKIIE-----NLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDI----KDWNSE 544
Cdd:PRK13649 2 GINLQNVSYTYQAGTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 545 ELRKNVGLMTQ--DGVLFRGSLSENLSYFDINYDPSKIQ-ESI--DKLNLSnyiqfqSINDILISEGGTNFSGGQRQRLA 619
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEaEALarEKLALV------GISESLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 620 MLRLFMKEYPILILDEPTNHLD---RETANAVIENIFAMPSTKIIITH-DENILERVDRVYELTDKKL----KQREIFSK 691
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDpkgRKELMTLFKKLHQSGMTIVLVTHlMDDVANYADFVYVLEKGKLvlsgKPKDIFQD 235
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
473-641 |
3.56e-17 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 82.21 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 473 GSIEFNNISFSFDD--KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDkGNILIDDrdiKDWNS---EELR 547
Cdd:cd03289 1 GQMTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDG---VSWNSvplQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 548 KNVGLMTQDGVLFRGSLSENLSYFDINYDpSKIQESIDKLNLSNYI-QFQSINDILISEGGTNFSGGQRQRLAMLRLFMK 626
Cdd:cd03289 77 KAFGVIPQKVFIFSGTFRKNLDPYGKWSD-EEIWKVAEEVGLKSVIeQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170
....*....|....*
gi 1261268082 627 EYPILILDEPTNHLD 641
Cdd:cd03289 156 KAKILLLDEPSAHLD 170
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
475-683 |
3.91e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.55 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF----DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL---- 546
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 547 RKNVGLMTQdgvlfRGSLSENLS----------YFDI--NYDPSKIQESIDKLNLSNYIQFQSindiliseggTNFSGGQ 614
Cdd:PRK10535 85 REHFGFIFQ-----RYHLLSHLTaaqnvevpavYAGLerKQRLLRAQELLQRLGLEDRVEYQP----------SQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 615 RQRLAMLRLFMKEYPILILDEPTNHLDR---ETANAVIENIFAMPSTKIIITHDENILERVDRVYELTDKKL 683
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDShsgEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
343-641 |
3.99e-17 |
|
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: 86.12 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 343 SLKAMYYVKATGIFSKIKSVWKKDYNK-------YLDTvhkrvlkqnaLESFNSSLSTIFIIIMLAVGFYNFS---KGEG 412
Cdd:TIGR01271 1070 SLKGLWTIRAFGRQSYFETLFHKALNLhtanwflYLST----------LRWFQMRIDIIFVFFFIAVTFIAIGtnqDGEG 1139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 413 DLSNIfffIAISSIIFSPVSTIIGSILNWNSVKPLLLRT---LDILEEELEKDGSDTKVNILR----------------G 473
Cdd:TIGR01271 1140 EVGII---LTLAMNILSTLQWAVNSSIDVDGLMRSVSRVfkfIDLPQEEPRPSGGGGKYQLSTvlvienphaqkcwpsgG 1216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNIS--FSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDkGNILIDDrdiKDWNSEEL---RK 548
Cdd:TIGR01271 1217 QMDVQGLTakYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDG---VSWNSVTLqtwRK 1292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 549 NVGLMTQDGVLFRGSLSENLSYFDiNYDPSKIQESIDKLNLSNYI-QFQSINDILISEGGTNFSGGQRQRLAMLRLFMKE 627
Cdd:TIGR01271 1293 AFGVIPQKVFIFSGTFRKNLDPYE-QWSDEEIWKVAEEVGLKSVIeQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSK 1371
|
330
....*....|....
gi 1261268082 628 YPILILDEPTNHLD 641
Cdd:TIGR01271 1372 AKILLLDEPSAHLD 1385
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
485-642 |
4.72e-17 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 84.74 E-value: 4.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 485 DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHtPDKGNILIDDRDIKDWNSEE---LRKNVGLMTQDGvlFr 561
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDP--F- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 562 GSLSENLSYFDInydpskIQE--SIDKLNLSNYIQFQSINDIL----ISEGGTN-----FSGGQRQRLAMLR-LFMKeyP 629
Cdd:COG4172 373 GSLSPRMTVGQI------IAEglRVHGPGLSAAERRARVAEALeevgLDPAARHrypheFSGGQRQRIAIARaLILE--P 444
|
170
....*....|....
gi 1261268082 630 -ILILDEPTNHLDR 642
Cdd:COG4172 445 kLLVLDEPTSALDV 458
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
472-683 |
4.78e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 84.94 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 472 RGSIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNIliddrdikDWnSEelRKNVG 551
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KW-SE--NANIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 552 LMTQDgvlfrgslseNLSYFDinydpskiqesiDKLNLSNYI-QF-------QSINDIL---------ISEGGTNFSGGQ 614
Cdd:PRK15064 386 YYAQD----------HAYDFE------------NDLTLFDWMsQWrqegddeQAVRGTLgrllfsqddIKKSVKVLSGGE 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 615 RQRLAMLRLFMKEYPILILDEPTNHLDRETA---NAVIENifaMPSTKIIITHDEnilERVD----RVYELTDKKL 683
Cdd:PRK15064 444 KGRMLFGKLMMQKPNVLVMDEPTNHMDMESIeslNMALEK---YEGTLIFVSHDR---EFVSslatRIIEITPDGV 513
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
475-650 |
5.29e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.29 E-value: 5.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF-----DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWnSEELR-K 548
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRaK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 549 NVGLMTQD---GVLFRGSLSENLS---------YFDINYDPSKI---QESIDKLNLSnyiqfqsINDILISEGGtNFSGG 613
Cdd:COG1101 81 YIGRVFQDpmmGTAPSMTIEENLAlayrrgkrrGLRRGLTKKRRelfRELLATLGLG-------LENRLDTKVG-LLSGG 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1261268082 614 QRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIE 650
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLE 189
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
178-445 |
8.60e-17 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 81.34 E-value: 8.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 178 LAFPFILKKFMD-ILNASkevDVRYLLIILGSLIVVIGIKSITSIIK----VNFQKEIDRKSTTKVFEHMFNIPIEKITS 252
Cdd:cd18570 19 IAGSFFFQILIDdIIPSG---DINLLNIISIGLILLYLFQSLLSYIRsyllLKLSQKLDIRLILGYFKHLLKLPLSFFET 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 253 RHAGDLNVRIMSLESIRGYILEDLIEMIISIVVIIPLLMYLLYTETFYTLILMFFIASSLFINISLGKFIYNANLVETYY 332
Cdd:cd18570 96 RKTGEIISRFNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMES 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 333 LGEHRGKINESLKAMYYVKATGIFSKIKSVWKKDYNKYLDTVHKRVLKQNALESFNSSLSTIFIIIMLAVGFYNFSKGEG 412
Cdd:cd18570 176 NAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQL 255
|
250 260 270
....*....|....*....|....*....|...
gi 1261268082 413 DLSNIFFFIAISSIIFSPVSTIIGSILNWNSVK 445
Cdd:cd18570 256 SLGQLIAFNALLGYFLGPIENLINLQPKIQEAK 288
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
472-693 |
8.82e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 80.73 E-value: 8.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 472 RGSIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLA---NLLLKLHTPDK--GNILIDDRDIKDWNSEEL 546
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPEARvsGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 547 RKNVGLMTQ-DGVLFRGSLSENLSY-FDINYD-------PSKIQESIDKLNLsnyiqFQSINDILISEGGtNFSGGQRQR 617
Cdd:PRK14247 81 RRRVQMVFQiPNPIPNLSIFENVALgLKLNRLvkskkelQERVRWALEKAQL-----WDEVKDRLDAPAG-KLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 618 LAMLRLFMKEYPILILDEPTNHLDRETaNAVIENIF---AMPSTKIIITHDENILERV-DRVYELTDKKLKQ----REIF 689
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPEN-TAKIESLFlelKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEwgptREVF 233
|
....
gi 1261268082 690 SKSK 693
Cdd:PRK14247 234 TNPR 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
485-665 |
1.05e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.60 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 485 DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLhTPDKGNILIDDRDIKDWNSEEL---RKNVGLMTQDGvlfR 561
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL-INSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP---N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 562 GSLSENLSYFDInydpskIQE--SIDKLNLSNYIQFQSINDILISEG---------GTNFSGGQRQRLAMLRLFMKEYPI 630
Cdd:PRK15134 373 SSLNPRLNVLQI------IEEglRVHQPTLSAAQREQQVIAVMEEVGldpetrhryPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1261268082 631 LILDEPTNHLDReTANAVIENIFAMPSTK-----IIITHD 665
Cdd:PRK15134 447 IILDEPTSSLDK-TVQAQILALLKSLQQKhqlayLFISHD 485
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
494-641 |
1.06e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.01 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 494 SLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKdwNSEELRKNVGLMTQDGVLFRG-SLSENLSyfd 572
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT--TTPPSRRPVSMLFQENNLFSHlTVAQNIG--- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261268082 573 INYDPSKiqesidKLNLSNYIQFQSIN-----DILISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLD 641
Cdd:PRK10771 94 LGLNPGL------KLNAAQREKLHAIArqmgiEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
439-675 |
1.08e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 84.70 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 439 LNWNSVKPLLLRTLDIleeELEKDGSD--TKVNILRGSIEFNNISFSFDDKK---IIENLSLNIKNNESIAIVGESGSGK 513
Cdd:PTZ00265 1131 LSFEKYYPLIIRKSNI---DVRDNGGIriKNKNDIKGKIEIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGK 1207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 514 STLANLLLKL--------------HTPD----------------------------------------KGNILIDDRDIK 539
Cdd:PTZ00265 1208 STVMSLLMRFydlkndhhivfkneHTNDmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDIC 1287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 540 DWNSEELRKNVGLMTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQ-FQSINDILISEGGTNFSGGQRQRL 618
Cdd:PTZ00265 1288 DYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIEsLPNKYDTNVGPYGKSLSGGQKQRI 1367
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261268082 619 AMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS----TKIIITHDENILERVDRV 675
Cdd:PTZ00265 1368 AIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAHRIASIKRSDKI 1428
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
475-683 |
1.54e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.90 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDK-----KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDW-------- 541
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 542 ----------------NSEELRKNVGLMTQ--DGVLFRGSLSENLSYFDINYDPSKiQESidKLNLSNYIQFQSINDILI 603
Cdd:PRK13651 83 vleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEA--KKRAAKYIELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 604 SEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIE---NIFAMPSTKIIITHD-ENILERVDRVYELT 679
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEifdNLNKQGKTIILVTHDlDNVLEWTKRTIFFK 239
|
....
gi 1261268082 680 DKKL 683
Cdd:PRK13651 240 DGKI 243
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
474-664 |
1.57e-16 |
|
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: 78.36 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFD------DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLL-KLHTP-DKGNILIDDRDIKDwnsEE 545
Cdd:cd03213 3 TLSFRNLTVTVKsspsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLgVSGEVLINGRPLDK---RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 546 LRKNVGLMTQDGVLFrgslsENLSyfdinydpskIQEsidklNLSNYIQFQSIndiliseggtnfSGGQRQRLAMLRLFM 625
Cdd:cd03213 80 FRKIIGYVPQDDILH-----PTLT----------VRE-----TLMFAAKLRGL------------SGGERKRVSIALELV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1261268082 626 KEYPILILDEPTNHLDRETANAVIENIFAMPS---TKIIITH 664
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtgrTIICSIH 169
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
475-675 |
1.92e-16 |
|
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: 80.87 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDK----KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTP---DKGNILIDDRDIKDWNSEELR 547
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 548 ----KNVGLMTQDGV-----LFR-G-SLSENLSYFDInYDPS----KIQESIDKLNLSNYIQ------FQsindiliseg 606
Cdd:COG0444 82 kirgREIQMIFQDPMtslnpVMTvGdQIAEPLRIHGG-LSKAeareRAIELLERVGLPDPERrldrypHE---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 607 gtnFSGGQRQR--LAM---LRlfmkeyP-ILILDEPTNHLD---------------RETANAVienifampstkIIITHD 665
Cdd:COG0444 151 ---LSGGMRQRvmIARalaLE------PkLLIADEPTTALDvtiqaqilnllkdlqRELGLAI-----------LFITHD 210
|
250
....*....|.
gi 1261268082 666 ENILERV-DRV 675
Cdd:COG0444 211 LGVVAEIaDRV 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
475-666 |
2.08e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.81 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDwnSEELRKNVGLMT 554
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLFRGSLSENLSYFDINYD-------PSKIQESIDKLNLSNYIQFQSindiliseggTNFSGGQRQRLAMLRLFMKE 627
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGLKQDklpkaeiASRVNEMLGLVHMQEFAKRKP----------HQLSGGQRQRVALARSLAKR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1261268082 628 YPILILDEPTNHLDRETAN----AVIENIFAMPSTKIIITHDE 666
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDrmqlEVVDILERVGVTCVMVTHDQ 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
492-685 |
2.30e-16 |
|
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: 79.61 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 492 NLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRK-----------NVGLMTQDGVLf 560
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkkismvfqSFALLPHRTVL- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 561 rgslsENLSY-FDINYDPSKI-----QESIDKLNLSNYIQFqsindiLISEggtnFSGGQRQRLAMLRLFMKEYPILILD 634
Cdd:cd03294 121 -----ENVAFgLEVQGVPRAEreeraAEALELVGLEGWEHK------YPDE----LSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 635 EPTNHLD----RETANAVIENIFAMPSTKIIITHDENILERV-DRVYELTDKKLKQ 685
Cdd:cd03294 186 EAFSALDplirREMQDELLRLQAELQKTIVFITHDLDEALRLgDRIAIMKDGRLVQ 241
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
475-672 |
3.47e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 82.09 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDrdikdwnseelrknvglmt 554
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE------------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 qdgvlfrgslSENLSYFDIN---YDPSK-----IQESIDKLNLSNYiqfqSINdiliSE---GGTNF------------S 611
Cdd:PRK11819 386 ----------TVKLAYVDQSrdaLDPNKtvweeISGGLDIIKVGNR----EIP----SRayvGRFNFkggdqqkkvgvlS 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261268082 612 GGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTKIIITHDENILERV 672
Cdd:PRK11819 448 GGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRI 508
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
475-681 |
3.51e-16 |
|
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: 77.53 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMT 554
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYiqfqsiNDILISEggtnFSGGQRQRLAMLRLFMKEYPILILD 634
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGF------EDRPVAQ----LSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 635 EPTNHLDRETAnAVIENIFAMPSTK----IIITH-DENILERVDRVYELTDK 681
Cdd:cd03231 151 EPTTALDKAGV-ARFAEAMAGHCARggmvVLTTHqDLGLSEAGARELDLGFK 201
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
486-654 |
3.68e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.61 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 486 DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGlmTQDGVlfRGSLS 565
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAM--KPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 566 --ENLSYF-DI-NYDPSKIQESIDKLNLSN--YIQFQsindiliseggtNFSGGQRQRLAMLRLFMKEYPILILDEPTNH 639
Cdd:PRK13539 90 vaENLEFWaAFlGGEELDIAAALEAVGLAPlaHLPFG------------YLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170
....*....|....*
gi 1261268082 640 LDReTANAVIENIFA 654
Cdd:PRK13539 158 LDA-AAVALFAELIR 171
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
487-675 |
3.87e-16 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 79.08 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 487 KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE---LRKNVGLMTQDGV----- 558
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDSPsavnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 559 --LFRGSLSE---NLSYFDINYDPSKIQESIDKLNLSNyiqfqSINDILISEggtnFSGGQRQRLAMLRLFMKEYPILIL 633
Cdd:TIGR02769 104 rmTVRQIIGEplrHLTSLDESEQKARIAELLDMVGLRS-----EDADKLPRQ----LSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1261268082 634 DEPTNHLDRETANAVIENIFAMPS----TKIIITHDENILERV-DRV 675
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQQafgtAYLFITHDLRLVQSFcQRV 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
475-698 |
4.44e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.98 E-value: 4.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDD------KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDW-NSEELR 547
Cdd:PRK13633 5 IKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 548 KNVGLMTQ--DGVLFRGSLSENLSYFDINY--DPSKIQESID----KLNLSNYIQFQSinDILiseggtnfSGGQRQRLA 619
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGPENLgiPPEEIRERVDeslkKVGMYEYRRHAP--HLL--------SGGQKQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 620 MLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS----TKIIITHDENILERVDRVYELTDKKLKQ----REIFSK 691
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkygiTIILITHYMEEAVEADRIIVMDSGKVVMegtpKEIFKE 234
|
....*...
gi 1261268082 692 -SKLQTLG 698
Cdd:PRK13633 235 vEMMKKIG 242
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
475-641 |
4.75e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.66 E-value: 4.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMT 554
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVL---FRGSL------SENLSYFDI--NYDPSKIQESIDKLNLSNYIQfQSIndiliseggTNFSGGQRQRLAMLRL 623
Cdd:PRK09536 84 QDTSLsfeFDVRQvvemgrTPHRSRFDTwtETDRAAVERAMERTGVAQFAD-RPV---------TSLSGGERQRVLLARA 153
|
170
....*....|....*...
gi 1261268082 624 FMKEYPILILDEPTNHLD 641
Cdd:PRK09536 154 LAQATPVLLLDEPTASLD 171
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
471-641 |
5.51e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.49 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 471 LRGsiefNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNV 550
Cdd:PRK10253 8 LRG----EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDGVLfRGSLS--ENLSYFDINYDPSKIQ-ESIDKLNLSNYIQFQSINDiLISEGGTNFSGGQRQRLAMLRLFMKE 627
Cdd:PRK10253 84 GLLAQNATT-PGDITvqELVARGRYPHQPLFTRwRKEDEEAVTKAMQATGITH-LADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170
....*....|....
gi 1261268082 628 YPILILDEPTNHLD 641
Cdd:PRK10253 162 TAIMLLDEPTTWLD 175
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
473-664 |
5.89e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 82.52 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 473 GSIEFNNISFSFDD--KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNV 550
Cdd:PTZ00243 1307 GSLVFEGVQMRYREglPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDGVLFRGSLSENLSYFdINYDPSKIQESIDKLNLSNYIQFQSIN-DILISEGGTNFSGGQRQRLAMLRLFMKEYP 629
Cdd:PTZ00243 1387 SMIPQDPVLFDGTVRQNVDPF-LEASSAEVWAALELVGLRERVASESEGiDSRVLEGGSNYSVGQRQLMCMARALLKKGS 1465
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1261268082 630 ILIL-DEPTNH----LDRETANAVIENIFAMpsTKIIITH 664
Cdd:PTZ00243 1466 GFILmDEATANidpaLDRQIQATVMSAFSAY--TVITIAH 1503
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
476-665 |
6.31e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 81.54 E-value: 6.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 476 EFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDR-DIK--DWNSEEL------ 546
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAyfDQHRAELdpektv 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 547 RKNVGLMTQDgVLFRGSLSENLSYF-DINYDPSKIQESIDKLnlsnyiqfqsindiliseggtnfSGGQRQRLAMLRLFM 625
Cdd:PRK11147 401 MDNLAEGKQE-VMVNGRPRHVLGYLqDFLFHPKRAMTPVKAL-----------------------SGGERNRLLLARLFL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1261268082 626 KEYPILILDEPTNHLDRETANAVIENIFAMPSTKIIITHD 665
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHD 496
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
489-685 |
6.76e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.55 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 489 IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSE---ELRKN-VGLMTQ-DGVLFRGS 563
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 564 LSENLSYFDI--NYDPSKIQ----ESIDKLNLSNYIQFQSindiliSEggtnFSGGQRQRLAMLRLFMKEYPILILDEPT 637
Cdd:PRK11629 104 ALENVAMPLLigKKKPAEINsralEMLAAVGLEHRANHRP------SE----LSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 638 NHLDRETANAVIENIFAMPSTK----IIITHDENILERVDRVYELTDKKLKQ 685
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQgtafLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
475-675 |
6.79e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 76.94 E-value: 6.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIkdwnSEELRKNVGLMT 554
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLFRG-SLSENLSYFD--INYDPSKIQESID----KLNLSNYiqfqsiNDILISEggtnFSGGQRQRLAMLRLFMKE 627
Cdd:cd03269 77 EERGLYPKmKVIDQLVYLAqlKGLKKEEARRRIDewleRLELSEY------ANKRVEE----LSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 628 YPILILDEPTNHLD---RETANAVIENIFAMPSTKIIITHDENILERV-DRV 675
Cdd:cd03269 147 PELLILDEPFSGLDpvnVELLKDVIRELARAGKTVILSTHQMELVEELcDRV 198
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
474-679 |
7.97e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.15 E-value: 7.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPD-----KGNILIDDRDI--KDWNSEEL 546
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 547 RKNVGLMTQDGVLFRGSLSENLSYFD--INYDPSK-----IQESIDKLNLSNYIQFQsindilISEGGTNFSGGQRQRLA 619
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGVkiVGWRPKLeiddiVESALKDADLWDEIKHK------IHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 620 MLRLFMKEYPILILDEPTNHLDrETANAVIENIFAMPS-----TKIIITHDeniLERVDRVYELT 679
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLD-PIASMKVESLIQSLRlrselTMVIVSHN---LHQVSRLSDFT 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
474-683 |
8.60e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.12 E-value: 8.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDK-----KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDD------------- 535
Cdd:PRK13631 21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 536 -----RDIKdwNSEELRKNVGLMTQ--DGVLFRGSLSENLSYFDINYDPSKIQEsidKLNLSNYIQFQSINDILISEGGT 608
Cdd:PRK13631 101 tnpysKKIK--NFKELRRRVSMVFQfpEYQLFKDTIEKDIMFGPVALGVKKSEA---KKLAKFYLNKMGLDDSYLERSPF 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261268082 609 NFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIF---AMPSTKIIITHD-ENILERVDRVYELTDKKL 683
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILdakANNKTVFVITHTmEHVLEVADEVIVMDKGKI 254
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
487-671 |
1.48e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.42 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 487 KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE---LRKNVGLMTQDGV----- 558
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQMVFQDSIsavnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 559 --LFRGSLSENLSYFdINYDPSKIQESIDKLnlsnyIQFQSINDILISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEP 636
Cdd:PRK10419 105 rkTVREIIREPLRHL-LSLDKAERLARASEM-----LRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 1261268082 637 TNHLDRETANAVIENIFAMPSTK----IIITHDENILER 671
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQFgtacLFITHDLRLVER 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
475-675 |
1.73e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.20 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKK----IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL---R 547
Cdd:COG1135 2 IELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 548 KNVGLMTQDGVLFRgslS----ENLSY-FDI-NYDPSKIQESIDKL----NLS----NYIqfqsindiliseggTNFSGG 613
Cdd:COG1135 82 RKIGMIFQHFNLLS---SrtvaENVALpLEIaGVPKAEIRKRVAELlelvGLSdkadAYP--------------SQLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261268082 614 QRQRLAMLR-LFMKeyP-ILILDEPTNHLDRETANAVIE---------NIfampsTKIIITHDENILERV-DRV 675
Cdd:COG1135 145 QKQRVGIARaLANN--PkVLLCDEATSALDPETTRSILDllkdinrelGL-----TIVLITHEMDVVRRIcDRV 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
505-690 |
1.80e-15 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 77.92 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 505 IVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEelRKNVGLMTQDGVLF-RGSLSENLSYfdinydPSKIQ-- 581
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFpHMTVEENVAF------GLKMRkv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 582 --ESIDK--LNLSNYIQFQSINDILISEggtnFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS 657
Cdd:TIGR01187 73 prAEIKPrvLEALRLVQLEEFADRKPHQ----LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1261268082 658 ----TKIIITHD-ENILERVDRVYELTDKKLKQ----REIFS 690
Cdd:TIGR01187 149 qlgiTFVFVTHDqEEAMTMSDRIAIMRKGKIAQigtpEEIYE 190
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
475-664 |
1.85e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 76.74 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLH--TPD---KGNILIDDRDIKDWNSE--ELR 547
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlNPEvtiTGSIVYNGHNIYSPRTDtvDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 548 KNVGLMTQDGVLFRGSLSENLSY-FDIN--YDPSKIQESIDKlNLSNYIQFQSINDILiSEGGTNFSGGQRQRLAMLRLF 624
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENVVYgLRLKgiKDKQVLDEAVEK-SLKGASIWDEVKDRL-HDSALGLSGGQQQRVCIARVL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1261268082 625 MKEYPILILDEPTNHLDRETANAVIENIFAMPS--TKIIITH 664
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTR 205
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
475-694 |
2.07e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.15 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKK--IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGN---ILIDDRDIKDWNSEELRKN 549
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 550 VGLMTQ--DGVLFRGSLSENLSYFDINYDPSK------IQESIDKLNLSNYIQFQSindiliseggTNFSGGQRQRLAML 621
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGLENRAVPRpemikiVRDVLADVGMLDYIDSEP----------ANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 622 RLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS----TKIIITHDENILERVDRVYELTDKKL----KQREIFSKSK 693
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknnlTVISITHDIDEANMADQVLVLDDGKLlaqgSPVEIFSKVE 235
|
.
gi 1261268082 694 L 694
Cdd:PRK13640 236 M 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
475-675 |
2.13e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 75.87 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDI-KDwnSEELRKNVGLM 553
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvRE--PREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLFRG-SLSENLSYFD--INYDPSKIQESIDKlnLSNYIQFQSINDILISeggtNFSGGQRQRLAMLRLFMKEYPI 630
Cdd:cd03265 79 FQDLSVDDElTGWENLYIHArlYGVPGAERRERIDE--LLDFVGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1261268082 631 LILDEPTNHLDRETANAVIENIFAMPS----TKIIITHD-ENILERVDRV 675
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEefgmTILLTTHYmEEAEQLCDRV 202
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
493-684 |
2.19e-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: 78.23 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 493 LSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDikdWNSEEL-------RKNVGLMTQDGVLF-RGSL 564
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRT---LFDSRKgiflppeKRRIGYVFQEARLFpHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 565 SENLSYFDINYDPSKIQESIDKLnlsnyIQFQSINDILISEGGTnFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRET 644
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFERV-----IELLGIGHLLGRLPGR-LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1261268082 645 ANAVI---ENI---FAMPStkIIITHDENILERV-DRVYELTDKKLK 684
Cdd:TIGR02142 167 KYEILpylERLhaeFGIPI--LYVSHSLQEVLRLaDRVVVLEDGRVA 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
474-641 |
2.36e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.35 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTlanlLLKLHT----PDKGNILIDDRDIKDWNSEELRKN 549
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKST----LLRALSgelsPDSGEVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 550 VGLMTQDGVL-FRGSLSE----NLSYFDINYDPSK--IQESIDKLNLSNYIQ--FQSIndiliseggtnfSGGQRQR--- 617
Cdd:PRK13548 78 RAVLPQHSSLsFPFTVEEvvamGRAPHGLSRAEDDalVAAALAQVDLAHLAGrdYPQL------------SGGEQQRvql 145
|
170 180
....*....|....*....|....*..
gi 1261268082 618 ---LAMLRLFMKEYPILILDEPTNHLD 641
Cdd:PRK13548 146 arvLAQLWEPDGPPRWLLLDEPTSALD 172
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
475-664 |
4.65e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.38 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDwNSEELRKNVGLMT 554
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 Q-DGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQFQSINDILISEggtnFSGGQRQRLAMLRLFMKEYPILIL 633
Cdd:PRK13537 87 QfDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190
....*....|....*....|....*....|....
gi 1261268082 634 DEPTNHLDRETANAVIE---NIFAMPSTKIIITH 664
Cdd:PRK13537 163 DEPTTGLDPQARHLMWErlrSLLARGKTILLTTH 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
475-685 |
8.73e-15 |
|
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: 77.54 E-value: 8.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLL--LKLHTPDKGNIL-------------------- 532
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 533 --------IDDRDIKDWNSEE-----LRKNVGLMTQDGVLFRG--SLSENL--SYFDINYdpsKIQESIDK-LNLSNYIQ 594
Cdd:TIGR03269 81 pcpvcggtLEPEEVDFWNLSDklrrrIRKRIAIMLQRTFALYGddTVLDNVleALEEIGY---EGKEAVGRaVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 595 FQSindiLISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETA----NAVIENIFAMPSTKIIITHDENILE 670
Cdd:TIGR03269 158 LSH----RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIE 233
|
250
....*....|....*.
gi 1261268082 671 RV-DRVYELTDKKLKQ 685
Cdd:TIGR03269 234 DLsDKAIWLENGEIKE 249
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
486-650 |
9.20e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 74.23 E-value: 9.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 486 DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLL---LKLHTPDKGNILIDDRDIKdwnSEELRKNVGLMTQDGVLFRG 562
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRK---PDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 563 -SLSENLSYfdinYDPSKIQESIDKLNLSNYIQFQSINDILISE-GGTNF---SGGQRQRLAMLRLFMKEYPILILDEPT 637
Cdd:cd03234 96 lTVRETLTY----TAILRLPRKSSDAIRKKRVEDVLLRDLALTRiGGNLVkgiSGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170
....*....|...
gi 1261268082 638 NHLDRETANAVIE 650
Cdd:cd03234 172 SGLDSFTALNLVS 184
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
488-683 |
1.07e-14 |
|
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: 77.15 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 488 KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKG--NILIDDrdikDWNSeelrknvglMTQDGVLFRGSLS 565
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGD----EWVD---------MTKPGPDGRGRAK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 566 ENLSYFDINYDPSKIQESIDKLNLSNYIQF-----------------------QSINDILISEggtnFSGGQRQRLAMLR 622
Cdd:TIGR03269 365 RYIGILHQEYDLYPHRTVLDNLTEAIGLELpdelarmkavitlkmvgfdeekaEEILDKYPDE----LSEGERHRVALAQ 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 623 LFMKEYPILILDEPTNHLDRETANAVIENIF----AMPSTKIIITHDEN-ILERVDRVYELTDKKL 683
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPITKVDVTHSILkareEMEQTFIIVSHDMDfVLDVCDRAALMRDGKI 506
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
473-696 |
1.13e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 473 GSIEFNNISFSFDDK-----KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDI-----KDWN 542
Cdd:PRK13645 5 KDIILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 543 SEELRKNVGLMTQ--DGVLFRGSLSENLSYFDINYDPSKiQESIDKlnLSNYIQFQSINDILISEGGTNFSGGQRQRLAM 620
Cdd:PRK13645 85 VKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENK-QEAYKK--VPELLKLVQLPEDYVKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 621 LRLFMKEYPILILDEPTNHLDRETANAVIeNIFAMPSTK-----IIITHD-ENILERVDRVYELTDKKLKQR----EIFS 690
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFI-NLFERLNKEykkriIMVTHNmDQVLRIADEVIVMHEGKVISIgspfEIFS 240
|
....*.
gi 1261268082 691 KSKLQT 696
Cdd:PRK13645 241 NQELLT 246
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
478-671 |
1.34e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 478 NNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMTQ-- 555
Cdd:PRK10575 15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQql 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 556 ---DGVLFRGSLSEN-------LSYFDINyDPSKIQESIDKLNLSNYIqfQSINDILiseggtnfSGGQRQR--LAMlrL 623
Cdd:PRK10575 95 paaEGMTVRELVAIGrypwhgaLGRFGAA-DREKVEEAISLVGLKPLA--HRLVDSL--------SGGERQRawIAM--L 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 624 FMKEYPILILDEPTNHLDRETANAVIENIFAMPS----TKIIITHDENILER 671
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQerglTVIAVLHDINMAAR 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
494-691 |
1.77e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 75.00 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 494 SLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE---LRKNVGLMTQD--GVL-----FRGS 563
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQNpyGSLnprkkVGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 564 LSENLsyfDINYDPS------KIQESIDKLNL--SNYIQFQSIndiliseggtnFSGGQRQRLAMLRLFMKEYPILILDE 635
Cdd:PRK11308 115 LEEPL---LINTSLSaaerreKALAMMAKVGLrpEHYDRYPHM-----------FSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 636 PTNHLDReTANAVIENIFA-----MPSTKIIITHDENILERV---------DRVYELTDKKlkqrEIFSK 691
Cdd:PRK11308 181 PVSALDV-SVQAQVLNLMMdlqqeLGLSYVFISHDLSVVEHIadevmvmylGRCVEKGTKE----QIFNN 245
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
338-689 |
1.81e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.47 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 338 GKINESLKAMYYVKATGifskiksvWKKDYNKYLDTVHKRVL----KQNALESFNSSLSTIFIIIMLAVGFYNFSKGEGD 413
Cdd:PLN03130 480 GLMNEVLAAMDTVKCYA--------WENSFQSKVQTVRDDELswfrKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGD 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 414 LSNIFFFIAIS--SIIFSPV---STIIGSILNWN-SVKPLllRTLDILEEELEKDGSDTKVNILRGSIEfnNISFSFD-- 485
Cdd:PLN03130 552 LTPARAFTSLSlfAVLRFPLfmlPNLITQAVNANvSLKRL--EELLLAEERVLLPNPPLEPGLPAISIK--NGYFSWDsk 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 486 -DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLL-KLHTPDKGNILIddrdikdwnseelRKNVGLMTQDGVLFRGS 563
Cdd:PLN03130 628 aERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLgELPPRSDASVVI-------------RGTVAYVPQVSWIFNAT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 564 LSENLsYFDINYDPSKIQESIDKLNLSNYIQFQSINDIL-ISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDR 642
Cdd:PLN03130 695 VRDNI-LFGSPFDPERYERAIDVTALQHDLDLLPGGDLTeIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1261268082 643 ETANAVIENIFA---MPSTKIIITHDENILERVDRVYELTDKKLKQREIF 689
Cdd:PLN03130 774 HVGRQVFDKCIKdelRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTY 823
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
475-682 |
1.84e-14 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 73.45 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLklHTPD----KGNILIDDRDIKDWNSEEL-RKN 549
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIA--GHPSyevtSGTILFKGQDLLELEPDERaRAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 550 VGLMTQ-----DGV----LFRGSLS--------ENLSYFDINydpSKIQESIDKLNLSNYIQFQSINdilisEGgtnFSG 612
Cdd:TIGR01978 79 LFLAFQypeeiPGVsnleFLRSALNarrsargeEPLDLLDFE---KLLKEKLALLDMDEEFLNRSVN-----EG---FSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 613 GQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTK---IIITHDENILERV--DRVYELTDKK 682
Cdd:TIGR01978 148 GEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDrsfLIITHYQRLLNYIkpDYVHVLLDGR 222
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
333-675 |
2.23e-14 |
|
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: 77.26 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 333 LGEHR----GKINESLkamyyVKATGIFSKIKSV----WKKDYNKYLDTVHKRVL----KQNALESFNSS--LSTIFIII 398
Cdd:TIGR01271 245 MMPYRdkraGKISERL-----AITSEIIENIQSVkaycWEEAMEKIIKNIRQDELkltrKIAYLRYFYSSafFFSGFFVV 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 399 MLAVGFYNFSKGEgDLSNIFFFIAISSIIFSPVS-TIIGSILNWNSVkpllLRTLDILEEELEKDGSDT-KVNILRGSIE 476
Cdd:TIGR01271 320 FLSVVPYALIKGI-ILRRIFTTISYCIVLRMTVTrQFPGAIQTWYDS----LGAITKIQDFLCKEEYKTlEYNLTTTEVE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 477 FNNISFSFDD----------------------------------KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLK 522
Cdd:TIGR01271 395 MVNVTASWDEgigelfekikqnnkarkqpngddglffsnfslyvTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 523 LHTPDKGNILIDDRdikdwnseelrknVGLMTQDGVLFRGSLSENLsYFDINYDPSKIQESIDKLNLSNYIQ-FQSINDI 601
Cdd:TIGR01271 475 ELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI-IFGLSYDEYRYTSVIKACQLEEDIAlFPEKDKT 540
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261268082 602 LISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFA---MPSTKIIITHDENILERVDRV 675
Cdd:TIGR01271 541 VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCklmSNKTRILVTSKLEHLKKADKI 617
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
486-674 |
2.24e-14 |
|
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: 76.51 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 486 DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDrDIK----------DwNSEELRKNV--GLM 553
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP-GIKvgylpqepqlD-PTKTVRENVeeGVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLFR-GSLSENLSYFDINYDP-----SKIQESIDKLNLSNYIQFQSI---------NDILIseggTNFSGGQRQRL 618
Cdd:TIGR03719 95 EIKDALDRfNEISAKYAEPDADFDKlaaeqAELQEIIDAADAWDLDSQLEIamdalrcppWDADV----TKLSGGERRRV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 619 AMLRLFMKEYPILILDEPTNHLDRETAnAVIENIFA-MPSTKIIITHD--------ENILErVDR 674
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLDAESV-AWLERHLQeYPGTVVAVTHDryfldnvaGWILE-LDR 233
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
455-675 |
2.60e-14 |
|
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: 73.74 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 455 LEEELEKDGSDTKVNILRGSIEFNNisFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILID 534
Cdd:cd03291 20 LLEKAKQENNDRKHSSDDNNLFFSN--LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 535 DRdikdwnseelrknVGLMTQDGVLFRGSLSENLsYFDINYDPSKIQESIDKLNLSNYI-QFQSINDILISEGGTNFSGG 613
Cdd:cd03291 98 GR-------------ISFSSQFSWIMPGTIKENI-IFGVSYDEYRYKSVVKACQLEEDItKFPEKDNTVLGEGGITLSGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 614 QRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFA--MPS-TKIIITHDENILERVDRV 675
Cdd:cd03291 164 QRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCklMANkTRILVTSKMEHLKKADKI 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
475-694 |
2.81e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 73.68 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFD-DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLM 553
Cdd:PRK13652 4 IETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQ--DGVLFRGSLSENLSYFDINYDpskIQESIDKLNLSNYIQFQSINDiLISEGGTNFSGGQRQRLAMLRLFMKEYPIL 631
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGPINLG---LDEETVAHRVSSALHMLGLEE-LRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 632 ILDEPTNHLDRETANAVIENIFAMPS----TKIIITHD-ENILERVDRVYELTDKKL----KQREIFSKSKL 694
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQlDLVPEMADYIYVMDKGRIvaygTVEEIFLQPDL 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
475-665 |
4.04e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.86 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNS--------EEL 546
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkgliRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 547 RKNVGLMTQDGVLF--RGSLsENLSYFDINYDPSKIQESID-------KLNLSnyiqfqsindiliseGGTN-----FSG 612
Cdd:PRK11264 84 RQHVGFVFQNFNLFphRTVL-ENIIEGPVIVKGEPKEEATArarellaKVGLA---------------GKETsyprrLSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 613 GQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS---TKIIITHD 665
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQekrTMVIVTHE 203
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
485-694 |
4.33e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 73.34 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 485 DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIkDWNSE---ELRKNVGLMTQ--DGVL 559
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRESVGMVFQdpDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 560 FRGSLSENLSYFDINYD-PSK-IQESIDKLNLSNYIQFqsindiLISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPT 637
Cdd:PRK13636 96 FSASVYQDVSFGAVNLKlPEDeVRKRVDNALKRTGIEH------LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 638 NHLD----RETANAVIENIFAMPSTKIIITHDENILE-RVDRVYELTDKKL----KQREIFSKSKL 694
Cdd:PRK13636 170 AGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVilqgNPKEVFAEKEM 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
479-683 |
4.80e-14 |
|
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: 72.19 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 479 NISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWN-SEELRKNVGLMTQDG 557
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 558 VLFRG-SLSENLS-YFDINYDPSKIQEsiDKLN-LSNYIQFQSINDILisegGTNFSGGQRQRLAMLRLFMKEYPILILD 634
Cdd:cd03218 85 SIFRKlTVEENILaVLEIRGLSKKERE--EKLEeLLEEFHITHLRKSK----ASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 635 EPTNHLDrETANAVIENIFAMPSTK---IIIThDEN---ILERVDRVYELTDKKL 683
Cdd:cd03218 159 EPFAGVD-PIAVQDIQKIIKILKDRgigVLIT-DHNvreTLSITDRAYIIYEGKV 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
475-676 |
6.19e-14 |
|
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: 71.70 E-value: 6.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL-RKNVGLM 553
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLFRG-SLSENL----------SYFDINYDPS------KIQESIDKLNLSNYIqfqsinDILISeggtNFSGGQRQ 616
Cdd:cd03219 81 FQIPRLFPElTVLENVmvaaqartgsGLLLARARREereareRAEELLERVGLADLA------DRPAG----ELSYGQQR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261268082 617 RLAMLRLFMKEYPILILDEPT---NHLDRETANAVIENIFAMPSTKIIITHDENILERV-DRVY 676
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLaDRVT 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
479-641 |
8.42e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.46 E-value: 8.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 479 NISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWN-SEELRKNVGLMTQDG 557
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 558 VLFRG-SLSENL-SYFDINYDPSKIQESIDKLNLSNYIQFQSINDILisegGTNFSGGQRQRLAMLRLFMKEYPILILDE 635
Cdd:PRK10895 88 SIFRRlSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM----GQSLSGGERRRVEIARALAANPKFILLDE 163
|
....*.
gi 1261268082 636 PTNHLD 641
Cdd:PRK10895 164 PFAGVD 169
|
|
| Peptidase_C39G |
cd02423 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
11-132 |
8.81e-14 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature.
Pssm-ID: 239103 [Multi-domain] Cd Length: 129 Bit Score: 68.45 E-value: 8.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 11 QMTSFDCGPSCLAMIM-HYYGSAVQASEIRNSKIINKKSAwSLLDIKKVSKSYGLSATAYRIeNITDLQRIQKPMIAFW- 88
Cdd:cd02423 6 QSYDFSCGPAALATLLrYYGGINITEQEVLKLMLIRSEGF-SMLDLKRYAEALGLKANGYRL-NLDKLNALQIPVIVLVn 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1261268082 89 --GFNHFVIIERVKANKFYIVDPKAGPMIIDIRSFEEMFCDYILVI 132
Cdd:cd02423 84 ngGYGHFVVIKGIDGDRVLVGDPALGNISMSREEFERIWTGNALFV 129
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
475-666 |
9.95e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.22 E-value: 9.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDwNSEELRkNVGLMT 554
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH-RSIQQR-DICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLF-RGSLSENLSY--FDINYDPSKIQESIDK-LNLSNYIQFQS--INDIliseggtnfSGGQRQRLAMLRLFMKEY 628
Cdd:PRK11432 85 QSYALFpHMSLGENVGYglKMLGVPKEERKQRVKEaLELVDLAGFEDryVDQI---------SGGQQQRVALARALILKP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1261268082 629 PILILDEPTNHLDRETANAVIENIFAMPS----TKIIITHDE 666
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQqfniTSLYVTHDQ 197
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
474-666 |
1.00e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.14 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDwnSEELRKNVGLM 553
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND--VPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLF-RGSLSENLSyFDI---NYDPSKIQESIDklNLSNYIQFqsinDILISEGGTNFSGGQRQRLAMLRLFMKEYP 629
Cdd:PRK11000 81 FQSYALYpHLSVAENMS-FGLklaGAKKEEINQRVN--QVAEVLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1261268082 630 ILILDEPTNHLD---RETANAVIENIFA-MPSTKIIITHDE 666
Cdd:PRK11000 154 VFLLDEPLSNLDaalRVQMRIEISRLHKrLGRTMIYVTHDQ 194
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
450-664 |
1.08e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 74.36 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 450 RTLDILEEELE-KDGSDTkVNILRGSIEFNNISFSF--DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTP 526
Cdd:PRK10789 289 RIRAMLAEAPVvKDGSEP-VPEGRGELDVNIRQFTYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 527 DKGNILIDDRDIKDWNSEELRKNVGLMTQDGVLFRGSLSENLSYFDINYDPSKIQESI-------DKLNLSNYIQFQsin 599
Cdd:PRK10789 368 SEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVArlasvhdDILRLPQGYDTE--- 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261268082 600 dilISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENI--FAMPSTKIIITH 664
Cdd:PRK10789 445 ---VGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLrqWGEGRTVIISAH 508
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
475-681 |
1.13e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 69.49 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISF-SFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDikdwnseelrkNVGLM 553
Cdd:cd03223 1 IELENLSLaTPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----------DLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLFRGSLSENLSYfdinydPSKiqesidklnlsnyiqfqsinDILiseggtnfSGGQRQRLAMLRLFMKEYPILIL 633
Cdd:cd03223 70 PQRPYLPLGTLREQLIY------PWD--------------------DVL--------SGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1261268082 634 DEPTNHLDRETANAVIENIFAMPSTKIIITHDENILERVDRVYELTDK 681
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGE 163
|
|
| Peptidase_C39E |
cd02424 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
6-132 |
1.74e-13 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family, which contains Colicin V perocessing peptidase.
Pssm-ID: 239104 [Multi-domain] Cd Length: 129 Bit Score: 67.75 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 6 IKFIPQMTSFDCGPSCLAMIMHYYGSAVQASEIRNSKIINKKSAWSLLDIKKVSKSYGLSATAYRIENITDLQRIQKPMI 85
Cdd:cd02424 1 MKIIKQTDLNDCGIAVIQMLYNHYYKKKYDLNELKIKANLKKNGLSIYDLENLAKKFGLETESYQGSFLEFLELKNKFII 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1261268082 86 AFW--GFNHFVIIERVKANKFYIVDPKAGPMIIDIRSFEEMFCDYILVI 132
Cdd:cd02424 81 LLKsnGLNHFVIVKKIKKNKFIVLDPKKGKYKITYKEFEKIFNNIIITV 129
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
475-654 |
2.39e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.45 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILiddrdikdWNSEELRKNVGLMT 554
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL--------WQGEPIRRQRDEYH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDgVLFRGSLS---------ENLSYF---DINYDPSKIQESIDKLNLSNYiqfqsiNDILISeggtNFSGGQRQRLAMLR 622
Cdd:PRK13538 74 QD-LLYLGHQPgikteltalENLRFYqrlHGPGDDEALWEALAQVGLAGF------EDVPVR----QLSAGQQRRVALAR 142
|
170 180 190
....*....|....*....|....*....|..
gi 1261268082 623 LFMKEYPILILDEPTNHLDREtANAVIENIFA 654
Cdd:PRK13538 143 LWLTRAPLWILDEPFTAIDKQ-GVARLEALLA 173
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
474-693 |
2.75e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.96 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFD-----DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDI----KDWNSE 544
Cdd:PRK13646 2 TIRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 545 ELRKNVGLMTQ--DGVLFRGSLSEnlsyfDINYDPSKIQESIDKLNLSNY---IQFQSINDILiSEGGTNFSGGQRQRLA 619
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVER-----EIIFGPKNFKMNLDEVKNYAHrllMDLGFSRDVM-SQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 620 MLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMP----STKIIITHDENILER-VDRVYELTDKKLKQ----REIFS 690
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVARyADEVIVMKEGSIVSqtspKELFK 235
|
...
gi 1261268082 691 KSK 693
Cdd:PRK13646 236 DKK 238
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
485-693 |
4.06e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.08 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 485 DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKL------HTPDKGNILIDDRDIKDWNSEELRKNVGLMTQDGV 558
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 559 LF-RGSLSENLSY-------FDINYDPSKIQESIDKLNLsnyiqFQSINDILISEgGTNFSGGQRQRLAMLRLFMKEYPI 630
Cdd:PRK14246 101 PFpHLSIYDNIAYplkshgiKEKREIKKIVEECLRKVGL-----WKEVYDRLNSP-ASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 631 LILDEPTNHLDRETANAVIENIFAMPS--TKIIITHDENILERV-DRVYELTDKKL----KQREIFSKSK 693
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVaDYVAFLYNGELvewgSSNEIFTSPK 244
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
475-678 |
4.41e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.53 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDK-----KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE---- 545
Cdd:PRK13643 2 IKFEKVNYTYQPNspfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 546 LRKNVGLMTQ--DGVLFRGSLSENLSYFDINYDPSKiqESIDKLnLSNYIQFQSINDILISEGGTNFSGGQRQRLAMLRL 623
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPK--EKAEKI-AAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1261268082 624 FMKEYPILILDEPTNHLD---RETANAVIENIFAMPSTKIIITH-DENILERVDRVYEL 678
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDpkaRIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLL 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
209-685 |
4.47e-13 |
|
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: 73.06 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 209 LIVVIGIKSITSIIKVNFQKEI-----DRKSTTkvfehmfnipiekitsrhAGDLnVRIMSLESIRGYILEDLIEMIISI 283
Cdd:TIGR00957 381 ICFVSGMRIKTAVMGAVYRKALvitnsARKSST------------------VGEI-VNLMSVDAQRFMDLATYINMIWSA 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 284 VVIIPLLMYLLYTEtfytlilmffIASSLFINISLGKFIYNANLV-----ETYYLGEHRGKINEsLKAMyyvkaTGIFSK 358
Cdd:TIGR00957 442 PLQVILALYFLWLN----------LGPSVLAGVAVMVLMVPLNAVmamktKTYQVAHMKSKDNR-IKLM-----NEILNG 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 359 IKSV----WKKDYNKYLDTVHK---RVLKQNALESFNSSLS---TIFII--IMLAVGFYNFSKGEGDLSNIFFFIAISSI 426
Cdd:TIGR00957 506 IKVLklyaWELAFLDKVEGIRQeelKVLKKSAYLHAVGTFTwvcTPFLValITFAVYVTVDENNILDAEKAFVSLALFNI 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 427 IFSPVS---TIIGSILNwNSVKPLLLRTLdILEEELEKDGSDTKvNILRG---SIEFNNISFSF--DDKKIIENLSLNIK 498
Cdd:TIGR00957 586 LRFPLNilpMVISSIVQ-ASVSLKRLRIF-LSHEELEPDSIERR-TIKPGegnSITVHNATFTWarDLPPTLNGITFSIP 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 499 NNESIAIVGESGSGKSTLANLLLKLHTPDKGNIliddrdikdwnseELRKNVGLMTQDGVLFRGSLSENLsYFDINYDPS 578
Cdd:TIGR00957 663 EGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQAWIQNDSLRENI-LFGKALNEK 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 579 KIQESIDKLNLSNYIQFQSIND-ILISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFA--- 654
Cdd:TIGR00957 729 YYQQVLEACALLPDLEILPSGDrTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGpeg 808
|
490 500 510
....*....|....*....|....*....|...
gi 1261268082 655 --MPSTKIIITHDENILERVDRVYELTDKKLKQ 685
Cdd:TIGR00957 809 vlKNKTRILVTHGISYLPQVDVIIVMSGGKISE 841
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
490-680 |
5.25e-13 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 69.03 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 490 IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKD----------------WNSeeLRKNVGLM 553
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpdrmvvfqnysllpWLT--VRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TqDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNlsnyiqfqsindiliseggTNFSGGQRQRLAMLRLFMKEYPILIL 633
Cdd:TIGR01184 79 V-DRVLPDLSKSERRAIVEEHIALVGLTEAADKRP-------------------GQLSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 634 DEPTNHLDRETANAVIENIFAMPS----TKIIITHD-ENILERVDRVYELTD 680
Cdd:TIGR01184 139 DEPFGALDALTRGNLQEELMQIWEehrvTVLMVTHDvDEALLLSDRVVMLTN 190
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
475-688 |
8.27e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.52 E-value: 8.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDdRDIKdwnseelrknVGLMT 554
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLI----------VARLQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QD------GVLFR------GSLSENL-SYFDINY----DPS--------KIQESIDKLNLsnyIQFQS-INDILISEGG- 607
Cdd:PRK11147 73 QDpprnveGTVYDfvaegiEEQAEYLkRYHDISHlvetDPSeknlnelaKLQEQLDHHNL---WQLENrINEVLAQLGLd 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 608 -----TNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTKIIITHDENILER-----VD---- 673
Cdd:PRK11147 150 pdaalSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNmatriVDldrg 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 1261268082 674 --------------------RVYELT----DKKLKQREI 688
Cdd:PRK11147 230 klvsypgnydqyllekeealRVEELQnaefDRKLAQEEV 268
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
504-672 |
1.10e-12 |
|
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: 68.69 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 504 AIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMTQ-----------DGVLFRGSLSENLSYFD 572
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVEQdsdtavpltvrDVVALGRIPHRSLWAGD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 573 INYDPSKIQESIDKLNLSNyiqfqsindiLISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLD----RETANAV 648
Cdd:TIGR03873 111 SPHDAAVVDRALARTELSH----------LADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDvraqLETLALV 180
|
170 180
....*....|....*....|....
gi 1261268082 649 IENIFAMPSTkIIITHDENILERV 672
Cdd:TIGR03873 181 RELAATGVTV-VAALHDLNLAASY 203
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
174-436 |
1.54e-12 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 68.74 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 174 QISILAFPFILKKFMDILNASKEVDVRYLLII--LGSLIVVIGIKSITSIIKVNFQKEIDRKSTTKVFEHMFNIPIEKIT 251
Cdd:cd18568 15 QLLGLALPLFTQIILDRVLVHKNISLLNLILIglLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 252 SRHAGDLNVRIMSLESIRGYILEDLIEMIISIVVIIPLLMYLLYTETFYTLILMFFIASSLFINISLGKFIyNANLVETY 331
Cdd:cd18568 95 SRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKL-KRNSREIF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 332 YLG-EHRGKINESLKAMYYVKATGIFSKIKSVWKKDYNKYLDTVHKRVLKQNALESFNSSLSTIFIIIMLAVGFYNFSKG 410
Cdd:cd18568 174 QANaEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISG 253
|
250 260
....*....|....*....|....*.
gi 1261268082 411 EGDLSNIFFFIAISSIIFSPVSTIIG 436
Cdd:cd18568 254 QLTIGQLVAFNMLFGSVINPLLALVG 279
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
175-438 |
1.54e-12 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 68.73 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 175 ISILAFPFILKKFMDILNASKevDVRYLLIILGSLIVVIGIKSITSIIK----VNFQKEIDRKSTTKVFEHMFNIPIEKI 250
Cdd:cd07346 13 ALGLALPLLTKLLIDDVIPAG--DLSLLLWIALLLLLLALLRALLSYLRrylaARLGQRVVFDLRRDLFRHLQRLSLSFF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 251 TSRHAGDLNVRIMS-LESIRGYILEDLIEMIISIVVIIPLLMYLLYTETFYTLILMFFIASSLFINISLGKFIYNANLVE 329
Cdd:cd07346 91 DRNRTGDLMSRLTSdVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 330 TYYLGEHRGKINESLKAMYYVKATGIFSKIKSVWKKDYNKYLDTVHKRVLKQNALESFNSSLSTIFIIIMLAVGFYNFSK 409
Cdd:cd07346 171 RESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQ 250
|
250 260
....*....|....*....|....*....
gi 1261268082 410 GEGDLSNIFFFIAISSIIFSPVSTIIGSI 438
Cdd:cd07346 251 GSLTIGELVAFLAYLGMLFGPIQRLANLY 279
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
474-672 |
1.59e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.94 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLA---NLLLKLHTPDK--GNILIDDRDI--KDWNSEEL 546
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfNRLLELNEEARveGEVRLFGRNIysPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 547 RKNVGLMTQDGVLF-RGSLSENLSyfdINYDPSKIQESIDKLN------LSNYIQFQSINDILiSEGGTNFSGGQRQRLA 619
Cdd:PRK14267 84 RREVGMVFQYPNPFpHLTIYDNVA---IGVKLNGLVKSKKELDervewaLKKAALWDEVKDRL-NDYPSNLSGGQRQRLV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 620 MLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS--TKIIITHDENILERV 672
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHSPAQAARV 214
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
479-652 |
2.03e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.51 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 479 NISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMTQDGV 558
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 559 LFRGSLSENlSYFDINYDPS--KIQESIDKLNLSNYIQFQSindiliseggTNFSGGQRQRLAMLRLFMKEYPILILDEP 636
Cdd:PRK13540 86 NPYLTLREN-CLYDIHFSPGavGITELCRLFSLEHLIDYPC----------GLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170
....*....|....*.
gi 1261268082 637 TNHLDRETANAVIENI 652
Cdd:PRK13540 155 LVALDELSLLTIITKI 170
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
479-693 |
2.80e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.72 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 479 NISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILiddrdikdWNSEEL----RKNVGLMT 554
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVL--------WQGKPLdyskRGLLALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLFRGSlSENLSYFDINYDpskIQESIDKLNLSNYIQFQSINDILISEGGTNF--------SGGQRQRLAMLRLFMK 626
Cdd:PRK13638 78 QVATVFQDP-EQQIFYTDIDSD---IAFSLRNLGVPEAEITRRVDEALTLVDAQHFrhqpiqclSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 627 EYPILILDEPTNHLD---RETANAVIENIFAMPSTKIIITHDenilerVDRVYELTDK--KLKQREIFSKSK 693
Cdd:PRK13638 154 QARYLLLDEPTAGLDpagRTQMIAIIRRIVAQGNHVIISSHD------IDLIYEISDAvyVLRQGQILTHGA 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
475-683 |
3.07e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.44 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF-DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE---LRKNV 550
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQD-GVLFRGSLSENLSYFDINYDPS------KIQESIDKLNLSNYIQFQSIndiliseggtNFSGGQRQRLAMLRL 623
Cdd:PRK10908 82 GMIFQDhHLLMDRTVYDNVAIPLIIAGASgddirrRVSAALDKVGLLDKAKNFPI----------QLSGGEQQRVGIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261268082 624 FMKEYPILILDEPTNHLDRETANAVI---ENIFAMPSTKIIITHDENILERVD-RVYELTDKKL 683
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDDALSEGILrlfEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
475-683 |
4.10e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.10 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL---RKNVG 551
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 552 LMTQDGVLFrgslsENLSYFD-INYD-------PSKIQESIDKLNLSNyIQFQSINDILISEggtnFSGGQRQRLAMLRL 623
Cdd:PRK11831 88 MLFQSGALF-----TDMNVFDnVAYPlrehtqlPAPLLHSTVMMKLEA-VGLRGAAKLMPSE----LSGGMARRAALARA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 624 FMKEYPILILDEPTNHLDRETANAVIENI----FAMPSTKIIITHD-ENILERVDRVYELTDKKL 683
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLIselnSALGVTCVVVSHDvPEVLSIADHAYIVADKKI 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
478-683 |
4.12e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.01 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 478 NNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIkdwnsEELRKNVGLMTQD- 556
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEAREDTRLMFQDa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 557 ------------GVLFRGslsenlsyfdiNYDPsKIQESIDKLNLSNYIQfqsindilisEGGTNFSGGQRQRLAMLRLF 624
Cdd:PRK11247 91 rllpwkkvidnvGLGLKG-----------QWRD-AALQALAAVGLADRAN----------EWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 625 MKEYPILILDEPTNHLD---RETANAVIENIFAMPS-TKIIITHDenILERV---DRVYELTDKKL 683
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDaltRIEMQDLIESLWQQHGfTVLLVTHD--VSEAVamaDRVLLIEEGKI 212
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
483-679 |
5.64e-12 |
|
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: 65.32 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 483 SFDDKKIIENLS-LNIknnesiaIVGESGSGKSTLANLLLKLHTPDKGNILID-DRDIKDWNSEELRKNVGLMtqdgvlF 560
Cdd:cd03240 11 SFHERSEIEFFSpLTL-------IVGQNGAGKTTIIEALKYALTGELPPNSKGgAHDPKLIREGEVRAQVKLA------F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 561 RGSLSENLsyfdinydpsKIQESIDKLNLSNYIQFQSINDILISEGGTnFSGGQRQ------RLAMLRLFMKEYPILILD 634
Cdd:cd03240 78 ENANGKKY----------TITRSLAILENVIFCHQGESNWPLLDMRGR-CSGGEKVlasliiRLALAETFGSNCGILALD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1261268082 635 EPTNHLDRETANAVIENIFAMPSTK-----IIITHDENILERVDRVYELT 679
Cdd:cd03240 147 EPTTNLDEENIEESLAEIIEERKSQknfqlIVITHDEELVDAADHIYRVE 196
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
475-679 |
7.21e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.34 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHtpD-------KGNILIDDRDI--KDWNSEE 545
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLN--DlipgfrvEGKVTFHGKNLyaPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 546 LRKNVGLMTQDGVLFRGSLSENLSY-FDINYDPSKIQESIDKlNLSNYIQFQSINDILiSEGGTNFSGGQRQRLAMLRLF 624
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIAYgARINGYKGDMDELVER-SLRQAALWDEVKDKL-KQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1261268082 625 MKEYPILILDEPTNHLDRETANAVIENIFAMPS--TKIIITHDeniLERVDRVYELT 679
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN---MQQAARVSDMT 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
479-693 |
7.25e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.66 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 479 NISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHtpDK-------GNILIDDRDIKDWNSE-ELRKNV 550
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMN--DKvsgyrysGDVLLGGRSIFNYRDVlEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLMTQDGVLFRGSLSENL--SYFDINYDPSKIQESIDKLNLSNYIQFQSINDILiSEGGTNFSGGQRQRLAMLRLFMKEY 628
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNVlaGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRL-SDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 629 PILILDEPTNHLDRETANAVIENIFAMPS--TKIIITHDENILERV-DRVYELTDKKLKQ----REIFSKSK 693
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARIsDRAALFFDGRLVEegptEQLFSSPK 254
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
475-692 |
1.02e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 66.20 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSL-----NIKNNESIAIVGESGSGKSTLA---NLLLKlhtPDKGNILIDDRDI----KDWN 542
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRALydvnvSIPSGSYVAIIGHTGSGKSTLLqhlNGLLQ---PTSGTVTIGERVItagkKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 543 SEELRKNVGLMTQ--DGVLFRGSLSENLSYFDINYDPS------KIQESIDKLNLSNYIQFQSINDIliseggtnfSGGQ 614
Cdd:PRK13634 80 LKPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSeedakqKAREMIELVGLPEELLARSPFEL---------SGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 615 RQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS----TKIIITHD-ENILERVDRVYELTDKKLKQ---- 685
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekglTTVLVTHSmEDAARYADQIVVMHKGTVFLqgtp 230
|
....*..
gi 1261268082 686 REIFSKS 692
Cdd:PRK13634 231 REIFADP 237
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
479-670 |
1.02e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.98 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 479 NISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLH--TPDKGNI------------LID----DRDIKD 540
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVdvpdnqfgreasLIDaigrKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 541 wnSEELRKNVGLmtQDGVLFRGSLSEnLSYfdinydpskiqesidklnlsnyiqfqsindiliseggtnfsgGQRQRLAM 620
Cdd:COG2401 115 --AVELLNAVGL--SDAVLWLRRFKE-LST------------------------------------------GQKFRFRL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1261268082 621 LRLFMKEYPILILDEPTNHLDRETANAVIENIFAM----PSTKIIITHDENILE 670
Cdd:COG2401 148 ALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarraGITLVVATHHYDVID 201
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
487-681 |
1.06e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.15 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 487 KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPD---KGNILIDDRDIkdwNSEELRKNVGLMTQDGvLFRGS 563
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI---DAKEMRAISAYVQQDD-LFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 564 LS--ENLSY---FDINYDPSK------IQESIDKLNLsnyiqfQSINDILISEGGT--NFSGGQRQRLAMLRLFMKEYPI 630
Cdd:TIGR00955 114 LTvrEHLMFqahLRMPRRVTKkekrerVDEVLQALGL------RKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 631 LILDEPTNHLDRETANAVIENI--FAMPSTKIIIThdenILERVDRVYELTDK 681
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLkgLAQKGKTIICT----IHQPSSELFELFDK 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
476-637 |
1.14e-11 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 65.24 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 476 EFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL-RKNVGLMT 554
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QDGVLF-RGSLSENL-SYFDINYDPSK-IQESIdklnlsnYIQFQSINDILISEGGtNFSGGQRQRLAMLRLFMKEYPIL 631
Cdd:TIGR03410 82 QGREIFpRLTVEENLlTGLAALPRRSRkIPDEI-------YELFPVLKEMLGRRGG-DLSGGQQQQLAIARALVTRPKLL 153
|
....*.
gi 1261268082 632 ILDEPT 637
Cdd:TIGR03410 154 LLDEPT 159
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
475-675 |
1.25e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.36 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE-LRKNVGLM 553
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLFRgSLS--ENL-------SYFDINYDP--SKIQESIDKLNLsnyiqfqSIN-DILISEggtnFSGGQRQRLAML 621
Cdd:COG3845 86 HQHFMLVP-NLTvaENIvlgleptKGGRLDRKAarARIRELSERYGL-------DVDpDAKVED----LSVGEQQRVEIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1261268082 622 RLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS---TKIIITH--DEnILERVDRV 675
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAegkSIIFITHklRE-VMAIADRV 211
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
464-672 |
1.54e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.05 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 464 SDTKVNILrgsiEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLL--KLHTPDKGNILIDDRDIKDW 541
Cdd:CHL00131 1 MNKNKPIL----EIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 542 NSEElRKNVGL-------MTQDGV----LFRGSLSENLSYFDIN-YDPSKIQESI-DKLNLSNYIQ-FQSINdilISEGg 607
Cdd:CHL00131 77 EPEE-RAHLGIflafqypIEIPGVsnadFLRLAYNSKRKFQGLPeLDPLEFLEIInEKLKLVGMDPsFLSRN---VNEG- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 608 tnFSGGQRQRLAMLRLFMKEYPILILDEPTNHLD----RETANAVieNIFAMPSTKII-ITHDENILERV 672
Cdd:CHL00131 152 --FSGGEKKRNEILQMALLDSELAILDETDSGLDidalKIIAEGI--NKLMTSENSIIlITHYQRLLDYI 217
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
480-683 |
3.30e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 66.35 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 480 ISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNIliddrdikdwnseELRKNVGLmtqdgvl 559
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLAKGIKL------- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 560 frGSLSEN-LSYFDINYDP----SKIQESIDKLNLSNYIQFQSINDILISEGGTNFSGGQRQRLaMLRLFMKEYP-ILIL 633
Cdd:PRK10636 378 --GYFAQHqLEFLRADESPlqhlARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARL-VLALIVWQRPnLLLL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1261268082 634 DEPTNHLDRETANAVIENIFAMPSTKIIITHDENILER-VDRVYELTDKKL 683
Cdd:PRK10636 455 DEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRStTDDLYLVHDGKV 505
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
475-652 |
3.39e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 64.26 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDK---------GNILIDD----RDIKdw 541
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREgrlaRDIR-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 542 nseELRKNVGLMTQD-GVLFRGSLSEN---------------LSYFDinydPSKIQESIDKLNLSNYIQF--QSIndili 603
Cdd:PRK09984 83 ---KSRANTGYIFQQfNLVNRLSVLENvligalgstpfwrtcFSWFT----REQKQRALQALTRVGMVHFahQRV----- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1261268082 604 seggTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENI 652
Cdd:PRK09984 151 ----STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTL 195
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
475-683 |
3.66e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.42 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKII-ENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNIliddrdikdWNSEELRknVGLM 553
Cdd:PLN03073 509 ISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV---------FRSAKVR--MAVF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQ---DGVlfrgSLSEN-LSYFDINYD---PSKIQESIDKLNLSNYIQFQSIndiliseggTNFSGGQRQRLAMLRLFMK 626
Cdd:PLN03073 578 SQhhvDGL----DLSSNpLLYMMRCFPgvpEQKLRAHLGSFGVTGNLALQPM---------YTLSGGQKSRVAFAKITFK 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261268082 627 EYPILILDEPTNHLDRETANAVIENIFAMPSTKIIITHDENILE-RVDRVYELTDKKL 683
Cdd:PLN03073 645 KPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
475-675 |
3.69e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.34 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENL---SLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVG 551
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 552 LMTQD-GVLFRGSLSENLSYFDINYDPSKIQESIDKLNLS----NYIQFQsindiliSEGGTNFSGGQRQRLAMLRLFMK 626
Cdd:PRK13642 85 MVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEAllavNMLDFK-------TREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 627 EYPILILDEPTNHLDRETANAVIENIFAMPS----TKIIITHDENILERVDRV 675
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyqlTVLSITHDLDEAASSDRI 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
475-665 |
4.05e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 64.11 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFD----DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDI------------ 538
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadrgvvfq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 539 KD----WNSeeLRKNVGLmtqdGVLFRG-SLSENLSyfdinydpsKIQESIDKLNLSNYIQFQsindilISEggtnFSGG 613
Cdd:COG4525 84 KDallpWLN--VLDNVAF----GLRLRGvPKAERRA---------RAEELLALVGLADFARRR------IWQ----LSGG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 614 QRQRLAMLRLFMKEYPILILDEPTNHLD---RETANAVIENIFAMPSTKI-IITHD 665
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFGALDaltREQMQELLLDVWQRTGKGVfLITHS 194
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
475-700 |
4.88e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.66 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLL--KLHTPDKGNILIDDRDIKDWNSEElRKNVGL 552
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 M-----------TQDGVLFRGSLSENLSYFDinydpskiQESIDKLNLSNYIQ-----FQSINDILISEGGTNFSGGQRQ 616
Cdd:PRK09580 81 FmafqypveipgVSNQFFLQTALNAVRSYRG--------QEPLDRFDFQDLMEekialLKMPEDLLTRSVNVGFSGGEKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 617 RLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTK---IIITHDENILERV--DRVYELTDKKLKQREIFSK 691
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKrsfIIVTHYQRILDYIkpDYVHVLYQGRIVKSGDFTL 232
|
250
....*....|
gi 1261268082 692 SK-LQTLGKG 700
Cdd:PRK09580 233 VKqLEEQGYG 242
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
486-674 |
8.00e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.14 E-value: 8.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 486 DKKIIENLSLNIKNNESIAIVGESGSGKSTLanllLKlhtpdkgnIL--IDdrdiKDWNSEELRK---NVGLMTQDGVLf 560
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTL----LR--------IMagVD----KEFEGEARPApgiKVGYLPQEPQL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 561 rgslsenlsyfdinyDPSK---------IQESIDKLNlsnyiQFQSIN----------DILISEGG-------------- 607
Cdd:PRK11819 82 ---------------DPEKtvrenveegVAEVKAALD-----RFNEIYaayaepdadfDALAAEQGelqeiidaadawdl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 608 --------------------TNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETAnAVIENIFA-MPSTKIIITHD- 665
Cdd:PRK11819 142 dsqleiamdalrcppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV-AWLEQFLHdYPGTVVAVTHDr 220
|
250
....*....|....*.
gi 1261268082 666 -------ENILErVDR 674
Cdd:PRK11819 221 yfldnvaGWILE-LDR 235
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
496-665 |
9.52e-11 |
|
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: 62.81 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 496 NIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKdWNSEELRKNvglmtqdgvlFRGSLSENLSyfdiNY 575
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKAD----------YEGTVRDLLS----SI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 576 DPSKIQESIDKLNLSNYIQFQSINDILIseggTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENI--F 653
Cdd:cd03237 86 TKDFYTHPYFKTEIAKPLQIEQILDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIrrF 161
|
170
....*....|....
gi 1261268082 654 AM--PSTKIIITHD 665
Cdd:cd03237 162 AEnnEKTAFVVEHD 175
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
475-693 |
9.56e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 64.05 E-value: 9.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFD-DKKIIE---NLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL---R 547
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 548 KNVGLMTQ-----------DGVLFRGSLsENLSYFDINydpSKIQESIDKLNLSN----YiqfqsindilisegGTNFSG 612
Cdd:PRK11153 82 RQIGMIFQhfnllssrtvfDNVALPLEL-AGTPKAEIK---ARVTELLELVGLSDkadrY--------------PAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 613 GQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIE---------NIfampsTKIIITHDENILERV-DRVYELTDKK 682
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILEllkdinrelGL-----TIVLITHEMDVVKRIcDRVAVIDAGR 218
|
250
....*....|....*
gi 1261268082 683 LKQR----EIFSKSK 693
Cdd:PRK11153 219 LVEQgtvsEVFSHPK 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
443-700 |
1.03e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.90 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 443 SVKPLLLRTLDILE----EELEKDGSDTKvNILRGSIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLAN 518
Cdd:PLN03211 34 SCYPITLKFMDVCYrvkfENMKNKGSNIK-RILGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 519 LLL-KLHTPD-KGNILIDDRDIkdwnSEELRKNVGLMTQDGVLF-RGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQF 595
Cdd:PLN03211 113 ALAgRIQGNNfTGTILANNRKP----TKQILKRTGFVTQDDILYpHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 596 QSINDILISEGGTNF----SGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPST-KIIIThdeNILE 670
Cdd:PLN03211 189 LGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKgKTIVT---SMHQ 265
|
250 260 270
....*....|....*....|....*....|
gi 1261268082 671 RVDRVYELTDKKLkqreIFSKSKLQTLGKG 700
Cdd:PLN03211 266 PSSRVYQMFDSVL----VLSEGRCLFFGKG 291
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
475-675 |
1.40e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.19 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDK-------------KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDW 541
Cdd:PRK15079 9 LEVADLKVHFDIKdgkqwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 542 NSEEL---RKNVGLMTQDGVlfrGSLSENLSYFDINYDPSKI-------QESIDKLN--------LSNyiqfqsindiLI 603
Cdd:PRK15079 89 KDDEWravRSDIQMIFQDPL---ASLNPRMTIGEIIAEPLRTyhpklsrQEVKDRVKammlkvglLPN----------LI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1261268082 604 SEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIeNIFA-----MPSTKIIITHDENILERV-DRV 675
Cdd:PRK15079 156 NRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVV-NLLQqlqreMGLSLIFIAHDLAVVKHIsDRV 232
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
174-402 |
1.47e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 62.86 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 174 QISILAFPFILKKFMDILNASKEVDVRYLLIILGSLIVVI--GIKSITSIIKVNFQKEIDRKSTTKVFEHMFNIPIEKIT 251
Cdd:cd18567 15 ELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLqaLLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 252 SRHAGDLNVRIMSLESIRGYILEDLIEMII-SIVVIIPLLMYLLYTETFyTLILMFFIASSLFINISLGKFIYNANLVET 330
Cdd:cd18567 95 KRHLGDIVSRFGSLDEIQQTLTTGFVEALLdGLMAILTLVMMFLYSPKL-ALIVLAAVALYALLRLALYPPLRRATEEQI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 331 YYLGEHRGKINESLKAMYYVKATGIFSKIKSVWkkdYNKYLDTVHKRVLKQNALESFNSSLSTIFIIIMLAV 402
Cdd:cd18567 174 VASAKEQSHFLETIRGIQTIKLFGREAEREARW---LNLLVDAINADIRLQRLQILFSAANGLLFGLENILV 242
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
484-665 |
1.57e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.29 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 484 FDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNVGLMTQDGVLfRGS 563
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQLRLL-RTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 564 LSENLSYFDI----NYDPSKIQESIDKLNLSN---------YIQFQSINDILISEGGTNFSGGQRQRLAMLRLFMKEYPI 630
Cdd:PRK10619 94 LTMVFQHFNLwshmTVLENVMEAPIQVLGLSKqeareravkYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1261268082 631 LILDEPTNHLDRETANAVI---ENIFAMPSTKIIITHD 665
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLrimQQLAEEGKTMVVVTHE 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
478-665 |
1.72e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.25 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 478 NNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWN----SEE-----LRK 548
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalSEAerrrlLRT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 549 NVGLMTQD-------GVLFRGSLSENL------SYFDINYDPSKIQESIDklnlsnyIQFQSINDIlisegGTNFSGGQR 615
Cdd:PRK11701 90 EWGFVHQHprdglrmQVSAGGNIGERLmavgarHYGDIRATAGDWLERVE-------IDAARIDDL-----PTTFSGGMQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 616 QRLAMLRLFMKEYPILILDEPTNHLD---------------RETANAVienifampstkIIITHD 665
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDvsvqarlldllrglvRELGLAV-----------VIVTHD 211
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
178-450 |
1.99e-10 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 62.22 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 178 LAFPFILKKFMD-ILNASKEVDVRYLLIILGSLIVVIGI-KSITSIIKVNFQKEIDRKSTTKVFEHMFNIPIEKITSRHA 255
Cdd:cd18782 19 LANPLLFQVIIDkVLVQQDLATLYVIGVVMLVAALLEAVlTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 256 GDLNVRIMSLESIRGYILE-------DLIEMIISIVVII---PLLmyllyteTFYTLILM-FFIASSLFInislGKFIYN 324
Cdd:cd18782 99 GELSTRISELDTIRGFLTGtalttllDVLFSVIYIAVLFsysPLL-------TLVVLATVpLQLLLTFLF----GPILRR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 325 ANLVETYYLGEHRGKINESLKAMYYVKATGIFSKIKSVWKKDYNKYLDTVHKRVLKQNALESFNSSLSTIFIIIMLAVGF 404
Cdd:cd18782 168 QIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1261268082 405 YNFSKGEGDLSNIFFFIAISSIIFSPVSTIIGSILNWNSVKPLLLR 450
Cdd:cd18782 248 YLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLER 293
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
475-680 |
3.07e-10 |
|
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: 60.81 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSF-DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKG-----NILIDDRDIKDWNSEElRK 548
Cdd:cd03290 1 VQVTNGYFSWgSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsNKNESEPSFEATRSRN-RY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 549 NVGLMTQDGVLFRGSLSENLSyFDINYDPSKIQESIDKLNLSNYIQFQSIND-ILISEGGTNFSGGQRQRLAMLRLFMKE 627
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENIT-FGSPFNKQRYKAVTDACSLQPDIDLLPFGDqTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261268082 628 YPILILDEPTNHLDRETANAVI-ENIFAM----PSTKIIITHDENILERVDRVYELTD 680
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMqEGILKFlqddKRTLVLVTHKLQYLPHADWIIAMKD 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
475-676 |
3.48e-10 |
|
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: 63.16 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDD----KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHtPD-----KGNILIDDRDIKDWNSEE 545
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLL-PDpaahpSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 546 LRKnvglmtqdgvlFRGSlsenlsyfDInydpSKI-QESIDKLNLSNYIQFQsINDILISEGGTN--------------- 609
Cdd:COG4172 86 LRR-----------IRGN--------RI----AMIfQEPMTSLNPLHTIGKQ-IAEVLRLHRGLSgaaararalellerv 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 610 ---------------FSGGQRQR--LAM---LRlfmkeyP-ILILDEPTNHLD---------------RETANAVienif 653
Cdd:COG4172 142 gipdperrldayphqLSGGQRQRvmIAMalaNE------PdLLIADEPTTALDvtvqaqildllkdlqRELGMAL----- 210
|
250 260
....*....|....*....|....
gi 1261268082 654 ampstkIIITHDENILERV-DRVY 676
Cdd:COG4172 211 ------LLITHDLGVVRRFaDRVA 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
490-685 |
5.05e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.97 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 490 IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELR-----------KNVGLMTQDGV 558
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 559 LFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQFQSindiliseggTNFSGGQRQRLAMLRLFMKEYPILILDEPTN 638
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYP----------DELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 639 HLD----RETANAVIENIFAMPSTKIIITHDENILERV-DRVYELTDKKLKQ 685
Cdd:PRK10070 194 ALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQ 245
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
475-680 |
6.30e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.96 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE-LRKNVGLM 553
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLFrGSLS--ENLsyFdINYDPSK------------IQESIDKLNLsnyiqfqSIN-DILISEggtnFSGGQRQRL 618
Cdd:COG1129 85 HQELNLV-PNLSvaENI--F-LGREPRRgglidwramrrrARELLARLGL-------DIDpDTPVGD----LSVAQQQLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 619 AMLRLFMKEYPILILDEPTNHL-DRETAN--AVIENIFAMPSTKIIITHdenileRVDRVYELTD 680
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLtEREVERlfRIIRRLKAQGVAIIYISH------RLDEVFEIAD 208
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
178-438 |
8.97e-10 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 60.14 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 178 LAFPFILKKFMDILNASkEVDVRYLLIILGSLIVVIGIKSITSIIkvnFQK---EIDRKSTTKVFEHMFNIPIEKITSRH 254
Cdd:cd18551 16 LAQPLLVKNLIDALSAG-GSSGGLLALLVALFLLQAVLSALSSYL---LGRtgeRVVLDLRRRLWRRLLRLPVSFFDRRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 255 AGDLNVRIMS-LESIRGYILEDLIEMIISIVVIIPLLMYLLYTETFYTLILMFFIASSLFINISLGKFIYNANLVETYYL 333
Cdd:cd18551 92 SGDLVSRVTNdTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 334 GEHRGKINESLKAMYYVKATGIFSKIksvwKKDYNKYLDTVHKRVLKQNALESFNSSLSTIF----IIIMLAVGFYNFSK 409
Cdd:cd18551 172 GELSAALERALSAIRTVKASNAEERE----TKRGGEAAERLYRAGLKAAKIEALIGPLMGLAvqlaLLVVLGVGGARVAS 247
|
250 260
....*....|....*....|....*....
gi 1261268082 410 GEGDLSNIFFFIAISSIIFSPVSTIIGSI 438
Cdd:cd18551 248 GALTVGTLVAFLLYLFQLITPLSQLSSFF 276
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
475-643 |
9.62e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 61.38 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKL--HTPDKGNILIDDRDIKDWN-SEELRKNVG 551
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNiRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 552 LMTQDGVLFRG-SLSENLsyF---DINYDPSKIQESIDKLNLSNYIQFQSINDILISEGGTNFSGGQRQRLAMLRLFMKE 627
Cdd:TIGR02633 82 IIHQELTLVPElSVAENI--FlgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170
....*....|....*.
gi 1261268082 628 YPILILDEPTNHLDRE 643
Cdd:TIGR02633 160 ARLLILDEPSSSLTEK 175
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
486-675 |
1.13e-09 |
|
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: 59.08 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 486 DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNIliddrdikdwnseELRKNVGLMTQDGVLFRGSLS 565
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-------------TVRGRVSSLLGLGGGFNPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 566 --ENLsYF-------DINYDPSKIQESIDKLNLSNYIqfqsinDILISeggtNFSGGQRQRLAmlrlF----MKEYPILI 632
Cdd:cd03220 101 grENI-YLngrllglSRKEIDEKIDEIIEFSELGDFI------DLPVK----TYSSGMKARLA----FaiatALEPDILL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1261268082 633 LDEPTNHLD---RETANAVIENIFAMPSTKIIITHDENILERV-DRV 675
Cdd:cd03220 166 IDEVLAVGDaafQEKCQRRLRELLKQGKTVILVSHDPSSIKRLcDRA 212
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
493-683 |
1.50e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.18 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 493 LSLNIKNNESIAIVGESGSGKSTLANLLLKLhTPDKGNILIDDRDIKDWNSEELRKnvglmtqdgvlFRGSLSENLS--- 569
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELAR-----------HRAYLSQQQTppf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 570 ------YFDInYDPSKIQESIDKLNLSNYIQFQSINDILISEGGTnFSGG--QRQRLAMlrLFMKEYP-------ILILD 634
Cdd:PRK03695 83 ampvfqYLTL-HQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQ-LSGGewQRVRLAA--VVLQVWPdinpagqLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 635 EPTNHLDRETANAVIENIFAMPSTKIII---THDEN-ILERVDRVYELTDKKL 683
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCQQGIAVvmsSHDLNhTLRHADRVWLLKQGKL 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
475-665 |
1.74e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.94 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE--LRKNVGL 552
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERgvVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 553 MTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQ---FQsindiliseggtnFSGGQRQRLAMLRLFMKEYP 629
Cdd:PRK11248 82 LPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKryiWQ-------------LSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1261268082 630 ILILDEPTNHLD---RETANAVIENIFAMPSTKI-IITHD 665
Cdd:PRK11248 149 LLLLDEPFGALDaftREQMQTLLLKLWQETGKQVlLITHD 188
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
480-648 |
3.51e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 480 ISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKdwNSEELRKNVGLMTQDGVL 559
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT--RGDRSRFMAYLGHLPGLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 560 FRGSLSENLSYFDI--NYDPSKIQES-IDKLNLSNYiqfqsiNDILISEggtnFSGGQRQRLAMLRLFMKEYPILILDEP 636
Cdd:PRK13543 95 ADLSTLENLHFLCGlhGRRAKQMPGSaLAIVGLAGY------EDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170
....*....|..
gi 1261268082 637 TNHLDRETANAV 648
Cdd:PRK13543 165 YANLDLEGITLV 176
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
487-641 |
3.82e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.12 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 487 KKIIENLSLNIK---NNESI-AIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSE-----ELRKnVGLMTQDG 557
Cdd:PRK11144 7 KQQLGDLCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiclppEKRR-IGYVFQDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 558 VLF-----RGslseNLSYFDINYDPSKiqesIDKLnlsnyIQFQSINDILISEGGTnFSGGQRQRLAMLRLFMKEYPILI 632
Cdd:PRK11144 86 RLFphykvRG----NLRYGMAKSMVAQ----FDKI-----VALLGIEPLLDRYPGS-LSGGEKQRVAIGRALLTAPELLL 151
|
....*....
gi 1261268082 633 LDEPTNHLD 641
Cdd:PRK11144 152 MDEPLASLD 160
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
475-680 |
4.29e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKN-VGLM 553
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQD-GVLFRGSLSENLSyfdINYDPSKiqeSIDKLNLSNYIQFQSINDILISEGG---------TNFSGGQRQRLAMLRL 623
Cdd:PRK09700 86 YQElSVIDELTVLENLY---IGRHLTK---KVCGVNIIDWREMRVRAAMMLLRVGlkvdldekvANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 624 FMKEYPILILDEPTNHLdretANAVIENIFAM------PSTKII-ITHDENILERV-DRVYELTD 680
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSL----TNKEVDYLFLImnqlrkEGTAIVyISHKLAEIRRIcDRYTVMKD 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
482-684 |
4.96e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.79 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 482 FSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDdrdikdwnseelrKNVGLMTQDGVLFR 561
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 562 GSLSENLSYFDiNYDPSKIQESIDKLNL-SNYIQFQSINDILISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHL 640
Cdd:PTZ00243 735 ATVRGNILFFD-EEDAARLADAVRVSQLeADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1261268082 641 DRETANAVIENIFA---MPSTKIIITHDENILERVDRVYELTDKKLK 684
Cdd:PTZ00243 814 DAHVGERVVEECFLgalAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
174-403 |
5.58e-09 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 57.89 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 174 QISILAFPFILKKFMDILNASKEVDVryLLIILGSLIVVIGIKSITSIIK----VNFQKEIDRKSTTKVFEHMFNIPIEK 249
Cdd:cd18588 15 QLFALVTPLFFQVIIDKVLVHRSLST--LDVLAIGLLVVALFEAVLSGLRtylfSHTTNRIDAELGARLFRHLLRLPLSY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 250 ITSRHAGDLNVRIMSLESIRGYILEDLIEMIISIVVIIPLLMYLLYTETFYTLILMFFIASSLFINISLGKfIYNANLVE 329
Cdd:cd18588 93 FESRQVGDTVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTP-ILRRRLEE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 330 TYYLG-EHRGKINESLKAMYYVKATGIFSKIKSVWKKDYNKYLDTVHKRVLKQNALESFNSSLSTIFIIIMLAVG 403
Cdd:cd18588 172 KFQRGaENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFG 246
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
479-675 |
6.44e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.10 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 479 NISFSFDDKKI--IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNseelRKNVGLMTQD 556
Cdd:PRK10261 19 NIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRS----RQVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 557 GVLFRGSLSENLSYfdINYDP-----------SKIQESI----------------DKLNLSNYIQFQSIndilISEGGTN 609
Cdd:PRK10261 95 AAQMRHVRGADMAM--IFQEPmtslnpvftvgEQIAESIrlhqgasreeamveakRMLDQVRIPEAQTI----LSRYPHQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 610 FSGGQRQRLaMLRLFMKEYP-ILILDEPTNHLDrETANAVIENIFA-----MPSTKIIITHDENILERV-DRV 675
Cdd:PRK10261 169 LSGGMRQRV-MIAMALSCRPaVLIADEPTTALD-VTIQAQILQLIKvlqkeMSMGVIFITHDMGVVAEIaDRV 239
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
178-431 |
8.10e-09 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 57.43 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 178 LAFPFILKKFMDILNASKevDVRYLLIILGSLIVVIGIKSITSIIKVNFQKEIDRKSTT----KVFEHMFNIPIEKITSR 253
Cdd:cd18552 16 AALAWLLKPLLDDIFVEK--DLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRdlrnDLFDKLLRLPLSFFDRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 254 HAGDLNVRIMS-LESIRGYILEDLIEMIISIVVIIPLLMYLLYTETFYTLILMFFIASSLFINISLGKFI--YNANLVET 330
Cdd:cd18552 94 SSGDLISRITNdVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLrkISRRSQES 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 331 yyLGEHRGKINESLKAMYYVKAtgiFSKIKSVwKKDYNKYLDTVHKRVLKQNALESFNSSLSTIFIIIMLAV----GFYN 406
Cdd:cd18552 174 --MGDLTSVLQETLSGIRVVKA---FGAEDYE-IKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALvlwyGGYQ 247
|
250 260
....*....|....*....|....*
gi 1261268082 407 FSKGEGDLSNIFFFIAISSIIFSPV 431
Cdd:cd18552 248 VISGELTPGEFISFITALLLLYQPI 272
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
490-664 |
1.17e-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: 58.87 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 490 IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDwNSEELRKNVGLMTQDGVLFRG-SLSENL 568
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 569 SYFdINYDPSKIQESidKLNLSNYIQFQSINDILiSEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAV 648
Cdd:TIGR01257 1025 LFY-AQLKGRSWEEA--QLEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170
....*....|....*...
gi 1261268082 649 IENIFAMPSTKIII--TH 664
Cdd:TIGR01257 1101 WDLLLKYRSGRTIImsTH 1118
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
490-672 |
1.56e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 490 IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDI---KDWNSEELRKNVGLMTQDGVlfrGSLSE 566
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPY---ASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 567 NLSYFDINYDPSKIQESIDKLNLSNYIQFQSINDILISEGG----TNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDR 642
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190
....*....|....*....|....*....|....
gi 1261268082 643 ETANAVIENIF----AMPSTKIIITHDENILERV 672
Cdd:PRK10261 497 SIRGQIINLLLdlqrDFGIAYLFISHDMAVVERI 530
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
178-445 |
1.99e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 56.44 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 178 LAFPFILKKFMDILNASKEVDVRYLLIILgsLIVVIGIKSITSIIKVNFQKEI----DRKSTTKVFEHMFNIPIEKITSR 253
Cdd:cd18566 19 LATPLFILQVYDRVIPNESIPTLQVLVIG--VVIAILLESLLRLLRSYILAWIgarfDHRLSNAAFEHLLSLPLSFFERE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 254 HAGDLNVRIMSLESIR----GYILEDLIEMIISIVVIIpLLMYLLYTETFYTLILM-FFIASSLFINIslgkfIYNANLV 328
Cdd:cd18566 97 PSGAHLERLNSLEQIRefltGQALLALLDLPFVLIFLG-LIWYLGGKLVLVPLVLLgLFVLVAILLGP-----ILRRALK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 329 ETYYLGEHRGK-INESLKAMYYVKATGIFSKIKSVWKKDYNKYLDTVHKRVLKQNALESFNSSLSTIFIIIMLAVGFYNF 407
Cdd:cd18566 171 ERSRADERRQNfLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLV 250
|
250 260 270
....*....|....*....|....*....|....*...
gi 1261268082 408 SKGEGDLSNIFFFIAISSIIFSPVSTIIGSILNWNSVK 445
Cdd:cd18566 251 INGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVR 288
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
494-680 |
2.08e-08 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 56.65 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 494 SLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRdikDWNSEELRKNV-------GLMTQDGVLF-----R 561
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE---VLQDSARGIFLpphrrriGYVFQEARLFphlsvR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 562 GslseNLSYfdiNYDPSKIQESidklnlsnYIQFQSINDIL-ISE----GGTNFSGGQRQRLAMLRLFMKEYPILILDEP 636
Cdd:COG4148 96 G----NLLY---GRKRAPRAER--------RISFDEVVELLgIGHlldrRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1261268082 637 TNHLDRETANAV---IENI---FAMPstkII-ITHDenilerVDRVYELTD 680
Cdd:COG4148 161 LAALDLARKAEIlpyLERLrdeLDIP---ILyVSHS------LDEVARLAD 202
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
475-641 |
2.11e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.89 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILiddrdikdwNSEELRknvglmt 554
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 qdgvlfrgslsenlsyfdINYDPSKIQ-ESIDKLNLSNYIQFQ---SINDI-----------LISEGGTNFSGGQRQRLA 619
Cdd:PRK09544 69 ------------------IGYVPQKLYlDTTLPLTVNRFLRLRpgtKKEDIlpalkrvqaghLIDAPMQKLSGGETQRVL 130
|
170 180
....*....|....*....|..
gi 1261268082 620 MLRLFMKEYPILILDEPTNHLD 641
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGVD 152
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
484-648 |
3.28e-08 |
|
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: 55.03 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 484 FDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDwNSEELRKNVGL-MTQDGVLF-- 560
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVvFGQKTQLWwd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 561 ---RGSLSENLSYFDInyDPSKIQESIDKLnlSNYIQFQSINDILISeggtNFSGGQRQRLAMLRLFMKEYPILILDEPT 637
Cdd:cd03267 110 lpvIDSFYLLAAIYDL--PPARFKKRLDEL--SELLDLEELLDTPVR----QLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170
....*....|.
gi 1261268082 638 NHLDRETANAV 648
Cdd:cd03267 182 IGLDVVAQENI 192
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
474-641 |
5.46e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 55.23 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSFDDK-KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIkdwNSEELR-KNVG 551
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV---NELEPAdRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 552 LMTQDGVLF-RGSLSENLSY---------FDINydpSKIQESIDKLNLSNYIQFQSindiliseggTNFSGGQRQRLAML 621
Cdd:PRK11650 80 MVFQNYALYpHMSVRENMAYglkirgmpkAEIE---ERVAEAARILELEPLLDRKP----------RELSGGQRQRVAMG 146
|
170 180
....*....|....*....|
gi 1261268082 622 RLFMKEYPILILDEPTNHLD 641
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLD 166
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
475-681 |
5.96e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKL--HTPDKGNILIDDRDIKDWN-SEELRKNVG 551
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNiRDTERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 552 LMTQDGVLFRG-SLSENL-------SYFDINYDP--SKIQESIDKLNLsnyiqfqsinDILISEGGTNFSGGQRQRLAML 621
Cdd:PRK13549 86 IIHQELALVKElSVLENIflgneitPGGIMDYDAmyLRAQKLLAQLKL----------DINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 622 RLFMKEYPILILDEPTNHL-DRETAN--AVIENIFAMPSTKIIITHdenileRVDRVYELTDK 681
Cdd:PRK13549 156 KALNKQARLLILDEPTASLtESETAVllDIIRDLKAHGIACIYISH------KLNEVKAISDT 212
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
483-678 |
6.59e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 53.39 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 483 SFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRdikdwnseelrKNVGLMTQdgvlfRG 562
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQ-----RS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 563 SLSENLsyfdinydPSKIQESI-----------------DKLnlsnyiqfqSINDILISEGGTNF--------SGGQRQR 617
Cdd:NF040873 65 EVPDSL--------PLTVRDLVamgrwarrglwrrltrdDRA---------AVDDALERVGLADLagrqlgelSGGQRQR 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261268082 618 LAMLRLFMKEYPILILDEPTNHLDRETANAVIENI---FAMPSTKIIITHDENILERVDRVYEL 678
Cdd:NF040873 128 ALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLaeeHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
490-641 |
8.53e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.03 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 490 IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIK----DWNSEELRknvgLMTQDgvlfrGSLS 565
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySYRSQRIR----MIFQD-----PSTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 566 ENlsyfdinydP-SKIQESID---KLN--LSNYIQFQSINDILISEGGTN---------FSGGQRQRLAMLRLFMKEYPI 630
Cdd:PRK15112 100 LN---------PrQRISQILDfplRLNtdLEPEQREKQIIETLRQVGLLPdhasyyphmLAPGQKQRLGLARALILRPKV 170
|
170
....*....|.
gi 1261268082 631 LILDEPTNHLD 641
Cdd:PRK15112 171 IIADEALASLD 181
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
478-675 |
1.25e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.71 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 478 NNISFSF----DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLK-LHTPD----KGNILIDDRDIKDWNSEELRK 548
Cdd:PRK15134 9 ENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRlLPSPPvvypSGDIRFHGESLLHASEQTLRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 549 ----NVGLMTQDGVL-------FRGSLSENLS-YFDINYDPSK--IQESIDKLNLSNyiQFQSINDIlisegGTNFSGGQ 614
Cdd:PRK15134 89 vrgnKIAMIFQEPMVslnplhtLEKQLYEVLSlHRGMRREAARgeILNCLDRVGIRQ--AAKRLTDY-----PHQLSGGE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261268082 615 RQR--LAMLRLFMKEypILILDEPTNHLDrETANAVIENIFA-----MPSTKIIITHDENILERV-DRV 675
Cdd:PRK15134 162 RQRvmIAMALLTRPE--LLIADEPTTALD-VSVQAQILQLLRelqqeLNMGLLFITHNLSIVRKLaDRV 227
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
475-641 |
1.46e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGN--ILIDDR--------DIKdwnse 544
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNdlTLFGRRrgsgetiwDIK----- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 545 elrKNVGLMTQDGVL-FRGSLSEN---LS-YFD-IN-YDP------SKIQESIDKLNLSNYIQ---FQSIndiliseggt 608
Cdd:PRK10938 336 ---KHIGYVSSSLHLdYRVSTSVRnviLSgFFDsIGiYQAvsdrqqKLAQQWLDILGIDKRTAdapFHSL---------- 402
|
170 180 190
....*....|....*....|....*....|....
gi 1261268082 609 nfSGGQrQRLAML-RLFMKEYPILILDEPTNHLD 641
Cdd:PRK10938 403 --SWGQ-QRLALIvRALVKHPTLLILDEPLQGLD 433
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
473-679 |
2.33e-07 |
|
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: 51.48 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 473 GSIEFNNISFSFD----DKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPD--KGNILIDDRDIKdwnsEEL 546
Cdd:cd03232 2 SVLTWKNLNYTVPvkggKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD----KNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 547 RKNVGLMTQdgvlfrgslsenlsyFDINYDPSKIQESidkLNLSNYIQFQSIndiliseggtnfsgGQRQRLAM-LRLFM 625
Cdd:cd03232 78 QRSTGYVEQ---------------QDVHSPNLTVREA---LRFSALLRGLSV--------------EQRKRLTIgVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 626 KeyP-ILILDEPTNHLDRETANAVIENI--FAMPSTKIIIT-H--DENILERVDRVYELT 679
Cdd:cd03232 126 K--PsILFLDEPTSGLDSQAAYNIVRFLkkLADSGQAILCTiHqpSASIFEKFDRLLLLK 183
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
178-441 |
2.49e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 52.93 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 178 LAFPFILKKFMDILNASKEVDVryLLIILGSLIVVIGIKSITSIIK----VNFQKEIDRKSTTKVFEHMFNIPIEKITSR 253
Cdd:cd18779 19 LALPLLTGVLVDRVIPRGDRDL--LGVLGLGLAALVLTQLLAGLLRshllLRLRTRLDTQLTLGFLEHLLRLPYRFFQQR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 254 HAGDLNVRIMSLESIRgyiledliEMIIS--IVVIIPLLMYLLYtetfytLILMFFiASSLFINISLG-KFIYNANLVET 330
Cdd:cd18779 97 STGDLLMRLSSNATIR--------ELLTSqtLSALLDGTLVLGY------LALLFA-QSPLLGLVVLGlAALQVALLLAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 331 YYL------------GEHRGKINESLKAMYYVKATGIFSKIKSVWKKDYNKYLDTVHKRVLKQNALESFNSSLSTIFIII 398
Cdd:cd18779 162 RRRvrelmarelaaqAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1261268082 399 MLAVGFYNFSKGEGDLSNIFFFIAISSIIFSPVSTIIGSILNW 441
Cdd:cd18779 242 LLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQL 284
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
489-683 |
3.38e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 489 IIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE---LRKNVGLMTQDGVLFRGSLS 565
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQEtpaLPQPALEYVIDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 566 ENLSYFDINYDPSKIQESIDKLNLSNYIQFQSINDILISEGG----------TNFSGGQRQRLAMLRLFMKEYPILILDE 635
Cdd:PRK10636 96 AQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGfsneqlerpvSDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 636 PTNHLDretANAVI---ENIFAMPSTKIIITHDENILER-VDRVYELTDKKL 683
Cdd:PRK10636 176 PTNHLD---LDAVIwleKWLKSYQGTLILISHDRDFLDPiVDKIIHIEQQSL 224
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
610-672 |
1.07e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 1.07e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 610 FSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTKIIITHDENILERV 672
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTV 407
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
474-536 |
1.17e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.47 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNISFSF----------------------DDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNI 531
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
....*
gi 1261268082 532 LIDDR 536
Cdd:COG1134 84 EVNGR 88
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
500-669 |
1.38e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.52 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 500 NESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDrdikdwnseelrknvglmtqdgvlfrgslsenlsyfdinydpsk 579
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 580 iqesidkLNLSNYIQFQSINDILISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTK 659
Cdd:smart00382 38 -------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLL 110
|
170
....*....|....*....
gi 1261268082 660 ---------IIITHDENIL 669
Cdd:smart00382 111 lkseknltvILTTNDEKDL 129
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
476-680 |
1.41e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.45 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 476 EFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE-LRKNVGLMT 554
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 555 QD----------------------GVLFRGSL----SENLSYFDINYDPSKiqesidKLNlsnyiqfqsindiliseggt 608
Cdd:PRK11288 86 QElhlvpemtvaenlylgqlphkgGIVNRRLLnyeaREQLEHLGVDIDPDT------PLK-------------------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 609 NFSGGQRQRLAMLRLFMKEYPILILDEPTNHLD-RETAN--AVIENIFAMPSTKIIITHdenileRVDRVYELTD 680
Cdd:PRK11288 140 YLSIGQRQMVEIAKALARNARVIAFDEPTSSLSaREIEQlfRVIRELRAEGRVILYVSH------RMEEIFALCD 208
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
497-665 |
1.47e-06 |
|
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: 51.32 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 497 IKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNIlidDRDIK-DWNSEELRKNVGLMTQDgvLFRGSLSENL--SYFdi 573
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLKiSYKPQYISPDYDGTVEE--FLRSANTDDFgsSYY-- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 574 nydpskIQESIDKLNLSNYIQfQSINDIliseggtnfSGGQRQRLAMLRLFMKEYPILILDEPTNHLD---RETANAVIE 650
Cdd:COG1245 436 ------KTEIIKPLGLEKLLD-KNVKDL---------SGGELQRVAIAACLSRDADLYLLDEPSAHLDveqRLAVAKAIR 499
|
170
....*....|....*...
gi 1261268082 651 NIfaMPSTK---IIITHD 665
Cdd:COG1245 500 RF--AENRGktaMVVDHD 515
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
478-665 |
1.80e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 478 NNISFSFDDKKI----IENLSLNIKNNESIAIVGESGSGK--STLANLLLkLHTPDK---GNILIDDRDIKDWNSEELRK 548
Cdd:PRK11022 7 DKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKsvSSLAIMGL-IDYPGRvmaEKLEFNGQDLQRISEKERRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 549 NVG----LMTQDGVlfrgsLSENLSY---FDI---------NYDPSKIQESIDKLNLSNYIQFQSINDILISEggtnFSG 612
Cdd:PRK11022 86 LVGaevaMIFQDPM-----TSLNPCYtvgFQImeaikvhqgGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQ----LSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261268082 613 GQRQRLaMLRLFMKEYP-ILILDEPTNHLDRETANAVIENIFAMPSTK----IIITHD 665
Cdd:PRK11022 157 GMSQRV-MIAMAIACRPkLLIADEPTTALDVTIQAQIIELLLELQQKEnmalVLITHD 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
475-665 |
2.87e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDkkiienLSLN-----IKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNIlidDRDIK-DWNSEELRK 548
Cdd:PRK13409 341 VEYPDLTKKLGD------FSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKiSYKPQYIKP 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 549 NvglmtqdgvlFRGSLSENLSYFDINYDPSKIQ-ESIDKLNLSNYIQfQSINDIliseggtnfSGGQRQRLAMLRLFMKE 627
Cdd:PRK13409 412 D----------YDGTVEDLLRSITDDLGSSYYKsEIIKPLQLERLLD-KNVKDL---------SGGELQRVAIAACLSRD 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1261268082 628 YPILILDEPTNHLD---RETANAVIENIfaMPSTK---IIITHD 665
Cdd:PRK13409 472 ADLYLLDEPSAHLDveqRLAVAKAIRRI--AEEREataLVVDHD 513
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
178-346 |
3.04e-06 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 49.40 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 178 LAFPFILKKFMD-ILNASKEVDVRYLLIILGSLIVV-IGIKSITSIIKVNFQKEIDRKSTTKVFEHMFNIPIEKITSRHA 255
Cdd:cd18569 19 LVIPVFSRIFIDdILVGGLPDWLRPLLLGMALTALLqGLLTWLQQYYLLRLETKLALSSSSRFFWHVLRLPVEFFSQRYA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 256 GDLNVRIMSLESIRGYILEDLIEMIISIVVIIpllmyllytetFYtLILMFF---------IASSLfINISLGKFIYNAN 326
Cdd:cd18569 99 GDIASRVQSNDRVANLLSGQLATTVLNLVMAV-----------FY-ALLMLQydvpltligIAIAL-LNLLVLRLVSRKR 165
|
170 180 190
....*....|....*....|....*....|
gi 1261268082 327 LVETYYLGEHRGKIN----------ESLKA 346
Cdd:cd18569 166 VDLNRRLLQDSGKLTgttmsglqmiETLKA 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
492-676 |
3.82e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.05 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 492 NLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEElRKNVGLM------TQDGVLFRGSLS 565
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 566 ENLSYFDINYDPSKIQESIDKLNLSNY-----IQFQSINDILiseggTNFSGGQRQRLAMLRLFMKEYPILILDEPTNHL 640
Cdd:PRK15439 360 WNVCALTHNRRGFWIKPARENAVLERYrralnIKFNHAEQAA-----RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1261268082 641 D---RETANAVIENIFAMPSTKIIITHD-ENILERVDRVY 676
Cdd:PRK15439 435 DvsaRNDIYQLIRSIAAQNVAVLFISSDlEEIEQMADRVL 474
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
479-682 |
5.13e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 479 NISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEE-LRKNVGLMTQDG 557
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 558 VLFRG-SLSENLsyFDINYDPSKIQESIDKLNLSNYIQFQSIN-DILISEGGTNFSGGQRQRLAMLRLFMKEYPILILDE 635
Cdd:PRK10982 83 NLVLQrSVMDNM--WLGRYPTKGMFVDQDKMYRDTKAIFDELDiDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1261268082 636 PTNHLDRETAN---AVIENIFAMPSTKIIITHD-ENILERVDRVYELTDKK 682
Cdd:PRK10982 161 PTSSLTEKEVNhlfTIIRKLKERGCGIVYISHKmEEIFQLCDEITILRDGQ 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
490-641 |
5.21e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.64 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 490 IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNvglmtqdGVLF-------RG 562
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL-------GVAYipedrlgRG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 563 -----SLSENL---SYFDINY------DPSKIQES----IDKLNlsnyIQFQSINDILiseggTNFSGGQRQRLAMLRLF 624
Cdd:COG3845 347 lvpdmSVAENLilgRYRRPPFsrggflDRKAIRAFaeelIEEFD----VRTPGPDTPA-----RSLSGGNQQKVILAREL 417
|
170
....*....|....*..
gi 1261268082 625 MKEYPILILDEPTNHLD 641
Cdd:COG3845 418 SRDPKLLIAAQPTRGLD 434
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
487-637 |
6.91e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 49.25 E-value: 6.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 487 KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDR--DIKDwNSEELRKNVGLMTQD----GVLF 560
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRS-PRDAIRAGIAYVPEDrkgeGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 561 RGSLSENLSYFDIN-------YDPSKI----QESIDKLNlsnyIQFQSInDILISeggtNFSGGQRQRLAMLRLFMKEYP 629
Cdd:COG1129 344 DLSIRENITLASLDrlsrgglLDRRREralaEEYIKRLR----IKTPSP-EQPVG----NLSGGNQQKVVLAKWLATDPK 414
|
....*...
gi 1261268082 630 ILILDEPT 637
Cdd:COG1129 415 VLILDEPT 422
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
490-678 |
7.88e-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: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 490 IENLSLNIKNNESIAIVGESGSGKSTLANLLLKlhtpdkgniliddrdikdwNSEELRKNVGLMT--QDGVLFRGSLSen 567
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY-------------------ASGKARLISFLPKfsRNKLIFIDQLQ-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 568 lsyfdinydpskiqeSIDKLNLsNYIqfqSINDILISeggtnFSGGQRQRLAMLR-LFMKEYPIL-ILDEPTNHLDRETA 645
Cdd:cd03238 70 ---------------FLIDVGL-GYL---TLGQKLST-----LSGGELQRVKLASeLFSEPPGTLfILDEPSTGLHQQDI 125
|
170 180 190
....*....|....*....|....*....|....*.
gi 1261268082 646 N---AVIENIFAMPSTKIIITHDENILERVDRVYEL 678
Cdd:cd03238 126 NqllEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
475-664 |
1.43e-05 |
|
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: 48.21 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISF-SFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHtPDKGNILIDDRDikdwnseelrKNVGLM 553
Cdd:TIGR00954 452 IKFENIPLvTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAK----------GKLFYV 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLFRGSLSENLSYfdinydPSKIQESIDK----LNLSNYIQFQSINDILISEGGTN--------FSGGQRQRLAML 621
Cdd:TIGR00954 521 PQRPYMTLGTLRDQIIY------PDSSEDMKRRglsdKDLEQILDNVQLTHILEREGGWSavqdwmdvLSGGEKQRIAMA 594
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1261268082 622 RLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTKIIITH 664
Cdd:TIGR00954 595 RLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
490-641 |
1.95e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 490 IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEELRKNvGLM------TQDGVLFRGS 563
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN-GIVyisedrKRDGLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 564 LSENLS-----YFdiNYDPSKIQESIDKLNLSNYIQFQSINDILISEGGTNFSGGQRQRLAMLRLFMKEYPILILDEPTN 638
Cdd:PRK10762 347 VKENMSltalrYF--SRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
...
gi 1261268082 639 HLD 641
Cdd:PRK10762 425 GVD 427
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
611-679 |
3.15e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.66 E-value: 3.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 611 SGGQRQRLAMLRLF----MKEYPILILDEPTNHLDRETANAVIENIFAM---PSTKIIITHDENILERVDRVYELT 679
Cdd:cd03227 79 SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvkGAQVIVITHLPELAELADKLIHIK 154
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
230-314 |
4.80e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 45.97 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 230 IDRKSTTKVFEHMFNIPIEKITSRHAGDLNVRIMSLESIR----GYILEDLIEMiISIVVIIPLLMYLLYTETFYTLILM 305
Cdd:cd18783 73 IDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQIERIRqfltGQLFGTLLDA-TSLLVFLPVLFFYSPTLALVVLAFS 151
|
....*....
gi 1261268082 306 FFIASSLFI 314
Cdd:cd18783 152 ALIALIILA 160
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
490-644 |
5.08e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 45.37 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 490 IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIKDWNSEEL-RKNVGLMTQDGVLFRG-SLSEN 567
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVRTFQHVRLFREmTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 568 L-----SYFDINY------DPSKIQESIDKLNLSNY-IQFQSINDILISEGGtNFSGGQRQRLAMLRLFMKEYPILILDE 635
Cdd:PRK11300 101 LlvaqhQQLKTGLfsgllkTPAFRRAESEALDRAATwLERVGLLEHANRQAG-NLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170
....*....|
gi 1261268082 636 PTNHLD-RET 644
Cdd:PRK11300 180 PAAGLNpKET 189
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
380-670 |
5.26e-05 |
|
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: 45.84 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 380 KQNALESFNSSLSTIFIIIMLAVGFYNFSkGEGDLSNIFFFIAISSIIFSPVSTIIGSILNWNSVKPLLLRTLDILEEEL 459
Cdd:pfam13304 12 KSNLLEALRFLADFDALVIGLTDERSRNG-GIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLEREDVEEKLSSK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 460 EKDGSDTKVNILRGSIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDIK 539
Cdd:pfam13304 91 PTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 540 DWNSEELRKNvgLMTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKLNLSNYIQFQSINDILISEggTNFSGGQRQ--- 616
Cdd:pfam13304 171 LAADLALFPD--LKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPA--FELSDGTKRlla 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261268082 617 RLAMLRLFMKEYPILILDEPTNHLDRETANAVIEnIFAMPSTK----IIITHDENILE 670
Cdd:pfam13304 247 LLAALLSALPKGGLLLIDEPESGLHPKLLRRLLE-LLKELSRNgaqlILTTHSPLLLD 303
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
474-665 |
8.06e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 474 SIEFNNIsFSFDDKKIIEnLSLNIknnesIAIVGESGSGKSTLAN---LLLKLHTPDKGNIlidDRDIKDWNSEELRKNV 550
Cdd:COG0419 4 RLRLENF-RSYRDTETID-FDDGL-----NLIVGPNGAGKSTILEairYALYGKARSRSKL---RSDLINVGSEEASVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 551 GLmTQDGVLFRGSLSENLSYFDINYDPSKIQESIDKL----------------------NLSNYIQFQSINDILISEGGT 608
Cdd:COG0419 74 EF-EHGGKRYRIERRQGEFAEFLEAKPSERKEALKRLlgleiyeelkerlkeleealesALEELAELQKLKQEILAQLSG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261268082 609 -----NFSGGQRQRLAMLRLFMkeypiLILDepTNHLDRETANAVIENIFAMpstkIIITHD 665
Cdd:COG0419 153 ldpieTLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEEL----AIITHV 203
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
505-670 |
9.12e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 44.66 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 505 IVGESGSGKSTLANLLLKLHTPDKGNIliDDRD-----IKDWNSEELRKNVGLMTQDGV--------------LFRGSLS 565
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKF--DDPPdwdeiLDEFRGSELQNYFTKLLEGDVkvivkpqyvdlipkAVKGKVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 566 ENLSYFDinyDPSKIQESIDKLNLSNYIQfQSINDIliseggtnfSGGQRQRLAMLRLFMKEYPILILDEPTNHLD---R 642
Cdd:cd03236 109 ELLKKKD---ERGKLDELVDQLELRHVLD-RNIDQL---------SGGELQRVAIAAALARDADFYFFDEPSSYLDikqR 175
|
170 180
....*....|....*....|....*...
gi 1261268082 643 ETANAVIENIFAMPSTKIIITHDENILE 670
Cdd:cd03236 176 LNAARLIRELAEDDNYVLVVEHDLAVLD 203
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
178-441 |
1.05e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 44.81 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 178 LAFPFILKKFMD--ILNASKEVDVRYLLIILGSLIVVIGIKSITSIIKVNFQKEIDRKST----TKVFEHMFNIPIEKIT 251
Cdd:cd18563 16 LVPPYLTKILIDdvLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITadlrRDLYEHLQRLSLSFFD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 252 SRHAGDLNVRIMS-LESIRGYILEDLIEMIISIVVIIPLLMYLLYTE---TFYTLILMFFIAsslFINISLGKFIYNAnl 327
Cdd:cd18563 96 KRQTGSLMSRVTSdTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNwklALLVLIPVPLVV---WGSYFFWKKIRRL-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 328 vetYYLGEHRGK-----INESLKAMYYVKAtgiFSKIKSVWKK--DYNKYLDTVHKRVLKQNAleSFNSSLS---TIFII 397
Cdd:cd18563 171 ---FHRQWRRWSrlnsvLNDTLPGIRVVKA---FGQEKREIKRfdEANQELLDANIRAEKLWA--TFFPLLTfltSLGTL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1261268082 398 IMLAVGFYNFSKGE---GDLSNiffFIAISSIIFSPVSTiIGSILNW 441
Cdd:cd18563 243 IVWYFGGRQVLSGTmtlGTLVA---FLSYLGMFYGPLQW-LSRLNNW 285
|
|
| Peptidase_C39A |
cd02549 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
17-125 |
1.11e-04 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.
Pssm-ID: 239109 [Multi-domain] Cd Length: 141 Bit Score: 42.78 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 17 CGPSCLAMIMHYYGSAVQASEIRNSKIINKKSAW----SLLDIKKVS-KSYGLSATayRIENITDLQR----------IQ 81
Cdd:cd02549 7 CGPTSLAMVLSYLGVKVTKPQLAAEGNTYDFAKDgygtYPKPIVSAAaRKYGLVVR--PLTGLLALLRqlaaghpvivSV 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1261268082 82 KPMIAFWGFNHFVIIERVKANK-FYIVDPKAG-PMIIDIRSFEEMF 125
Cdd:cd02549 85 NLGVSITPSGHAMVVIGYDRKGnVYVNDPGGGrRLVVSFDEFEKAW 130
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
487-684 |
1.41e-04 |
|
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: 44.82 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 487 KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHtPDK--GNILIDDRDIKDWNSE-----------ELRKNVGLM 553
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGKPVDIRNPAqairagiamvpEDRKRHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLFRGSLSENLSY-----FDINYDPSKIQESIDKLNLSNYIQFQSIndiliseggTNFSGGQRQRLAMLRLFMKEY 628
Cdd:TIGR02633 352 PILGVGKNITLSVLKSFcfkmrIDAAAELQIIGSAIQRLKVKTASPFLPI---------GRLSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 629 PILILDEPTNHLDRETANAVIENIFAMPS--TKIIITHDE--NILERVDRVYELTDKKLK 684
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQLAQegVAIIVVSSElaEVLGLSDRVLVIGEGKLK 482
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
487-641 |
1.53e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.92 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 487 KKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHtPDK--GNILIDDRDIKDWNSE-----------ELRKNVGLM 553
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRweGEIFIDGKPVKIRNPQqaiaqgiamvpEDRKRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 554 TQDGVLFRGSLSeNLSYF------DINYDPSKIQESIDKLNLSNYIQFQSIndiliseggTNFSGGQRQRLAMLRLFMKE 627
Cdd:PRK13549 354 PVMGVGKNITLA-ALDRFtggsriDDAAELKTILESIQRLKVKTASPELAI---------ARLSGGNQQKAVLAKCLLLN 423
|
170
....*....|....
gi 1261268082 628 YPILILDEPTNHLD 641
Cdd:PRK13549 424 PKILILDEPTRGID 437
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
466-679 |
3.15e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.57 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 466 TKVNILRGSIEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLAnLLLKLHTPDKGNiliddrdiKDW---- 541
Cdd:NF000106 5 TISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR--------RPWrf*t 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 542 ---NSEELRKNVGLMTQDGVLFRGSLS--ENLSYFDINYDPSK------IQESIDKLNLSNyiqfqsindiLISEGGTNF 610
Cdd:NF000106 76 wcaNRRALRRTIG*HRPVR*GRRESFSgrENLYMIGR*LDLSRkdararADELLERFSLTE----------AAGRAAAKY 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 611 SGGQRQRLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPSTKIIITHDENILERVDRV-YELT 679
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLaHELT 215
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
175-434 |
3.19e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 43.24 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 175 ISILAFPFILKKFMDILNASKEVDVRYLLIILGSLIVVigiKSITSIIKVNFQKEIDR-----KS--TTKVFEHMFNIPI 247
Cdd:cd18579 11 LLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLV---SLLQSLLLHQYFFLSFRlgmrvRSalSSLIYRKALRLSS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 248 EKITSRHAGDLnVRIMS--LESIrGYILEDLIEMIISIVVIIpLLMYLLYTE----TFYTLILMFFIassLFINISLGKF 321
Cdd:cd18579 88 SARQETSTGEI-VNLMSvdVQRI-EDFFLFLHYLWSAPLQII-VALYLLYRLlgwaALAGLGVLLLL---IPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 322 IynanlvetyylGEHRGKINES----LKAMyyvkaTGIFSKIKSV----WKKDYNKYLDTVHKR----VLKQNALESFNS 389
Cdd:cd18579 162 I-----------SKLRKKLMKAtderVKLT-----NEILSGIKVIklyaWEKPFLKRIEELRKKelkaLRKFGYLRALNS 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1261268082 390 SL--STIFIIIMLAVGFYNFSKGEGDLSNIFFFIAISSIIFSPVSTI 434
Cdd:cd18579 226 FLffSTPVLVSLATFATYVLLGNPLTAAKVFTALSLFNLLRFPLLML 272
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
630-672 |
3.45e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 3.45e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1261268082 630 ILILDEPTNHLDRETANAVIENIFAMPSTKIIITHDENILERV 672
Cdd:PRK15064 176 ILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSV 218
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
178-322 |
4.59e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 42.86 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 178 LAFPFILKKFMDILNASKEVDVryLLIILGSLIVVIGIKSITSIIKVNFQKEIDRKSTT----KVFEHMFNIPIEKITSR 253
Cdd:cd18576 13 LVFPLLAGQLIDAALGGGDTAS--LNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVAdlrkDLYRHLQRLPLSFFHER 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 254 HAGDLNVRIMS-LESIRGYILEDLIEMIISIVVIIPLLMYLLYTETFYTLILMFFIASSLFINISLGKFI 322
Cdd:cd18576 91 RVGELTSRLSNdVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRI 160
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
565-674 |
7.85e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 565 SENLSYFDINYDPSKIQESIDKLNLSNYIQFQSINDILISEGGtNFSGGQRQ------RLAMLRLFMKEYPILILDEPTN 638
Cdd:TIGR00606 1156 GQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRG-RCSAGQKVlasliiRLALAETFCLNCGIIALDEPTT 1234
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1261268082 639 HLDRET----ANAVIENIFAMPSTK----IIITHDENILERVDR 674
Cdd:TIGR00606 1235 NLDRENieslAHALVEIIKSRSQQRnfqlLVITHDEDFVELLGR 1278
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
475-682 |
8.74e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.30 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 475 IEFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILIDDRDI-----KDwnSEElrKN 549
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpKS--SQE--AG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 550 VGLMTQDGVLFRG-SLSENL--------SYFDINYDpsKIQESIDKLNLSNYIQFQSinDILISEggtnFSGGQRQRLAM 620
Cdd:PRK10762 81 IGIIHQELNLIPQlTIAENIflgrefvnRFGRIDWK--KMYAEADKLLARLNLRFSS--DKLVGE----LSIGEQQMVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 621 LRLFMKEYPILILDEPTNHL-DRETAN--AVIENIFAMPSTKIIITHD-ENILERVDRVYELTDKK 682
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALtDTETESlfRVIRELKSQGRGIVYISHRlKEIFEICDDVTVFRDGQ 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
579-669 |
1.18e-03 |
|
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: 42.08 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 579 KIQESIDKLNLSNYIQfQSINDIliseggtnfSGGQRQRLAMLRLFMKEYPILILDEPTNHLD---RETANAVIENIFAM 655
Cdd:COG1245 192 KLDELAEKLGLENILD-RDISEL---------SGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqRLNVARLIRELAEE 261
|
90
....*....|....
gi 1261268082 656 PSTKIIITHDENIL 669
Cdd:COG1245 262 GKYVLVVEHDLAIL 275
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
175-308 |
1.62e-03 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 41.06 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 175 ISILAfPFILKKFMDILNASK----EVDVRYLLIILGSLIVVIGIKSITSIIKVNFQKEIDRKSTTKVFEHMFNIPIEKI 250
Cdd:cd18560 11 CNVLA-PLFLGRAVNALTLAKvkdlESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWH 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 251 TSRHAGDLnVRIM-----SLESIRGYILEDLIEMIISIVVIIPLLMYLLYTETFYTLILMFFI 308
Cdd:cd18560 90 LSKKTGEV-VRIMdrgteSANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVLL 151
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
488-585 |
1.65e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 41.04 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 488 KIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLhTPDKGNILID-----DRDIKDWNSEELRKnvgLMTQD-GVLFR 561
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADrfrwnGIDLLKLSPRERRK---IIGREiAMIFQ 96
|
90 100
....*....|....*....|....*....
gi 1261268082 562 gslsENLSYFdinyDPSK-----IQESID 585
Cdd:COG4170 97 ----EPSSCL----DPSAkigdqLIEAIP 117
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
445-641 |
1.72e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 41.92 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 445 KPLLLRTLDILEEELEKDGSDTKVNILRGSiEFNNIsFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLH 524
Cdd:TIGR01257 1912 EPIFDEDDDVAEERQRIISGGNKTDILRLN-ELTKV-YSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDT 1989
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 525 TPDKGNILIDDRDIKDwNSEELRKNVGLMTQ-DGV--LFRGSlsENLS-YFDINYDPSKIQE-----SIDKLNLSNYIqf 595
Cdd:TIGR01257 1990 TVTSGDATVAGKSILT-NISDVHQNMGYCPQfDAIddLLTGR--EHLYlYARLRGVPAEEIEkvanwSIQSLGLSLYA-- 2064
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1261268082 596 qsinDILiseGGTnFSGGQRQRLAMLRLFMKEYPILILDEPTNHLD 641
Cdd:TIGR01257 2065 ----DRL---AGT-YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
497-669 |
1.92e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 497 IKNNESIAIVGESGSGKSTLANLLlklhtpdkgniliddrdikdwnSEELRKNVGLM----TQDGVL--FRGSlsENLSY 570
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL----------------------SGELIPNLGDYeeepSWDEVLkrFRGT--ELQNY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 571 FDINYDPS-----KIQ---------------------------ESIDKLNLSNYIQfQSINDIliseggtnfSGGQRQRL 618
Cdd:PRK13409 152 FKKLYNGEikvvhKPQyvdlipkvfkgkvrellkkvdergkldEVVERLGLENILD-RDISEL---------SGGELQRV 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1261268082 619 AMLRLFMKEYPILILDEPTNHLD-RE---TANAVIEniFAMPSTKIIITHDENIL 669
Cdd:PRK13409 222 AIAAALLRDADFYFFDEPTSYLDiRQrlnVARLIRE--LAEGKYVLVVEHDLAVL 274
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
605-675 |
2.30e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 605 EGGTNF-SGGQRQ------RLAMLRLFMKEYPILILDEPTNHLDRETANA---VIENIFAMPSTKIIITHDENILERVDR 674
Cdd:PRK03918 783 ERPLTFlSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKlvdIMERYLRKIPQVIIVSHDEELKDAADY 862
|
.
gi 1261268082 675 V 675
Cdd:PRK03918 863 V 863
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
476-675 |
2.52e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 476 EFNNISFSFDDKKIIENLSLNIKNNESIAIVGESGSGKSTLANLLLKLH---TPDkGNILIDD-----RDIKDwnSEelR 547
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYphgSYE-GEILFDGevcrfKDIRD--SE--A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 548 KNVGLMTQDGVLFRG-SLSENL-------SYFDINYDP--SKIQESIDKLNLsnyiqfqSIN-DILISEGGTnfsgGQRQ 616
Cdd:NF040905 78 LGIVIIHQELALIPYlSIAENIflgneraKRGVIDWNEtnRRARELLAKVGL-------DESpDTLVTDIGV----GKQQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261268082 617 RLAMLRLFMKEYPILILDEPTNHLDRETANAVIENIFAMPS---TKIIITHDENILERV-DRV 675
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAqgiTSIIISHKLNEIRRVaDSI 209
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
502-566 |
4.85e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 37.71 E-value: 4.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261268082 502 SIAIVGESGSGKSTLANLLL-KLHTPDKGNILIDDRDIKDWnsEELRKNVGLMTQDGVLFRGSLSE 566
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLLeQLPEVRDSVVFVDLPSGTSP--KDLLRALLRALGLPLSGRLSKEE 70
|
|
| Peptidase_C39_likeA |
cd02417 |
A sub-family of peptidase C39 which contains Cyclolysin and Hemolysin processing peptidases. ... |
16-123 |
7.65e-03 |
|
A sub-family of peptidase C39 which contains Cyclolysin and Hemolysin processing peptidases. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in this sub-family.
Pssm-ID: 239098 [Multi-domain] Cd Length: 121 Bit Score: 36.84 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261268082 16 DCGPSCLAMIMHYYGSAVQASEIRNsKIINKKSAWSLLDIKKVSKSYGLSATAYRIEnITDLQRIQKPMIAFWGFNHFVI 95
Cdd:cd02417 6 DSGLLALVLLARYHGIAADPEQLRH-EFGLAGEPFNSTELLLAAKSLGLKAKAVRQP-VERLARLPLPALAWDDDGGHFI 83
|
90 100
....*....|....*....|....*....
gi 1261268082 96 IERVKANKFYIVDPKAG-PMIIDIRSFEE 123
Cdd:cd02417 84 LAKLDGQKYLIQDPISQrPEVLSREEFEA 112
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
490-533 |
8.79e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.10 E-value: 8.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1261268082 490 IENLSLNIKNNESIAIVGESGSGKSTLANLLLKLHTPDKGNILI 533
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83
|
|
| |
