|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
40-687 |
0e+00 |
|
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: 830.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 40 IGKRLKQSGRGKKKeeayPAAENREILHCTETTCKTPSPGVNADFFKQLLELRKILFPKLVTAETGWLCLHSVALISRTF 119
Cdd:TIGR00954 35 LKRERAADRRGDKS----GKEELTIVGKHSTIEGAKKKAHVNGVFLGKLDFLLKILIPRVFCKETGLLILIAFLLVSRTY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 120 LSIYVAGLDGKIVKSIVEKKPWTFIIKLIKWLMIAIPATFVNSAIRYLECKLALAFRTRLVDHAYETYFTNQTYYKVINM 199
Cdd:TIGR00954 111 LSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 200 DGRLANPDQSLTEDIMMFSQSVAHLYSNLTKPILDVILTSYTLIQTATSRGASPIGPTLLAglvvytTAKVLKACSPKFG 279
Cdd:TIGR00954 191 DSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTALGSVGPAGLFAYLFA------TGVVLTKLRPPIG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 280 KLVAEEAHRKGYLRYVHSRIIANVEEIAFYRGHKVEMKQLQKSYKALADQINLILSKRLWYIMIEQFLMKYVWSSSGLIM 359
Cdd:TIGR00954 265 KLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNLIIKFRFSYGFLDNIVAKYTWSAVGLVA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 360 VAVPIITATGFADGDLEDgqkqamvSERTEAFTTARNLLASGADAIERIMSSYKEITELAGYTARVYNMFWVFDEVNRGI 439
Cdd:TIGR00954 345 VSIPIFDKTHPAFLEMSE-------EELMQEFYNNGRLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGN 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 440 YKRTAVIQEPENHSKNEVTMELPLSdtltikGNVIDVDHGIICENVPIITPTGEVVASRLNFKVQEGMHLLITGPNGCGK 519
Cdd:TIGR00954 418 FKRPRVEEIESGREGGRNSNLVPGR------GIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGK 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 520 SSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLGSLRDQVIYPDSVDEMHDKGYTDQDLECILRNVHLYHIVQREG 599
Cdd:TIGR00954 492 SSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREG 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 600 GWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQAAKGAGISLLSITHRPSLWKYHTHLLQF 679
Cdd:TIGR00954 572 GWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYM 651
|
....*...
gi 586469518 680 DGEGGWRF 687
Cdd:TIGR00954 652 DGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
91-365 |
3.87e-125 |
|
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family of ABC transporters and shares sequence similarity with pfam00664. Mutations in this domain in Swiss:P28288 are believed responsible for Zellweger Syndrome-2; mutations in Swiss:P33897 are responsible for recessive X-linked adrenoleukodystrophy. A Saccharomyces cerevisiae homolog is involved in the import of long-chain fatty acids.
Pssm-ID: 399466 Cd Length: 269 Bit Score: 373.87 E-value: 3.87e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 91 LRKILFPKLVTAETGWLCLHSVALISRTFLSIYVAGLDGKIVKSIVEKKPWTFIIKLIKWLMIAIPATFVNSAIRYLECK 170
Cdd:pfam06472 1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 171 LALAFRTRLVDHAYETYFTNQTYYKVINMDGRLANPDQSLTEDIMMFSQSVAHLYSNLTKPILDVILTSYTLIQTATSRG 250
Cdd:pfam06472 81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 251 aspigpTLLAGLVVYTTAKVLKACSPKFGKLVAEEAHRKGYLRYVHSRIIANVEEIAFYRGHKVEMKQLQKSYKALADQI 330
Cdd:pfam06472 161 ------PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHM 234
|
250 260 270
....*....|....*....|....*....|....*
gi 586469518 331 NLILSKRLWYIMIEQFLMKYVWSSSGLIMVAVPII 365
Cdd:pfam06472 235 RRILRRRLWYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
142-692 |
2.73e-90 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 294.02 E-value: 2.73e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 142 TFIIKLIKWLMIAIPATFVNSAIRYLECKLALAFRTRLVDHAYETYFTNQTYYKVINMDGRLANPDQSLTEDIMMFSQSV 221
Cdd:COG4178 62 AFWQQLGVFALLAAISILLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDIRLFTETT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 222 AHLYSNLTKPILDVIltSYTLI-------QTATSRGASPIGPTLLA-GLVVYT-TAKVLkacSPKFGK----LVAEEAHR 288
Cdd:COG4178 142 LSLSLGLLSSVVTLI--SFIGIlwslsgsLTFTLGGYSITIPGYMVwAALIYAiIGTLL---THLIGRplirLNFEQQRR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 289 KGYLRY--VHSRiiANVEEIAFYRGHKVEMKQLQKSYKALADQINLILSKRLwyimieqflmKYVW--SSSGLIMVAVPI 364
Cdd:COG4178 217 EADFRFalVRVR--ENAESIALYRGEAAERRRLRRRFDAVIANWRRLIRRQR----------NLTFftTGYGQLAVIFPI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 365 -ITATGFADGDLEDGQkqamVSERTEAFTTARNllasgadAIERIMSSYKEITELAGYTARVYNmfwvFDEVnrgiykrt 443
Cdd:COG4178 285 lVAAPRYFAGEITLGG----LMQAASAFGQVQG-------ALSWFVDNYQSLAEWRATVDRLAG----FEEA-------- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 444 avIQEPENHSKNEVTMELPLSDTLTIkgnvidvdhgiicENVPIITPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLF 523
Cdd:COG4178 342 --LEAADALPEAASRIETSEDGALAL-------------EDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 524 RILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLGSLRDQVIYPDSVDEmhdkgYTDQDLECILRNVHLYHIVQReggWDA 603
Cdd:COG4178 407 RAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTLREALLYPATAEA-----FSDAELREALEAVGLGHLAER---LDE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 604 VMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQA--AKGAGISLLSITHRPSLWKYHTHLLQFDG 681
Cdd:COG4178 479 EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLlrEELPGTTVISVGHRSTLAAFHDRVLELTG 558
|
570
....*....|.
gi 586469518 682 EGGWRFEQLDT 692
Cdd:COG4178 559 DGSWQLLPAEA 569
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
480-685 |
6.41e-84 |
|
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: 262.86 E-value: 6.41e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 480 IICENVPIITPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLGSL 559
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 560 RDQVIYPdsvdemhdkgytdqdlecilrnvhlyhivqreggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDECTS 639
Cdd:cd03223 81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 586469518 640 AVSIDVEGKIFQAAKGAGISLLSITHRPSLWKYHTHLLQFDGEGGW 685
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
488-665 |
1.06e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 114.14 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 488 ITPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYK-------PPPQH---MFYIPQRPYMSL 556
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGeIYLDgkplsamPPPEWrrqVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 557 GSLRDQVIYPDSvdeMHDKGYTDQDLECILRNVHLYhivqreggwDAVMDWK-DVLSGGEKQRMGMARMFYHKPKYALLD 635
Cdd:COG4619 88 GTVRDNLPFPFQ---LRERKFDRERALELLERLGLP---------PDILDKPvERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190
....*....|....*....|....*....|....
gi 586469518 636 ECTSAVSID----VEGKIFQAAKGAGISLLSITH 665
Cdd:COG4619 156 EPTSALDPEntrrVEELLREYLAEEGRAVLWVSH 189
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
480-669 |
2.97e-26 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 114.08 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 480 IICENVPIITPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL---------YKPPP--QHMFYI 548
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdLDPASwrRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 549 PQRPYMSLGSLRDQViypdsvdEMHDKGYTDQDLECILRNVHLYHIVQR-EGGWDAVmdwkdV------LSGGEKQRMGM 621
Cdd:COG4988 417 PQNPYLFAGTIRENL-------RLGRPDASDEELEAALEAAGLDEFVAAlPDGLDTP-----LgeggrgLSGGQAQRLAL 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 586469518 622 ARMFYHKPKYALLDECTSAVSIDVEGKIFQA--AKGAGISLLSITHRPSL 669
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQAlrRLAKGRTVILITHRLAL 534
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
480-669 |
8.48e-26 |
|
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: 104.39 E-value: 8.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 480 IICENVPIITPTGEV-VASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhMFYIPQRPYmSLGS 558
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL------IDGVDLRDL-DLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 559 LRDQViypdsvdemhdkGYTDQDlecilrnVHLYHivqreggwDAVMDwkDVLSGGEKQRMGMARMFYHKPKYALLDECT 638
Cdd:cd03228 74 LRKNI------------AYVPQD-------PFLFS--------GTIRE--NILSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190
....*....|....*....|....*....|...
gi 586469518 639 SAVSIDVEGKIFQA--AKGAGISLLSITHRPSL 669
Cdd:cd03228 125 SALDPETEALILEAlrALAKGKTVIVIAHRLST 157
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
91-668 |
4.72e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.17 E-value: 4.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 91 LRKILfpKLVTAETGWLCLHSVALISRTFLSIYVAGLDGKIVKSIVEKKPWTFIIKLIkWLMIAIpaTFVNSAIRYLEC- 169
Cdd:COG1132 9 LRRLL--RYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLL-LLLLGL--ALLRALLSYLQRy 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 170 -------KLALAFRTRLVDHAYE---TYFTNQTYYKVINMdgrlanpdqsLTEDIMMFSQSVAHLYSNLTKPILDVILTS 239
Cdd:COG1132 84 llarlaqRVVADLRRDLFEHLLRlplSFFDRRRTGDLLSR----------LTNDVDAVEQFLAHGLPQLVRSVVTLIGAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 240 YTLIQTatsrgaSP-IGPTLLAGLVVYTtakvlkACSPKFGKLVAEEAHRkgyLRYVHSRIIANVEEiaFYRGHKVeMK- 317
Cdd:COG1132 154 VVLFVI------DWrLALIVLLVLPLLL------LVLRLFGRRLRKLFRR---VQEALAELNGRLQE--SLSGIRV-VKa 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 318 --QLQKSYKALADQINLILSKRLWYIMIEQFLMKYVWSSSGLIMVAVPIITATGFADGDLEDGQkqamvserteaFTTAR 395
Cdd:COG1132 216 fgREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGD-----------LVAFI 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 396 NLLASGADAIERIMSSYKEITELAGYTARVynmFWVFDEVNRgiykrtavIQEPENhsknevtmELPLSDtltikgnvid 475
Cdd:COG1132 285 LYLLRLFGPLRQLANVLNQLQRALASAERI---FELLDEPPE--------IPDPPG--------AVPLPP---------- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 476 VDHGIICENVpiiT---PTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VL--------YKPP-- 541
Cdd:COG1132 336 VRGEIEFENV---SfsyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGrILidgvdirdLTLEsl 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 542 PQHMFYIPQRPYMSLGSLRDQVIYPDsvdemhdKGYTDQDLECILRNVHLYHIVQR-EGGWDAVmdwkdV------LSGG 614
Cdd:COG1132 413 RRQIGVVPQDTFLFSGTIRENIRYGR-------PDATDEEVEEAAKAAQAHEFIEAlPDGYDTV-----VgergvnLSGG 480
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 586469518 615 EKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQAAKG--AGISLLSITHRPS 668
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERlmKGRTTIVIAHRLS 536
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
499-669 |
1.73e-23 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 106.07 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY------KPPP----QHMFYIPQRPYMSLGSLRDQVIypd 567
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGrILIdgidlrQIDPaslrRQIGVVLQDVFLFSGTIRENIT--- 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 568 svdeMHDKGYTDQDLECILRNVHLYHIVQR-EGGWDA-VMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDV 645
Cdd:COG2274 571 ----LGDPDATDEEIIEAARLAGLHDFIEAlPMGYDTvVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAET 646
|
170 180
....*....|....*....|....*.
gi 586469518 646 EGKIFQA--AKGAGISLLSITHRPSL 669
Cdd:COG2274 647 EAIILENlrRLLKGRTVIIIAHRLST 672
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
480-669 |
5.58e-22 |
|
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: 93.43 E-value: 5.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 480 IICENVPIITP-TGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhmfyIPQRPYMSLGS 558
Cdd:cd03246 1 LEVENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR---------LDGADISQWDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 559 --LRDQViypdsvdemhdkGYTDQDLEcilrnvhLYhivqrEGgwdAVMDwkDVLSGGEKQRMGMARMFYHKPKYALLDE 636
Cdd:cd03246 72 neLGDHV------------GYLPQDDE-------LF-----SG---SIAE--NILSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190
....*....|....*....|....*....|....*.
gi 586469518 637 CTSAVSIDVEGKIFQA---AKGAGISLLSITHRPSL 669
Cdd:cd03246 123 PNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPET 158
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
498-639 |
2.01e-20 |
|
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: 88.47 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 498 RLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY----------KPPPQHMFYIPQRP-YMSLGSLRDQVIY 565
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGtILLdgqdltdderKSLRKEIGYVFQDPqLFPRLTVRENLRL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586469518 566 PDSVDEMHDKGYTDQdLECILRNVHLYHIVQReggwdAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTS 639
Cdd:pfam00005 83 GLLLKGLSKREKDAR-AEEALEKLGLGDLADR-----PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
495-668 |
3.18e-20 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 95.22 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 495 VASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV-------LYKPPP----QHMFYIPQRPYMSLGSLRD-- 561
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSitlggvdLRDLDEddlrRRIAVVPQRPHLFDTTLREnl 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 562 QVIYPDSvdemhdkgyTDQDLECILRNVHLYHIVQR-EGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLDECTS 639
Cdd:COG4987 430 RLARPDA---------TDEELWAALERVGLGDWLAAlPDGLDTWLGEGGRrLSGGERRRLALARALLRDAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|...
gi 586469518 640 AVSIDVEGKI----FQAAKGAgiSLLSITHRPS 668
Cdd:COG4987 501 GLDAATEQALladlLEALAGR--TVLLITHRLA 531
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
494-669 |
6.62e-20 |
|
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: 86.92 E-value: 6.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 494 VVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhmFYIPQRPYMSLGSLRDQViypdsvdemh 573
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL-------IDGKDIAKLPLEELRRRI---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 574 dkGYTDQdlecilrnvhlyhivqreggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQAA 653
Cdd:cd00267 76 --GYVPQ------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELL 123
|
170
....*....|....*....
gi 586469518 654 KGA---GISLLSITHRPSL 669
Cdd:cd00267 124 RELaeeGRTVIIVTHDPEL 142
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
480-669 |
8.18e-20 |
|
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: 93.51 E-value: 8.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 480 IICENVPIITPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV-------LYKPPPQHMF----YI 548
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavngvpLADADADSWRdqiaWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 549 PQRPYMSLGSLRDQViypdsvdEMHDKGYTDQDLECILRNVHLYHIVQ-REGGWDAVMDWKDV-LSGGEKQRMGMARMFY 626
Cdd:TIGR02857 402 PQHPFLFAGTIAENI-------RLARPDASDAEIREALERAGLDEFVAaLPQGLDTPIGEGGAgLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 586469518 627 HKPKYALLDECTSAVSIDVEGKIFQA----AKGAgiSLLSITHRPSL 669
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEAlralAQGR--TVLLVTHRLAL 519
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
499-669 |
1.15e-19 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 88.42 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY------KPPP----QHMFYIPQRPYMSLGSLRDQVI--Y 565
Cdd:cd03245 23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGsVLLdgtdirQLDPadlrRNIGYVPQDVTLFYGTLRDNITlgA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 566 PDSVDEM----------------HDKGYtdqDLECilrnvhlyhivqREGGwdavmdwkDVLSGGEKQRMGMARMFYHKP 629
Cdd:cd03245 103 PLADDERilraaelagvtdfvnkHPNGL---DLQI------------GERG--------RGLSGGQRQAVALARALLNDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 586469518 630 KYALLDECTSAVSIDVEGKIFQAAKG--AGISLLSITHRPSL 669
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQllGDKTLIIITHRPSL 201
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
492-667 |
2.68e-18 |
|
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: 84.07 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYK---------PPPQHMFYIPQRPymslgslrd 561
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGeVLWNgepirdareDYRRRLAYLGHAD--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 562 qVIYPD-SVDE-------MHDKGYTDQDLECILRNVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYAL 633
Cdd:COG4133 85 -GLKPElTVREnlrfwaaLYGLRADREAIDEALEAVGLAGLADLPVR---------QLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 586469518 634 LDECTSAvsIDVEGK-----IFQAAKGAGISLLSITHRP 667
Cdd:COG4133 155 LDEPFTA--LDAAGVallaeLIAAHLARGGAVLLTTHQP 191
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
450-669 |
2.50e-17 |
|
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: 85.96 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 450 ENHSKNEVTMELPLSdtltiKGNvIDVdhgiicENVPIITP-TGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSG 528
Cdd:COG4618 313 AAVPAEPERMPLPRP-----KGR-LSV------ENLTVVPPgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 529 LWPVYEGV-------LYKPPP----QHMFYIPQRPymSL--GSLRdQVI--YPDSVDE----------MHD------KGY 577
Cdd:COG4618 381 VWPPTAGSvrldgadLSQWDReelgRHIGYLPQDV--ELfdGTIA-ENIarFGDADPEkvvaaaklagVHEmilrlpDGY 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 578 tDQDLEcilrnvhlyhivqrEGGwdavmdwkDVLSGGEKQRMGMARMFYHKPKYALLDECTSavSIDVEG-----KIFQA 652
Cdd:COG4618 458 -DTRIG--------------EGG--------ARLSGGQRQRIGLARALYGDPRLVVLDEPNS--NLDDEGeaalaAAIRA 512
|
250
....*....|....*..
gi 586469518 653 AKGAGISLLSITHRPSL 669
Cdd:COG4618 513 LKARGATVVVITHRPSL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
495-681 |
1.65e-16 |
|
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: 79.44 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 495 VASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPPPQ--HMFY------IPQRPYMSLGSLRDQV 563
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPISQyeHKYLhskvslVGQEPVLFARSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 564 IYpdsvdemhdkGYTDQDLECILRNVHLYH----IVQREGGWDAVMDWK-DVLSGGEKQRMGMARMFYHKPKYALLDECT 638
Cdd:cd03248 109 AY----------GLQSCSFECVKEAAQKAHahsfISELASGYDTEVGEKgSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 586469518 639 SAVSIDVEGKIFQAAKG--AGISLLSITHRPSLWKYHTHLLQFDG 681
Cdd:cd03248 179 SALDAESEQQVQQALYDwpERRTVLVIAHRLSTVERADQILVLDG 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
492-669 |
1.83e-16 |
|
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: 79.70 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KP----PP----QHMFYIPQRPYMSLG-SL 559
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDlaslSRrelaRRIAYVPQEPPAPFGlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 560 RDQVI---YPdsvdemHDK---GYTDQDLECI---LRNVHLYHIVQREggWDAvmdwkdvLSGGEKQRMGMARMFYHKPK 630
Cdd:COG1120 93 RELVAlgrYP------HLGlfgRPSAEDREAVeeaLERTGLEHLADRP--VDE-------LSGGERQRVLIARALAQEPP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 586469518 631 YALLDECTSAV----SIDVEGKIFQAAKGAGISLLSITHRPSL 669
Cdd:COG1120 158 LLLLDEPTSHLdlahQLEVLELLRRLARERGRTVVMVLHDLNL 200
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
492-682 |
2.42e-16 |
|
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: 78.34 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG---VLYKPPPQ--HMF-YIPQRPYMSlgslRDqviY 565
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGsirVFGKPLEKerKRIgYVPQRRSID----RD---F 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 566 PDSVDEM----------HDKGYTDQDLECI---LRNVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYA 632
Cdd:cd03235 84 PISVRDVvlmglyghkgLFRRLSKADKAKVdeaLERVGLSELADRQIG---------ELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 586469518 633 LLDECTSAVsiDVEGK-----IFQAAKGAGISLLSITH-RPSLWKYHTHLLQFDGE 682
Cdd:cd03235 155 LLDEPFAGV--DPKTQediyeLLRELRREGMTILVVTHdLGLVLEYFDRVLLLNRT 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
499-665 |
2.94e-16 |
|
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: 78.07 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQH-------MFYIPQRPYMSLG--SLRDQVIYpdS 568
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGsILLNGKPIKakerrksIGYVMQDVDYQLFtdSVREELLL--G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 569 VDEMHDKGytdQDLECILRNVHLYhivqreggwdavmDWKDV----LSGGEKQRMGMARMFYHKPKYALLDECTSAV--- 641
Cdd:cd03226 97 LKELDAGN---EQAETVLKDLDLY-------------ALKERhplsLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLdyk 160
|
170 180
....*....|....*....|....
gi 586469518 642 SIDVEGKIFQAAKGAGISLLSITH 665
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITH 184
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
499-640 |
3.61e-16 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 78.38 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV-------LYKPPPQHMFYIP-----------QRPYMSLGSLR 560
Cdd:cd03260 19 ISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegevlLDGKDIYDLDVDVlelrrrvgmvfQKPNPFPGSIY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 561 DQVIYPDSVDEMHDKGYTDQDLECILRNVHLyhivqreggWDAVMDWKDV--LSGGEKQRMGMARMFYHKPKYALLDECT 638
Cdd:cd03260 99 DNVAYGLRLHGIKLKEELDERVEEALRKAAL---------WDEVKDRLHAlgLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
..
gi 586469518 639 SA 640
Cdd:cd03260 170 SA 171
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
499-673 |
5.16e-16 |
|
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: 77.51 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPP----------QHMFYIPQRPymslgslRDQVIYPd 567
Cdd:cd03225 20 ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGeVLVDGKDltklslkelrRKVGLVFQNP-------DDQFFGP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 568 SVDEmhdkgytdqDLECILRNVHLYH--IVQR------EGGWDAVMDWK-DVLSGGEKQRMGMARMFYHKPKYALLDECT 638
Cdd:cd03225 92 TVEE---------EVAFGLENLGLPEeeIEERveealeLVGLEGLRDRSpFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 586469518 639 SavSIDVEG-----KIFQAAKGAGISLLSITHRPSLWKYH 673
Cdd:cd03225 163 A--GLDPAGrrellELLKKLKAEGKTIIIVTHDLDLLLEL 200
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
480-668 |
7.06e-16 |
|
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: 77.65 E-value: 7.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 480 IICENVPIITPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-----------KPPPQHMFYI 548
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgidirdisrKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 549 PQRPYMSLGSLRDQVIYPDSvdemhdkGYTDQDLECILRNVHLYHIVQR-EGGWDAVM-DWKDVLSGGEKQRMGMARMFY 626
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRP-------NATDEEVIEAAKEAGAHDFIMKlPNGYDTVLgENGGNLSQGERQLLAIARAML 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 586469518 627 HKPKYALLDECTSavSIDVEG-KIFQAAKGA---GISLLSITHRPS 668
Cdd:cd03254 156 RDPKILILDEATS--NIDTETeKLIQEALEKlmkGRTSIIIAHRLS 199
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
499-651 |
8.93e-16 |
|
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: 76.35 E-value: 8.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPpqHMFYIPQRPYMSLGSLRDQVIYPDSVDEmhdKGYT 578
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEPWIQNGTIRENILFGKPFDE---ERYE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 579 --------DQDLEcILRNVHLYHIvqREGGwdaVMdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIF 650
Cdd:cd03250 99 kvikacalEPDLE-ILPDGDLTEI--GEKG---IN-----LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIF 167
|
.
gi 586469518 651 Q 651
Cdd:cd03250 168 E 168
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
492-669 |
1.27e-15 |
|
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: 75.55 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPP----QHMFYIPQrpymslgslr 560
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILldgkdlaSLSPkelaRKIAYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 561 dqviypdsvdemhdkgytdqdlecILRNVHLYHIVQREggwdaVMDwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSA 640
Cdd:cd03214 81 ------------------------ALELLGLAHLADRP-----FNE----LSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190
....*....|....*....|....*....|...
gi 586469518 641 V----SIDVEGKIFQAAKGAGISLLSITHRPSL 669
Cdd:cd03214 128 LdiahQIELLELLRRLARERGKTVVMVLHDLNL 160
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
492-667 |
2.67e-15 |
|
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: 75.22 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQHMfyipQRPymslgSLRDQVIYPDSVD 570
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGrVLLNGGPLDF----QRD-----SIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 571 EMhdKGytdqdLECILRNVHLYH-IVQREGGWDAVMD-----WKDV----LSGGEKQRMGMARMFYHKPKYALLDECTSA 640
Cdd:cd03231 83 GI--KT-----TLSVLENLRFWHaDHSDEQVEEALARvglngFEDRpvaqLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|
gi 586469518 641 VSIDVEGKIFQAAKG---AGISLLSITHRP 667
Cdd:cd03231 156 LDKAGVARFAEAMAGhcaRGGMVVLTTHQD 185
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
480-668 |
2.80e-15 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 75.73 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 480 IICENVPIITPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY------KPPPQHMF-----YI 548
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdiREVTLDSLrraigVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 549 PQrpymslgslrDQVIYPDSVdeMHDKGY-----TDQDLECILRNVHLYHIVQR-EGGWDAVMDWKDV-LSGGEKQRMGM 621
Cdd:cd03253 81 PQ----------DTVLFNDTI--GYNIRYgrpdaTDEEVIEAAKAAQIHDKIMRfPDGYDTIVGERGLkLSGGEKQRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 586469518 622 ARMFYHKPKYALLDECTSAVSIDVEGKIFQAAK--GAGISLLSITHRPS 668
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRdvSKGRTTIVIAHRLS 197
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
490-666 |
3.62e-15 |
|
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: 75.22 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 490 PTGEVVASRLNFKVQEGMHLLITGPNGCGKSS----LFRILsglwPVYEGVLY-------KPPP----QHMFYIPQRPYM 554
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILidgvdisKIGLhdlrSRISIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 555 SLGSLRDQViypDSVDEmhdkgYTDQDLECILRNVHLY-HIVQREGGWDA-VMDWKDVLSGGEKQRMGMARMFYHKPKYA 632
Cdd:cd03244 90 FSGTIRSNL---DPFGE-----YSDEELWQALERVGLKeFVESLPGGLDTvVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 586469518 633 LLDECTSAVSIDVEGKIFQAAKG--AGISLLSITHR 666
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREafKDCTVLTIAHR 197
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
500-672 |
5.41e-15 |
|
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: 74.45 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 500 NFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPP--------QHMFYIPQR----PYMSLgslR 560
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdisKLSEkelaafrrRHIGFVFQSfnllPDLTA---L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 561 DQVIYPDSVDEMHDKGYTDQDLEcILRNVHLYHIVQREGGWdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSA 640
Cdd:cd03255 101 ENVELPLLLAGVPKKERRERAEE-LLERVGLGDRLNHYPSE---------LSGGQQQRVAIARALANDPKIILADEPTGN 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 586469518 641 V----SIDVEGKIFQAAKGAGISLLSITHRPSLWKY 672
Cdd:cd03255 171 LdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEY 206
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
495-666 |
1.01e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.56 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 495 VASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPPP--------QHMFYIPQRPYMSLGSLRDQV 563
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlngQPIAdyseaalrQAISVVSQRVHLFSATLRDNL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 564 IypdsvdeMHDKGYTDQDLECILRNVHLYHIVQREGGWDAVM-DWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVS 642
Cdd:PRK11160 435 L-------LAAPNASDEALIEVLQQVGLEKLLEDDKGLNAWLgEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
170 180
....*....|....*....|....*.
gi 586469518 643 IDVEGKIFQ--AAKGAGISLLSITHR 666
Cdd:PRK11160 508 AETERQILEllAEHAQNKTVLMITHR 533
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
492-667 |
1.36e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.37 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQHmfyipqrpymsLGSLRDQVIYPDSVD 570
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtIKLDGGDID-----------DPDVAEACHYLGHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 571 EMHD--------------KGYTDQDLECILRNVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMAR-MFYHKPKYaLLD 635
Cdd:PRK13539 83 AMKPaltvaenlefwaafLGGEELDIAAALEAVGLAPLAHLPFG---------YLSAGQKRRVALARlLVSNRPIW-ILD 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 586469518 636 ECTSAvsIDVEGK-----IFQA-AKGAGISLLSiTHRP 667
Cdd:PRK13539 153 EPTAA--LDAAAValfaeLIRAhLAQGGIVIAA-THIP 187
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
480-666 |
3.21e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.04 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 480 IICENVPIITPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPvYEGVLyK---------PPP---QHMFY 547
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSL-KingielrelDPEswrKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 548 IPQRPYMSLGSLRDQVIypdsvdeMHDKGYTDQDLECILRNVHLYHIVQR-EGGWD-AVMDWKDVLSGGEKQRMGMARMF 625
Cdd:PRK11174 428 VGQNPQLPHGTLRDNVL-------LGNPDASDEQLQQALENAWVSEFLPLlPQGLDtPIGDQAAGLSVGQAQRLALARAL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 586469518 626 YHKPKYALLDECTSAVSIDVEGKIFQAAKGA--GISLLSITHR 666
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQ 543
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
467-665 |
3.45e-14 |
|
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: 72.91 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 467 LTIKGnvIDVDHGIICENVPIItptgevvaSRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-------VLYK 539
Cdd:COG1124 2 LEVRN--LSVSYGQGGRRVPVL--------KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGevtfdgrPVTR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 540 PPPQHMF----YIPQRPYMSL---GSLRDQVIYPDSVdemHDKGYTDQDLECILRNVHLYhivqreggwDAVMD-WKDVL 611
Cdd:COG1124 72 RRRKAFRrrvqMVFQDPYASLhprHTVDRILAEPLRI---HGLPDREERIAELLEQVGLP---------PSFLDrYPHQL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 586469518 612 SGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKI---FQAAKGA-GISLLSITH 665
Cdd:COG1124 140 SGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEIlnlLKDLREErGLTYLFVSH 197
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
490-667 |
6.08e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 75.09 E-value: 6.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 490 PTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQHMF----------YIPQRPYMSLGS 558
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGeVTLDGVPVSSLdqdevrrrvsVCAQDAHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 559 LRDQVIY--PDSvdemhdkgyTDQDLECILRNVHLY-HIVQREGGWDAVM-DWKDVLSGGEKQRMGMARMFYHKPKYALL 634
Cdd:TIGR02868 425 VRENLRLarPDA---------TDEELWAALERVGLAdWLRALPDGLDTVLgEGGARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*
gi 586469518 635 DECTSAVSIDVEGKIFQ--AAKGAGISLLSITHRP 667
Cdd:TIGR02868 496 DEPTEHLDAETADELLEdlLAALSGRTVVLITHHL 530
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
492-665 |
8.42e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.28 E-value: 8.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL---------YKPPP--QHMFYIPQRPYMSLGSLR 560
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegedistLKPEIyrQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 561 DQVIYP-----DSVDEMH---DKGYTDQDLECILRNVhlyhivqreggwdavmdwkDVLSGGEKQRMGMARMFYHKPKYA 632
Cdd:PRK10247 99 DNLIFPwqirnQQPDPAIfldDLERFALPDTILTKNI-------------------AELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 586469518 633 LLDECTSAVS----IDVEGKIFQAAKGAGISLLSITH 665
Cdd:PRK10247 160 LLDEITSALDesnkHNVNEIIHRYVREQNIAVLWVTH 196
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
492-665 |
1.21e-13 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 71.27 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG---VLYKPPPQHMF---YIPQRPYMSLGslrdqviY 565
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGtvrLFGKPPRRARRrigYVPQRAEVDWD-------F 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 566 PDSVDEM------HDKG----YTDQDLECI---LRNVHLYHIVQR---EggwdavmdwkdvLSGGEKQRMGMARMFYHKP 629
Cdd:COG1121 91 PITVRDVvlmgryGRRGlfrrPSRADREAVdeaLERVGLEDLADRpigE------------LSGGQQQRVLLARALAQDP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 586469518 630 KYALLDECTSAVsiDVEG-----KIFQAAKGAGISLLSITH 665
Cdd:COG1121 159 DLLLLDEPFAGV--DAATeealyELLRELRREGKTILVVTH 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
499-665 |
1.26e-13 |
|
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: 69.35 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEG--MHLLitGPNGCGKSSLFRILSGLWPVYEG---VLYKPPP-------QHMFYIPQRPYmslgslrdqvIYP 566
Cdd:cd03230 19 ISLTVEKGeiYGLL--GPNGAGKTTLIKIILGLLKPDSGeikVLGKDIKkepeevkRRIGYLPEEPS----------LYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 567 D-SVDEmhdkgytdqdlecilrnvHLYhivqreggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDV 645
Cdd:cd03230 87 NlTVRE------------------NLK------------------LSGGMKQRLALAQALLHDPELLILDEPTSG--LDP 128
|
170 180
....*....|....*....|....*
gi 586469518 646 EG-----KIFQAAKGAGISLLSITH 665
Cdd:cd03230 129 ESrrefwELLRELKKEGKTILLSSH 153
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
499-669 |
1.47e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.37 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPPPQ--HMFY------IPQRPYMSLGSLRDQVIYpd 567
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgVPLVQydHHYLhrqvalVGQEPVLFSGSVRENIAY-- 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 568 svdemhdkGYTDQDLECILR-----NVHLYhIVQREGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLDECTSAV 641
Cdd:TIGR00958 578 --------GLTDTPDEEIMAaakaaNAHDF-IMEFPNGYDTEVGEKGSqLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180
....*....|....*....|....*...
gi 586469518 642 SIDVEGKIFQAAKGAGISLLSITHRPSL 669
Cdd:TIGR00958 649 DAECEQLLQESRSRASRTVLLIAHRLST 676
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
499-668 |
1.68e-13 |
|
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: 70.65 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL---------YKPP--PQHMFYIPQRPYMSLGSLRDQVIY-- 565
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdLNLRwlRSQIGLVSQEPVLFDGTIAENIRYgk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 566 PDSVDEMHDKGytdqdleCILRNVHLYhIVQREGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLDECTSAVSID 644
Cdd:cd03249 102 PDATDEEVEEA-------AKKANIHDF-IMSLPDGYDTLVGERGSqLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180
....*....|....*....|....*.
gi 586469518 645 VEGKIFQAAKGA--GISLLSITHRPS 668
Cdd:cd03249 174 SEKLVQEALDRAmkGRTTIVIAHRLS 199
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
489-636 |
3.93e-13 |
|
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: 69.04 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 489 TPTGEVVA-SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY-----KPPPQHMFYIPQR----PYMslg 557
Cdd:cd03293 12 GGGGAVTAlEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGeVLVdgepvTGPGPDRGYVFQQdallPWL--- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586469518 558 SLRDQVIYPDSVDEMHDKGYTDQDLECiLRNVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDE 636
Cdd:cd03293 89 TVLDNVALGLELQGVPKAEARERAEEL-LELVGLSGFENA---------YPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
480-670 |
4.23e-13 |
|
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: 72.24 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 480 IICENVPIITPTGEVVASR-LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWP---------VYEGV-LYKPPPQ----H 544
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDgVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrisgevLLDGRdLLELSEAlrgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 545 MFYIPQRPYMSLGSLR--DQVIYPDSVDEMHDKGYTDQDLEcILRNVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMA 622
Cdd:COG1123 85 IGMVFQDPMTQLNPVTvgDQIAEALENLGLSRAEARARVLE-LLEAVGLERRLDR---------YPHQLSGGQRQRVAIA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 586469518 623 RMFYHKPKYALLDECTSA----VSIDVEGKIFQAAKGAGISLLSITHRPSLW 670
Cdd:COG1123 155 MALALDPDLLIADEPTTAldvtTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
500-636 |
6.02e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 500 NFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLG-SLRDQVIYPDS-----VDEMH 573
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDlTVLDTVLDGDAelralEAELE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 574 ----DKGYTDQDLEcilRNVHLYHIVQREGGWDA------VM--------DW-KDV--LSGGEKQRMGMARMFYHKPKYA 632
Cdd:COG0488 98 eleaKLAEPDEDLE---RLAELQEEFEALGGWEAearaeeILsglgfpeeDLdRPVseLSGGWRRRVALARALLSEPDLL 174
|
....
gi 586469518 633 LLDE 636
Cdd:COG0488 175 LLDE 178
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
492-667 |
6.56e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 68.15 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKP---------PPQHMFYIPQRPYMSlGSLrd 561
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGeVRWNGtplaeqrdePHENILYLGHLPGLK-PEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 562 qviypdSVDE-----MHDKGYTDQDLECILRNVHLYHIVQREGGWdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDE 636
Cdd:TIGR01189 89 ------SALEnlhfwAAIHGGAQRTIEDALAAVGLTGFEDLPAAQ---------LSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 586469518 637 CTsaVSIDVEG-----KIFQAAKGAGISLLSITHRP 667
Cdd:TIGR01189 154 PT--TALDKAGvallaGLLRAHLARGGIVLLTTHQD 187
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
488-665 |
1.43e-12 |
|
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: 70.70 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 488 ITPTGEVVA-SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY-------------KPPPQHMFYIPQRP 552
Cdd:COG1123 272 VRGKGGVRAvDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGsILFdgkdltklsrrslRELRRRVQMVFQDP 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 553 YMSL---GSLRDQVIYPDSVDEMHDKGYTDQDLECILRNVHLYhivqreggwDAVMDWK-DVLSGGEKQRMGMARMFYHK 628
Cdd:COG1123 352 YSSLnprMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP---------PDLADRYpHELSGGQRQRVAIARALALE 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 586469518 629 PKYALLDECTSA--VSIdvegkifQA---------AKGAGISLLSITH 665
Cdd:COG1123 423 PKLLILDEPTSAldVSV-------QAqilnllrdlQRELGLTYLFISH 463
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
489-636 |
1.79e-12 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 68.19 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 489 TPTGEVVA-SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY------KPPPQHMFYIPQRPymslgSL-- 559
Cdd:COG1116 19 TGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvTGPGPDRGVVFQEP-----ALlp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 560 ----RDQVIYPDSVDEMhDKGYTDQDLECILRNVHLyhivqreggwDAVMD-WKDVLSGGEKQRMGMARMFYHKPKYALL 634
Cdd:COG1116 94 wltvLDNVALGLELRGV-PKAERRERARELLELVGL----------AGFEDaYPHQLSGGMRQRVAIARALANDPEVLLM 162
|
..
gi 586469518 635 DE 636
Cdd:COG1116 163 DE 164
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
495-649 |
2.09e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 495 VASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQR----PYMSLGSLRDQVIYPdsvd 570
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlyldTTLPLTVNRFLRLRP---- 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586469518 571 emhdkGYTDQDLECILRNVHLYHIVqreggwDAVMdwkDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVsiDVEGKI 649
Cdd:PRK09544 95 -----GTKKEDILPALKRVQAGHLI------DAPM---QKLSGGETQRVLLARALLNRPQLLVLDEPTQGV--DVNGQV 157
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
492-665 |
5.24e-12 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 66.24 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVA-SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG---VLYKPPP-------QHMFYIPQRPYMslgslr 560
Cdd:COG1131 11 GDKTAlDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGevrVLGEDVArdpaevrRRIGYVPQEPAL------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 561 dqviYPD-SVDEM---------HDKGYTDQDLECILRNVHLyhivqreggwDAVMDWK-DVLSGGEKQRMGMARMFYHKP 629
Cdd:COG1131 85 ----YPDlTVRENlrffarlygLPRKEARERIDELLELFGL----------TDAADRKvGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 586469518 630 KYALLDECTSAVsiDVEG-----KIFQAAKGAGIS-LLSiTH 665
Cdd:COG1131 151 ELLILDEPTSGL--DPEArrelwELLRELAAEGKTvLLS-TH 189
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
490-668 |
1.58e-11 |
|
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: 64.81 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 490 PTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VL-------------YKpppQHMFYIPQRPYMS 555
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrVLvdghdlaladpawLR---RQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 556 LGSLRDQVIYPDSVDEMHDKGYTDQdleciLRNVHLYhIVQREGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALL 634
Cdd:cd03252 89 NRSIRDNIALADPGMSMERVIEAAK-----LAGAHDF-ISELPEGYDTIVGEQGAgLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 586469518 635 DECTSAVSIDVEGKIFQAAKG--AGISLLSITHRPS 668
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDicAGRTVIIIAHRLS 198
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
492-666 |
2.18e-11 |
|
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: 62.83 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVA-SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhmfyipqrpymslgsLRDQVIYPDSVD 570
Cdd:cd03216 11 GGVKAlDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL--------------------VDGKEVSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 571 EMHDKGytdqdleciLRNVHlyhivQreggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSI-DVE--G 647
Cdd:cd03216 71 DARRAG---------IAMVY-----Q--------------LSVGERQMVEIARALARNARLLILDEPTAALTPaEVErlF 122
|
170
....*....|....*....
gi 586469518 648 KIFQAAKGAGISLLSITHR 666
Cdd:cd03216 123 KVIRRLRAQGVAVIFISHR 141
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
499-649 |
2.20e-11 |
|
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: 63.75 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLItGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPP---QHMFYIPQ--RPYMSLgSLRDQVIYP 566
Cdd:cd03264 19 VSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRidgqdvlKQPQklrRRIGYLPQefGVYPNF-TVREFLDYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 567 DSVDEMHDKGyTDQDLECILRNVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDECTsaVSIDVE 646
Cdd:cd03264 97 AWLKGIPSKE-VKARVDEVLELVNLGDRAKKKIG---------SLSGGMRRRVGIAQALVGDPSILIVDEPT--AGLDPE 164
|
...
gi 586469518 647 GKI 649
Cdd:cd03264 165 ERI 167
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
493-669 |
4.50e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 493 EVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLwpvyegvLYKPPPQHMFYIPQRPYMSLGSLRDQViypDSVDEM 572
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA-------LKGTPVAGCVDVPDNQFGREASLIDAI---GRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 573 HDKGYtdqdlecILRNVHLYhivqreggwDAVMdWK---DVLSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDVE--- 646
Cdd:COG2401 113 KDAVE-------LLNAVGLS---------DAVL-WLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSH--LDRQtak 173
|
170 180
....*....|....*....|....*.
gi 586469518 647 --GKIFQ-AAKGAGISLLSITHRPSL 669
Cdd:COG2401 174 rvARNLQkLARRAGITLVVATHHYDV 199
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
480-669 |
6.47e-11 |
|
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: 62.74 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 480 IICENVPIITPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY-------KPPP---QHMFYI 548
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGeVLVdgkditkKNLRelrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 549 PQRPymslgslRDQVIYPD--------------SVDEMHDKgyTDQdlecILRNVHLYHIVQReggwdAVMDwkdvLSGG 614
Cdd:COG1122 81 FQNP-------DDQLFAPTveedvafgpenlglPREEIRER--VEE----ALELVGLEHLADR-----PPHE----LSGG 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 615 EKQRMGMARMFYHKPKYALLDECTSavSIDVEGK-----IFQAAKGAGISLLSITHRPSL 669
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTA--GLDPRGRrelleLLKRLNKEGKTVIIVTHDLDL 196
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
490-665 |
7.02e-11 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 62.06 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 490 PTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSG-LWPVYEGVLYKPPP------------QHMFYIPQRPymsl 556
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGlLRPQSGAVLIDGEPldysrkgllerrQRVGLVFQDP---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 557 gslRDQVIYPDsvdemhdkgyTDQDLECILRNVHLY--HIVQREGGWDAVMDWKDV-------LSGGEKQRMGMARMFYH 627
Cdd:TIGR01166 78 ---DDQLFAAD----------VDQDVAFGPLNLGLSeaEVERRVREALTAVGASGLrerpthcLSGGEKKRVAIAGAVAM 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 586469518 628 KPKYALLDECTSAVsiDVEG-----KIFQAAKGAGISLLSITH 665
Cdd:TIGR01166 145 RPDVLLLDEPTAGL--DPAGreqmlAILRRLRAEGMTVVISTH 185
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
499-665 |
1.21e-10 |
|
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: 62.18 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY------KPPP---QHMFYIPQRPYMSLG-SLRDQViypd 567
Cdd:COG4555 20 VSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGsILIdgedvrKEPRearRQIGVLPDERGLYDRlTVRENI---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 568 svdEMHDKGYTDQDLECILRnvhLYHIVQREGGWDaVMD--WKDvLSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDV 645
Cdd:COG4555 96 ---RYFAELYGLFDEELKKR---IEELIELLGLEE-FLDrrVGE-LSTGMKKKVALARALVHDPKVLLLDEPTNG--LDV 165
|
170 180
....*....|....*....|....*
gi 586469518 646 EG-----KIFQAAKGAGISLLSITH 665
Cdd:COG4555 166 MArrllrEILRALKKEGKTVLFSSH 190
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
511-668 |
1.46e-10 |
|
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: 61.54 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 511 ITGPNGCGKSSLFRILSGLWPVYEGVLY-------------KPPPQ--HMFYIPQR----PYMS--------LGSLRDQV 563
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkiNLPPQqrKIGLVFQQyalfPHLNvrenlafgLKRKRNRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 564 IYpDSVDEMhdkgytdqdleciLRNVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSI 643
Cdd:cd03297 108 DR-ISVDEL-------------LDLLGLDHLLNR---------YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180
....*....|....*....|....*....
gi 586469518 644 DVEGKIF----QAAKGAGISLLSITHRPS 668
Cdd:cd03297 165 ALRLQLLpelkQIKKNLNIPVIFVTHDLS 193
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
492-666 |
2.89e-10 |
|
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: 60.76 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASR-LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL---YKP----PPQHMFYIPQR----PYMslgSL 559
Cdd:cd03269 11 GRVTALDdISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdGKPldiaARNRIGYLPEErglyPKM---KV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 560 RDQVIYPDSVdemhdKGYTDQDlecILRNVHLYhiVQREGgwdaVMDWKDV----LSGGEKQRMGMARMFYHKPKYALLD 635
Cdd:cd03269 88 IDQLVYLAQL-----KGLKKEE---ARRRIDEW--LERLE----LSEYANKrveeLSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190
....*....|....*....|....*....|....
gi 586469518 636 ECTSA---VSIDVEGKIFQAAKGAGISLLSITHR 666
Cdd:cd03269 154 EPFSGldpVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
492-665 |
3.26e-10 |
|
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: 60.81 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY--------KPPPQHMF-YIPQR----PYMSLG- 557
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditnLPPEKRDIsYVPQNyalfPHMTVYk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 558 ----SLRDQVIypdsvdemhDKGYTDQDLECILRNVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYAL 633
Cdd:cd03299 91 niayGLKKRKV---------DKKEIERKVLEIAEMLGIDHLLNRKPE---------TLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 586469518 634 LDECTSAVSIDVEGKIFQ----AAKGAGISLLSITH 665
Cdd:cd03299 153 LDEPFSALDVRTKEKLREelkkIRKEFGVTVLHVTH 188
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
499-672 |
4.31e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.85 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLwPVYE----GVLYKP------PPQH-----MFYIPQRPYmslgslrdqv 563
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEvtegEILFKGeditdlPPEErarlgIFLAFQYPP---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 564 iypdsvdEMHdkGYTDQDLeciLRNVHlyhivqrEGgwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSI 643
Cdd:cd03217 88 -------EIP--GVKNADF---LRYVN-------EG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190
....*....|....*....|....*....|..
gi 586469518 644 D---VEGKIFQAAKGAGISLLSITHRPSLWKY 672
Cdd:cd03217 138 DalrLVAEVINKLREEGKSVLIITHYQRLLDY 169
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
489-668 |
5.68e-10 |
|
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: 60.32 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 489 TPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-----------VLYKPPPQHMFYIPQRPYMSLG 557
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGrilidghdvrdYTLASLRRQIGLVSQDVFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 558 SLRDQVIYPDSvdemhdkGYTDQDLECILRNVHLYHIVQR-EGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLD 635
Cdd:cd03251 91 TVAENIAYGRP-------GATREEVEEAARAANAHEFIMElPEGYDTVIGERGVkLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 586469518 636 ECTSAVSIDVEgKIFQAAKG---AGISLLSITHRPS 668
Cdd:cd03251 164 EATSALDTESE-RLVQAALErlmKNRTTFVIAHRLS 198
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
499-661 |
8.19e-10 |
|
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: 59.37 E-value: 8.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKP------PPQHMF-----YIPQrpymslgslrDQVIYP 566
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsIRFDGrditglPPHERAragigYVPE----------GRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 567 D-SVDEmhdkgytdqdlecilrNVHLYHIVQREGGWDAVMDW--------KD-------VLSGGEKQRMGMARMFYHKPK 630
Cdd:cd03224 89 ElTVEE----------------NLLLGAYARRRAKRKARLERvyelfprlKErrkqlagTLSGGEQQMLAIARALMSRPK 152
|
170 180 190
....*....|....*....|....*....|....
gi 586469518 631 YALLDECTSAVSIDVEGKIFQAAKG---AGISLL 661
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRElrdEGVTIL 186
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
492-668 |
8.84e-10 |
|
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: 59.07 E-value: 8.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVA-SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPPQhmfyipQR------------ 551
Cdd:cd03259 11 GSVRAlDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrdvtGVPPE------RRnigmvfqdyalf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 552 PYMslgSLRDQVIYPDSVDEMhDKGYTDQDLECILRNVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKY 631
Cdd:cd03259 85 PHL---TVAENIAFGLKLRGV-PKAEIRARVRELLELVGLEGLLNR---------YPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 586469518 632 ALLDECTSAvsIDVE------GKIFQAAKGAGISLLSITHRPS 668
Cdd:cd03259 152 LLLDEPLSA--LDAKlreelrEELKELQRELGITTIYVTHDQE 192
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
499-666 |
8.87e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 58.96 E-value: 8.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY------KPPPQH-----MFYIPQRPYMSLGSLRDQViypD 567
Cdd:cd03369 27 VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidiSTIPLEdlrssLTIIPQDPTLFSGTIRSNL---D 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 568 SVDEmhdkgYTDQDLECILRnvhlyhivQREGGwdavmdwkDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEG 647
Cdd:cd03369 104 PFDE-----YSDEEIYGALR--------VSEGG--------LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180
....*....|....*....|.
gi 586469518 648 KIFQAAKG--AGISLLSITHR 666
Cdd:cd03369 163 LIQKTIREefTNSTILTIAHR 183
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
499-665 |
9.38e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.27 E-value: 9.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKpppQHMFYIPQRPYMSLGSLRDQVIYPDSVDEmhdkGY 577
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGhVHMK---GSVAYVPQQAWIQNDSLRENILFGKALNE----KY 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 578 TDQDLE-CILrnvhLYHIVQREGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQAAKG 655
Cdd:TIGR00957 730 YQQVLEaCAL----LPDLEILPSGDRTEIGEKGVnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIG 805
|
170
....*....|....*
gi 586469518 656 -----AGISLLSITH 665
Cdd:TIGR00957 806 pegvlKNKTRILVTH 820
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
492-666 |
1.17e-09 |
|
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: 59.37 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVA-SRLNFKVQEG-MHLLItGPNGCGKSSLFRILSGLWPVYEG-VLYK-------PPPQ--HM-----FYIPqRPYM 554
Cdd:cd03219 11 GGLVAlDDVSFSVRPGeIHGLI-GPNGAGKTTLFNLISGFLRPTSGsVLFDgeditglPPHEiaRLgigrtFQIP-RLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 555 SLgSLRDQVI---YPDSVDEMHDKGYTDQDLEC------ILRNVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMF 625
Cdd:cd03219 89 EL-TVLENVMvaaQARTGSGLLLARARREEREAreraeeLLERVGLADLADRPAG---------ELSYGQQRRLEIARAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 586469518 626 YHKPKYALLDECTSAVS---IDVEGKIFQAAKGAGISLLSITHR 666
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNpeeTEELAELIRELRERGITVLLVEHD 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
489-665 |
1.32e-09 |
|
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: 59.06 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 489 TPTGEVVA-SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYK-----PPPQHMF--------YIPQRPY 553
Cdd:cd03257 13 TGGGSVKAlDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGsIIFDgkdllKLSRRLRkirrkeiqMVFQDPM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 554 MSLG---SLRDQVIYPDSVdemHDKGYTDQDLECI----LRNVHLYhivqreggwDAVMDWK-DVLSGGEKQRMGMARMF 625
Cdd:cd03257 93 SSLNprmTIGEQIAEPLRI---HGKLSKKEARKEAvlllLVGVGLP---------EEVLNRYpHELSGGQRQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 586469518 626 YHKPKYALLDECTSAVSIDVEGKI----FQAAKGAGISLLSITH 665
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQIldllKKLQEELGLTLLFITH 204
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
494-682 |
1.41e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.61 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 494 VVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLGSLRDQVIYPD--SVDE 571
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdiTVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 572 MHDKG-YTDQDLECILRNVH---LYHIVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAV----SI 643
Cdd:PRK10253 101 LVARGrYPHQPLFTRWRKEDeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLdishQI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 586469518 644 DVEGKIFQAAKGAGISLLSITHR-PSLWKYHTHLLQF-DGE 682
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALrEGK 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
497-667 |
1.61e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 497 SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPP---------QHMFYIPQRPymslGslrdqvIYP 566
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGeVLWQGEPirrqrdeyhQDLLYLGHQP----G------IKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 567 D-SVDE-------MHDKgYTDQDLECILRNVHLyhiVQREggwdavmdwkDV----LSGGEKQRMGMARMFYHKPKYALL 634
Cdd:PRK13538 88 ElTALEnlrfyqrLHGP-GDDEALWEALAQVGL---AGFE----------DVpvrqLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 586469518 635 DECTSAvsIDVEG-KIFQA-----AKGAGISLLSiTHRP 667
Cdd:PRK13538 154 DEPFTA--IDKQGvARLEAllaqhAEQGGMVILT-THQD 189
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
499-677 |
2.62e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.54 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEG-MHLlITGPNGCGKSSLFRILSGLwPVYE---G-VLYK-------PPPQH----MFYIPQRP---------- 552
Cdd:COG0396 19 VNLTIKPGeVHA-IMGPNGSGKSTLAKVLMGH-PKYEvtsGsILLDgedilelSPDERaragIFLAFQYPveipgvsvsn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 553 --YMSLGSLRDQVIY-PDSVDEMHDKGYT---DQDLecILRNVHlyhivqrEGgwdavmdwkdvLSGGEKQRMGMARMFY 626
Cdd:COG0396 97 flRTALNARRGEELSaREFLKLLKEKMKElglDEDF--LDRYVN-------EG-----------FSGGEKKRNEILQMLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 586469518 627 HKPKYALLDECTSAVSID---VEGKIFQAAKGAGISLLSITHRPSLWKY----HTHLL 677
Cdd:COG0396 157 LEPKLAILDETDSGLDIDalrIVAEGVNKLRSPDRGILIITHYQRILDYikpdFVHVL 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
492-669 |
2.63e-09 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 58.13 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVA-SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY--------KPPPQ-------HMFYIPQR---- 551
Cdd:COG1136 19 GEVTAlRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdissLSERElarlrrrHIGFVFQFfnll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 552 PYMSLgslRDQVIYPDSVDEMHDKGyTDQDLECILRNVHLYHIvqreggwdavMDWK-DVLSGGEKQRMGMARMFYHKPK 630
Cdd:COG1136 99 PELTA---LENVALPLLLAGVSRKE-RRERARELLERVGLGDR----------LDHRpSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 586469518 631 YALLDECTSAV----SIDVEGKIFQAAKGAGISLLSITHRPSL 669
Cdd:COG1136 165 LILADEPTGNLdsktGEEVLELLRELNRELGTTIVMVTHDPEL 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
493-666 |
3.36e-09 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 56.94 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 493 EVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPPP-------QHMFYIPQRPYMSLGSLRDQ 562
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITldgVPVSdlekalsSLISVLNQRPYLFDTTLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 563 VIYPdsvdemhdkgytdqdlecilrnvhlyhivqreggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTsaVS 642
Cdd:cd03247 95 LGRR--------------------------------------------FSGGERQRLALARILLQDAPIVLLDEPT--VG 128
|
170 180 190
....*....|....*....|....*....|
gi 586469518 643 IDVEGK------IFQAAKGAgiSLLSITHR 666
Cdd:cd03247 129 LDPITErqllslIFEVLKDK--TLIWITHH 156
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
477-652 |
3.49e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.69 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 477 DHGIICENVPI-ITPtgevVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLykpppQH---MFYIPQRP 552
Cdd:TIGR01271 426 DDGLFFSNFSLyVTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----KHsgrISFSPQTS 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 553 YMSLGSLRDQVIYPDSVDEMHdkgYTDQDLECILR-NVHLY----HIVQREGGWdavmdwkdVLSGGEKQRMGMARMFYH 627
Cdd:TIGR01271 497 WIMPGTIKDNIIFGLSYDEYR---YTSVIKACQLEeDIALFpekdKTVLGEGGI--------TLSGGQRARISLARAVYK 565
|
170 180
....*....|....*....|....*
gi 586469518 628 KPKYALLDECTSAVSIDVEGKIFQA 652
Cdd:TIGR01271 566 DADLYLLDSPFTHLDVVTEKEIFES 590
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
494-665 |
4.07e-09 |
|
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: 57.44 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 494 VVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY----------KPPPQHMFYipqrpymslgsLRDQ 562
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsILVrhdggwvdlaQASPREILA-----------LRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 563 VIypdsvdemhdkGYTDQDLECILRnVHLYHIVQ---REGGWD---AVMDWKDVL-----------------SGGEKQRM 619
Cdd:COG4778 94 TI-----------GYVSQFLRVIPR-VSALDVVAeplLERGVDreeARARARELLarlnlperlwdlppatfSGGEQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 586469518 620 GMARMFYHKPKYALLDECTSavSIDVEGK-----IFQAAKGAGISLLSITH 665
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTA--SLDAANRavvveLIEEAKARGTAIIGIFH 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
492-636 |
5.04e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.89 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASR-LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKpPPQHMFYIP--QRpymSLGSL-RDQVIYP- 566
Cdd:PRK11000 14 GDVVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRMNDVPpaER---GVGMVfQSYALYPh 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586469518 567 -DSVDEMH--------DKGYTDQDLECILRNVHLYHIVQREGgwdavmdwKDvLSGGEKQRMGMARMFYHKPKYALLDE 636
Cdd:PRK11000 90 lSVAENMSfglklagaKKEEINQRVNQVAEVLQLAHLLDRKP--------KA-LSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
511-667 |
8.04e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.36 E-value: 8.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 511 ITGPNGCGKSSLFRILSGLWPVYEG-------VLY-------------KPPPQHMFYIPQrPYMSLgSLRDQVIYPDSVD 570
Cdd:PRK14246 41 IMGPSGSGKSTLLKVLNRLIEIYDSkikvdgkVLYfgkdifqidaiklRKEVGMVFQQPN-PFPHL-SIYDNIAYPLKSH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 571 EMHDKGYTDQDLECILRNVHLYHIVqreggWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSI----DVE 646
Cdd:PRK14246 119 GIKEKREIKKIVEECLRKVGLWKEV-----YDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIvnsqAIE 193
|
170 180
....*....|....*....|.
gi 586469518 647 GKIFQAAKGAGISLLSitHRP 667
Cdd:PRK14246 194 KLITELKNEIAIVIVS--HNP 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
499-665 |
9.53e-09 |
|
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: 56.71 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGL-WPVYEGVLYK------PPPQHMFYIPQRPYMSLGSLRDQVIYpdSVDE 571
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEgkqitePGPDRMVVFQNYSLLPWLTVRENIAL--AVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 572 -MHDKGYTDQdlECILRnvhlyHIVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSI----DVE 646
Cdd:TIGR01184 82 vLPDLSKSER--RAIVE-----EHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgNLQ 154
|
170
....*....|....*....
gi 586469518 647 GKIFQAAKGAGISLLSITH 665
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTH 173
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
498-640 |
1.11e-08 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 56.66 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 498 RLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY--KP----PPQH-------MfyiPQRPYMSLGSLRDQV 563
Cdd:COG4559 19 DVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGeVRLngRPlaawSPWElarrravL---PQHSSLAFPFTVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 564 I----YPDSVDEMHDkgytDQDLECILRNVHLYHIVQReggwdavmDWKDvLSGGEKQRMGMAR-------MFYHKPKYA 632
Cdd:COG4559 96 ValgrAPHGSSAAQD----RQIVREALALVGLAHLAGR--------SYQT-LSGGEQQRVQLARvlaqlwePVDGGPRWL 162
|
....*...
gi 586469518 633 LLDECTSA 640
Cdd:COG4559 163 FLDEPTSA 170
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
499-665 |
1.16e-08 |
|
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: 55.27 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLwpvyegvlyKPPPQHMFYIPQRPYMSLGSLRdqviypdsVDEMHDKGYT 578
Cdd:cd03229 19 VSLNIEAGEIVALLGPSGSGKSTLLRCIAGL---------EEPDSGSILIDGEDLTDLEDEL--------PPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 579 DQDLecilrnvhlyhivqreggwdAVMDWKDV-------LSGGEKQRMGMARMFYHKPKYALLDECTSA----VSIDVEG 647
Cdd:cd03229 82 FQDF--------------------ALFPHLTVlenialgLSGGQQQRVALARALAMDPDVLLLDEPTSAldpiTRREVRA 141
|
170
....*....|....*...
gi 586469518 648 KIFQAAKGAGISLLSITH 665
Cdd:cd03229 142 LLKSLQAQLGITVVLVTH 159
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
511-638 |
1.16e-08 |
|
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: 58.41 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 511 ITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPY------------MSLGSLRDQViypDSVDEMHDKgYT 578
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQldptktvrenveEGVAEIKDAL---DRFNEISAK-YA 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586469518 579 DQDLE---CILRNVHLYHIVQREGGWDA------VMD------WK-DV--LSGGEKQRMGMARMFYHKPKYALLDECT 638
Cdd:TIGR03719 112 EPDADfdkLAAEQAELQEIIDAADAWDLdsqleiAMDalrcppWDaDVtkLSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
513-649 |
1.21e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.71 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 513 GPNGCGKSSLFRIL---SGLWP---VYEGVLYKpppQHMFYIP---------------QRPYMSLGSLRDQVIYPDSVDE 571
Cdd:PRK14239 38 GPSGSGKSTLLRSInrmNDLNPevtITGSIVYN---GHNIYSPrtdtvdlrkeigmvfQQPNPFPMSIYENVVYGLRLKG 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586469518 572 MHDKGYTDQDLECILRNVHLYHIVQreggwDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKI 649
Cdd:PRK14239 115 IKDKQVLDEAVEKSLKGASIWDEVK-----DRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKI 187
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
480-638 |
1.24e-08 |
|
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: 54.38 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 480 IICENVPIITPtGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQrpymslgsl 559
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586469518 560 rdqviypdsvdemhdkgytdqdlecilrnvhlyhivqreggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECT 638
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
492-636 |
2.66e-08 |
|
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: 54.95 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVA-SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPPQH----MFYipQR----PYMs 555
Cdd:cd03301 11 GNVTAlDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtDLPPKDrdiaMVF--QNyalyPHM- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 556 lgSLRDQVIYPDSVDEMhDKGYTDQDLECILRNVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKPKYALLD 635
Cdd:cd03301 88 --TVYDNIAFGLKLRKV-PKDEIDERVREVAELLQIEHLLDRK---------PKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
.
gi 586469518 636 E 636
Cdd:cd03301 156 E 156
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
492-640 |
2.88e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.49 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPPQH-----------MFyipqrPY 553
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMldgqditHVPAENrhvntvfqsyaLF-----PH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 554 MSLgslRDQVIY-------PDS-----VDEMhdkgytdqdleciLRNVHLYHIVQREggwdavmdwKDVLSGGEKQRMGM 621
Cdd:PRK09452 101 MTV---FENVAFglrmqktPAAeitprVMEA-------------LRMVQLEEFAQRK---------PHQLSGGQQQRVAI 155
|
170
....*....|....*....
gi 586469518 622 ARMFYHKPKYALLDECTSA 640
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSA 174
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
492-665 |
3.33e-08 |
|
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: 54.94 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQHMFYIPQR------------PYMSLGs 558
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGeILLDGKDITNLPPHKRpvntvfqnyalfPHLTVF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 559 lrDQVIYPDSVDEMhDKGYTDQDLECILRNVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKPKYALLDECT 638
Cdd:cd03300 91 --ENIAFGLRLKKL-PKAEIKERVAEALDLVQLEGYANRK---------PSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|...
gi 586469518 639 SAV------SIDVEGKIFQaaKGAGISLLSITH 665
Cdd:cd03300 159 GALdlklrkDMQLELKRLQ--KELGITFVFVTH 189
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
492-667 |
4.50e-08 |
|
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: 54.71 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSG-LWPVYEGVLY--------------KPppqHMFYI-P--QRPY 553
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRlfgerrggedvwelRK---RIGLVsPalQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 554 MSLGSLRDQVI---YpDSVDeMHDKgYTDQDLE---CILRNVHLYHIVQREggwdavmdWKDvLSGGEKQRMGMARMFYH 627
Cdd:COG1119 92 PRDETVLDVVLsgfF-DSIG-LYRE-PTDEQRErarELLELLGLAHLADRP--------FGT-LSQGEQRRVLIARALVK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 586469518 628 KPKYALLDECTSavSIDVEGK------IFQAAKGAGISLLSITHRP 667
Cdd:COG1119 160 DPELLILDEPTA--GLDLGARelllalLDKLAAEGAPTLVLVTHHV 203
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
495-652 |
6.67e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 54.86 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 495 VASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLykpppQH---MFYIPQRPYMSLGSLRDQVIYPDSVDE 571
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----KHsgrISFSSQFSWIMPGTIKENIIFGVSYDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 572 MHDKGYTD--QDLECILRNVHLYHIVQREGGWdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKI 649
Cdd:cd03291 127 YRYKSVVKacQLEEDITKFPEKDNTVLGEGGI--------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
...
gi 586469518 650 FQA 652
Cdd:cd03291 199 FES 201
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
495-665 |
7.70e-08 |
|
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: 53.37 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 495 VASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL---------YKPPPQHMFYIPQRP--YMSLgSLRDQV 563
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItfdgksyqkNIEALRRIGALIEAPgfYPNL-TARENL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 564 IYPDSVdemhdKGYTDQDLECILRNVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDECTSAvsI 643
Cdd:cd03268 94 RLLARL-----LGIRKKRIDEVLDVVGLKDSAKKKVK---------GFSLGMKQRLGIALALLGNPDLLILDEPTNG--L 157
|
170 180
....*....|....*....|....*..
gi 586469518 644 DVEG-----KIFQAAKGAGISLLSITH 665
Cdd:cd03268 158 DPDGikelrELILSLRDQGITVLISSH 184
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
492-666 |
2.18e-07 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 54.36 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPP----------QHMFYIPQRPYMSLGSLR 560
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGeILLNGFSlkdidrhtlrQFINYLPQEPYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 561 DQVIY---PDSVDEMHDKGYTDQDLECILRNVHL-YHIVQREGGWDavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDE 636
Cdd:TIGR01193 566 ENLLLgakENVSQDEIWAACEIAEIKDDIENMPLgYQTELSEEGSS--------ISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190
....*....|....*....|....*....|
gi 586469518 637 CTSAVSIDVEGKIFQaakgagiSLLSITHR 666
Cdd:TIGR01193 638 STSNLDTITEKKIVN-------NLLNLQDK 660
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
492-666 |
3.77e-07 |
|
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: 51.77 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVAsrlnfkvqegmhLLitGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPPQH-----MFYIPQRP--YMSLg 557
Cdd:cd03218 26 GEIVG------------LL--GPNGAGKTTTFYMIVGLVKPDSGKILldgqditKLPMHKrarlgIGYLPQEAsiFRKL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 558 SLRDQVIypdSVDEMHDKGYTDQD--LECILRNVHLYHIVQREGgwdavmdwkDVLSGGEKQRMGMARMFYHKPKYALLD 635
Cdd:cd03218 91 TVEENIL---AVLEIRGLSKKEREekLEELLEEFHITHLRKSKA---------SSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 586469518 636 ECTSAVS----IDVEGKI-FQAAKGAGI--------SLLSITHR 666
Cdd:cd03218 159 EPFAGVDpiavQDIQKIIkILKDRGIGVlitdhnvrETLSITDR 202
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
495-713 |
6.56e-07 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 51.34 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 495 VASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLwpvyegvlYKPPPQHMFYIPQRPYMSLGSLRD------QVIYPDS 568
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL--------EKPAQGTVSFRGQDLYQLDRKQRRafrrdvQLVFQDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 569 VDEMHDKGYTDQDLECILRNV----------HLYHIVQREGGWDAVMD-WKDVLSGGEKQRMGMARMFYHKPKYALLDEC 637
Cdd:TIGR02769 98 PSAVNPRMTVRQIIGEPLRHLtsldeseqkaRIAELLDMVGLRSEDADkLPRQLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 638 TSAVSIDVEGKIFQAAKG----AGISLLSITHRPSL-WKYHTHLLQFDgeGGWRFEQLDTAIRLTLSEE--KQKLESQLA 710
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKlqqaFGTAYLFITHDLRLvQSFCQRVAVMD--KGQIVEECDVAQLLSFKHPagRNLQSAVLP 255
|
...
gi 586469518 711 GVP 713
Cdd:TIGR02769 256 EHP 258
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
480-669 |
7.75e-07 |
|
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: 51.03 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 480 IICENVPIITPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhmFY---IPQRPYMSL 556
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL-------IDgtdINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 557 GSLRDQViypdsvdemhdkGYTDQDLECILR-----NV---------------HLYHIVQREGGWDAV----MDWK---- 608
Cdd:cd03256 74 RQLRRQI------------GMIFQQFNLIERlsvleNVlsgrlgrrstwrslfGLFPKEEKQRALAALervgLLDKayqr 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586469518 609 -DVLSGGEKQRMGMARMFYHKPKYALLDECTSAV----SIDVEGKIFQAAKGAGISLLSITHRPSL 669
Cdd:cd03256 142 aDQLSGGQQQRVAIARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLHQVDL 207
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
497-652 |
9.07e-07 |
|
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: 50.41 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 497 SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPPPQHMF------------YIPQRPYMSLGSLRD 561
Cdd:cd03290 18 SNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnKNESEPSFeatrsrnrysvaYAAQKPWLLNATVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 562 QVIYPDSVDEMHDKGYTDQdleCILR-NVHLY-HIVQREGGWDAVMdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTS 639
Cdd:cd03290 98 NITFGSPFNKQRYKAVTDA---CSLQpDIDLLpFGDQTEIGERGIN-----LSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170
....*....|...
gi 586469518 640 AVSIDVEGKIFQA 652
Cdd:cd03290 170 ALDIHLSDHLMQE 182
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
470-665 |
1.07e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 50.95 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 470 KGNVIDVDHgiicenVPIITPTGEV-VASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGL------------------- 529
Cdd:PRK13640 2 KDNIVEFKH------VSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnskitvdgitlt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 530 ----WPVYE--GVLYKPPPQHMFYipqrpymslGSLRDQVIYpdsvdEMHDKGYTDQDLECILRNVhlyhiVQREGGWDA 603
Cdd:PRK13640 76 aktvWDIREkvGIVFQNPDNQFVG---------ATVGDDVAF-----GLENRAVPRPEMIKIVRDV-----LADVGMLDY 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586469518 604 VMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDVEGK------IFQAAKGAGISLLSITH 665
Cdd:PRK13640 137 IDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSM--LDPAGKeqilklIRKLKKKNNLTVISITH 202
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
492-665 |
1.08e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 50.66 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV------------LYKPPPQHMFYIPQRPYMslgsL 559
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddedisllpLHARARRGIGYLPQEASI----F 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 560 RDQVIYPD--SVDEMHDKGYTDQD---LECILRNVHLYHIVQREGgwdavmdwkDVLSGGEKQRMGMARMFYHKPKYALL 634
Cdd:PRK10895 91 RRLSVYDNlmAVLQIRDDLSAEQRedrANELMEEFHIEHLRDSMG---------QSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 586469518 635 DECTSAVS----IDVEgKIFQAAKGAGISLLSITH 665
Cdd:PRK10895 162 DEPFAGVDpisvIDIK-RIIEHLRDSGLGVLITDH 195
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
492-636 |
1.32e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.60 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRpymslgslRDQVIYPDSV-D 570
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQH--------QEELDPDKTVlD 398
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 571 EMHDkGYTDqdleciLRNVHLYHIVQREG--GWDAvmdWK--DVLSGGEKQRMGMARMFYHKPKYALLDE 636
Cdd:COG0488 399 ELRD-GAPG------GTEQEVRGYLGRFLfsGDDA---FKpvGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
480-638 |
1.42e-06 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 50.05 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 480 IICENVPIITPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhMF-----YIPQR--P 552
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVL------VNgqdlsRLKRReiP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 553 YM--SLGslrdqVIYPD-------SVDE-----MHDKGYTDQDlecILRNVHlyhivqreggwdAVMDW-----K----- 608
Cdd:COG2884 76 YLrrRIG-----VVFQDfrllpdrTVYEnvalpLRVTGKSRKE---IRRRVR------------EVLDLvglsdKakalp 135
|
170 180 190
....*....|....*....|....*....|
gi 586469518 609 DVLSGGEKQRMGMARMFYHKPKYALLDECT 638
Cdd:COG2884 136 HELSGGEQQRVAIARALVNRPELLLADEPT 165
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
499-669 |
1.90e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.49 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLwpvyegvlYKPPPQHMFY----IPQRPYMSLGSLRDQV--IYPDSVDEM 572
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGI--------ERPSAGKIWFsghdITRLKNREVPFLRRQIgmIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 573 HDKGYTDQDLECILRNVHLYHIVQRE-------GGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECT----SAV 641
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDDIRRRVsaaldkvGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTgnldDAL 172
|
170 180
....*....|....*....|....*...
gi 586469518 642 SIDVEgKIFQAAKGAGISLLSITHRPSL 669
Cdd:PRK10908 173 SEGIL-RLFEEFNRVGVTVLMATHDIGL 199
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
488-665 |
1.98e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 49.40 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 488 ITPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSG-LWPV--YEGVLY--------KPPPQ-HMFYIPQR---- 551
Cdd:COG4136 9 ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLlngrrltaLPAEQrRIGILFQDdllf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 552 PYMSLG-------------SLRDQVIypdsvdemhdkgytDQDLEcilrNVHLYHIVQReggwdavmdwkDV--LSGGEK 616
Cdd:COG4136 89 PHLSVGenlafalpptigrAQRRARV--------------EQALE----EAGLAGFADR-----------DPatLSGGQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 586469518 617 QRMGMARMFYHKPKYALLDECTS----AVSIDVEGKIFQAAKGAGISLLSITH 665
Cdd:COG4136 140 ARVALLRALLAEPRALLLDEPFSkldaALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
499-652 |
2.31e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 51.12 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILsglwpvyegvlykpppqHMFYIPQRPY----------MSLGSLRD------- 561
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLL-----------------QRVFDPQSGRilidgtdirtVTRASLRRniavvfq 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 562 -------------QVIYPDSVD-EMHDKGYTDQDLECILRnvhlyhivqREGGWDAVMDWK-DVLSGGEKQRMGMARMFY 626
Cdd:PRK13657 417 daglfnrsiedniRVGRPDATDeEMRAAAERAQAHDFIER---------KPDGYDTVVGERgRQLSGGERQRLAIARALL 487
|
170 180
....*....|....*....|....*.
gi 586469518 627 HKPKYALLDECTSAVSIDVEGKIFQA 652
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAA 513
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
495-665 |
2.40e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 49.68 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 495 VASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQH--------MF----YIPQRpymslgslrd 561
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGeLLAGTAPLAearedtrlMFqdarLLPWK---------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 562 QVIypDSVDEMHDKGYTDQDLECiLRNVHLYhivqreggwDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAV 641
Cdd:PRK11247 97 KVI--DNVGLGLKGQWRDAALQA-LAAVGLA---------DRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180
....*....|....*....|....*...
gi 586469518 642 S----IDVEGKIFQAAKGAGISLLSITH 665
Cdd:PRK11247 165 DaltrIEMQDLIESLWQQHGFTVLLVTH 192
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
499-681 |
2.47e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.08 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPP-----PQHMFYIPQrpymsLGSLRDQViypDSVD 570
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQidgKTAtrgdrSRFMAYLGH-----LPGLKADL---STLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 571 EMHdkgytdqdlecILRNVHLYHIVQREGGWDAVM---DWKDV----LSGGEKQRMGMARMFYHKPKYALLDEctSAVSI 643
Cdd:PRK13543 102 NLH-----------FLCGLHGRRAKQMPGSALAIVglaGYEDTlvrqLSAGQKKRLALARLWLSPAPLWLLDE--PYANL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 586469518 644 DVEG-----KIFQAAKGAGISLLSITH--RPSLwKYHTHLLQFDG 681
Cdd:PRK13543 169 DLEGitlvnRMISAHLRGGGAALVTTHgaYAAP-PVRTRMLTLEA 212
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
492-677 |
2.72e-06 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 48.38 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRpymslGSLRDQviYPDSVDE 571
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR-----SEVPDS--LPLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 572 MHDKG----------YTDQD---LECILRNVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKPKYALLDECT 638
Cdd:NF040873 77 LVAMGrwarrglwrrLTRDDraaVDDALERVGLADLAGRQ---------LGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 586469518 639 SAVSIDVEGKIFQ---AAKGAGISLLSITHRPSLWKYHTHLL 677
Cdd:NF040873 148 TGLDAESRERIIAllaEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
499-668 |
2.96e-06 |
|
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: 50.59 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGlwpvyegvlykpppqhmFYIPQ-----------RPYmSLGSLR------- 560
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFR-----------------FYDVTsgrilidgqdiRDV-TQASLRaaigivp 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 561 -DQVIYPDSVdemhdkGY---------TDQDLECILRNVHLYHIVQR-EGGWDAVmdwkdV------LSGGEKQRMGMAR 623
Cdd:COG5265 439 qDTVLFNDTI------AYniaygrpdaSEEEVEAAARAAQIHDFIESlPDGYDTR-----VgerglkLSGGEKQRVAIAR 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 586469518 624 MFYHKPKYALLDECTSAVSIDVEGKIFQAAK--GAGISLLSITHRPS 668
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALRevARGRTTLVIAHRLS 554
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
490-648 |
4.63e-06 |
|
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: 48.27 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 490 PTGEVVA-SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY----------KPPPQHMFYIPQrpymslgs 558
Cdd:cd03263 11 KKGTKPAvDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYingysirtdrKAARQSLGYCPQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 559 lrDQVIYPD-SVDEMhdkgytdqdLE--CILRNVHLYHIvQREGGWDAVM----DWKDV----LSGGEKQRMGMARMFYH 627
Cdd:cd03263 83 --FDALFDElTVREH---------LRfyARLKGLPKSEI-KEEVELLLRVlgltDKANKrartLSGGMKRKLSLAIALIG 150
|
170 180
....*....|....*....|.
gi 586469518 628 KPKYALLDECTSavSIDVEGK 648
Cdd:cd03263 151 GPSVLLLDEPTS--GLDPASR 169
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
492-665 |
4.75e-06 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 48.88 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVA-SRLNFKVQEG-MHLLItGPNGCGKSSLFRILSGLWPVYEG-VLYK-------PPPQ--HM-----FYIPQ---- 550
Cdd:COG0411 15 GGLVAvDDVSLEVERGeIVGLI-GPNGAGKTTLFNLITGFYRPTSGrILFDgrditglPPHRiaRLgiartFQNPRlfpe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 551 --------------RPYMSLGSLRDQVIYPDSVDEMHDKGYTdqdlecILRNVHLYHIVQREGGwdavmdwkdVLSGGEK 616
Cdd:COG0411 94 ltvlenvlvaaharLGRGLLAALLRLPRARREEREARERAEE------LLERVGLADRADEPAG---------NLSYGQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 586469518 617 QRMGMARMFYHKPKYALLDECTSAVSI----DVEGKIFQAAKGAGISLLSITH 665
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPeeteELAELIRRLRDERGITILLIEH 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
499-665 |
5.82e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 48.86 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLykpppqhmfyipqrpymslgSLRDQVIYPDSVDEMHDK--- 575
Cdd:PRK13635 26 VSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI--------------------TVGGMVLSEETVWDVRRQvgm 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 576 ----------GYTDQD-----LECI--------------LRNVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFY 626
Cdd:PRK13635 86 vfqnpdnqfvGATVQDdvafgLENIgvpreemvervdqaLRQVGMEDFLNRE---------PHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 586469518 627 HKPKYALLDECTSAVS----IDVEGKIFQAAKGAGISLLSITH 665
Cdd:PRK13635 157 LQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITH 199
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
490-668 |
6.20e-06 |
|
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: 49.72 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 490 PTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG--VLYKPPPQHMfyipqrpymSLGSLRDQV---- 563
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGqiLLDGHDLADY---------TLASLRRQValvs 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 564 ----IYPDSVDEMHDKGYTDQ----DLECILRNVHLYHIVQR-EGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYAL 633
Cdd:TIGR02203 413 qdvvLFNDTIANNIAYGRTEQadraEIERALAAAYAQDFVDKlPLGLDTPIGENGVlLSGGQRQRLAIARALLKDAPILI 492
|
170 180 190
....*....|....*....|....*....|....*...
gi 586469518 634 LDECTSAVSIDVEGKIfQAAKGA---GISLLSITHRPS 668
Cdd:TIGR02203 493 LDEATSALDNESERLV-QAALERlmqGRTTLVIAHRLS 529
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
467-677 |
8.78e-06 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 47.64 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 467 LTIKGNVIDVDHGIICENVPIITPTGEVVAsrlnfkvqegmhllITGPNGCGKSSLFRILSGlWPVYEgvlykpppqhmf 546
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHA--------------IMGPNGSGKSTLSKTIAG-HPSYE------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 547 yipqrpyMSLGS--LRDQVIYPDSVDEMHDKGY-------------TDQDLeciLRNVhlYHIVQREGGWDA--VMDWKD 609
Cdd:TIGR01978 54 -------VTSGTilFKGQDLLELEPDERARAGLflafqypeeipgvSNLEF---LRSA--LNARRSARGEEPldLLDFEK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 610 VL----------------------SGGEKQRMGMARMFYHKPKYALLDECTSAVSID-----VEGkiFQAAKGAGISLLS 662
Cdd:TIGR01978 122 LLkeklalldmdeeflnrsvnegfSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDalkivAEG--INRLREPDRSFLI 199
|
250
....*....|....*....
gi 586469518 663 ITHRPSLWKY----HTHLL 677
Cdd:TIGR01978 200 ITHYQRLLNYikpdYVHVL 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
511-641 |
1.41e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 47.31 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 511 ITGPNGCGKSSLFRILSGLW-PVYEGVLYKPPPqhMFYIPQrpymSLGSLRDQV--IYPDSVDEMHdkgYT--DQDLECI 585
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKP--LDYSKR----GLLALRQQVatVFQDPEQQIF---YTdiDSDIAFS 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586469518 586 LRN--VHLYHIVQREGGWDAVMDWK-------DVLSGGEKQRMGMARMFYHKPKYALLDECTSAV 641
Cdd:PRK13638 103 LRNlgVPEAEITRRVDEALTLVDAQhfrhqpiQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
498-687 |
1.84e-05 |
|
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: 48.01 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 498 RLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQrpymSLGSLRD-----QVIyPDSVD-- 570
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQ----SRDALDPnktvwEEI-SGGLDii 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 571 -----EMHDKGY--------TDQdlecilrnvhlyhivQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDEC 637
Cdd:TIGR03719 415 klgkrEIPSRAYvgrfnfkgSDQ---------------QKKVG---------QLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 586469518 638 TSavSIDVEgkIFQAAKGA-----GISLLsITH-RPSLWKYHTHLLQFDGEGGWRF 687
Cdd:TIGR03719 471 TN--DLDVE--TLRALEEAllnfaGCAVV-ISHdRWFLDRIATHILAFEGDSHVEW 521
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
499-668 |
1.99e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 46.76 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV------------LYKPPPQ---------HMFYIPQrPYMSLg 557
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEArvegevrlfgrnIYSPDVDpievrrevgMVFQYPN-PFPHL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 558 SLRDQVIYPDSVDEM-HDKGYTDQDLECILRNVHLYHIVQreggwDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDE 636
Cdd:PRK14267 101 TIYDNVAIGVKLNGLvKSKKELDERVEWALKKAALWDEVK-----DRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 586469518 637 CTSAV----SIDVEGKIFQAAKGAGISLlsITHRPS 668
Cdd:PRK14267 176 PTANIdpvgTAKIEELLFELKKEYTIVL--VTHSPA 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
478-668 |
2.32e-05 |
|
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: 46.00 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 478 HGIICENVPIITPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGL--WPVYEG-VLYKPPPQHMF-------Y 547
Cdd:cd03213 7 RNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGeVLINGRPLDKRsfrkiigY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 548 IPQrpymslgslrDQVIYPD-SVDEMhdkgytdqdlecilrnvhLYHIVQREGgwdavmdwkdvLSGGEKQRMGMARMFY 626
Cdd:cd03213 87 VPQ----------DDILHPTlTVRET------------------LMFAAKLRG-----------LSGGERKRVSIALELV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 586469518 627 HKPKYALLDECTS----AVSIDVEGKIFQAAKGaGISLLSITHRPS 668
Cdd:cd03213 128 SNPSLLFLDEPTSgldsSSALQVMSLLRRLADT-GRTIICSIHQPS 172
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
499-672 |
2.74e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.32 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLykpppqhmfYIPQRPyMSLG-----SLRDQVIYPDSVDEMH 573
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL---------LIDDHP-LHFGdysyrSQRIRMIFQDPSTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 574 DKGYTDQDLECILR-NVHL------YHIVQ--REGGW--DAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVS 642
Cdd:PRK15112 102 PRQRISQILDFPLRlNTDLepeqreKQIIEtlRQVGLlpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190
....*....|....*....|....*....|....
gi 586469518 643 IDVEGKI----FQAAKGAGISLLSITHRPSLWKY 672
Cdd:PRK15112 182 MSMRSQLinlmLELQEKQGISYIYVTQHLGMMKH 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
491-665 |
2.92e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.54 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 491 TGEVVA-SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL--------------YKPPPQHMFYIPQRPYMS 555
Cdd:PRK10261 334 TREVHAvEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIifngqridtlspgkLQALRRDIQFIFQDPYAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 556 LG---SLRDQVIYPDSVDEMHDKGYTDQDLECILRNVHLyhivQREGGWDavmdWKDVLSGGEKQRMGMARMFYHKPKYA 632
Cdd:PRK10261 414 LDprqTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGL----LPEHAWR----YPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190
....*....|....*....|....*....|....*..
gi 586469518 633 LLDECTSAVSIDVEGKI----FQAAKGAGISLLSITH 665
Cdd:PRK10261 486 IADEAVSALDVSIRGQIinllLDLQRDFGIAYLFISH 522
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
493-680 |
3.43e-05 |
|
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: 47.63 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 493 EVVASRLNFKVQEGMHLLITGPNGCGKSS----LFRILSGLWP--VYEGVLYKPPPQH-----MFYIPQRPYMSLGSLRD 561
Cdd:TIGR00957 1299 DLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINESAEGeiIIDGLNIAKIGLHdlrfkITIIPQDPVLFSGSLRM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 562 QViypDSVDEmhdkgYTDQDLECILRNVHLYHIVQR----------EGGwdavmdwkDVLSGGEKQRMGMARMFYHKPKY 631
Cdd:TIGR00957 1379 NL---DPFSQ-----YSDEEVWWALELAHLKTFVSAlpdkldhecaEGG--------ENLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 586469518 632 ALLDECTSAVSIDVEGKIfQA---AKGAGISLLSITHRPSLWKYHTHLLQFD 680
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLI-QStirTQFEDCTVLTIAHRLNTIMDYTRVIVLD 1493
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
480-653 |
3.54e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 46.94 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 480 IICENVPIITPTGEVVASR-LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhMFYIPQRPYmSLGS 558
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRnINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL------LDGHDLRDY-TLAS 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 559 LRDQV--------IYPDSVDE-----MHDKgYTDQDLECILRNVH-LYHIVQREGGWDAVMDWKDV-LSGGEKQRMGMAR 623
Cdd:PRK11176 415 LRNQValvsqnvhLFNDTIANniayaRTEQ-YSREQIEEAARMAYaMDFINKMDNGLDTVIGENGVlLSGGQRQRIAIAR 493
|
170 180 190
....*....|....*....|....*....|
gi 586469518 624 MFYHKPKYALLDECTSAVSIDVEGKIfQAA 653
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAI-QAA 522
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
499-665 |
3.67e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 46.26 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY----KPPPQHMFYIPQRPYMSLGSLRDQVIYPDSVDE--- 571
Cdd:PRK13650 26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIidgdLLTEENVWDIRHKIGMVFQNPDNQFVGATVEDDvaf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 572 -MHDKGYTDQDLecILRNVHLYHIVqreggwdAVMDWKDV----LSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDVE 646
Cdd:PRK13650 106 gLENKGIPHEEM--KERVNEALELV-------GMQDFKEReparLSGGQKQRVAIAGAVAMRPKIIILDEATSM--LDPE 174
|
170 180
....*....|....*....|....*
gi 586469518 647 GK--IFQAAKGA----GISLLSITH 665
Cdd:PRK13650 175 GRleLIKTIKGIrddyQMTVISITH 199
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
495-535 |
3.77e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 45.99 E-value: 3.77e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 586469518 495 VASRL---NFKVQEGMHLLITGPNGCGKSSLFRILSGLWPvYEG 535
Cdd:COG4138 8 VAGRLgpiSAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQG 50
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
499-665 |
4.21e-05 |
|
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: 45.21 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWP------VYEGVLYKPPPQHMFYIPQR-----------PYMSLgsLRD 561
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiIIDGLKLTDDKKNINELRQKvgmvfqqfnlfPHLTV--LEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 562 QVIYPDSVDEMHDKGYTDQDLEcILRNVHLYHivqREGGWDAVmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSA- 640
Cdd:cd03262 97 ITLAPIKVKGMSKAEAEERALE-LLEKVGLAD---KADAYPAQ------LSGGQQQRVAIARALAMNPKVMLFDEPTSAl 166
|
170 180
....*....|....*....|....*...
gi 586469518 641 ---VSIDVEGKIFQAAKgAGISLLSITH 665
Cdd:cd03262 167 dpeLVGEVLDVMKDLAE-EGMTMVVVTH 193
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
490-636 |
4.64e-05 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 45.36 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 490 PTGEVVAsrlnfkvqegmhlLItGPNGCGKSSLFRILSGLWPVYEG-VLYK-------PPPQ----HMFYIPQRpymslg 557
Cdd:COG0410 27 EEGEIVA-------------LL-GRNGAGKTTLLKAISGLLPPRSGsIRFDgeditglPPHRiarlGIGYVPEG------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 558 slRDqvIYPD-SVDE--------MHDKGYTDQDLECIL----RnvhLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARM 624
Cdd:COG0410 87 --RR--IFPSlTVEEnlllgayaRRDRAEVRADLERVYelfpR---LKERRRQRAG---------TLSGGEQQMLAIGRA 150
|
170
....*....|..
gi 586469518 625 FYHKPKYALLDE 636
Cdd:COG0410 151 LMSRPKLLLLDE 162
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
492-667 |
5.14e-05 |
|
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: 46.72 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGL--WPVYEG-VLYkpppqHMFYIPQRPYMSL------------ 556
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGrIIY-----HVALCEKCGYVERpskvgepcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 557 GSLRDQVI---------------------------YPDS------VDEMHDKGYTDQdlECILRNVHLYHIVQREggwDA 603
Cdd:TIGR03269 87 GTLEPEEVdfwnlsdklrrrirkriaimlqrtfalYGDDtvldnvLEALEEIGYEGK--EAVGRAVDLIEMVQLS---HR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 604 VMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSavSID------VEGKIFQAAKGAGISLLSITHRP 667
Cdd:TIGR03269 162 ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTG--TLDpqtaklVHNALEEAVKASGISMVLTSHWP 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
489-665 |
5.28e-05 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 45.26 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 489 TPTGEVVA-SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY-------------KPPPQHMFYIPQRpY 553
Cdd:cd03258 13 DTGGKVTAlKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGsVLVdgtdltllsgkelRKARRRIGMIFQH-F 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 554 MSLGSL--RDQVIYPDSVDEMhDKGYTDQDLECILRNVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKY 631
Cdd:cd03258 92 NLLSSRtvFENVALPLEIAGV-PKAEIEERVLELLELVGLEDKADA---------YPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 586469518 632 ALLDECTSAVSIDVEGKIFQAAKGA----GISLLSITH 665
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDInrelGLTIVLITH 199
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
500-672 |
5.52e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 45.85 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 500 NFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY----------------KPPPQHMFYIPQ---RPYMSLGS- 558
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGeVAWlgkdllgmkddewravRSDIQMIFQDPLaslNPRMTIGEi 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 559 ----LRdqVIYPdsvdEMHDKGYTDQDLECILRNVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALL 634
Cdd:PRK15079 121 iaepLR--TYHP----KLSRQEVKDRVKAMMLKVGLLPNLINR---------YPHEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 586469518 635 DECTSAVSIDVEGKIF----QAAKGAGISLLSITHRPSLWKY 672
Cdd:PRK15079 186 DEPVSALDVSIQAQVVnllqQLQREMGLSLIFIAHDLAVVKH 227
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
499-651 |
6.60e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPppQHMFYIPQRPYMSLGSLRDQVIYPDSVDE--MHDKG 576
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--RSIAYVPQQAWIMNATVRGNILFFDEEDAarLADAV 756
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586469518 577 YTDQdLECILRnvhlyhivQREGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQ 651
Cdd:PTZ00243 757 RVSQ-LEADLA--------QLGGGLETEIGEKGVnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVE 823
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
492-638 |
7.28e-05 |
|
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: 44.67 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 492 GEVVASR-LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG--------VLYKPPP--QHMFYIPQRPymslgSLR 560
Cdd:cd03265 11 GDFEAVRgVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghdVVREPREvrRRIGIVFQDL-----SVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 561 DQVIYPDSVdEMHDKGY------TDQDLECILRNVHLyhivqreggwdavMDWKDVL----SGGEKQRMGMARMFYHKPK 630
Cdd:cd03265 86 DELTGWENL-YIHARLYgvpgaeRRERIDELLDFVGL-------------LEAADRLvktySGGMRRRLEIARSLVHRPE 151
|
....*...
gi 586469518 631 YALLDECT 638
Cdd:cd03265 152 VLFLDEPT 159
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
611-666 |
7.35e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 7.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 611 LSGGEKQRMGMARMFYHKPKYALLDECTSAVSID----VEGKIFQAAKGAGISLLSITHR 666
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHR 1418
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
495-665 |
8.02e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.85 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 495 VASRLNFKVQEGMHLLITGPNGCGKS----SLFRILSGLWPVY---------EGVLYKPPPQ-------HMFYIPQRPYM 554
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYpsgdirfhgESLLHASEQTlrgvrgnKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 555 SLG---SLRDQVIYPDSVDE-MHDKGYTDQDLECILRnVHLYHIVQReggwdaVMDWKDVLSGGEKQRMGMARMFYHKPK 630
Cdd:PRK15134 104 SLNplhTLEKQLYEVLSLHRgMRREAARGEILNCLDR-VGIRQAAKR------LTDYPHQLSGGERQRVMIAMALLTRPE 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 586469518 631 YALLDECTSAVSIDVEGKIFQAAKG----AGISLLSITH 665
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRElqqeLNMGLLFITH 215
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
489-529 |
1.20e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 44.30 E-value: 1.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 586469518 489 TPTGEVVA-SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGL 529
Cdd:COG1134 34 TRREEFWAlKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI 75
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
499-535 |
1.27e-04 |
|
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: 44.06 E-value: 1.27e-04
10 20 30
....*....|....*....|....*....|....*..
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG 535
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG 77
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
499-666 |
1.30e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.74 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL-----------YKPPPQHMFYIPQRPYMSLGSLRDQViypD 567
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRImiddcdvakfgLTDLRRVLSIIPQSPVLFSGTVRFNI---D 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 568 SVDEmhdkgYTDQDLECILRNVHLYHIVQREG-GWDA-VMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDV 645
Cdd:PLN03232 1332 PFSE-----HNDADLWEALERAHIKDVIDRNPfGLDAeVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180
....*....|....*....|...
gi 586469518 646 EGKIFQAAKGA--GISLLSITHR 666
Cdd:PLN03232 1407 DSLIQRTIREEfkSCTMLVIAHR 1429
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
494-665 |
1.46e-04 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 43.93 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 494 VVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY------KPPPQHMFYIPQRPYM---------SLGS 558
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkvNDPKVDERLIRQEAGMvfqqfylfpHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 559 LRDQVIYPDSVDEMHDKGYTDQDLEcILRNVHLyhiVQREGGWDAVmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECT 638
Cdd:PRK09493 95 LENVMFGPLRVRGASKEEAEKQARE-LLAKVGL---AERAHHYPSE------LSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190
....*....|....*....|....*....|..
gi 586469518 639 SAvsIDVE-----GKIFQAAKGAGISLLSITH 665
Cdd:PRK09493 165 SA--LDPElrhevLKVMQDLAEEGMTMVIVTH 194
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
499-665 |
2.37e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 43.46 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY----------KPPPQHMFYIPQR-----------PYMSLg 557
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdfskTPSDKAIRELRRNvgmvfqqynlwPHLTV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 558 sLRDQVIYPDSVDEMhDKGYTDQDLECILRNVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDEC 637
Cdd:PRK11124 100 -QQNLIEAPCRVLGL-SKDQALARAEKLLERLRLKPYADR---------FPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190
....*....|....*....|....*....|.
gi 586469518 638 TSAVSIDVEG---KIFQAAKGAGISLLSITH 665
Cdd:PRK11124 169 TAALDPEITAqivSIIRELAETGITQVIVTH 199
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
452-528 |
5.56e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 5.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586469518 452 HSKNEVTMELPLSDTLTIKGNVIDVDHGIICENVpIITPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSG 528
Cdd:PRK10938 233 HSEQLEGVQLPEPDEPSARHALPANEPRIVLNNG-VVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
611-640 |
7.42e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 42.48 E-value: 7.42e-04
10 20 30
....*....|....*....|....*....|
gi 586469518 611 LSGGEKQRMGMARMFYHKPKYALLDECTSA 640
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSA 170
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
500-640 |
1.02e-03 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 41.52 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 500 NFKVQEGMHLLITGPNGCGKSSLFRILSGLWP------VYEGVLYKPPPQHMFYIPQR-----------PYMSLgslRDQ 562
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiTVDGEDLTDSKKDINKLRRKvgmvfqqfnlfPHLTV---LEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 563 VIYPdsvdEMHDKGYTDQDLECI----LRNVHLYhivqreggwdavmDWKDV----LSGGEKQRMGMAR---MfyhKPKY 631
Cdd:COG1126 98 VTLA----PIKVKKMSKAEAEERamelLERVGLA-------------DKADAypaqLSGGQQQRVAIARalaM---EPKV 157
|
....*....
gi 586469518 632 ALLDECTSA 640
Cdd:COG1126 158 MLFDEPTSA 166
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
490-639 |
1.11e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 41.60 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 490 PTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPP------------QHMFYIPQRPymsl 556
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGeVLIKGEPikydkksllevrKTVGIVFQNP---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 557 gslRDQVIYPdSVDEmhDKGYTDQDL-----ECILRNVHLYHIVQREGGWDAVmdwKDVLSGGEKQRMGMARMFYHKPKY 631
Cdd:PRK13639 88 ---DDQLFAP-TVEE--DVAFGPLNLglskeEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKKRVAIAGILAMKPEI 158
|
....*...
gi 586469518 632 ALLDECTS 639
Cdd:PRK13639 159 IVLDEPTS 166
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
611-665 |
1.74e-03 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 40.72 E-value: 1.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 586469518 611 LSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEG---KIFQAAKGAGISLLSITH 665
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQQLAEEGKTMVVVTH 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
609-665 |
1.93e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 40.93 E-value: 1.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586469518 609 DVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSI----DVEGKIFQAAKGAGISLLSITH 665
Cdd:PRK10575 146 DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLH 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
611-640 |
1.95e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 41.22 E-value: 1.95e-03
10 20 30
....*....|....*....|....*....|
gi 586469518 611 LSGGEKQRMGMARMFYHKPKYALLDECTSA 640
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
489-639 |
2.25e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 41.43 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 489 TPTGEVVASRLNFKVQEGMHLLITGPNGCGKSSLF----RILSGLWPV------YEGVLYKPPPQHMFYIPQRPYMSLGS 558
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLSTEGEIqidgvsWNSVTLQTWRKAFGVIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 559 LRDQViypdsvdEMHDKgYTDQDLECILRNVHLYHIV-QREGGWDAVM-DWKDVLSGGEKQRMGMARMFYHKPKYALLDE 636
Cdd:TIGR01271 1308 FRKNL-------DPYEQ-WSDEEIWKVAEEVGLKSVIeQFPDKLDFVLvDGGYVLSNGHKQLMCLARSILSKAKILLLDE 1379
|
...
gi 586469518 637 CTS 639
Cdd:TIGR01271 1380 PSA 1382
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
499-538 |
2.37e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 40.98 E-value: 2.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY 538
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIW 62
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
611-665 |
2.92e-03 |
|
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: 40.11 E-value: 2.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586469518 611 LSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDVEGK------IFQAAKGAGISLLSITH 665
Cdd:TIGR04520 137 LSGGQKQRVAIAGVLAMRPDIIILDEATSM--LDPKGRkevletIRKLNKEEGITVISITH 195
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
493-638 |
3.02e-03 |
|
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: 40.01 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 493 EVVASR-LNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-------VLYKPPPQHMFYIP----QR--------P 552
Cdd:cd03267 33 EVEALKgISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGevrvaglVPWKRRKKFLRRIGvvfgQKtqlwwdlpV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 553 YMSLGSLRDqvIYpdSVDEMHDKGYTDQdLECILRNVHLYHIVQREggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYA 632
Cdd:cd03267 113 IDSFYLLAA--IY--DLPPARFKKRLDE-LSELLDLEELLDTPVRQ------------LSLGQRMRAEIAAALLHEPEIL 175
|
....*.
gi 586469518 633 LLDECT 638
Cdd:cd03267 176 FLDEPT 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
497-535 |
4.51e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 4.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 586469518 497 SRLNFKVQEG-MHLLItGPNGCGKSSLFRILSGLWP--VYEG 535
Cdd:NF040905 18 DDVNLSVREGeIHALC-GENGAGKSTLMKVLSGVYPhgSYEG 58
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
499-665 |
4.93e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 39.45 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 499 LNFKVQEGMHLLITGPNGCGKSSLFRILSG-LWPVYEGVLYKPPP------------QHMFYIPQRPymslgslrDQVIY 565
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGiLKPSSGRILFDGKPidysrkglmklrESVGMVFQDP--------DNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 566 PDSVDEmhDKGYTDQDLECILRNVH--LYHIVQREGgwdaVMDWKD----VLSGGEKQRMGMARMFYHKPKYALLDECTS 639
Cdd:PRK13636 97 SASVYQ--DVSFGAVNLKLPEDEVRkrVDNALKRTG----IEHLKDkpthCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190
....*....|....*....|....*....|..
gi 586469518 640 AvsIDVEGK------IFQAAKGAGISLLSITH 665
Cdd:PRK13636 171 G--LDPMGVseimklLVEMQKELGLTIIIATH 200
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
497-650 |
5.68e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.11 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 497 SRLNFKVQEGMHLLITGPNGCGKSSLFRILSGLWPVYEG--VLYKpppQHMFYIPQRPYMSLGSLRDQVIY-----PDSV 569
Cdd:PLN03130 634 SNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDasVVIR---GTVAYVPQVSWIFNATVRDNILFgspfdPERY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586469518 570 DEMHDKGYTDQDLEcILRNVHLYHIVQRegGWDavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKI 649
Cdd:PLN03130 711 ERAIDVTALQHDLD-LLPGGDLTEIGER--GVN--------ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQV 779
|
.
gi 586469518 650 F 650
Cdd:PLN03130 780 F 780
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
611-669 |
6.62e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 38.99 E-value: 6.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586469518 611 LSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKI----FQAAKGAGISLLSITHRPSL 669
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIadllFSLNREHGTTLILVTHDLQL 209
|
|
| |
