|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
341-931 |
1.56e-141 |
|
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: 436.49 E-value: 1.56e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 341 RVAAMAKVLVPTLLDKQGAQLFAVALLVVTRTWISDRIASLNGTSVKYVLEQDKAAFIRLTGISVLQSAASSIVAPSLRY 420
Cdd:TIGR00954 78 KLDFLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 421 LTARLALGWRIRLTQHLLKNYLRKNAFYKVFHMSGHDIDADQRISHDVEKLTTDLSGLVTGMVKPTVDILWFTWRMKLLT 500
Cdd:TIGR00954 158 LLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTAL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 501 GRRGVAILYAYMLLGLGFLRSITPDFGDLTSREQELEGTFRFMHTRLRTHAESVAFFGGGSREKAMVDSRFQELLDHCRM 580
Cdd:TIGR00954 238 GSVGPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 581 LLKKKWLFGILDDFITKqlphnVTWGLSLLYA-----MEHKGDRALTSTQGELAHAL----RFLASVVSqsflAFGDILE 651
Cdd:TIGR00954 318 IIKFRFSYGFLDNIVAK-----YTWSAVGLVAvsipiFDKTHPAFLEMSEEELMQEFynngRLLLKAAD----ALGRLML 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 652 LNRKYLLLSGGINRIFELEELLDSAKNG------VSLPESQSMFKKDD---------VTTEDIISFSEVDIITPAQKLLA 716
Cdd:TIGR00954 389 AGRDMTRLAGFTARVDTLLQVLDDVKSGnfkrprVEEIESGREGGRNSnlvpgrgivEYQDNGIKFENIPLVTPNGDVLI 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPcqnikdvggSRC-VFYVPQRPYTCLGTLRDQIIYPL 795
Cdd:TIGR00954 469 ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP---------AKGkLFYVPQRPYMTLGTLRDQIIYPD 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 796 SQEEaelsvVKMLGTGDNSddrahildthLRSILERVRLIYLLEREGGWDASVNWEDILSLGEQQRLGMARLFFHNPKFG 875
Cdd:TIGR00954 540 SSED-----MKRRGLSDKD----------LEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFA 604
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 720069164 876 ILDECTNATSVDVEEHLYKLANEMGITVVTTSQRPALIPFHSLELQlIDGEGKWEL 931
Cdd:TIGR00954 605 ILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLY-MDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
345-613 |
1.08e-93 |
|
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: 296.83 E-value: 1.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 345 MAKVLVPTLLDKQGAQLFAVALLVVTRTWISDRIASLNGTSVKYVLEQDKAAFIRLTGISVLQSAASSIVAPSLRYLTAR 424
Cdd:pfam06472 1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 425 LALGWRIRLTQHLLKNYLRKNAFYKVFHMSGHDIDADQRISHDVEKLTTDLSGLVTGMVKPTVDILWFTWRMKLLTGRRG 504
Cdd:pfam06472 81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 505 VAILYAYMLLGLGFLRSITPDFGDLTSREQELEGTFRFMHTRLRTHAESVAFFGGGSREKAMVDSRFQELLDHCRMLLKK 584
Cdd:pfam06472 161 PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILRR 240
|
250 260
....*....|....*....|....*....
gi 720069164 585 KWLFGILDDFITKQLPHNVTWGLSLLYAM 613
Cdd:pfam06472 241 RLWYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
361-934 |
2.31e-86 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 287.86 E-value: 2.31e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 361 LFAVALLVVTRTWISDRIASLNG---TSvkyvLEQ-DKAAFIRLTGISVLQSAASSIVAPSLRYLTARLALGWRIRLTQH 436
Cdd:COG4178 27 LALLLLLTLASVGLNVLLNFWNRdfyDA----LQArDAAAFWQQLGVFALLAAISILLAVYQTYLRQRLQIRWREWLTER 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 437 LLKNYLRKNAFYKVfHMSGHDID-ADQRISHDVEKLTTDLSGLVTGMVKPTVD------ILW-------FTWRMKLLTGR 502
Cdd:COG4178 103 LLDRWLSNRAYYRL-QLSGGEIDnPDQRIAEDIRLFTETTLSLSLGLLSSVVTlisfigILWslsgsltFTLGGYSITIP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 503 RG-VAILYAYMLLG--LGFLrsitpdFG----DLTSREQELEGTFRFMHTRLRTHAESVAFFGGGSREKAMVDSRFQELL 575
Cdd:COG4178 182 GYmVWAALIYAIIGtlLTHL------IGrpliRLNFEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 576 DHCRMLLKK-----------KWLFGILDDFItkQLP----HNVTWGLSLLYAMehkgdrALTSTQGelahALRFLASvvs 640
Cdd:COG4178 256 ANWRRLIRRqrnltffttgyGQLAVIFPILV--AAPryfaGEITLGGLMQAAS------AFGQVQG----ALSWFVD--- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 641 qsflAFGDILELnrkylllSGGINRIFELEELLDSAKngvSLPESQSmfkKDDVTTEDIISFSEVDIITPAQKLLARQLT 720
Cdd:COG4178 321 ----NYQSLAEW-------RATVDRLAGFEEALEAAD---ALPEAAS---RIETSEDGALALEDLTLRTPDGRPLLEDLS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 721 FDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNikdvggsrCVFYVPQRPYTCLGTLRDQIIYPLSQEEA 800
Cdd:COG4178 384 LSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA--------RVLFLPQRPYLPLGTLREALLYPATAEAF 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 801 elsvvkmlgtgdnSDDRahildthLRSILERVRLIYLLEReggWDASVNWEDILSLGEQQRLGMARLFFHNPKFGILDEC 880
Cdd:COG4178 456 -------------SDAE-------LREALEAVGLGHLAER---LDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 720069164 881 TNATSVDVEEHLYKLANEM--GITVVTTSQRPALIPFHSLELQLiDGEGKWELRSI 934
Cdd:COG4178 513 TSALDEENEAALYQLLREElpGTTVISVGHRSTLAAFHDRVLEL-TGDGSWQLLPA 567
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
43-251 |
1.36e-79 |
|
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: 255.16 E-value: 1.36e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGigsdlNKEIFYVPQRPYT 122
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----GEDLLFLPQRPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 123 AVGTLRDQLIYPltvaeesepltqegmvellknvdleylldryppekeinWGDELSLGEQQRLGMARLFYHKPKFAILDE 202
Cdd:cd03223 76 PLGTLREQLIYP--------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 720069164 203 CTSAVTTDMEERFCAKVRAMGTSCITISHRPALVAFHDMVLSLDGEGGW 251
Cdd:cd03223 118 ATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
3-252 |
5.44e-77 |
|
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: 264.69 E-value: 5.44e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 3 SGYADRIHELMfisrelSVIHD---------------------KSSIQRNGGSNYFSEANYIEFAGVKVVTPTGNVLVED 61
Cdd:TIGR00954 397 AGFTARVDTLL------QVLDDvksgnfkrprveeiesgreggRNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDVLIES 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 62 LTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGSdlnkeIFYVPQRPYTAVGTLRDQLIYPLTVAEES 141
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGK-----LFYVPQRPYMTLGTLRDQIIYPDSSEDMK 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 142 EP-LTQEGMVELLKNVDLEYLLDRYPPEKEI-NWGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKV 219
Cdd:TIGR00954 546 RRgLSDKDLEQILDNVQLTHILEREGGWSAVqDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC 625
|
250 260 270
....*....|....*....|....*....|...
gi 720069164 220 RAMGTSCITISHRPALVAFHDMVLSLDGEGGWK 252
Cdd:TIGR00954 626 REFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQ 658
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-255 |
6.53e-66 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 231.62 E-value: 6.53e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 5 YADRIHELMfisrelSVIHDKSSIQRNGGSNYFSEANYIEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSS 84
Cdd:COG4178 331 TVDRLAGFE------EALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKST 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 85 LFRVLGGLWPLVSGYIFKPGigsdlNKEIFYVPQRPYTAVGTLRDQLIYPLTvaeeSEPLTQEGMVELLKNVDLEYLLDR 164
Cdd:COG4178 405 LLRAIAGLWPYGSGRIARPA-----GARVLFLPQRPYLPLGTLREALLYPAT----AEAFSDAELREALEAVGLGHLAER 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 165 YppEKEINWGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDMV 242
Cdd:COG4178 476 L--DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGHRSTLAAFHDRV 553
|
250
....*....|...
gi 720069164 243 LSLDGEGGWKVHS 255
Cdd:COG4178 554 LELTGDGSWQLLP 566
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
700-929 |
1.25e-61 |
|
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: 206.24 E-value: 1.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 700 ISFSEVDIITPAQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNikdvggsrCVFYVPQR 779
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE--------DLLFLPQR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 780 PYTCLGTLRDQIIYPlsqeeaelsvvkmlgtgdnsddrahildthlrsilervrliyllereggwdasvnWEDILSLGEQ 859
Cdd:cd03223 73 PYLPLGTLREQLIYP-------------------------------------------------------WDDVLSGGEQ 97
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 860 QRLGMARLFFHNPKFGILDECTNATSVDVEEHLYKLANEMGITVVTTSQRPALIPFHSLELQLiDGEGKW 929
Cdd:cd03223 98 QRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDL-DGEGGW 166
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
43-247 |
1.30e-27 |
|
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: 109.78 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLV-EDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI------GSDLNKEIFY 115
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 116 VPQRPYtavgtlrdqlIYPLTVAEesepltqegmvellkNVdleylldryppekeinwgdeLSLGEQQRLGMARLFYHKP 195
Cdd:cd03228 81 VPQDPF----------LFSGTIRE---------------NI--------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 720069164 196 KFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDMVLSLDG 247
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALakGKTVIVIAHRLSTIRDADRIIVLDD 169
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
43-237 |
3.84e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.91 E-value: 3.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVvTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYI-FKpgiGSDLN--------KEI 113
Cdd:COG4619 1 LELEGLSF-RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyLD---GKPLSampppewrRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 114 FYVPQRPYTAVGTLRDQLIYPLTVAEEsePLTQEGMVELLKNVDL-EYLLDryppeKEInwgDELSLGEQQRLGMARLFY 192
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLPFPFQLRER--KFDRERALELLERLGLpPDILD-----KPV---ERLSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 720069164 193 HKPKFAILDECTSAVTTDMEERFCAKVRAM----GTSCITISHRPALVA 237
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIE 195
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
43-247 |
5.37e-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: 113.70 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI------GSDLNKEIFYV 116
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 117 PQRPYTAVGTLRDQLiyplTVAEESepLTQEGMVELLKNVDLEYLLDRYP--PEKEInwGDE---LSLGEQQRLGMARLF 191
Cdd:COG4988 417 PQNPYLFAGTIRENL----RLGRPD--ASDEELEAALEAAGLDEFVAALPdgLDTPL--GEGgrgLSGGQAQRLALARAL 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 720069164 192 YHKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDMVLSLDG 247
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQADRILVLDD 546
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
55-247 |
1.30e-23 |
|
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: 99.48 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG-----SDLNKEIFYVPQRPytavgtlrd 129
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirdarEDYRRRLAYLGHAD--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 130 qLIYP-LTVAEE--------SEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAIL 200
Cdd:COG4133 85 -GLKPeLTVRENlrfwaalyGLRADREAIDEALEAVGLAGLADLPV--------RQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 720069164 201 DECTSAVTTDMEERFCAKVRAM---GTSCITISHRPALVAFHDmVLSLDG 247
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAAR-VLDLGD 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
43-245 |
1.92e-23 |
|
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: 98.06 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTP-TGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG------SDLNKEIFY 115
Cdd:cd03246 1 LEVENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADisqwdpNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 116 VPQRpytavgtlrDQLiYPLTVAEesepltqegmvellkNVdleylldryppekeinwgdeLSLGEQQRLGMARLFYHKP 195
Cdd:cd03246 81 LPQD---------DEL-FSGSIAE---------------NI--------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 720069164 196 KFAILDECTSAVTTDMEERFCAKVRAM---GTSCITISHRPALVAFHDMVLSL 245
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALkaaGATRIVIAHRPETLASADRILVL 168
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
43-238 |
4.44e-23 |
|
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: 98.73 E-value: 4.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGN---VLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYI-FKPGIGSDLN-------- 110
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIiFDGKDLLKLSrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 111 KEIFYVPQRPYTAVG---TLRDQLIYPLTVA--EESEPLTQEGMVELLKNVDL-EYLLDRYPpekeinwgDELSLGEQQR 184
Cdd:cd03257 82 KEIQMVFQDPMSSLNprmTIGEQIAEPLRIHgkLSKKEARKEAVLLLLVGVGLpEEVLNRYP--------HELSGGQRQR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 720069164 185 LGMARLFYHKPKFAILDECTSA--VTT---------DMEERFcakvramGTSCITISHRPALVAF 238
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSAldVSVqaqildllkKLQEEL-------GLTLLFITHDLGVVAK 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
43-247 |
6.64e-23 |
|
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: 98.05 E-value: 6.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTP-TGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG------SDLNKEIFY 115
Cdd:cd03245 3 IEFRNVSFSYPnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDirqldpADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 116 VPQRPYTAVGTLRDQLIYPLTVAEESEpltqegMVELLKNVDLEYLLDRYPP--EKEI-NWGDELSLGEQQRLGMARLFY 192
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAPLADDER------ILRAAELAGVTDFVNKHPNglDLQIgERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 720069164 193 HKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDMVLSLDG 247
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLLDLVDRIIVMDS 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
55-248 |
7.00e-23 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 97.60 E-value: 7.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG-SDLNKEIFYVPQRPYtavgTLRDqliY 133
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPlEKERKRIGYVPQRRS----IDRD---F 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 134 PLTVAE-----------ESEPLTQEGM---VELLKNVDLEYLLDRyppekEInwgDELSLGEQQRLGMARLFYHKPKFAI 199
Cdd:cd03235 84 PISVRDvvlmglyghkgLFRRLSKADKakvDEALERVGLSELADR-----QI---GELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 720069164 200 LDECTSAVTTDMEERF---CAKVRAMGTSCITISHRPALV-AFHDMVLSLDGE 248
Cdd:cd03235 156 LDEPFAGVDPKTQEDIyelLRELRREGMTILVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
59-205 |
7.40e-23 |
|
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: 95.79 E-value: 7.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYI------FKPGIGSDLNKEIFYVPQ----RPYTavgTLR 128
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdLTDDERKSLRKEIGYVFQdpqlFPRL---TVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 720069164 129 DQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPPEKeinwGDELSLGEQQRLGMARLFYHKPKFAILDECTS 205
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGER----PGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
53-247 |
8.48e-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: 104.53 E-value: 8.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 53 PTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFkpgIG---------SDLNKEIFYVPQRPYTA 123
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL---IDgidlrqidpASLRRQIGVVLQDVFLF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 124 VGTLRDQliypLTVAEESepLTQEGMVELLKNVDLEYLLDRYP-------PEKeinwGDELSLGEQQRLGMARLFYHKPK 196
Cdd:COG2274 562 SGTIREN----ITLGDPD--ATDEEIIEAARLAGLHDFIEALPmgydtvvGEG----GSNLSGGQRQRLAIARALLRNPR 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 720069164 197 FAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDMVLSLDG 247
Cdd:COG2274 632 ILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRLADRIIVLDK 684
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
43-248 |
9.39e-23 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 97.56 E-value: 9.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVE---DLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI----------GSDL 109
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQalkGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 110 NKEIFYVPQRpYTAVGTL--RDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGM 187
Cdd:cd03255 81 RRHIGFVFQS-FNLLPDLtaLENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYP--------SELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 720069164 188 ARLFYHKPKFAILDECTSAVTTDMEER----FCAKVRAMGTSCITISHRPALVAFHDMVLSL-DGE 248
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEvmelLRELNKEAGTTIVVVTHDPELAEYADRIIELrDGK 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
44-237 |
1.34e-22 |
|
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: 96.77 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 44 EFAGVKVVTPTGNVLV-EDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI------GSDLNKEIFYV 116
Cdd:cd03225 1 ELKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklsLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 117 PQRPytavgtlRDQLIYPlTVAEE----------SEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLG 186
Cdd:cd03225 81 FQNP-------DDQFFGP-TVEEEvafglenlglPEEEIEERVEEALELVGLEGLRDRSP--------FTLSGGQKQRVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 720069164 187 MARLFYHKPKFAILDECTSAV----TTDMEERFcAKVRAMGTSCITISHRPALVA 237
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLdpagRRELLELL-KKLKAEGKTIIIVTHDLDLLL 198
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
43-247 |
5.02e-22 |
|
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: 95.76 E-value: 5.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI-GSDLNKE-----IFYV 116
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdIRDISRKslrsmIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 117 PQRPYTAVGTLRDQLIY---PLTVAEESEPLTQEGMVELLKNvdLEYLLDRYPPEKeinwGDELSLGEQQRLGMARLFYH 193
Cdd:cd03254 83 LQDTFLFSGTIMENIRLgrpNATDEEVIEAAKEAGAHDFIMK--LPNGYDTVLGEN----GGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 720069164 194 KPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDMVLSLDG 247
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAHRLSTIKNADKILVLDD 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
43-245 |
1.35e-21 |
|
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: 99.67 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG------SDLNKEIFYV 116
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadaDSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 117 PQRPYTAVGTLRDQLIYPL---TVAEESEPLTQEGMVELLKnvDLEYLLDRYPPEKeinwGDELSLGEQQRLGMARLFYH 193
Cdd:TIGR02857 402 PQHPFLFAGTIAENIRLARpdaSDAEIREALERAGLDEFVA--ALPQGLDTPIGEG----GAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 720069164 194 KPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDMVLSL 245
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLALAALADRIVVL 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
43-237 |
2.46e-21 |
|
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: 98.82 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNV-LVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP---LVSGYIFKPGI------GSDLNKE 112
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRdllelsEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 113 IFYVPQRPYTAV--GTLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARL 190
Cdd:COG1123 85 IGMVFQDPMTQLnpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYP--------HQLSGGQRQRVAIAMA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 720069164 191 FYHKPKFAILDECTSA--VTTDME--ERFCAKVRAMGTSCITISHRPALVA 237
Cdd:COG1123 157 LALDPDLLIADEPTTAldVTTQAEilDLLRELQRERGTTVLLITHDLGVVA 207
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
43-237 |
2.81e-20 |
|
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: 90.85 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIF------KPGIGSDLNKEIFYV 116
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdgkdiTKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 117 PQRPytavgtlRDQLIYPlTVAEE----------SEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLG 186
Cdd:COG1122 81 FQNP-------DDQLFAP-TVEEDvafgpenlglPREEIRERVEEALELVGLEHLADRPP--------HELSGGQKQRVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 720069164 187 MARLFYHKPKFAILDECTSAVttDMEER-----FCAKVRAMGTSCITISHRPALVA 237
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGL--DPRGRrelleLLKRLNKEGKTVIIVTHDLDLVA 198
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
668-913 |
5.99e-20 |
|
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: 94.82 E-value: 5.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 668 ELEELLDSAKngvslPESQSMFKKDDVTTEDIISFSEVDIITPAQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLR 747
Cdd:COG4988 310 KIFALLDAPE-----PAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 748 GVWPIATGRLV---KPCQNIKDVGGSRCVFYVPQRPYTCLGTLRDQIiyplsqeeaelsvvkMLGTGDNSDDRahildth 824
Cdd:COG4988 385 GFLPPYSGSILingVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL---------------RLGRPDASDEE------- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 825 LRSILERVRLIYLLER-EGGWDASV-----NwediLSLGEQQRLGMARLFFHNPKFGILDECTnaTSVDVE------EHL 892
Cdd:COG4988 443 LEAALEAAGLDEFVAAlPDGLDTPLgeggrG----LSGGQAQRLALARALLRDAPLLLLDEPT--AHLDAEteaeilQAL 516
|
250 260
....*....|....*....|.
gi 720069164 893 YKLANemGITVVTTSQRPALI 913
Cdd:COG4988 517 RRLAK--GRTVILITHRLALL 535
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
55-237 |
1.85e-19 |
|
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: 87.70 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIF---KPGIGSDLNKEIFYVPQRPYTAVG--TLRD 129
Cdd:cd03226 12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngKPIKAKERRKSIGYVMQDVDYQLFtdSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 130 QLIYPLTVAEESEPLTQegmvELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTT 209
Cdd:cd03226 92 ELLLGLKELDAGNEQAE----TVLKDLDLYALKERHP--------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190
....*....|....*....|....*....|.
gi 720069164 210 DMEERFCAKVR---AMGTSCITISHRPALVA 237
Cdd:cd03226 160 KNMERVGELIRelaAQGKAVIVITHDYEFLA 190
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
43-247 |
2.40e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.80 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSG--YIFkpgiGSDLNK----EIFYV 116
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGqvLVN----GQDLSRlkrrEIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 117 PQRpytaVG------------TLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPPekeinwgdELSLGEQQR 184
Cdd:COG2884 78 RRR----IGvvfqdfrllpdrTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPH--------ELSGGEQQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 720069164 185 LGMARLFYHKPKFAILDECTSAVTTDMEER----FcAKVRAMGTSCITISHRPALV-AFHDMVLSLDG 247
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEimelL-EEINRRGTTVLIATHDLELVdRMPKRVLELED 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
55-246 |
5.60e-19 |
|
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: 84.60 E-value: 5.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSG--YIFKPGIGSDLNKE----IFYVPQrpytavgtlr 128
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGeiLIDGKDIAKLPLEElrrrIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 129 dqliypltvaeesepltqegmvellknvdleylldryppekeinwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSAVT 208
Cdd:cd00267 81 ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 720069164 209 TDMEERFCAKVRAM---GTSCITISHRPALVAFH-DMVLSLD 246
Cdd:cd00267 113 PASRERLLELLRELaeeGRTVIIVTHDPELAELAaDRVIVLK 154
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
55-248 |
6.10e-19 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 87.07 E-value: 6.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYI--FKPGIGSDLNKeIFYVPQRpyTAVGtlRDqli 132
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlFGKPPRRARRR-IGYVPQR--AEVD--WD--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 133 YPLTVAEesepltqegMV-----------------------ELLKNVDLEYLLDRYppekeINwgdELSLGEQQRLGMAR 189
Cdd:COG1121 90 FPITVRD---------VVlmgrygrrglfrrpsradreavdEALERVGLEDLADRP-----IG---ELSGGQQQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 720069164 190 LFYHKPKFAILDECTSAVTTDMEERFCA---KVRAMGTSCITISHRPALVAFH-DMVLSLDGE 248
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYEllrELRREGKTILVVTHDLGAVREYfDRVLLLNRG 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
43-239 |
7.36e-19 |
|
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: 91.12 E-value: 7.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVV----TPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIF---------KPGIGSDL 109
Cdd:COG1123 261 LEVRNLSKRypvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgkdltklSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 110 NKEIFYVPQRPYTavgtlrdQLIYPLTVAEE-SEPLTQEGMV----------ELLKNVDLEY-LLDRYPpekeinwgDEL 177
Cdd:COG1123 341 RRRVQMVFQDPYS-------SLNPRMTVGDIiAEPLRLHGLLsraerrervaELLERVGLPPdLADRYP--------HEL 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 720069164 178 SLGEQQRLGMARLFYHKPKFAILDECTSA----VTTDMEERFCAKVRAMGTSCITISHRPALVAFH 239
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSAldvsVQAQILNLLRDLQRELGLTYLFISHDLAVVRYI 471
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
708-913 |
1.16e-18 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 85.25 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 708 ITPAQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLV---KPCQNIKDVGGSRCVFYVPQRPYTCL 784
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgKPLSAMPPPEWRRQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 785 GTLRDQIIYPLSQEEAELSvvkmlgtgdnsddrahilDTHLRSILERVRL--IYLleregGWDAsvnweDILSLGEQQRL 862
Cdd:COG4619 88 GTVRDNLPFPFQLRERKFD------------------RERALELLERLGLppDIL-----DKPV-----ERLSGGERQRL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 720069164 863 GMARLFFHNPKFGILDECTNA----TSVDVEEHLYKLANEMGITVVTTSQRPALI 913
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSAldpeNTRRVEELLREYLAEEGRAVLWVSHDPEQI 194
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-247 |
2.95e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 89.45 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 1 MNSGYADRIHELMFISRELSVIHDKSSIQRNGGSnyfseanyIEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGS 80
Cdd:COG1132 306 RALASAERIFELLDEPPEIPDPPGAVPLPPVRGE--------IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 81 GKSSLFRVLGGLWPLVSGYIFkpgIG---------SDLNKEIFYVPQRPYTAVGTLRDQLIYPLTVAeeseplTQEGMVE 151
Cdd:COG1132 378 GKSTLVNLLLRFYDPTSGRIL---IDgvdirdltlESLRRQIGVVPQDTFLFSGTIRENIRYGRPDA------TDEEVEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 152 LLKNVDLEYLLDRYPP-------EKeinwGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEerfcAKV-RAM- 222
Cdd:COG1132 449 AAKAAQAHEFIEALPDgydtvvgER----GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETE----ALIqEALe 520
|
250 260
....*....|....*....|....*....
gi 720069164 223 ----GTSCITISHRPALVAFHDMVLSLDG 247
Cdd:COG1132 521 rlmkGRTTIVIAHRLSTIRNADRILVLDD 549
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
55-234 |
6.41e-18 |
|
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: 83.34 E-value: 6.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFkpgIGsdlNKEIFYVP--QRPytaVG------- 125
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIL---ID---GRDVTGVPpeRRN---IGmvfqdya 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 126 -----TLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAIL 200
Cdd:cd03259 83 lfphlTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYP--------HELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 720069164 201 DECTSAVTTDMEERFCAKVRAM----GTSCITISHRPA 234
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqrelGITTIYVTHDQE 192
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
55-237 |
7.51e-18 |
|
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: 82.10 E-value: 7.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI------GSDLNKEIFYVPQrpytavgtlr 128
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslsPKELARKIAYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 129 dqliypltvaeesepltqegmveLLKNVDLEYLLDRYppekeINwgdELSLGEQQRLGMARLFYHKPKFAILDECTSAVt 208
Cdd:cd03214 81 -----------------------ALELLGLAHLADRP-----FN---ELSGGERQRVLLARALAQEPPILLLDEPTSHL- 128
|
170 180 190
....*....|....*....|....*....|....*
gi 720069164 209 tDME------ERFCAKVRAMGTSCITISHRPALVA 237
Cdd:cd03214 129 -DIAhqiellELLRRLARERGKTVVMVLHDLNLAA 162
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
359-913 |
4.55e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 85.60 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 359 AQLFAVALLVVTRTWISDriaslngtsvkYVLEQDKAAFIRLTGISVLQSAASSIvapsLRYLTARLAlgwrIRLTQHLL 438
Cdd:COG1132 33 SALLELLLPLLLGRIIDA-----------LLAGGDLSALLLLLLLLLGLALLRAL----LSYLQRYLL----ARLAQRVV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 439 KNyLRKNAFYKVFHMSGHDIDADQ------RISHDVEKLTTDLSGLVTGMVKPTVDI-------LWFTWRMKLLTgrrgV 505
Cdd:COG1132 94 AD-LRRDLFEHLLRLPLSFFDRRRtgdllsRLTNDVDAVEQFLAHGLPQLVRSVVTLigalvvlFVIDWRLALIV----L 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 506 AILYAYMLLGLGFLRSITPDFGDLTSREQELegtFRFMHTRLRTHAESVAFfGGGSREKAMVDSRFQELLDHCRMLLKKK 585
Cdd:COG1132 169 LVLPLLLLVLRLFGRRLRKLFRRVQEALAEL---NGRLQESLSGIRVVKAF-GREERELERFREANEELRRANLRAARLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 586 WLFGILDDFITkqlphNVTWGLSLLYAmehkGDRALTS--TQGELAhALRFLASVVSQSFLAFGDILELNRKYLllsGGI 663
Cdd:COG1132 245 ALFFPLMELLG-----NLGLALVLLVG----GLLVLSGslTVGDLV-AFILYLLRLFGPLRQLANVLNQLQRAL---ASA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 664 NRIFEL---EELLDSAKNGVSLPEsqsmfKKDDVTTEDIiSFSevdiITPAQKLLaRQLTFDITPGKSLLVTGPNGSGKS 740
Cdd:COG1132 312 ERIFELldePPEIPDPPGAVPLPP-----VRGEIEFENV-SFS----YPGDRPVL-KDISLTIPPGETVALVGPSGSGKS 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 741 SIFRVLRGVWPIATGRLVKPCQNIKDVGGS---RCVFYVPQRPYtcL--GTLRDQIIYplsqeeaelsvvkmlGTGDNSD 815
Cdd:COG1132 381 TLVNLLLRFYDPTSGRILIDGVDIRDLTLEslrRQIGVVPQDTF--LfsGTIRENIRY---------------GRPDATD 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 816 DRahildthLRSILERVRLIYLLER-EGGWDASVNwED--ILSLGEQQRLGMARLFFHNPKFGILDECTNATSVDVEEHL 892
Cdd:COG1132 444 EE-------VEEAAKAAQAHEFIEAlPDGYDTVVG-ERgvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALI 515
|
570 580
....*....|....*....|...
gi 720069164 893 YK-LANEM-GITVVTTSQRPALI 913
Cdd:COG1132 516 QEaLERLMkGRTTIVIAHRLSTI 538
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
55-206 |
5.19e-17 |
|
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: 81.63 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIF---KPgIGS----DLNKEIFYVPQRPYTAvgtl 127
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRD-LASlsrrELARRIAYVPQEPPAP---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 128 rdqliYPLTVAEesepltqegMVEL-----------------------LKNVDLEYLLDRYPpekeinwgDELSLGEQQR 184
Cdd:COG1120 88 -----FGLTVRE---------LVALgryphlglfgrpsaedreaveeaLERTGLEHLADRPV--------DELSGGERQR 145
|
170 180
....*....|....*....|..
gi 720069164 185 LGMARLFYHKPKFAILDECTSA 206
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSH 167
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
712-920 |
1.19e-16 |
|
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: 79.45 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 712 QKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS--RCVFYVPQRP--YTCLgTL 787
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyrRRLAYLGHADglKPEL-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 788 RDQIIYplsqeeaelsVVKMLGTGDNSDDrahildthLRSILERVRLIYLLEREGGwdasvnwedILSLGEQQRLGMARL 867
Cdd:COG4133 93 RENLRF----------WAALYGLRADREA--------IDEALEAVGLAGLADLPVR---------QLSAGQKRRVALARL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 720069164 868 FFHNPKFGILDECTNA---TSVD-VEEHLYKLANEMGITVVTTSQRPALIPFHSLEL 920
Cdd:COG4133 146 LLSPAPLWLLDEPFTAldaAGVAlLAELIAAHLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
54-247 |
1.21e-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: 79.44 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 54 TGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFkpgigsdLNKEIFYVPQRPYTAVGTLRDQLIY 133
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS-------VPGSIAYVSQEPWIQNGTIRENILF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 134 pltvaeeSEPLTQEGMVELLKNVDLEYLLDRYPP-------EKEINwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSA 206
Cdd:cd03250 89 -------GKPFDEERYEKVIKACALEPDLEILPDgdlteigEKGIN----LSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 720069164 207 VTTDMEERFCAKV----RAMGTSCITISHRPALVAFHDMVLSLDG 247
Cdd:cd03250 158 VDAHVGRHIFENCilglLLNNKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
700-913 |
1.54e-16 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 78.41 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 700 ISFSEVDIITP-AQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS---RCVFY 775
Cdd:cd03246 1 LEVENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNelgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 776 VPQrpytclgtlrdqiiyplsqeeaelsvvkmlgtgdnsDDRahildthlrsilervrliyLLereggwDASVNwEDILS 855
Cdd:cd03246 81 LPQ------------------------------------DDE-------------------LF------SGSIA-ENILS 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 720069164 856 LGEQQRLGMARLFFHNPKFGILDECTNATSVDVEEHLYKLANEM---GITVVTTSQRPALI 913
Cdd:cd03246 99 GGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALkaaGATRIVIAHRPETL 159
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
43-247 |
2.45e-16 |
|
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: 79.45 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKV-VTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP------LVSGYIFKPGIGSDLNKEIFY 115
Cdd:cd03252 1 ITFEHVRFrYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVpengrvLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 116 VPQRPYTAVGTLRDQliypltVAEESEPLTQEGMVELLKNVDLEYLLDRYPPEKEINWGDE---LSLGEQQRLGMARLFY 192
Cdd:cd03252 81 VLQENVLFNRSIRDN------IALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQgagLSGGQRQRIAIARALI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 720069164 193 HKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDMVLSLDG 247
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADRIIVMEK 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
662-914 |
4.35e-16 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 82.33 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 662 GINRIFELEELLDSAknGVSLPESQSMFKKDDVTtediISFSEVDIITPAQKLLARQLTFDITPGKSLLVTGPNGSGKSS 741
Cdd:TIGR02857 290 GVAAAEALFAVLDAA--PRPLAGKAPVTAAPASS----LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKST 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 742 IFRVLRGVWPIATGRLV---KPCQNIKDVGGSRCVFYVPQRPYTCLGTLRDQIiyplsqeeaelsvvkMLGTGDNSDDRa 818
Cdd:TIGR02857 364 LLNLLLGFVDPTEGSIAvngVPLADADADSWRDQIAWVPQHPFLFAGTIAENI---------------RLARPDASDAE- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 819 hildthLRSILERVRLIYLL-EREGGWDASVNwED--ILSLGEQQRLGMARLFFHNPKFGILDECT----NATSVDVEEH 891
Cdd:TIGR02857 428 ------IREALERAGLDEFVaALPQGLDTPIG-EGgaGLSGGQAQRLALARAFLRDAPLLLLDEPTahldAETEAEVLEA 500
|
250 260
....*....|....*....|...
gi 720069164 892 LYKLANemGITVVTTSQRPALIP 914
Cdd:TIGR02857 501 LRALAQ--GRTVLLVTHRLALAA 521
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
43-246 |
5.62e-16 |
|
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: 77.92 E-value: 5.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKV-VTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG------SDLNKEIFY 115
Cdd:cd03244 3 IEFKNVSLrYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskiglHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 116 VPQRPYTAVGTLRDQLIyPLTVAEESEpltqegMVELLKNVDLEYLLDRYPP---EKEINWGDELSLGEQQRLGMARLFY 192
Cdd:cd03244 83 IPQDPVLFSGTIRSNLD-PFGEYSDEE------LWQALERVGLKEFVESLPGgldTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 720069164 193 HKPKFAILDECTSAVTTDMEERFCAKVRAMGTSC--ITISHRPALVAFHDMVLSLD 246
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCtvLTIAHRLDTIIDSDRILVLD 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
38-202 |
9.33e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 78.21 E-value: 9.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 38 SEANYIEFAGVKVV--TPTGNVLV-EDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPG-IGSDLNKEI 113
Cdd:COG1116 3 AAAPALELRGVSKRfpTGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 114 FYVPQRPytavgTL------RDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGM 187
Cdd:COG1116 83 GVVFQEP-----ALlpwltvLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYP--------HQLSGGMRQRVAI 149
|
170
....*....|....*
gi 720069164 188 ARLFYHKPKFAILDE 202
Cdd:COG1116 150 ARALANDPEVLLMDE 164
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-232 |
1.08e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.41 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 6 ADRIHELmfisrelsvIHDKSSIQRNGGSNYFSEANYIEFAGVKVVTPTGNVLV-EDLTLRVEPGSNLLITGPNGSGKSS 84
Cdd:PRK11160 311 ARRINEI---------TEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVlKGLSLQIKAGEKVALLGRTGCGKST 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 85 LFRVLGGLWPLVSGYIFKPGIG------SDLNKEIFYVPQRPYTAVGTLRDQliypLTVAeeSEPLTQEGMVELLKNVDL 158
Cdd:PRK11160 382 LLQLLTRAWDPQQGEILLNGQPiadyseAALRQAISVVSQRVHLFSATLRDN----LLLA--APNASDEALIEVLQQVGL 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 159 EYLLDRyppEKEIN-W----GDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVR--AMGTSCITISH 231
Cdd:PRK11160 456 EKLLED---DKGLNaWlgegGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAehAQNKTVLMITH 532
|
.
gi 720069164 232 R 232
Cdd:PRK11160 533 R 533
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
43-202 |
1.80e-15 |
|
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: 76.36 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGN---VLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYI---FKPGIGSdlNKEIFYV 116
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdGEPVTGP--GPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 117 PQRPY-----TAvgtlRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLF 191
Cdd:cd03293 79 FQQDAllpwlTV----LDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYP--------HQLSGGMRQRVALARAL 146
|
170
....*....|.
gi 720069164 192 YHKPKFAILDE 202
Cdd:cd03293 147 AVDPDVLLLDE 157
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
42-233 |
1.82e-15 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 80.48 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 42 YIEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP------LVSGYIFKPGIGSDLNKEIFY 115
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDplqgevTLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 116 VPQRPYTAVGTLRDQLiypLTVAEESeplTQEGMVELLKNVDLEYLLDRYPPEKEINWGDE---LSLGEQQRLGMARLFY 192
Cdd:TIGR02868 414 CAQDAHLFDTTVRENL---RLARPDA---TDEELWAALERVGLADWLRALPDGLDTVLGEGgarLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 720069164 193 HKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRP 233
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLAAlsGRTVVLITHHL 530
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
55-207 |
1.84e-15 |
|
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: 76.82 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGSD-----LNKEIFYVPQRPY-TAVGTLR 128
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkepreARRQIGVLPDERGlYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 129 DQL-----IYPLTVAEeseplTQEGMVELLKNVDLEYLLDRyppekeiNWGdELSLGEQQRLGMARLFYHKPKFAILDEC 203
Cdd:COG4555 93 ENIryfaeLYGLFDEE-----LKKRIEELIELLGLEEFLDR-------RVG-ELSTGMKKKVALARALVHDPKVLLLDEP 159
|
....
gi 720069164 204 TSAV 207
Cdd:COG4555 160 TNGL 163
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
719-913 |
2.19e-15 |
|
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: 74.73 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 719 LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGgsrcvfyvpqrpytcLGTLRDQIIYpLSQe 798
Cdd:cd03228 21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---------------LESLRKNIAY-VPQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 799 eaelsvvkmlgtgdnsddrahilDTHLrsilervrliyllereggWDASVnWEDILSLGEQQRLGMARLFFHNPKFGILD 878
Cdd:cd03228 84 -----------------------DPFL------------------FSGTI-RENILSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190
....*....|....*....|....*....|....*....
gi 720069164 879 ECT----NATSVDVEEHLYKLANEMgiTVVTTSQRPALI 913
Cdd:cd03228 122 EATsaldPETEALILEALRALAKGK--TVIVIAHRLSTI 158
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
55-206 |
2.64e-15 |
|
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: 76.12 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGigsdlnKEIFYVP--QRPYTAVG------- 125
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG------KDITNLPphKRPVNTVFqnyalfp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 126 --TLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDEC 203
Cdd:cd03300 86 hlTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKP--------SQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
...
gi 720069164 204 TSA 206
Cdd:cd03300 158 LGA 160
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
43-213 |
2.77e-15 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 76.07 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLvEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGY------------IFKPGIG-SDL 109
Cdd:cd03260 1 IELRDLNVYYGDKHAL-KDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegevlldgkdIYDLDVDvLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 110 NKEIFYVPQRPYTAVGTLRDQLIYPLTVAEESEPLTQEGMVE-LLKNVDL-EYLLDRYPpekeinwGDELSLGEQQRLGM 187
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEeALRKAALwDEVKDRLH-------ALGLSGGQQQRLCL 152
|
170 180 190
....*....|....*....|....*....|
gi 720069164 188 ARLFYHKPKFAILDECTSAV----TTDMEE 213
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALdpisTAKIEE 182
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
719-889 |
3.16e-15 |
|
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: 76.11 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 719 LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS---RCVFYVPQRPYTCLGTLRDQIIY-- 793
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKslrSMIGVVLQDTFLFSGTIMENIRLgr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 794 PLSQEEAELSVVKMLGTGDNSDDRAHILDTHLRsilervrliyllerEGGwdasvnweDILSLGEQQRLGMARLFFHNPK 873
Cdd:cd03254 102 PNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLG--------------ENG--------GNLSQGERQLLAIARAMLRDPK 159
|
170
....*....|....*.
gi 720069164 874 FGILDECTnaTSVDVE 889
Cdd:cd03254 160 ILILDEAT--SNIDTE 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
43-207 |
5.55e-15 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 75.41 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI------GSDLNKEIFYV 116
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdireqdPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 117 PQRpytaVG-----TLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLE--YLLDRYPpekeinwgDELSLGEQQRLGMAR 189
Cdd:cd03295 81 IQQ----IGlfphmTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYP--------HELSGGQQQRVGVAR 148
|
170
....*....|....*...
gi 720069164 190 LFYHKPKFAILDECTSAV 207
Cdd:cd03295 149 ALAADPPLLLMDEPFGAL 166
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
55-245 |
6.02e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.19 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGigsdlNKEIFYVPQRpytavGTLRDQLiyP 134
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----GARVAYVPQR-----SEVPDSL--P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 135 LTVAEESE-----------PLTQEGMVEL---LKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAIL 200
Cdd:NF040873 72 LTVRDLVAmgrwarrglwrRLTRDDRAAVddaLERVGLADLAGRQL--------GELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 720069164 201 DECTSAVTTDMEERFCAKVR---AMGTSCITISHRPALVAFHDMVLSL 245
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAeehARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
719-907 |
7.98e-15 |
|
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: 74.49 E-value: 7.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 719 LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGSrcVFYVPQRpytcLGTLRDqiiYPLSQE 798
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR--IGYVPQR----RSIDRD---FPISVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 799 EaelsVVKM-------LGTGDNSDDRAHILDthlrsILERVRLIYLLEREGGwdasvnwedILSLGEQQRLGMARLFFHN 871
Cdd:cd03235 89 D----VVLMglyghkgLFRRLSKADKAKVDE-----ALERVGLSELADRQIG---------ELSGGQQQRVLLARALVQD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 720069164 872 PKFGILDECTnaTSVDV--EEHLYKLANEM---GITVVTTS 907
Cdd:cd03235 151 PDLLLLDEPF--AGVDPktQEDIYELLRELrreGMTILVVT 189
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
59-207 |
1.03e-14 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 74.71 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSnllIT---GPNGSGKSSLFRVLGGLWPLVSG--YIFkpgiGSDLNKE-------IFYVPQRPYtavgt 126
Cdd:COG1131 16 LDGVSLTVEPGE---IFgllGPNGAGKTTTIRMLLGLLRPTSGevRVL----GEDVARDpaevrrrIGYVPQEPA----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 127 lrdqlIYP-LTVAE----------ESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKP 195
Cdd:COG1131 84 -----LYPdLTVREnlrffarlygLPRKEARERIDELLELFGLTDAADRKV--------GTLSGGMKQRLGLALALLHDP 150
|
170
....*....|..
gi 720069164 196 KFAILDECTSAV 207
Cdd:COG1131 151 ELLILDEPTSGL 162
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
378-913 |
1.69e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.84 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 378 IASLNGTSVKYV-------LEQDKA--AFIRLTGISVLQSAASSIVA----PSLRYLTARLALgwRIRLtqHLLKNYLRK 444
Cdd:TIGR00958 172 LSSLGEMFIPFYtgrvidtLGGDKGppALASAIFFMCLLSIASSVSAglrgGSFNYTMARINL--RIRE--DLFRSLLRQ 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 445 N-AFYKVfHMSGhdiDADQRISHDV----EKLTTDLSGLVTGMVKPTVDI---LWFTWRMKLLTgrrgvailyaymLLGL 516
Cdd:TIGR00958 248 DlGFFDE-NKTG---ELTSRLSSDTqtmsRSLSLNVNVLLRNLVMLLGLLgfmLWLSPRLTMVT------------LINL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 517 GFLRSITPDFG---DLTSRE-QELEGTFRFMHTRLRTHAESVAFFGGGSREKamvdSRFQELLDHCRMLLKKK------- 585
Cdd:TIGR00958 312 PLVFLAEKVFGkryQLLSEElQEAVAKANQVAEEALSGMRTVRSFAAEEGEA----SRFKEALEETLQLNKRKalayagy 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 586 -WLFGILDDFITKqlphNVTW-GLSLLYAMEHKGDrALTS---TQGELAHALRFLASVvsqsflaFGDILELnrkylllS 660
Cdd:TIGR00958 388 lWTTSVLGMLIQV----LVLYyGGQLVLTGKVSSG-NLVSfllYQEQLGEAVRVLSYV-------YSGMMQA-------V 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 661 GGINRIFELeelLDSAKNgvsLPESQSMFKKDDvttEDIISFSEVDIITPAQ--KLLARQLTFDITPGKSLLVTGPNGSG 738
Cdd:TIGR00958 449 GASEKVFEY---LDRKPN---IPLTGTLAPLNL---EGLIEFQDVSFSYPNRpdVPVLKGLTFTLHPGEVVALVGPSGSG 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 739 KSSIFRVLRGVWPIATGRLV---KPCQNIKDVGGSRCVFYVPQRPYTCLGTLRDQIIYPLSQEEAE--LSVVKMLGTGDn 813
Cdd:TIGR00958 520 KSTVAALLQNLYQPTGGQVLldgVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEeiMAAAKAANAHD- 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 814 sddrahildthlrsilervrliYLLEREGGWDASVNWE-DILSLGEQQRLGMARLFFHNPKFGILDECTNATSVDVEEHL 892
Cdd:TIGR00958 599 ----------------------FIMEFPNGYDTEVGEKgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
570 580
....*....|....*....|.
gi 720069164 893 YKLANEMGITVVTTSQRPALI 913
Cdd:TIGR00958 657 QESRSRASRTVLLIAHRLSTV 677
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
665-910 |
1.95e-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: 77.02 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 665 RIFELEELLDSAKNGVSLPESQSMFKKDDVTTEDIiSFSEvdiitPAQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFR 744
Cdd:TIGR02868 306 RIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDL-SAGY-----PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 745 VLRGVWPIATGRLV---KPCQNIKDVGGSRCVFYVPQRPYTCLGTLRDQIiyplsqeeaelsvvkMLGTGDNSDDrahil 821
Cdd:TIGR02868 380 TLAGLLDPLQGEVTldgVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENL---------------RLARPDATDE----- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 822 dtHLRSILERVRL-IYLLEREGGWDASVNwED--ILSLGEQQRLGMARLFFHNPKFGILDECTNATSVDVEEHLYK--LA 896
Cdd:TIGR02868 440 --ELWAALERVGLaDWLRALPDGLDTVLG-EGgaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEdlLA 516
|
250
....*....|....
gi 720069164 897 NEMGITVVTTSQRP 910
Cdd:TIGR02868 517 ALSGRTVVLITHHL 530
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
700-924 |
2.70e-14 |
|
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: 73.01 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 700 ISFSEVDIITPAQKLLA-RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS---RCVFY 775
Cdd:cd03245 3 IEFRNVSFSYPNQEIPAlDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlrRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 776 VPQRPYTCLGTLRDQII--YPLSQEEAELSVVKMLGTGDNSDDRAHILDTHLrsilervrliylleREGGwdasvnweDI 853
Cdd:cd03245 83 VPQDVTLFYGTLRDNITlgAPLADDERILRAAELAGVTDFVNKHPNGLDLQI--------------GERG--------RG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 720069164 854 LSLGEQQRLGMARLFFHNPKFGILDECTNATSVDVEEHLYKLANEM--GITVVTTSQRPALipfhsleLQLID 924
Cdd:cd03245 141 LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSL-------LDLVD 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
59-231 |
2.71e-14 |
|
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: 71.66 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI-----GSDLNKEIFYVPQRPYtavgtlrdqlIY 133
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKdikkePEEVKRRIGYLPEEPS----------LY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 134 P-LTVaeesepltqegmvellknvdLEYLldryppekeinwgdELSLGEQQRLGMARLFYHKPKFAILDECTSAVttDME 212
Cdd:cd03230 86 EnLTV--------------------RENL--------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL--DPE 129
|
170 180
....*....|....*....|....
gi 720069164 213 ER-----FCAKVRAMGTSCITISH 231
Cdd:cd03230 130 SRrefweLLRELKKEGKTILLSSH 153
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
53-247 |
3.63e-14 |
|
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: 72.89 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 53 PTGNVLvEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIF---KPGIGSD---LNKEIFYVPQRPYTAVGT 126
Cdd:cd03248 25 PDTLVL-QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPISQYEhkyLHSKVSLVGQEPVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 127 LRDQLIYPLTVAEE---SEPLTQEGMVELLKNVDLEYllDRYPPEKeinwGDELSLGEQQRLGMARLFYHKPKFAILDEC 203
Cdd:cd03248 104 LQDNIAYGLQSCSFecvKEAAQKAHAHSFISELASGY--DTEVGEK----GSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 720069164 204 TSAVTTDMEERFCAKVRA--MGTSCITISHRPALVAFHDMVLSLDG 247
Cdd:cd03248 178 TSALDAESEQQVQQALYDwpERRTVLVIAHRLSTVERADQILVLDG 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
55-221 |
3.83e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.21 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGSDLNKeifYVPQRPYtaVGTlRDQLIYP 134
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---VAEACHY--LGH-RNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 135 LTVAEE---------SEPLtqeGMVELLKNVDLEYLLDRypPEKeinwgdELSLGEQQRLGMARLF-YHKPKFaILDECT 204
Cdd:PRK13539 88 LTVAENlefwaaflgGEEL---DIAAALEAVGLAPLAHL--PFG------YLSAGQKRRVALARLLvSNRPIW-ILDEPT 155
|
170
....*....|....*..
gi 720069164 205 SAVTTDMEERFCAKVRA 221
Cdd:PRK13539 156 AALDAAAVALFAELIRA 172
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
43-232 |
3.99e-14 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 72.96 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPT--GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG-SDLN-----KEIF 114
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDiRDLNlrwlrSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 115 YVPQRPYTAVGTLRDQLIY---PLTVAEESEPLTQEGMVELLKNvdleyLLDRYppEKEI-NWGDELSLGEQQRLGMARL 190
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYgkpDATDEEVEEAAKKANIHDFIMS-----LPDGY--DTLVgERGSQLSGGQKQRIAIARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 720069164 191 FYHKPKFAILDECTSAVTTDMEERFCAKV-RAM-GTSCITISHR 232
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALdRAMkGRTTIVIAHR 197
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
43-246 |
4.81e-14 |
|
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: 72.65 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG------SDLNKEIFYV 116
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDirevtlDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 117 PQRPYTAVGTLRDQLIYPLTVAeeseplTQEGMVELLKNVDLEYLLDRYPPEKEINWGD---ELSLGEQQRLGMARLFYH 193
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDA------TDEEVIEAAKAAQIHDKIMRFPDGYDTIVGErglKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 720069164 194 KPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDMVLSLD 246
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLSTIVNADKIIVLK 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
50-231 |
4.95e-14 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 73.45 E-value: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 50 VVTPTGNVL-VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFkpgI-GSDLN------------KEIFY 115
Cdd:cd03294 30 ILKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVL---IdGQDIAamsrkelrelrrKKISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 116 V-------PQRpytavgTLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMA 188
Cdd:cd03294 107 VfqsfallPHR------TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYP--------DELSGGMQQRVGLA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 720069164 189 RLFYHKPKFAILDECTSA----VTTDMEERFCAKVRAMGTSCITISH 231
Cdd:cd03294 173 RALAVDPDILLMDEAFSAldplIRREMQDELLRLQAELQKTIVFITH 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
43-205 |
7.67e-14 |
|
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: 72.42 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTpTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGG-LWPLVSG--YIF--KPGIGS--DLNKEIFY 115
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNdvRLFgeRRGGEDvwELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 116 V-P--QRPYTAVGTLRDqliyplTVA----------EESEPLTQEGMVELLKNVDLEYLLDRYppekeinWGdELSLGEQ 182
Cdd:COG1119 83 VsPalQLRFPRDETVLD------VVLsgffdsiglyREPTDEQRERARELLELLGLAHLADRP-------FG-TLSQGEQ 148
|
170 180
....*....|....*....|...
gi 720069164 183 QRLGMARLFYHKPKFAILDECTS 205
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTA 171
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
43-207 |
8.28e-14 |
|
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: 72.22 E-value: 8.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIgsDLNKEIFYVPQRPYT 122
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT--DINKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 123 AVGTLRDQ--LIYPLTVAE---------------------ESEpltQEGMVELLKNVDLEylldryppEKEINWGDELSL 179
Cdd:cd03256 79 QIGMIFQQfnLIERLSVLEnvlsgrlgrrstwrslfglfpKEE---KQRALAALERVGLL--------DKAYQRADQLSG 147
|
170 180
....*....|....*....|....*...
gi 720069164 180 GEQQRLGMARLFYHKPKFAILDECTSAV 207
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASL 175
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
664-913 |
8.83e-14 |
|
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: 75.17 E-value: 8.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 664 NRIFELEELLDSAKNGVSLPESQSmfkkddvttedIISFSEVDIITP-AQKLLARQLTFDITPGKSLLVTGPNGSGKSSI 742
Cdd:COG4618 306 RRLNELLAAVPAEPERMPLPRPKG-----------RLSVENLTVVPPgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 743 FRVLRGVWPIATG--RL--VKPCQNIKDVGGsRCVFYVPQRPYtcL--GTLRDQIiyplsqeeAELsvvkmlgtGDNSDD 816
Cdd:COG4618 375 ARLLVGVWPPTAGsvRLdgADLSQWDREELG-RHIGYLPQDVE--LfdGTIAENI--------ARF--------GDADPE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 817 R---------AH--IL------DTHLrsilervrliylleregGWDASVnwediLSLGEQQRLGMARLFFHNPKFGILDE 879
Cdd:COG4618 436 KvvaaaklagVHemILrlpdgyDTRI-----------------GEGGAR-----LSGGQRQRIGLARALYGDPRLVVLDE 493
|
250 260 270
....*....|....*....|....*....|....*....
gi 720069164 880 cTNAtSVDV--EEHLY---KLANEMGITVVTTSQRPALI 913
Cdd:COG4618 494 -PNS-NLDDegEAALAaaiRALKARGATVVVITHRPSLL 530
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-245 |
9.32e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 75.53 E-value: 9.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 2 NSGYADRIHElmFISRelsvihdKSSIQRNGGSNYFSEANYIEFAGVKVVTPT-GNVLV-EDLTLRVEPGSNLLITGPNG 79
Cdd:TIGR00958 447 AVGASEKVFE--YLDR-------KPNIPLTGTLAPLNLEGLIEFQDVSFSYPNrPDVPVlKGLTFTLHPGEVVALVGPSG 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 80 SGKSSLFRVLGGLWPLVSGYIF---KPGIGSD---LNKEIFYVPQRPYTAVGTLRDQLIYPLTVAEESEPLTqegmVELL 153
Cdd:TIGR00958 518 SGKSTVAALLQNLYQPTGGQVLldgVPLVQYDhhyLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMA----AAKA 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 154 KNVD-----LEYLLDRYPPEKeinwGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAMGTSCIT 228
Cdd:TIGR00958 594 ANAHdfimeFPNGYDTEVGEK----GSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLL 669
|
250
....*....|....*..
gi 720069164 229 ISHRPALVAFHDMVLSL 245
Cdd:TIGR00958 670 IAHRLSTVERADQILVL 686
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
712-906 |
1.13e-13 |
|
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: 72.00 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 712 QKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLV---KPCQNI--KDVggSRCVFYVPQRPytclgt 786
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDLASLsrREL--ARRIAYVPQEP------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 787 lrdQIIYPLSQEEaelsVVkMLG--------TGDNSDDRAHIldthlRSILERVRLIYLLEREggWDAsvnwediLSLGE 858
Cdd:COG1120 85 ---PAPFGLTVRE----LV-ALGryphlglfGRPSAEDREAV-----EEALERTGLEHLADRP--VDE-------LSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 720069164 859 QQRLGMARLFFHNPKFGILDECTNA----TSVDVEEHLYKLANEMGITVVTT 906
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHldlaHQLEVLELLRRLARERGRTVVMV 194
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
717-882 |
1.35e-13 |
|
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: 69.21 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLV-----KPCQNIKDVGGSrcVFYVPQrpYTCLG---TLR 788
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdLTDDERKSLRKE--IGYVFQ--DPQLFprlTVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 789 DQIIYPLSqeeaelsvVKMLGTgDNSDDRAHIldthlrsILERVRLIYLLEREGGWDASVnwediLSLGEQQRLGMARLF 868
Cdd:pfam00005 78 ENLRLGLL--------LKGLSK-REKDARAEE-------ALEKLGLGDLADRPVGERPGT-----LSGGQRQRVAIARAL 136
|
170
....*....|....
gi 720069164 869 FHNPKFGILDECTN 882
Cdd:pfam00005 137 LTKPKLLLLDEPTA 150
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
697-890 |
2.41e-13 |
|
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: 70.58 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 697 EDIISFSEVDIITPAQ--KLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLV---KPCQNIKDVGGSR 771
Cdd:cd03248 9 KGIVKFQNVTFAYPTRpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 772 CVFYVPQRPYTCLGTLRDQIIYPLSQeeAELSVVKMLGTGDNSDDrahildthlrsilervrliYLLEREGGWDASVNWE 851
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHS-------------------FISELASGYDTEVGEK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 720069164 852 -DILSLGEQQRLGMARLFFHNPKFGILDECTNATSVDVEE 890
Cdd:cd03248 148 gSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
701-926 |
2.54e-13 |
|
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: 68.43 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 701 SFSEVDIITPAQKLLaRQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLV---KPCQNIKDVGGSRCVFYVP 777
Cdd:cd00267 1 EIENLSFRYGGRTAL-DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILidgKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 778 QrpytclgtlrdqiiyplsqeeaelsvvkmlgtgdnsddrahildthlrsilervrliyllereggwdasvnwediLSLG 857
Cdd:cd00267 80 Q---------------------------------------------------------------------------LSGG 84
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 720069164 858 EQQRLGMARLFFHNPKFGILDECTNATSVD----VEEHLYKLANEmGITVVTTSQRPALIPFHSLE-LQLIDGE 926
Cdd:cd00267 85 QRQRVALARALLLNPDLLLLDEPTSGLDPAsrerLLELLRELAEE-GRTVIIVTHDPELAELAADRvIVLKDGK 157
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
55-202 |
3.15e-13 |
|
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: 69.59 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFkpgIGS-DLNK------EIFYVPQR----PYTA 123
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY---IGGrDVTDlppkdrDIAMVFQNyalyPHMT 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 720069164 124 VgtlRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDE 202
Cdd:cd03301 89 V---YDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKP--------KQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
55-233 |
3.25e-13 |
|
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: 69.44 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGSD-----LNKEIFYVPQRPytAVGTLrd 129
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDfqrdsIARGLLYLGHAP--GIKTT-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 130 qliypLTVAEESEPL----TQEGMVELLKNVDLEYLLDRYppekeinwGDELSLGEQQRLGMARLFYHKPKFAILDECTS 205
Cdd:cd03231 88 -----LSVLENLRFWhadhSDEQVEEALARVGLNGFEDRP--------VAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|.
gi 720069164 206 AVTTDMEERFCAKVR---AMGTSCITISHRP 233
Cdd:cd03231 155 ALDKAGVARFAEAMAghcARGGMVVLTTHQD 185
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
43-246 |
3.55e-13 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 69.95 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKV-VTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG------SDLNKEIFY 115
Cdd:cd03251 1 VEFKNVTFrYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDvrdytlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 116 VPQRPYTAVGTLRDQLIYPLTVAeeseplTQEGMVELLKNVDLEYLLDRYPPEKEINWGD---ELSLGEQQRLGMARLFY 192
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGA------TREEVEEAARAANAHEFIMELPEGYDTVIGErgvKLSGGQRQRIAIARALL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 720069164 193 HKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDMVLSLD 246
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAHRLSTIENADRIVVLE 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
717-913 |
4.51e-13 |
|
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: 69.03 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGG---SRCVFYVPQRPytclgtlRDQIIY 793
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkelRRKVGLVFQNP-------DDQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 794 PLSQEEAELSVVKMLGTGDNSDDRAhildthlRSILERVRLIYLLEReggwdasvnweDI--LSLGEQQRLGMARLFFHN 871
Cdd:cd03225 91 PTVEEEVAFGLENLGLPEEEIEERV-------EEALELVGLEGLRDR-----------SPftLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 720069164 872 PKFGILDECTN----ATSVDVEEHLYKLANEmGITVVTTSQRPALI 913
Cdd:cd03225 153 PDILLLDEPTAgldpAGRRELLELLKKLKAE-GKTIIIVTHDLDLL 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
61-238 |
5.29e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 61 DLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLwplvsgYIFKPGIGSdlnkeiFYVPQRPYTAVGTLRDQlIYPLTVAEE 140
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA------LKGTPVAGC------VDVPDNQFGREASLIDA-IGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 141 SepltqegmVELLKNVDLE--YLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAK 218
Cdd:COG2401 115 A--------VELLNAVGLSdaVLWLRRF--------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARN 178
|
170 180
....*....|....*....|....
gi 720069164 219 V----RAMGTSCITISHRPALVAF 238
Cdd:COG2401 179 LqklaRRAGITLVVATHHYDVIDD 202
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
55-221 |
6.73e-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: 68.54 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGSDLNKEIfyvPQRPYTAVGTlRDQLIYP 134
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE---PHENILYLGH-LPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 135 LTVAE---------ESEPLTQEGMVELLKNVDLEYLLDRYppekeinwgdeLSLGEQQRLGMARLFYHKPKFAILDECTS 205
Cdd:TIGR01189 88 LSALEnlhfwaaihGGAQRTIEDALAAVGLTGFEDLPAAQ-----------LSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170
....*....|....*.
gi 720069164 206 AVTTDMEERFCAKVRA 221
Cdd:TIGR01189 157 ALDKAGVALLAGLLRA 172
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
43-210 |
8.35e-13 |
|
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: 68.76 E-value: 8.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGV-KVVTPTGN--VLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI------GSDL---N 110
Cdd:cd03258 2 IELKNVsKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllsGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 111 KEIFYVPQ-------RpytavgTLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQ 183
Cdd:cd03258 82 RRIGMIFQhfnllssR------TVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYP--------AQLSGGQKQ 147
|
170 180 190
....*....|....*....|....*....|
gi 720069164 184 RLGMARLFYHKPKFAILDECTSAV---TTD 210
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALdpeTTQ 177
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
700-881 |
1.22e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.39 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 700 ISFSEVDIITPAQKLLA-RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS---RCVFY 775
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVlKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalrQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 776 VPQRPYTCLGTLRDQIIypLSQEEAelsvvkmlgtgdnSDDRahildthLRSILERVRLIYLLEREGGWDAsvnWedI-- 853
Cdd:PRK11160 419 VSQRVHLFSATLRDNLL--LAAPNA-------------SDEA-------LIEVLQQVGLEKLLEDDKGLNA---W--Lge 471
|
170 180 190
....*....|....*....|....*....|..
gi 720069164 854 ----LSLGEQQRLGMARLFFHNPKFGILDECT 881
Cdd:PRK11160 472 ggrqLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
43-214 |
1.44e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.58 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGV-KVVTPTgnVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI----GSDLNKEI---- 113
Cdd:PRK09493 2 IEFKNVsKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvndPKVDERLIrqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 114 ------FYV-PQrpYTAvgtLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLG 186
Cdd:PRK09493 80 gmvfqqFYLfPH--LTA---LENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYP--------SELSGGQQQRVA 146
|
170 180
....*....|....*....|....*...
gi 720069164 187 MARLFYHKPKFAILDECTSAVttDMEER 214
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSAL--DPELR 172
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
55-202 |
1.49e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.52 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI-----GSDLNKEIFYVPQRPytavGtlrd 129
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrqRDEYHQDLLYLGHQP----G---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 130 qlIYPLTVAEE--------SEPLTQEGMVELLKNVDL---EYLLDRYppekeinwgdeLSLGEQQRLGMARLFYHKPKFA 198
Cdd:PRK13538 85 --IKTELTALEnlrfyqrlHGPGDDEALWEALAQVGLagfEDVPVRQ-----------LSAGQQRRVALARLWLTRAPLW 151
|
....
gi 720069164 199 ILDE 202
Cdd:PRK13538 152 ILDE 155
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
55-231 |
1.66e-12 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 68.13 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG-SDLNKE---IFYVPQR----PYTavgT 126
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDiTNLPPEkrdISYVPQNyalfPHM---T 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 127 LRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDECTSA 206
Cdd:cd03299 88 VYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKP--------ETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180
....*....|....*....|....*....
gi 720069164 207 VTTDMEERFCAKV----RAMGTSCITISH 231
Cdd:cd03299 160 LDVRTKEKLREELkkirKEFGVTVLHVTH 188
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
43-239 |
1.75e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 67.43 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG-SDL-NKEIFYVPQRP 120
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvSDLrGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 121 YTAVGTLR--------DQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFY 192
Cdd:cd03292 81 GVVFQDFRllpdrnvyENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALP--------AELSGGEQQRVAIARAIV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 720069164 193 HKPKFAILDECTSAVTTDMEERFC---AKVRAMGTSCITISHRPALVAFH 239
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMnllKKINKAGTTVVVATHAKELVDTT 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
43-214 |
2.07e-12 |
|
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: 67.22 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVeDLTLRVEPG-SNLLitGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI-----GSDLNKEIFYV 116
Cdd:cd03264 1 LQLENLTKRYGKKRALD-GVSLTLGPGmYGLL--GPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 117 PQ--RPYTAVgTLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEyllDRYppEKEINwgdELSLGEQQRLGMARLFYHK 194
Cdd:cd03264 78 PQefGVYPNF-TVREFLDYIAWLKGIPSKEVKARVDEVLELVNLG---DRA--KKKIG---SLSGGMRRRVGIAQALVGD 148
|
170 180
....*....|....*....|
gi 720069164 195 PKFAILDECTsaVTTDMEER 214
Cdd:cd03264 149 PSILIVDEPT--AGLDPEER 166
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
713-920 |
3.05e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 713 KLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVG-GSRCVFyvpqrpytcLGTlRDQI 791
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvAEACHY---------LGH-RNAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 792 iyplsqeEAELSVVkmlgtgDNSDDRAHILDTHLRSI---LERVRLIYLLEREGGWdasvnwediLSLGEQQRLGMARLF 868
Cdd:PRK13539 85 -------KPALTVA------ENLEFWAAFLGGEELDIaaaLEAVGLAPLAHLPFGY---------LSAGQKRRVALARLL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 869 FHNPKFGILDECTNATSVD--------VEEHLyklaNEMGITVVTTSQRPALIPFHSLEL 920
Cdd:PRK13539 143 VSNRPIWILDEPTAALDAAavalfaelIRAHL----AQGGIVIAATHIPLGLPGARELDL 198
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
715-920 |
3.12e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 66.61 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 715 LARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGSRcvfyvpqrpytclgtlRDQIIY- 793
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP----------------HENILYl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 794 -PLSQEEAELSVVkmlgtgDNSDDRAHILDTHLRSILERVRLIYLLEREggwDASVNWediLSLGEQQRLGMARLFFHNP 872
Cdd:TIGR01189 79 gHLPGLKPELSAL------ENLHFWAAIHGGAQRTIEDALAAVGLTGFE---DLPAAQ---LSAGQQRRLALARLWLSRR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 720069164 873 KFGILDECTNATSVD--------VEEHLYKlaneMGITVVTTSQRPALIPFHSLEL 920
Cdd:TIGR01189 147 PLWILDEPTTALDKAgvallaglLRAHLAR----GGIVLLTTHQDLGLVEARELRL 198
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
59-236 |
3.13e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 66.92 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGSDLNKE--IFYVPQ-RPYTAVGTLRDQLIYpl 135
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARnrIGYLPEeRGLYPKMKVIDQLVY-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 136 tvaeesepLTQ-EGM--VELLKNVDleYLLDRYP-PEKEINWGDELSLGEQQRLGMARLFYHKPKFAILDECTSA---VT 208
Cdd:cd03269 94 --------LAQlKGLkkEEARRRID--EWLERLElSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGldpVN 163
|
170 180
....*....|....*....|....*...
gi 720069164 209 TDMEERFCAKVRAMGTSCITISHRPALV 236
Cdd:cd03269 164 VELLKDVIRELARAGKTVILSTHQMELV 191
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
717-907 |
3.62e-12 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 67.42 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRL----VKPCQNIKDVGgsrcvfYVPQRpytclGTL-RDqi 791
Cdd:COG1121 23 EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgKPPRRARRRIG------YVPQR-----AEVdWD-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 792 iYPLSQEEaelsVVKM-------LGTGDNSDDRAHILDthlrsILERVRLIYLLEReggwdasvnweDI--LSLGEQQRL 862
Cdd:COG1121 90 -FPITVRD----VVLMgrygrrgLFRRPSRADREAVDE-----ALERVGLEDLADR-----------PIgeLSGGQQQRV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 720069164 863 GMARLFFHNPKFGILDECTnaTSVDV--EEHLYKL---ANEMGITVVTTS 907
Cdd:COG1121 149 LLARALAQDPDLLLLDEPF--AGVDAatEEALYELlreLRREGKTILVVT 196
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
59-247 |
5.03e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 67.35 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGS------DLNKEIFYVPQRPYTA-VG-TLRDQ 130
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLseetvwDVRRQVGMVFQNPDNQfVGaTVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 131 LIYPLtvaeESEPLTQEGMVE----LLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDECTSA 206
Cdd:PRK13635 103 VAFGL----ENIGVPREEMVErvdqALRQVGMEDFLNREP--------HRLSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 720069164 207 VTTDMEERFCAKVRAM----GTSCITISHRPALVAFHDMVLSLDG 247
Cdd:PRK13635 171 LDPRGRREVLETVRQLkeqkGITVLSITHDLDEAAQADRVIVMNK 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
700-909 |
5.51e-12 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 66.48 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 700 ISFSEVDIITPAQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS---RCVFYV 776
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDslrRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 777 PQRpyTCL--GTLRDQIIY--PLSQEEAELSVVKmlgtgdnsddRAHILDTHLRSilervrliyllerEGGWDASVNWED 852
Cdd:cd03253 81 PQD--TVLfnDTIGYNIRYgrPDATDEEVIEAAK----------AAQIHDKIMRF-------------PDGYDTIVGERG 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 853 I-LSLGEQQRLGMARLFFHNPKFGILDECTNATSVDVEEHLYKLANEM--GITVVTTSQR 909
Cdd:cd03253 136 LkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHR 195
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
55-206 |
6.83e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 6.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG-SDLNKEIF-----YVPQRPYTAVGTLR 128
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDiSTLKPEIYrqqvsYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 720069164 129 DQLIYPLTVAEEsepltQEGMVELLKnvDLEYL-LDRYPPEKEINwgdELSLGEQQRLGMARLFYHKPKFAILDECTSA 206
Cdd:PRK10247 99 DNLIFPWQIRNQ-----QPDPAIFLD--DLERFaLPDTILTKNIA---ELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
61-233 |
9.52e-12 |
|
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: 65.39 E-value: 9.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 61 DLTLRVE---PGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPG-IGSDLNKEIFYVPQRpyTAVG----------- 125
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtVLFDSRKKINLPPQQ--RKIGlvfqqyalfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 126 -TLRDQLIYPLTVAEESEPLTQEGmvELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDECT 204
Cdd:cd03297 90 lNVRENLAFGLKRKRNREDRISVD--ELLDLLGLDHLLNRYP--------AQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190
....*....|....*....|....*....|...
gi 720069164 205 SAVTTDMEERFCAKVRAMGTS----CITISHRP 233
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNlnipVIFVTHDL 192
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
45-245 |
1.01e-11 |
|
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: 65.92 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 45 FAGVKVVTptgnvlveDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYI-FKpgiGSDLNK----EI------ 113
Cdd:cd03219 10 FGGLVALD--------DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlFD---GEDITGlpphEIarlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 114 --FYVPqRPYT--------AVG-TLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQ 182
Cdd:cd03219 79 rtFQIP-RLFPeltvlenvMVAaQARTGSGLLLARARREEREARERAEELLERVGLADLADRPA--------GELSYGQQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 720069164 183 QRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAMGTSCITIshrpaLVAFHDM--VLSL 245
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITV-----LLVEHDMdvVMSL 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
59-246 |
1.03e-11 |
|
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: 65.13 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG------SDLNKEIFYVPQRPYTAVGTLRDqli 132
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDistiplEDLRSSLTIIPQDPTLFSGTIRS--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 133 ypltvaeesepltqegmvellkNVDLEyllDRYPpEKEI-------NWGDELSLGEQQRLGMARLFYHKPKFAILDECTS 205
Cdd:cd03369 101 ----------------------NLDPF---DEYS-DEEIygalrvsEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 720069164 206 AVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDMVLSLD 246
Cdd:cd03369 155 SIDYATDALIQKTIREEftNSTILTIAHRLRTIIDYDKILVMD 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
712-906 |
1.04e-11 |
|
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: 64.38 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 712 QKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLV---KPCQNIKDVGGSRCVFYVPQrpytclgtlr 788
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILldgKDLASLSPKELARKIAYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 789 dqiiyplsqeeaelsvvkmlgtgdnsddrahildthlrsILERVRLIYLLEReggwdasvNWEDiLSLGEQQRLGMARLF 868
Cdd:cd03214 81 ---------------------------------------ALELLGLAHLADR--------PFNE-LSGGERQRVLLARAL 112
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 720069164 869 FHNPKFGILDECTNA----TSVDVEEHLYKLANEMGITVVTT 906
Cdd:cd03214 113 AQEPPILLLDEPTSHldiaHQIELLELLRRLARERGKTVVMV 154
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
55-246 |
1.08e-11 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 68.61 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGSD------LNKEIFYVPQRPYTAVGTLR 128
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdidrhtLRQFINYLPQEPYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 129 DQLIYpltvaEESEPLTQEGMVELLKNVDLEYLLDRYPP--EKEINW-GDELSLGEQQRLGMARLFYHKPKFAILDECTS 205
Cdd:TIGR01193 566 ENLLL-----GAKENVSQDEIWAACEIAEIKDDIENMPLgyQTELSEeGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 720069164 206 AVTTDMEERFCAKVRAMG-TSCITISHRPALVAFHDMVLSLD 246
Cdd:TIGR01193 641 NLDTITEKKIVNNLLNLQdKTIIFVAHRLSVAKQSDKIIVLD 682
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
720-904 |
1.13e-11 |
|
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: 68.39 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 720 TFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS------RCVFYVPQRPYTCL---GTLRDQ 790
Cdd:COG1123 285 SLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrelrRRVQMVFQDPYSSLnprMTVGDI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 791 IIYPLsqeeaelsvvKMLGTGDNSDDRAHIldthlRSILERVRLIY-LLER---EggwdasvnwediLSLGEQQRLGMAR 866
Cdd:COG1123 365 IAEPL----------RLHGLLSRAERRERV-----AELLERVGLPPdLADRyphE------------LSGGQRQRVAIAR 417
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 720069164 867 LFFHNPKFGILDECTNA--TSV--DVEEHLYKLANEMGITVV 904
Cdd:COG1123 418 ALALEPKLLILDEPTSAldVSVqaQILNLLRDLQRELGLTYL 459
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
55-206 |
1.67e-11 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 65.52 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYI---------FKPGigsDLNKeifyvpQRpytAVG 125
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVrlngrplaaWSPW---ELAR------RR---AVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 126 TLRDQLIYPLTVAE--------------ESEPLTQEGMVEllknVDLEYLLDR-YPpekeinwgdELSLGEQQRLGMARL 190
Cdd:COG4559 81 PQHSSLAFPFTVEEvvalgraphgssaaQDRQIVREALAL----VGLAHLAGRsYQ---------TLSGGEQQRVQLARV 147
|
170 180
....*....|....*....|...
gi 720069164 191 F-------YHKPKFAILDECTSA 206
Cdd:COG4559 148 LaqlwepvDGGPRWLFLDEPTSA 170
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
59-220 |
1.71e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 65.05 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI-GSDLN---KEIFYVPQRpYTAVG--TLRDQLI 132
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdATDVPvqeRNVGFVFQH-YALFRhmTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 133 YPLTV----AEESEPLTQEGMVELLKNVDLEYLLDRYPPekeinwgdELSLGEQQRLGMARLFYHKPKFAILDECTSAVT 208
Cdd:cd03296 97 FGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPA--------QLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170
....*....|..
gi 720069164 209 tdmeerfcAKVR 220
Cdd:cd03296 169 --------AKVR 172
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
59-202 |
1.80e-11 |
|
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: 64.55 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGSDLNKEifyvpqrPYTAVGTLRD-QLIYPLTV 137
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-------ALRRIGALIEaPGFYPNLT 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 720069164 138 AEESEPLTQEGMVELLKNVD--LEYLLDRYPPEKEINwgdELSLGEQQRLGMARLFYHKPKFAILDE 202
Cdd:cd03268 89 ARENLRLLARLLGIRKKRIDevLDVVGLKDSAKKKVK---GFSLGMKQRLGIALALLGNPDLLILDE 152
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
52-231 |
2.08e-11 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 66.23 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 52 TPTGNV-LVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP---LVSGYI-FKpgiGSDLN------------KEIF 114
Cdd:COG0444 13 TRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEIlFD---GEDLLklsekelrkirgREIQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 115 YVPQRPYTA---VGTLRDQLIYPLTV---AEESEPLTQegMVELLKNVDL---EYLLDRYPpekeinwgDELSLGEQQRL 185
Cdd:COG0444 90 MIFQDPMTSlnpVMTVGDQIAEPLRIhggLSKAEARER--AIELLERVGLpdpERRLDRYP--------HELSGGMRQRV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 720069164 186 GMARLFYHKPKFAILDECTSA--VTT---------DMEERFcakvramGTSCITISH 231
Cdd:COG0444 160 MIARALALEPKLLIADEPTTAldVTIqaqilnllkDLQREL-------GLAILFITH 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
61-206 |
2.44e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 64.65 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 61 DLTLRVEPGSNLLITGPNGSGKSSLFRVL--------GGLwpLVSGYIF------KPGIGSDLNKEIFYVPQR----PYT 122
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprsGTL--NIAGNHFdfsktpSDKAIRELRRNVGMVFQQynlwPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 123 avgTLRDQLI-YPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPPEkeinwgdeLSLGEQQRLGMARLFYHKPKFAILD 201
Cdd:PRK11124 98 ---TVQQNLIeAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLH--------LSGGQQQRVAIARALMMEPQVLLFD 166
|
....*
gi 720069164 202 ECTSA 206
Cdd:PRK11124 167 EPTAA 171
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
56-276 |
3.10e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.90 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 56 NVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFkpgI-GSDL------NKEIFYVPQR----PYTAV 124
Cdd:PRK11432 19 NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF---IdGEDVthrsiqQRDICMVFQSyalfPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 125 GtlrDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDECT 204
Cdd:PRK11432 96 G---ENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYV--------DQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 720069164 205 SAVTTDMEERFCAKVRAM----GTSCITISH-RPALVAFHDMVLSLDGEGGWKVHSKREDSPQPAEVRLSSFMIRSS 276
Cdd:PRK11432 165 SNLDANLRRSMREKIRELqqqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDAN 241
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
663-913 |
3.55e-11 |
|
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: 67.17 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 663 INRIFELEELLDSAKNGVSLPESQSMFKKDDVttediiSFSevdiITPAQKLLARQLTFDITPGKSLLVTGPNGSGKSSI 742
Cdd:COG2274 448 LDDILDLPPEREEGRSKLSLPRLKGDIELENV------SFR----YPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 743 FRVLRGVWPIATGRLVKPCQNIKDVGGS---RCVFYVPQRPYTCLGTLRDQIIY---PLSQEEAeLSVVKMLGTGDNSDD 816
Cdd:COG2274 518 LKLLLGLYEPTSGRILIDGIDLRQIDPAslrRQIGVVLQDVFLFSGTIRENITLgdpDATDEEI-IEAARLAGLHDFIEA 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 817 RAHILDTHLRsilervrliyllerEGGwdasvnweDILSLGEQQRLGMARLFFHNPKFGILDECTNATSVDVEEHLYKLA 896
Cdd:COG2274 597 LPMGYDTVVG--------------EGG--------SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL 654
|
250
....*....|....*....
gi 720069164 897 NEM--GITVVTTSQRPALI 913
Cdd:COG2274 655 RRLlkGRTVIIIAHRLSTI 673
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-232 |
4.16e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.79 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 4 GYADRIHELMfisrELSVIHdkssiQRNGGSNYFSE-ANYIEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGK 82
Cdd:PRK11174 319 GAAESLVTFL----ETPLAH-----PQQGEKELASNdPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 83 SSLFRVLGGLWP-----LVSGYIFkpgigSDLN-----KEIFYVPQRPYTAVGTLRDQliypLTVAEESepLTQEGMVEL 152
Cdd:PRK11174 390 TSLLNALLGFLPyqgslKINGIEL-----RELDpeswrKHLSWVGQNPQLPHGTLRDN----VLLGNPD--ASDEQLQQA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 153 LKNVDLEYLLDRYP-----PEKEINWGdeLSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFC-AKVRAM-GTS 225
Cdd:PRK11174 459 LENAWVSEFLPLLPqgldtPIGDQAAG--LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMqALNAASrRQT 536
|
....*..
gi 720069164 226 CITISHR 232
Cdd:PRK11174 537 TLMVTHQ 543
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
717-905 |
4.61e-11 |
|
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: 63.74 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVK---------PCQNIKDVGGSRC----VFyvpQRPYTC 783
Cdd:cd03260 17 KDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEgevlldgkdIYDLDVDVLELRRrvgmVF---QKPNPF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 784 LGTLRDQIIYPL------SQEEAELSVVKML---GTGDNSDDRAHILDthlrsilervrliyllereggwdasvnwediL 854
Cdd:cd03260 94 PGSIYDNVAYGLrlhgikLKEELDERVEEALrkaALWDEVKDRLHALG-------------------------------L 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 720069164 855 SLGEQQRLGMARLFFHNPKFGILDECTNA----TSVDVEEHLYKLANEMGITVVT 905
Cdd:cd03260 143 SGGQQQRLCLARALANEPEVLLLDEPTSAldpiSTAKIEELIAELKKEYTIVIVT 197
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
717-904 |
5.31e-11 |
|
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: 63.28 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLV---KPCQNIKDVGGS----RCVFYVPQRpYTCLGTL-- 787
Cdd:cd03255 21 KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgTDISKLSEKELAafrrRHIGFVFQS-FNLLPDLta 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 788 RDQIIYPLsqeeaELSVVKmlgtGDNSDDRAHildthlrSILERVRLIYLLEReggwdaSVNWediLSLGEQQRLGMARL 867
Cdd:cd03255 100 LENVELPL-----LLAGVP----KKERRERAE-------ELLERVGLGDRLNH------YPSE---LSGGQQQRVAIARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 720069164 868 FFHNPKFGILDECTNA----TSVDVEEHLYKLANEMGITVV 904
Cdd:cd03255 155 LANDPKIILADEPTGNldseTGKEVMELLRELNKEAGTTIV 195
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
61-207 |
7.01e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 61 DLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGigsdlNKEIFYVPQRPYTAVgTLrdqliyPLTVAE- 139
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----KLRIGYVPQKLYLDT-TL------PLTVNRf 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 140 -ESEPLTQEG-MVELLKNVDLEYLLDrYPPEKeinwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSAV 207
Cdd:PRK09544 90 lRLRPGTKKEdILPALKRVQAGHLID-APMQK-------LSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
56-246 |
7.74e-11 |
|
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: 66.51 E-value: 7.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 56 NVLVEDLTLRVEPGSNLLITGPNGSGKSS----LFRVLGGlwplVSGYIFKPGIG------SDLNKEIFYVPQRPYTAVG 125
Cdd:TIGR00957 1299 DLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINES----AEGEIIIDGLNiakiglHDLRFKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 126 TLRDQLiypltvaeesEPLTQEGMVELLKNVDLEYLLD--RYPPEKeINW-----GDELSLGEQQRLGMARLFYHKPKFA 198
Cdd:TIGR00957 1375 SLRMNL----------DPFSQYSDEEVWWALELAHLKTfvSALPDK-LDHecaegGENLSVGQRQLVCLARALLRKTKIL 1443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 720069164 199 ILDECTSAVTTDMEERFCAKVRAMGTSC--ITISHRPALVAFHDMVLSLD 246
Cdd:TIGR00957 1444 VLDEATAAVDLETDNLIQSTIRTQFEDCtvLTIAHRLNTIMDYTRVIVLD 1493
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
45-232 |
8.01e-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: 61.29 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 45 FAGVKVVtptgnvlvEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGigsdlnKEifYVPQRPYTAv 124
Cdd:cd03216 10 FGGVKAL--------DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG------KE--VSFASPRDA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 125 gtlRDQLIypltvaeesepltqeGMVellknvdleylldrYppekeinwgdELSLGEQQRLGMARLFYHKPKFAILDECT 204
Cdd:cd03216 73 ---RRAGI---------------AMV--------------Y----------QLSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190
....*....|....*....|....*....|.
gi 720069164 205 SAVTTDMEERFCA---KVRAMGTSCITISHR 232
Cdd:cd03216 111 AALTPAEVERLFKvirRLRAQGVAVIFISHR 141
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
55-206 |
9.14e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 63.25 E-value: 9.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLgglwplvSGYIfKPGIGS-DLNkeifyvpQRPYT----------- 122
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL-------SGEL-SPDSGEvRLN-------GRPLAdwspaelarrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 123 AVgtLRDQ--LIYPLTVAE--------------ESEPLTQEGMVEllknVDLEYLLDR-YPpekeinwgdELSLGEQQRL 185
Cdd:PRK13548 79 AV--LPQHssLSFPFTVEEvvamgraphglsraEDDALVAAALAQ----VDLAHLAGRdYP---------QLSGGEQQRV 143
|
170 180
....*....|....*....|....*..
gi 720069164 186 GMARLF------YHKPKFAILDECTSA 206
Cdd:PRK13548 144 QLARVLaqlwepDGPPRWLLLDEPTSA 170
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
39-206 |
9.66e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 64.35 E-value: 9.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 39 EANYIEFAGVkVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFkpgIGsdlNKEIFYVP- 117
Cdd:COG3842 2 AMPALELENV-SKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL---LD---GRDVTGLPp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 118 -QRPytaVGTL-RDQLIYP-LTVAEE-SEPLTQEGM--------V-ELLKNVDLEYLLDRYPpekeinwgDELSLGEQQR 184
Cdd:COG3842 75 eKRN---VGMVfQDYALFPhLTVAENvAFGLRMRGVpkaeirarVaELLELVGLEGLADRYP--------HQLSGGQQQR 143
|
170 180
....*....|....*....|..
gi 720069164 185 LGMARLFYHKPKFAILDECTSA 206
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSA 165
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
59-202 |
1.05e-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: 62.45 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSG---------------YIFKPGIGsdlnkeifYVPQrpyta 123
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsirfdgrditglpphERARAGIG--------YVPE----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 124 vgtlrDQLIYP-LTVAEE----SEPLTQEGMVEllknvDLEYLLDRYPPEKEI--NWGDELSLGEQQRLGMARLFYHKPK 196
Cdd:cd03224 83 -----GRRIFPeLTVEENlllgAYARRRAKRKA-----RLERVYELFPRLKERrkQLAGTLSGGEQQMLAIARALMSRPK 152
|
....*.
gi 720069164 197 FAILDE 202
Cdd:cd03224 153 LLLLDE 158
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
713-922 |
1.45e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.74 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 713 KLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLvkpCQNIKDVGGSRCVFYvpqRPYTCLGTLRDqiI 792
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV---LWQGEPIRRQRDEYH---QDLLYLGHQPG--I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 793 YP-LSQEE-----AELSvvkmlgtGDNSDDRAHildthlrSILERVRliyLLEREggwDASVNwedILSLGEQQRLGMAR 866
Cdd:PRK13538 86 KTeLTALEnlrfyQRLH-------GPGDDEALW-------EALAQVG---LAGFE---DVPVR---QLSAGQQRRVALAR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 867 LFFHNPKFGILDECTNA---TSVDV-EEHLYKLANEMGITVVTTSQRPALIPFHSLELQL 922
Cdd:PRK13538 143 LWLTRAPLWILDEPFTAidkQGVARlEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRL 202
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
45-231 |
2.36e-10 |
|
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: 61.98 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 45 FAGVKVVtptgnvlvEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYI-FKpgiGSDLNK------------ 111
Cdd:COG0411 14 FGGLVAV--------DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlFD---GRDITGlpphriarlgia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 112 ------EIF---------YVPQRPYTAVGTLRDQLIYPLTVAEESEpLTQEGMvELLKNVDLEYLLDRYPpekeinwgDE 176
Cdd:COG0411 83 rtfqnpRLFpeltvlenvLVAAHARLGRGLLAALLRLPRARREERE-ARERAE-ELLERVGLADRADEPA--------GN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 720069164 177 LSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRA----MGTSCITISH 231
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRlrdeRGITILLIEH 211
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
59-236 |
5.35e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.03 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFkpGIGSDL-----------NKEIFYVPQRPYTAVG-- 125
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVA--WLGKDLlgmkddewravRSDIQMIFQDPLASLNpr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 126 -TLRDQLIYPLTV------AEESEPLTQEGM--VELLKNvdleyLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPK 196
Cdd:PRK15079 115 mTIGEIIAEPLRTyhpklsRQEVKDRVKAMMlkVGLLPN-----LINRYP--------HEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 720069164 197 FAILDECTSAVTTDMEerfcAKV--------RAMGTSCITISHRPALV 236
Cdd:PRK15079 182 LIICDEPVSALDVSIQ----AQVvnllqqlqREMGLSLIFIAHDLAVV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
697-913 |
5.93e-10 |
|
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: 62.61 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 697 EDIISFSEVDIITPAQKLLA-RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIA---TGRLVKPCQNIKDVGG--- 769
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAvDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEalr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 770 SRCVFYVPQRPYTCL--GTLRDQIIYPLsqeeaelsvvkMLGTGDNSDDRAHILDthlrsILERVRLIYLLEReggwdas 847
Cdd:COG1123 82 GRRIGMVFQDPMTQLnpVTVGDQIAEAL-----------ENLGLSRAEARARVLE-----LLEAVGLERRLDR------- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 848 vnWEDILSLGEQQRLGMARLFFHNPKFGILDECTNA----TSVDVEEHLYKLANEMGITVVTTSQRPALI 913
Cdd:COG1123 139 --YPHQLSGGQRQRVAIAMALALDPDLLIADEPTTAldvtTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
55-202 |
6.21e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.77 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFkpgIGSDLnkEIFYVPQRpytavgtlRDQLIYP 134
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK---LGETV--KIGYFDQH--------QEELDPD 393
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 720069164 135 LTVAEESEPLTQEGMVELLKNVdLEYLLdrYPPE---KEINwgdELSLGEQQRLGMARLFYHKPKFAILDE 202
Cdd:COG0488 394 KTVLDELRDGAPGGTEQEVRGY-LGRFL--FSGDdafKPVG---VLSGGEKARLALAKLLLSPPNVLLLDE 458
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
717-913 |
6.38e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 59.55 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVkpcqnikdVGGSRCVFYVPQRpytclGTLRDQIiyPLS 796
Cdd:NF040873 9 HGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR--------RAGGARVAYVPQR-----SEVPDSL--PLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 797 QEEAelsvVKM-------LGTGDNSDDRAHILDthlrsILERVRLIYLLEREggwdasvnwEDILSLGEQQRLGMARLFF 869
Cdd:NF040873 74 VRDL----VAMgrwarrgLWRRLTRDDRAAVDD-----ALERVGLADLAGRQ---------LGELSGGQRQRALLAQGLA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 720069164 870 HNPKFGILDECTNATSVDVEEHLYKLANEM---GITVVTTSQRPALI 913
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEEharGATVVVVTHDLELV 182
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
55-206 |
6.96e-10 |
|
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: 59.85 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI-----GSDLN---KEIFYVPQR----PYT 122
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltddKKNINelrQKVGMVFQQfnlfPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 123 AVgtLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDE 202
Cdd:cd03262 92 TV--LENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYP--------AQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
....
gi 720069164 203 CTSA 206
Cdd:cd03262 162 PTSA 165
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
719-908 |
8.83e-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: 60.26 E-value: 8.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 719 LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLvkpcqNIKDVGGSRC-------VFYVPQRPYTCLG-TLRDQ 790
Cdd:COG4555 20 VSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSI-----LIDGEDVRKEprearrqIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 791 I-----IYPLSQEEAELSVvkmlgtgdnsddrahildthlRSILERVRLIYLLEReggwdasvNWEDiLSLGEQQRLGMA 865
Cdd:COG4555 95 IryfaeLYGLFDEELKKRI---------------------EELIELLGLEEFLDR--------RVGE-LSTGMKKKVALA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 720069164 866 RLFFHNPKFGILDECTNAtsVDVE------EHLYKLANEmGITVVTTSQ 908
Cdd:COG4555 145 RALVHDPKVLLLDEPTNG--LDVMarrllrEILRALKKE-GKTVLFSSH 190
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
718-923 |
9.96e-10 |
|
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: 59.15 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 718 QLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRlvkpcqnIKDVGGSrcvfyvPQRPYTCL---GTLRD-QIIY 793
Cdd:cd03268 18 DISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGE-------ITFDGKS------YQKNIEALrriGALIEaPGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 794 P-LSQEEAELSVVKMLGTGDNSDDRahILDT-HLRSIL-ERVRLiyllereggwdasvnwediLSLGEQQRLGMARLFFH 870
Cdd:cd03268 85 PnLTARENLRLLARLLGIRKKRIDE--VLDVvGLKDSAkKKVKG-------------------FSLGMKQRLGIALALLG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 720069164 871 NPKFGILDECTNATSVD----VEEHLYKLANEmGITVvttsqrpaLIPFHSL-ELQLI 923
Cdd:cd03268 144 NPDLLILDEPTNGLDPDgikeLRELILSLRDQ-GITV--------LISSHLLsEIQKV 192
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
55-206 |
1.23e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.12 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGigsdlnKEIFYVP--QRPYTAV-------- 124
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG------QDITHVPaeNRHVNTVfqsyalfp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 125 -GTLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDEC 203
Cdd:PRK09452 100 hMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKP--------HQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
...
gi 720069164 204 TSA 206
Cdd:PRK09452 172 LSA 174
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
57-232 |
1.28e-09 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 59.30 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 57 VLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIgsDLNKEIFYVPQRpytaVGTLRDQL-IYP- 134
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF--DVVKEPAEARRR----LGFVSDSTgLYDr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 135 LTVAEESE---------PLTQEGMVE-LLKNVDLEYLLDRYppekeinwGDELSLGEQQRLGMARLFYHKPKFAILDECT 204
Cdd:cd03266 93 LTARENLEyfaglyglkGDELTARLEeLADRLGMEELLDRR--------VGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180 190
....*....|....*....|....*....|.
gi 720069164 205 SA---VTTDMEERFCAKVRAMGTSCITISHR 232
Cdd:cd03266 165 TGldvMATRALREFIRQLRALGKCILFSTHI 195
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
51-202 |
1.32e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 59.70 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 51 VTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGL--WPLVSGYI-FKpgiGSDL---------NKEIFYVPQ 118
Cdd:COG0396 8 VSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSIlLD---GEDIlelspderaRAGIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 119 RP------------YTAVGTLRDQliypltvaEESEPLTQEGMVELLKNVDL-EYLLDRYppekeINWGdeLSLGEQQR- 184
Cdd:COG0396 85 YPveipgvsvsnflRTALNARRGE--------ELSAREFLKLLKEKMKELGLdEDFLDRY-----VNEG--FSGGEKKRn 149
|
170 180
....*....|....*....|
gi 720069164 185 --LGMARLfyhKPKFAILDE 202
Cdd:COG0396 150 eiLQMLLL---EPKLAILDE 166
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
718-922 |
1.35e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 58.66 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 718 QLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS--RCVFYVPQRPYTclgtlrdqiiypl 795
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiaRGLLYLGHAPGI------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 796 sqeEAELSVVKMLGTGDNSDDRAHILDThlrsiLERVRLiyllerEGGWDASVNWediLSLGEQQRLGMARLFFHNPKFG 875
Cdd:cd03231 85 ---KTTLSVLENLRFWHADHSDEQVEEA-----LARVGL------NGFEDRPVAQ---LSAGQQRRVALARLLLSGRPLW 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 720069164 876 ILDECTNA---TSVD-VEEHLYKLANEMGITVVTTSQRPALIPFHSLELQL 922
Cdd:cd03231 148 ILDEPTTAldkAGVArFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
43-246 |
1.52e-09 |
|
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: 61.66 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTP-TGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG------SDLNKEIFY 115
Cdd:TIGR02203 331 VEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDladytlASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 116 VPQRPYTAVGTLRDQLIYpltvaEESEPLTQEGMVELLKNVDLEYLLDRYPPEKEINWGDE---LSLGEQQRLGMARLFY 192
Cdd:TIGR02203 411 VSQDVVLFNDTIANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENgvlLSGGQRQRLAIARALL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 720069164 193 HKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDMVLSLD 246
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLmqGRTTLVIAHRLSTIEKADRIVVMD 541
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
64-248 |
1.63e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.02 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 64 LRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKpgIGSDLN------------KEIFYVPQRpYTAVGTL--RD 129
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL--VGQPLHqmdeearaklraKHVGFVFQS-FMLIPTLnaLE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 130 QLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPPEkeinwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSAVTT 209
Cdd:PRK10584 108 NVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ--------LSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 720069164 210 DMEERFCAKV----RAMGTSCITISHRPALVAFHDMVLSL-DGE 248
Cdd:PRK10584 180 QTGDKIADLLfslnREHGTTLILVTHDLQLAARCDRRLRLvNGQ 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
59-202 |
1.78e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.12 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSnllIT---GPNGSGKSSLFRVLGGLWPLVSGYIF---KPgIGSDLNKEIFYVPQ-RpytavG-----T 126
Cdd:COG4152 17 VDDVSFTVPKGE---IFgllGPNGAGKTTTIRIILGILAPDSGEVLwdgEP-LDPEDRRRIGYLPEeR-----GlypkmK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 127 LRDQLIYpltvaeesepLTQegmvelLKNVD-------LEYLLDRYppekEI--NWGD---ELSLGEQQRLGMARLFYHK 194
Cdd:COG4152 88 VGEQLVY----------LAR------LKGLSkaeakrrADEWLERL----GLgdRANKkveELSKGNQQKVQLIAALLHD 147
|
....*...
gi 720069164 195 PKFAILDE 202
Cdd:COG4152 148 PELLILDE 155
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-245 |
1.93e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.27 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 7 DRIHELMfisrelsvihdKSSIQRNGGSNYFSEANYIEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLF 86
Cdd:PRK10790 316 ERVFELM-----------DGPRQQYGNDDRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLA 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 87 RVLGGLWPLVSGYIFKPG------IGSDLNKEIFYVPQRPYTAVGTLRDQLiyplTVAEEsepLTQEGMVELLKNVDLEY 160
Cdd:PRK10790 385 SLLMGYYPLTEGEIRLDGrplsslSHSVLRQGVAMVQQDPVVLADTFLANV----TLGRD---ISEEQVWQALETVQLAE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 161 LLDRYPPEKEINWGDE---LSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEE---RFCAKVRAMgTSCITISHRPA 234
Cdd:PRK10790 458 LARSLPDGLYTPLGEQgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQaiqQALAAVREH-TTLVVIAHRLS 536
|
250
....*....|.
gi 720069164 235 LVAFHDMVLSL 245
Cdd:PRK10790 537 TIVEADTILVL 547
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
700-920 |
2.46e-09 |
|
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: 58.50 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 700 ISFSEVDIITPAQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLV--------KPCQNI-KDVGgs 770
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdgkditkKNLRELrRKVG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 771 rcvfYVPQRPytclgtlRDQIIYP--------------LSQEEAElsvvkmlgtgdnsdDRAhildthlRSILERVRLIY 836
Cdd:COG1122 79 ----LVFQNP-------DDQLFAPtveedvafgpenlgLPREEIR--------------ERV-------EEALELVGLEH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 837 LLEREggwdasvnwedI--LSLGEQQRLGMARLFFHNPKFGILDECTN----ATSVDVEEHLYKLaNEMGITVVTTSqrp 910
Cdd:COG1122 127 LADRP-----------PheLSGGQKQRVAIAGVLAMEPEVLVLDEPTAgldpRGRRELLELLKRL-NKEGKTVIIVT--- 191
|
250
....*....|
gi 720069164 911 alipfHSLEL 920
Cdd:COG1122 192 -----HDLDL 196
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
699-904 |
3.49e-09 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 58.14 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 699 IISFSEVDIITPAQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGSR------- 771
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 772 --CVFY----VPQRpytclgTLRDQIIYPLsqeeaelsvvKMLGTgdnsdDRAHIlDTHLRSILERVRliyLLEREggwD 845
Cdd:COG2884 81 igVVFQdfrlLPDR------TVYENVALPL----------RVTGK-----SRKEI-RRRVREVLDLVG---LSDKA---K 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 720069164 846 ASVnweDILSLGEQQRLGMARLFFHNPKFGILDECTN----ATSVDVEEHLYKLaNEMGITVV 904
Cdd:COG2884 133 ALP---HELSGGEQQRVAIARALVNRPELLLADEPTGnldpETSWEIMELLEEI-NRRGTTVL 191
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
717-907 |
4.07e-09 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 58.15 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGK--SLLvtGPNGSGKSSIFRVLRGVWPIATGRL----VKPCQNIKDVggSRCVFYVPQRPYtclgtlrdq 790
Cdd:COG1131 17 DGVSLTVEPGEifGLL--GPNGAGKTTTIRMLLGLLRPTSGEVrvlgEDVARDPAEV--RRRIGYVPQEPA--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 791 iIYPlsqeeaELSVVKMLG-TGDNSDDRAHILDTHLRSILERVRLIYLLEREGGWdasvnwediLSLGEQQRLGMARLFF 869
Cdd:COG1131 84 -LYP------DLTVRENLRfFARLYGLPRKEARERIDELLELFGLTDAADRKVGT---------LSGGMKQRLGLALALL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 720069164 870 HNPKFGILDECTNAtsVDVE------EHLYKLANEmGITVVTTS 907
Cdd:COG1131 148 HDPELLILDEPTSG--LDPEarrelwELLRELAAE-GKTVLLST 188
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
58-237 |
4.35e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.52 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 58 LVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPG----IGSD--------LNKEIFYVPQRPYTAVG 125
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlyFGKDifqidaikLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 126 -TLRDQLIYPLT---VAEESEplTQEGMVELLKNVDL-EYLLDRYPPEkeinwGDELSLGEQQRLGMARLFYHKPKFAIL 200
Cdd:PRK14246 105 lSIYDNIAYPLKshgIKEKRE--IKKIVEECLRKVGLwKEVYDRLNSP-----ASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 720069164 201 DECTSAV----TTDMEERFCAKVRAMgtSCITISHRPALVA 237
Cdd:PRK14246 178 DEPTSMIdivnSQAIEKLITELKNEI--AIVIVSHNPQQVA 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
45-232 |
5.25e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 45 FAGVKVVtptgnvlvEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIfkpgigSDLNKEI-FYVPQRPYTA 123
Cdd:PRK10762 14 FPGVKAL--------SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSI------LYLGKEVtFNGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 124 -VGTLRDQL--IYPLTVAEE----SEPLTQEGMVE----------LLKNVDLeylldRYPPEKEINwgdELSLGEQQRLG 186
Cdd:PRK10762 80 gIGIIHQELnlIPQLTIAENiflgREFVNRFGRIDwkkmyaeadkLLARLNL-----RFSSDKLVG---ELSIGEQQMVE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 720069164 187 MARLFYHKPKFAILDECTSAVT-TDMEERFcaKV----RAMGTSCITISHR 232
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALTdTETESLF--RVirelKSQGRGIVYISHR 200
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
717-894 |
5.58e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 57.09 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVkpcqnikdVGGSrcVFYVPQRPYTCLGTLRDQII--YP 794
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS--------VPGS--IAYVSQEPWIQNGTIRENILfgKP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 795 LSQEEAElSVVK---------MLGTGDNSDdrahildthlrsILERvrliyllereggwdaSVNwediLSLGEQQRLGMA 865
Cdd:cd03250 92 FDEERYE-KVIKacalepdleILPDGDLTE------------IGEK---------------GIN----LSGGQKQRISLA 139
|
170 180
....*....|....*....|....*....
gi 720069164 866 RLFFHNPKFGILDECTNATSVDVEEHLYK 894
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIFE 168
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
55-204 |
5.74e-09 |
|
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: 55.53 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLgglwplvsgyifkpgigsdlnkeifyvpqrpytavgtlrdqliyp 134
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI--------------------------------------------- 46
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 135 ltvAEESEPltQEGMVELLKNVDLEYLldryppekeinwgDELSLGEQQRLGMARLFYHKPKFAILDECT 204
Cdd:cd03221 47 ---AGELEP--DEGIVTWGSTVKIGYF-------------EQLSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
717-889 |
5.78e-09 |
|
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: 57.50 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS---RCVFYVPQRPYTCLGTLRDQiIY 793
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHdlrSRISIIPQDPVLFSGTIRSN-LD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 794 PLSQeeaelsvvkmlgtgdNSDDRahildthLRSILERVRLI-YLLEREGGWDASV-NWEDILSLGEQQRLGMARLFFHN 871
Cdd:cd03244 100 PFGE---------------YSDEE-------LWQALERVGLKeFVESLPGGLDTVVeEGGENLSVGQRQLLCLARALLRK 157
|
170
....*....|....*...
gi 720069164 872 PKFGILDECTnaTSVDVE 889
Cdd:cd03244 158 SKILVLDEAT--ASVDPE 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
719-907 |
6.42e-09 |
|
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: 56.25 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 719 LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS--RCVFYVPQRPYtclgtlrdqiIYPls 796
Cdd:cd03230 19 ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvkRRIGYLPEEPS----------LYE-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 797 qeeaELSVVKMLgtgdnsddrahildthlrsilervrliyllereggwdasvnwedILSLGEQQRLGMARLFFHNPKFGI 876
Cdd:cd03230 87 ----NLTVRENL--------------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190
....*....|....*....|....*....|....*
gi 720069164 877 LDECTNA----TSVDVEEHLYKLANEmGITVVTTS 907
Cdd:cd03230 119 LDEPTSGldpeSRREFWELLRELKKE-GKTILLSS 152
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
55-202 |
6.53e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.60 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIF---------------KPGIGsdlnkeifYVPQR 119
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplharaRRGIG--------YLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 120 PytavGTLRDQLIYP--LTVAEESEPLTQEG----MVELLKNVDLEYLLDryppekeiNWGDELSLGEQQRLGMARLFYH 193
Cdd:PRK10895 87 A----SIFRRLSVYDnlMAVLQIRDDLSAEQredrANELMEEFHIEHLRD--------SMGQSLSGGERRRVEIARALAA 154
|
....*....
gi 720069164 194 KPKFAILDE 202
Cdd:PRK10895 155 NPKFILLDE 163
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
59-202 |
6.60e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 57.30 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYI-FKpgiGSDLNKE---------IFYVPQRpytavgtlR 128
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIrFD---GEDITGLpphriarlgIGYVPEG--------R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 129 DqlIYP-LTVAE---------ESEPLTQEgmvellknvDLEYLLDRYPPEKEI--NWGDELSLGEQQRLGMARLFYHKPK 196
Cdd:COG0410 88 R--IFPsLTVEEnlllgayarRDRAEVRA---------DLERVYELFPRLKERrrQRAGTLSGGEQQMLAIGRALMSRPK 156
|
....*.
gi 720069164 197 FAILDE 202
Cdd:COG0410 157 LLLLDE 162
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
58-232 |
7.62e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 7.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 58 LVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYI--FKPGIGSDL---NKEIFYVPQR----PYTavgTLR 128
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlfERQSIKKDLctyQKQLCFVGHRsginPYL---TLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 129 DQLIYPLTVAEeseplTQEGMVELLKNVDLEYLLDrYPpekeinwGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVT 208
Cdd:PRK13540 93 ENCLYDIHFSP-----GAVGITELCRLFSLEHLID-YP-------CGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180
....*....|....*....|....*..
gi 720069164 209 TDMEERFCAKV---RAMGTSCITISHR 232
Cdd:PRK13540 160 ELSLLTIITKIqehRAKGGAVLLTSHQ 186
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
700-889 |
7.87e-09 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 57.11 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 700 ISFSEVDI-ITPAQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS---RCVFY 775
Cdd:cd03252 1 ITFEHVRFrYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlrRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 776 VPQRPYTCLGTLRDQIiyplsqeeaelsvvkmlGTGDNSDDRahildthlRSILERVRLI----YLLEREGGWDASVNWE 851
Cdd:cd03252 81 VLQENVLFNRSIRDNI-----------------ALADPGMSM--------ERVIEAAKLAgahdFISELPEGYDTIVGEQ 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 720069164 852 DI-LSLGEQQRLGMARLFFHNPKFGILDECTNATSVDVE 889
Cdd:cd03252 136 GAgLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
62-246 |
8.13e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 8.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 62 LTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIF-------KPGIgSDLNKEIFYVPQRPYTAVGTLRDQLiyp 134
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMiddcdvaKFGL-TDLRRVLSIIPQSPVLFSGTVRFNI--- 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 135 ltvaeesEPLTQE---GMVELLKNVDLEYLLDRYP--PEKEINWGDE-LSLGEQQRLGMARLFYHKPKFAILDECTSAVT 208
Cdd:PLN03232 1331 -------DPFSEHndaDLWEALERAHIKDVIDRNPfgLDAEVSEGGEnFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 720069164 209 TDMEERFCAKVRAMGTSC--ITISHRPALVAFHDMVLSLD 246
Cdd:PLN03232 1404 VRTDSLIQRTIREEFKSCtmLVIAHRLNTIIDCDKILVLS 1443
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
43-231 |
8.38e-09 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 57.13 E-value: 8.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVkVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSG--YIFKPGIGSDLNKEIFYVPQRp 120
Cdd:cd03261 1 IELRGL-TKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGevLIDGEDISGLSEAELYRLRRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 121 ytaVGTLRDQ--LIYPLTVAE-----------ESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGM 187
Cdd:cd03261 79 ---MGMLFQSgaLFDSLTVFEnvafplrehtrLSEEEIREIVLEKLEAVGLRGAEDLYP--------AELSGGMKKRVAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 720069164 188 AR--------LFYHKPkFAILDECTSAVTTDMEERFcakVRAMGTSCITISH 231
Cdd:cd03261 148 ARalaldpelLLYDEP-TAGLDPIASGVIDDLIRSL---KKELGLTSIMVTH 195
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
719-904 |
1.14e-08 |
|
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: 56.75 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 719 LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGR-------LVKPCQNIKDVGGSRcVFYVPQRPYTCLG---TLR 788
Cdd:cd03257 24 VSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSiifdgkdLLKLSRRLRKIRRKE-IQMVFQDPMSSLNprmTIG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 789 DQIIYPLsqeeaelsvvKMLGTGDNSDDRAHILDTHLRSILERVRLIYLLEREggwdasvnwediLSLGEQQRLGMARLF 868
Cdd:cd03257 103 EQIAEPL----------RIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHE------------LSGGQRQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 720069164 869 FHNPKFGILDECTNA----TSVDVEEHLYKLANEMGITVV 904
Cdd:cd03257 161 ALNPKLLIADEPTSAldvsVQAQILDLLKKLQEELGLTLL 200
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
55-204 |
1.19e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 56.75 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVE---DLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSG-YIFKpgiGSDLNKeifyvpqRPYTAVGTLRDQ 130
Cdd:PRK11629 18 GSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdVIFN---GQPMSK-------LSSAAKAELRNQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 131 ---LIY-----------------PLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARL 190
Cdd:PRK11629 88 klgFIYqfhhllpdftalenvamPLLIGKKKPAEINSRALEMLAAVGLEHRANHRP--------SELSGGERQRVAIARA 159
|
170
....*....|....
gi 720069164 191 FYHKPKFAILDECT 204
Cdd:PRK11629 160 LVNNPRLVLADEPT 173
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
59-243 |
1.19e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.43 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGS------DLNKEIFYVPQRPYTA-VG-TLRDQ 130
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteenvwDIRHKIGMVFQNPDNQfVGaTVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 131 LIYPLtvaeESEPLTQEGMV----ELLKNVDLEYLLDRYPPekeinwgdELSLGEQQRLGMARLFYHKPKFAILDECTSA 206
Cdd:PRK13650 103 VAFGL----ENKGIPHEEMKervnEALELVGMQDFKEREPA--------RLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 720069164 207 VTTDMEERFCAKVRAM----GTSCITISHRPALVAFHDMVL 243
Cdd:PRK13650 171 LDPEGRLELIKTIKGIrddyQMTVISITHDLDEVALSDRVL 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
55-231 |
1.26e-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: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIgsDLNKEIFYVPQRPyTAVGTL-RDQLIY 133
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE--DLTDLEDELPPLR-RRIGMVfQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 134 P-LTVAEesepltqegmvellkNVdleylldRYPpekeinwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSA---VTT 209
Cdd:cd03229 89 PhLTVLE---------------NI-------ALG----------LSGGQQQRVALARALAMDPDVLLLDEPTSAldpITR 136
|
170 180
....*....|....*....|...
gi 720069164 210 DMEERFCAKVRAM-GTSCITISH 231
Cdd:cd03229 137 REVRALLKSLQAQlGITVVLVTH 159
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
61-232 |
1.29e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.50 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 61 DLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIF---KP------------GIGsdlnkeifYVPQRPytavg 125
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILidgKPvrirsprdaialGIG--------MVHQHF----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 126 tlrdQLIYPLTVAE------ESEPLTQEGMVELLKnvDLEYLLDRY----PPEKEInwgDELSLGEQQRLGMARLFYHKP 195
Cdd:COG3845 90 ----MLVPNLTVAEnivlglEPTKGGRLDRKAARA--RIRELSERYgldvDPDAKV---EDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 720069164 196 KFAILDECTsAVTTDME-ERF---CAKVRAMGTSCITISHR 232
Cdd:COG3845 161 RILILDEPT-AVLTPQEaDELfeiLRRLAAEGKSIIFITHK 200
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
700-881 |
1.29e-08 |
|
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: 56.11 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 700 ISFSevdiiTPAQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGSRCVFYVPQR 779
Cdd:cd03226 5 ISFS-----YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 780 PYTCLGTlrdqiiyplSQEEAELsvvkMLGTGDNSDDRAHIldthlRSILERVRLIYLLEREgGWDasvnwediLSLGEQ 859
Cdd:cd03226 80 VDYQLFT---------DSVREEL----LLGLKELDAGNEQA-----ETVLKDLDLYALKERH-PLS--------LSGGQK 132
|
170 180
....*....|....*....|..
gi 720069164 860 QRLGMARLFFHNPKFGILDECT 881
Cdd:cd03226 133 QRLAIAAALLSGKDLLIFDEPT 154
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
44-232 |
1.82e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.11 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 44 EFAGVKVVtptgnvlvEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIF---KP----GIGSDLNKEIFYV 116
Cdd:COG1129 13 SFGGVKAL--------DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILldgEPvrfrSPRDAQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 117 PQRPytavgtlrdQLIYPLTVAE----ESEPlTQEGMV----------ELLKNVDLEylLDrypPEKEInwgDELSLGEQ 182
Cdd:COG1129 85 HQEL---------NLVPNLSVAEniflGREP-RRGGLIdwramrrrarELLARLGLD--ID---PDTPV---GDLSVAQQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 720069164 183 QRLGMARLFYHKPKFAILDECTSAVTTDMEERF---CAKVRAMGTSCITISHR 232
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTEREVERLfriIRRLKAQGVAIIYISHR 199
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
44-232 |
1.85e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.02 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 44 EFAGVKVVtptgnvlvEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPL--VSGYIF---------------KPGIg 106
Cdd:PRK13549 14 TFGGVKAL--------DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIfegeelqasnirdteRAGI- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 107 SDLNKEIFYVPQrpytavgtlrdqliypLTVAEE----SEPlTQEGMV----------ELLKNVDLEylLDRYPPEKein 172
Cdd:PRK13549 85 AIIHQELALVKE----------------LSVLENiflgNEI-TPGGIMdydamylraqKLLAQLKLD--INPATPVG--- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 720069164 173 wgdELSLGEQQRLGMARLFYHKPKFAILDECTSAVT---TDMEERFCAKVRAMGTSCITISHR 232
Cdd:PRK13549 143 ---NLGLGQQQLVEIAKALNKQARLLILDEPTASLTeseTAVLLDIIRDLKAHGIACIYISHK 202
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
55-238 |
1.88e-08 |
|
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: 55.23 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGlwplVSGYIFKPGigsdlnkEIfyvpqrpytavgTLRDQLIYP 134
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----HPKYEVTEG-------EI------------LFKGEDITD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 135 LTVAEESepltQEGMvellknvdleYLLDRYPPE----------KEINWGdeLSLGEQQRLGMARLFYHKPKFAILDECT 204
Cdd:cd03217 69 LPPEERA----RLGI----------FLAFQYPPEipgvknadflRYVNEG--FSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190
....*....|....*....|....*....|....*..
gi 720069164 205 SAVTTD---MEERFCAKVRAMGTSCITISHRPALVAF 238
Cdd:cd03217 133 SGLDIDalrLVAEVINKLREEGKSVLIITHYQRLLDY 169
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
57-246 |
2.01e-08 |
|
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: 55.01 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 57 VLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPG-----IGSDLNKEIFYVPQRPYTAVGTLRDql 131
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdLEKALSSLISVLNQRPYLFDTTLRN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 132 iypltvaeesepltqegmvellknvdleylldryppekeiNWGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDM 211
Cdd:cd03247 94 ----------------------------------------NLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190
....*....|....*....|....*....|....*..
gi 720069164 212 EERFCAKVRAM--GTSCITISHRPALVAFHDMVLSLD 246
Cdd:cd03247 134 ERQLLSLIFEVlkDKTLIWITHHLTGIEHMDKILFLE 170
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
717-912 |
2.28e-08 |
|
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: 55.60 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVG-GSRCVFYVPQRP--YTCLgTLRDQIIY 793
Cdd:cd03259 17 DDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPpERRNIGMVFQDYalFPHL-TVAENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 794 PLsqeeaelsvVKMLGTGDNSDDRAHildthlrSILERVRLIYLLEReggwdasvnWEDILSLGEQQRLGMARLFFHNPK 873
Cdd:cd03259 96 GL---------KLRGVPKAEIRARVR-------ELLELVGLEGLLNR---------YPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 720069164 874 FGILDECTNAtsVDVE------EHLYKLANEMGITV--VTTSQRPAL 912
Cdd:cd03259 151 LLLLDEPLSA--LDAKlreelrEELKELQRELGITTiyVTHDQEEAL 195
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
710-882 |
2.46e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 57.77 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 710 PAQKLLaRQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPcQNIKdVGgsrcvfYVPQRPYTCLG-TLR 788
Cdd:COG0488 9 GGRPLL-DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR-IG------YLPQEPPLDDDlTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 789 DQIIY---PLSQEEAELSVV--KMLGTGDNSDDRAHI-----------LDTHLRSILERVRLiylleREGGWDASVNwed 852
Cdd:COG0488 80 DTVLDgdaELRALEAELEELeaKLAEPDEDLERLAELqeefealggweAEARAEEILSGLGF-----PEEDLDRPVS--- 151
|
170 180 190
....*....|....*....|....*....|
gi 720069164 853 ILSLGEQQRLGMARLFFHNPKFGILDECTN 882
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTN 181
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
717-892 |
2.70e-08 |
|
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: 55.70 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS---RCVFYVPQRPYTCLGTLRDQIIY 793
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAslrRQIGLVSQDVFLFNDTVAENIAY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 794 plsqeeaelsvvkmlGTGDNSDDRahildthlrsILERVRLIYLLE----REGGWDASVNWEDI-LSLGEQQRLGMARLF 868
Cdd:cd03251 99 ---------------GRPGATREE----------VEEAARAANAHEfimeLPEGYDTVIGERGVkLSGGQRQRIAIARAL 153
|
170 180
....*....|....*....|....*
gi 720069164 869 FHNPKFGILDECTNAtsVDVE-EHL 892
Cdd:cd03251 154 LKDPPILILDEATSA--LDTEsERL 176
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
45-232 |
3.37e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.14 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 45 FAGVKVVtptgnvlvEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP--LVSGYIFKPgiGSDLNKEIFYVPQRPYT 122
Cdd:TIGR02633 11 FGGVKAL--------DGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWS--GSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 123 AVGTLRDQLIYPLTVAEE---SEPLTQEG-------MVELLKNVDLEYLLDRYPPEKEINwgdELSLGEQQRLGMARLFY 192
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENiflGNEITLPGgrmaynaMYLRAKNLLRELQLDADNVTRPVG---DYGGGQQQLVEIAKALN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 720069164 193 HKPKFAILDECTSAVTTDMEERFCAKVR---AMGTSCITISHR 232
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRdlkAHGVACVYISHK 200
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
59-247 |
4.25e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.46 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG-SDLNKE--------IFYVPQRPYTAVG---T 126
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlAKLNRAqrkafrrdIQMVFQDSISAVNprkT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 127 LRDQLIYP---LTVAEESEplTQEGMVELLKNVDL-EYLLDRYPPekeinwgdELSLGEQQRLGMARLFYHKPKFAILDE 202
Cdd:PRK10419 108 VREIIREPlrhLLSLDKAE--RLARASEMLRAVDLdDSVLDKRPP--------QLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 720069164 203 CTS-----------AVTTDMEERFcakvramGTSCITISHRPALVA-FHDMVLSLDG 247
Cdd:PRK10419 178 AVSnldlvlqagviRLLKKLQQQF-------GTACLFITHDLRLVErFCQRVMVMDN 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
55-231 |
4.28e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 56.38 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIgsDLNkeifYVP--QRPYTAVgtLRDQLI 132
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV--DLS----HVPpyQRPINMM--FQSYAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 133 YPLTVAEESEP--LTQEGMV---------ELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILD 201
Cdd:PRK11607 103 FPHMTVEQNIAfgLKQDKLPkaeiasrvnEMLGLVHMQEFAKRKP--------HQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190
....*....|....*....|....*....|....
gi 720069164 202 ECTSAVTTDMEERFCAKV----RAMGTSCITISH 231
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVvdilERVGVTCVMVTH 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
55-202 |
5.39e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 56.61 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGigsdlNKEIFYVPQRPYTAVG-TLRD---- 129
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----GLRIGYLPQEPPLDDDlTVLDtvld 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 130 ------QLIYPLTVAEESEPLTQEGMVELLK-------------NVDLEYLLDR-----YPPEKEINwgdELSLGEQQRL 185
Cdd:COG0488 85 gdaelrALEAELEELEAKLAEPDEDLERLAElqeefealggweaEARAEEILSGlgfpeEDLDRPVS---ELSGGWRRRV 161
|
170
....*....|....*..
gi 720069164 186 GMARLFYHKPKFAILDE 202
Cdd:COG0488 162 ALARALLSEPDLLLLDE 178
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
717-904 |
5.52e-08 |
|
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: 54.36 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRlvkpcqnI----KDVGGSRC-------VFYVPQrpytclg 785
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGS-------IrfdgRDITGLPPheraragIGYVPE------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 786 tlrDQIIYPlsqeeaELSVVK--MLGTGDNSDDRAhildthlRSILERV-----RLIYLLEREGGwdasvnwedILSLGE 858
Cdd:cd03224 83 ---GRRIFP------ELTVEEnlLLGAYARRRAKR-------KARLERVyelfpRLKERRKQLAG---------TLSGGE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 720069164 859 QQRLGMARLFFHNPKFGILDECTNATS---VD-VEEHLYKLaNEMGITVV 904
Cdd:cd03224 138 QQMLAIARALMSRPKLLLLDEPSEGLApkiVEeIFEAIREL-RDEGVTIL 186
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
51-201 |
5.63e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.23 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 51 VTPtgnvLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGigsdlnkEIFYVPQRPYTAVGTLRDQ 130
Cdd:TIGR01271 438 VTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 720069164 131 LIYPLTVAEESepltqegMVELLKNVDLEYLLDRYPPEKEINWGD---ELSLGEQQRLGMARLFYHKPKFAILD 201
Cdd:TIGR01271 507 IIFGLSYDEYR-------YTSVIKACQLEEDIALFPEKDKTVLGEggiTLSGGQRARISLARAVYKDADLYLLD 573
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
59-246 |
5.84e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.51 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG------SDLNKEIFYVPQRPYTAVGTLRDQLi 132
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDirtvtrASLRRNIAVVFQDAGLFNRSIEDNI- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 133 yplTVAEESEplTQEGMVELLKNVDLEYLLDRYPPEKEINWGD---ELSLGEQQRLGMARLFYHKPKFAILDECTSAVTT 209
Cdd:PRK13657 430 ---RVGRPDA--TDEEMRAAAERAQAHDFIERKPDGYDTVVGErgrQLSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
170 180 190
....*....|....*....|....*....|....*....
gi 720069164 210 DMEERFCAKVRAM--GTSCITISHRPALVAFHDMVLSLD 246
Cdd:PRK13657 505 ETEAKVKAALDELmkGRTTFIIAHRLSTVRNADRILVFD 543
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
54-888 |
8.72e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 54 TGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFR-VLGGLWPLVSGYIfkpgigsDLNKEIFYVPQRPYTAVGTLRDQLI 132
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSV-------VIRGSVAYVPQVSWIFNATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 133 YpltvAEESEPltqEGMVELLKNVDLEYLLDRYPPEKEINWGDE---LSLGEQQRLGMARLFYHKPKFAILDECTSAVTT 209
Cdd:PLN03232 701 F----GSDFES---ERYWRAIDVTALQHDLDLLPGRDLTEIGERgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 210 DMEERF---CAKVRAMGTSCITISHRPALVAFHDMVLsLDGEGGWKVHSKREDSPQPAEV--RL---SSFMIRSSEMNRQ 281
Cdd:PLN03232 774 HVAHQVfdsCMKDELKGKTRVLVTNQLHFLPLMDRII-LVSEGMIKEEGTFAELSKSGSLfkKLmenAGKMDATQEVNTN 852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 282 SDALA-VQQAFSVTIKDSAFPNSKEQSYVGEVLATSPPVDHKVplpvvpqlqMTPRTLPLRVAAMAKVLVPTLLdkQGAQ 360
Cdd:PLN03232 853 DENILkLGPTVTIDVSERNLGSTKQGKRGRSVLVKQEERETGI---------ISWNVLMRYNKAVGGLWVVMIL--LVCY 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 361 LFAVALLVVTRTWISdrIASLNGTSVKYvleqDKAAFIRLTGISVLQSAASSIvAPSLRYLTARLALGwrIRLTQHLLKN 440
Cdd:PLN03232 922 LTTEVLRVSSSTWLS--IWTDQSTPKSY----SPGFYIVVYALLGFGQVAVTF-TNSFWLISSSLHAA--KRLHDAMLNS 992
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 441 YLRKNAFYkvFHM--SGHDIDadqRISHDVEKLTTDLSGLVTGMVkptvDILWFTWRMKLLTGRRGVAILYAYMLLGLGF 518
Cdd:PLN03232 993 ILRAPMLF--FHTnpTGRVIN---RFSKDIGDIDRNVANLMNMFM----NQLWQLLSTFALIGTVSTISLWAIMPLLILF 1063
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 519 LRSITpdFGDLTSREQElegtfrfmhtRLrthaESVAffgggsreKAMVDSRFQELLDHCRMLLKKKwLFGILDDFITKQ 598
Cdd:PLN03232 1064 YAAYL--YYQSTSREVR----------RL----DSVT--------RSPIYAQFGEALNGLSSIRAYK-AYDRMAKINGKS 1118
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 599 LPHNVTWGLSLLyamehKGDRALTSTQGELAHALRFLASVVS-------QSFLAFGDILELNRKYL-----LLSGGINRI 666
Cdd:PLN03232 1119 MDNNIRFTLANT-----SSNRWLTIRLETLGGVMIWLTATFAvlrngnaENQAGFASTMGLLLSYTlnittLLSGVLRQA 1193
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 667 FELEELLDSAK---NGVSLPESQSMFKKDDVT-----TEDIISFSEVDI-ITPAQKLLARQLTFDITPGKSLLVTGPNGS 737
Cdd:PLN03232 1194 SKAENSLNSVErvgNYIDLPSEATAIIENNRPvsgwpSRGSIKFEDVHLrYRPGLPPVLHGLSFFVSPSEKVGVVGRTGA 1273
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 738 GKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS---RCVFYVPQRPYTCLGTLRDQiIYPLSqEEAELSVVKMLgtgdns 814
Cdd:PLN03232 1274 GKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTdlrRVLSIIPQSPVLFSGTVRFN-IDPFS-EHNDADLWEAL------ 1345
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 720069164 815 dDRAHILDTHLRSILervrliylleregGWDASV-NWEDILSLGEQQRLGMARLFFHNPKFGILDECTnaTSVDV 888
Cdd:PLN03232 1346 -ERAHIKDVIDRNPF-------------GLDAEVsEGGENFSVGQRQLLSLARALLRRSKILVLDEAT--ASVDV 1404
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
712-899 |
8.86e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.35 E-value: 8.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 712 QKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGvwpiatgrLVKPCQNIKDVGGSRCVFYVPQRpytclgtLRDQI 791
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLG--------LVAPDEGVIKRNGKLRIGYVPQK-------LYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 792 IYPLSqeeaeLSVVKMLGTGDNSDDrahILdthlrSILERVRLIYLLEREggwdasvnwEDILSLGEQQRLGMARLFFHN 871
Cdd:PRK09544 81 TLPLT-----VNRFLRLRPGTKKED---IL-----PALKRVQAGHLIDAP---------MQKLSGGETQRVLLARALLNR 138
|
170 180
....*....|....*....|....*...
gi 720069164 872 PKFGILDECTNATSVDVEEHLYKLANEM 899
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQL 166
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
43-205 |
9.06e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 54.61 E-value: 9.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKV-VTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIgsDLNKE--------- 112
Cdd:PRK13632 8 IKVENVSFsYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI--TISKEnlkeirkki 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 113 --IFYVPQRPYtaVG-TLRDQLIYPLtvaeESEPLTQEGM----VELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRL 185
Cdd:PRK13632 86 giIFQNPDNQF--IGaTVEDDIAFGL----ENKKVPPKKMkdiiDDLAKKVGMEDYLDKEP--------QNLSGGQKQRV 151
|
170 180
....*....|....*....|
gi 720069164 186 GMARLFYHKPKFAILDECTS 205
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTS 171
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
59-231 |
1.01e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.42 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPG--IGSDLNKEIFYVPQRPYTAV---------GTL 127
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdIAKISDAELREVRRKKIAMVfqsfalmphMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 128 RDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDECTSA- 206
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYP--------DELSGGMRQRVGLARALAINPDILLMDEAFSAl 195
|
170 180
....*....|....*....|....*...
gi 720069164 207 ---VTTDMEERFCAKVRAMGTSCITISH 231
Cdd:PRK10070 196 dplIRTEMQDELVKLQAKHQRTIVFISH 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
43-237 |
1.17e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPG--IGSDLNKEIFYVPQRp 120
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdITRLKNREVPFLRRQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 121 ytaVG------------TLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLeylLDryppeKEINWGDELSLGEQQRLGMA 188
Cdd:PRK10908 81 ---IGmifqdhhllmdrTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGL---LD-----KAKNFPIQLSGGEQQRVGIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 720069164 189 RLFYHKPKFAILDECTSAVTTDMEE---RFCAKVRAMGTSCITISHRPALVA 237
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEgilRLFEEFNRVGVTVLMATHDIGLIS 201
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
55-204 |
1.22e-07 |
|
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: 53.53 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSG--YIFkpgiGSDLNKE-------IFYVPQRPytavg 125
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGraTVA----GHDVVREprevrrrIGIVFQDL----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 126 TLRDQL-----------IYPLTVAEESEPLTqegmvELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHK 194
Cdd:cd03265 83 SVDDELtgwenlyiharLYGVPGAERRERID-----ELLDFVGLLEAADRLV--------KTYSGGMRRRLEIARSLVHR 149
|
170
....*....|
gi 720069164 195 PKFAILDECT 204
Cdd:cd03265 150 PEVLFLDEPT 159
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
29-201 |
1.28e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 54.09 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 29 QRNGGSNYFSEANYIEFAGVKVVtptGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFR-VLGGLWPlVSGYIFKPGigs 107
Cdd:cd03291 26 QENNDRKHSSDDNNLFFSNLCLV---GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEP-SEGKIKHSG--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 108 dlnkEIFYVPQRPYTAVGTLRDQLIYPLTVAEESepltqegMVELLKNVDLEYLLDRYPPEKEINWGD---ELSLGEQQR 184
Cdd:cd03291 99 ----RISFSSQFSWIMPGTIKENIIFGVSYDEYR-------YKSVVKACQLEEDITKFPEKDNTVLGEggiTLSGGQRAR 167
|
170
....*....|....*..
gi 720069164 185 LGMARLFYHKPKFAILD 201
Cdd:cd03291 168 ISLARAVYKDADLYLLD 184
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
700-905 |
1.97e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.38 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 700 ISFSEVDIItpaqkllaRQLTFDITPGKSLLVTGPNGSGKSSIFRVLRgvwpiatgRLVKPCQNIKDVG----GSRCVFY 775
Cdd:PRK14247 11 VSFGQVEVL--------DGVNLEIPDNTITALMGPSGSGKSTLLRVFN--------RLIELYPEARVSGevylDGQDIFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 776 VPqrpyTCLGTLRDQIIYPLSQEEAELSVVKMLGTGDnsddRAHILDTHLRSILERVRliYLLEREGGWDASVNWEDI-- 853
Cdd:PRK14247 75 MD----VIELRRRVQMVFQIPNPIPNLSIFENVALGL----KLNRLVKSKKELQERVR--WALEKAQLWDEVKDRLDApa 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 720069164 854 --LSLGEQQRLGMARLFFHNPKFGILDECTN----ATSVDVEEHLYKLANEMGITVVT 905
Cdd:PRK14247 145 gkLSGGQQQRLCIARALAFQPEVLLADEPTAnldpENTAKIESLFLELKKDMTIVLVT 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
49-211 |
2.05e-07 |
|
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: 52.89 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 49 KVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSG--YIFKPGIGSDLNK---EIFYVPQrpyta 123
Cdd:cd03263 8 KTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtaYINGYSIRTDRKAarqSLGYCPQ----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 124 vgtlrDQLIYP-LTVAE--------ESEPLTQEGMV--ELLKNVDLEYLLDRyppekEINwgdELSLGEQQRLGMARLFY 192
Cdd:cd03263 83 -----FDALFDeLTVREhlrfyarlKGLPKSEIKEEveLLLRVLGLTDKANK-----RAR---TLSGGMKRKLSLAIALI 149
|
170
....*....|....*....
gi 720069164 193 HKPKFAILDEctsaVTTDM 211
Cdd:cd03263 150 GGPSVLLLDE----PTSGL 164
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
43-210 |
2.40e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 53.93 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGN---VLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFkpgI-GSDLN-------- 110
Cdd:COG1135 2 IELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVL---VdGVDLTalserelr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 111 ---KEIFYVPQ-------RpytavgTLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLG 180
Cdd:COG1135 79 aarRKIGMIFQhfnllssR------TVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYP--------SQLSGG 144
|
170 180 190
....*....|....*....|....*....|....*
gi 720069164 181 EQQRLGMARLFYHKPKfaIL--DECTSAV---TTD 210
Cdd:COG1135 145 QKQRVGIARALANNPK--VLlcDEATSALdpeTTR 177
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
49-204 |
2.55e-07 |
|
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: 54.56 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 49 KVVTPTGNVLvEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSG-YIFKPGIgsdlnkEIFYVPQRPY------ 121
Cdd:TIGR03719 12 KVVPPKKEIL-KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGeARPQPGI------KVGYLPQEPQldptkt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 122 ------TAVGTLRDQL-----IYpLTVAEESEPLT-----QEGMVELLKNVD-------LEYLLD--RYPPekeinwGD- 175
Cdd:TIGR03719 85 vrenveEGVAEIKDALdrfneIS-AKYAEPDADFDklaaeQAELQEIIDAADawdldsqLEIAMDalRCPP------WDa 157
|
170 180 190
....*....|....*....|....*....|..
gi 720069164 176 ---ELSLGEQQRLGMARLFYHKPKFAILDECT 204
Cdd:TIGR03719 158 dvtKLSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
712-914 |
3.50e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.88 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 712 QKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGvwpIATGRLVKPCQNIKDVggsrcvfyvpqrpytclgtlrdqi 791
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---ALKGTPVAGCVDVPDN------------------------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 792 iyPLSQeeaELSVVKMLGTGDNSDDRahildthlrsilervrlIYLLEREGGWDAsVNWE---DILSLGEQQRLGMARLF 868
Cdd:COG2401 95 --QFGR---EASLIDAIGRKGDFKDA-----------------VELLNAVGLSDA-VLWLrrfKELSTGQKFRFRLALLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 720069164 869 FHNPKFGILDECTNA----TSVDVEEHLYKLANEMGITVVTTSQRP----ALIP 914
Cdd:COG2401 152 AERPKLLVIDEFCSHldrqTAKRVARNLQKLARRAGITLVVATHHYdvidDLQP 205
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
53-205 |
4.56e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.39 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 53 PTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPG--IGSDlNKEIFYVPQRpytaVGTL--- 127
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYD-KKSLLEVRKT----VGIVfqn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 128 -RDQLIYPlTVAEE----------SEPLTQEGMVELLKNVDLEYlLDRYPPEkeinwgdELSLGEQQRLGMARLFYHKPK 196
Cdd:PRK13639 87 pDDQLFAP-TVEEDvafgplnlglSKEEVEKRVKEALKAVGMEG-FENKPPH-------HLSGGQKKRVAIAGILAMKPE 157
|
....*....
gi 720069164 197 FAILDECTS 205
Cdd:PRK13639 158 IIVLDEPTS 166
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
62-246 |
8.03e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 8.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 62 LTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG------SDLNKEIFYVPQRPYTAVGTLRDQLiypl 135
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDiskfglMDLRKVLGIIPQAPVLFSGTVRFNL---- 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 136 tvaeesEPLTQEGMVELLKNVDLEYLLD--RYPP---EKEINWGDE-LSLGEQQRLGMARLFYHKPKFAILDECTSAVTT 209
Cdd:PLN03130 1334 ------DPFNEHNDADLWESLERAHLKDviRRNSlglDAEVSEAGEnFSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407
|
170 180 190
....*....|....*....|....*....|....*....
gi 720069164 210 DMEERFCAKVRAMGTSC--ITISHRPALVAFHDMVLSLD 246
Cdd:PLN03130 1408 RTDALIQKTIREEFKSCtmLIIAHRLNTIIDCDRILVLD 1446
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
41-246 |
8.47e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.72 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 41 NYIEFAGVKVVTP-TGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGG-LWP--------LVSGYIFKPGIGSDLN 110
Cdd:PRK13640 4 NIVEFKHVSFTYPdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPddnpnskiTVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 111 KEIFYVPQRPYTA-VG-TLRDQLIYPLtvaeESEPLTQEGMVELLKNVDLEYLLDRYPPEKEINwgdeLSLGEQQRLGMA 188
Cdd:PRK13640 84 EKVGIVFQNPDNQfVGaTVGDDVAFGL----ENRAVPRPEMIKIVRDVLADVGMLDYIDSEPAN----LSGGQKQRVAIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 720069164 189 RLFYHKPKFAILDECTSAVTTDMEERFCAKVRAM----GTSCITISHRPALVAFHDMVLSLD 246
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITHDIDEANMADQVLVLD 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
710-909 |
9.42e-07 |
|
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: 51.00 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 710 PAQKLLaRQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS---RCVFYVPQRPYTCLGT 786
Cdd:cd03249 14 PDVPIL-KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwlrSQIGLVSQEPVLFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 787 LRDQIIY---PLSQEEAElSVVKMLGTGDNSDDRAHILDTHLRsilervrliyllerEGGwdasvnweDILSLGEQQRLG 863
Cdd:cd03249 93 IAENIRYgkpDATDEEVE-EAAKKANIHDFIMSLPDGYDTLVG--------------ERG--------SQLSGGQKQRIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 720069164 864 MARLFFHNPKFGILDECTNATSVDVE----EHLYKLAneMGITVVTTSQR 909
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEklvqEALDRAM--KGRTTIVIAHR 197
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
43-248 |
9.64e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.80 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVE---DLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG-SDLNKEIFYVPQ 118
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEvlkGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 119 RPYTAVGTLRDQLIYPLTVAEESE-PLTQEGM---------VELLKNVDLEYLLDrYPPekeinwgDELSLGEQQRLGMA 188
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEvPAVYAGLerkqrllraQELLQRLGLEDRVE-YQP-------SQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 720069164 189 RLFYHKPKFAILDECTSAVTTDMEERFCA---KVRAMGTSCITISHRPALVAFHDMVLSL-DGE 248
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAilhQLRDRGHTVIIVTHDPQVAAQAERVIEIrDGE 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
59-236 |
1.08e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGSD---------LNKEIFYVPQRPYTAVG---T 126
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspgklqaLRRDIQFIFQDPYASLDprqT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 127 LRDQLIYPLTV-----AEESepltQEGMVELLKNVDLEylldrypPEKEINWGDELSLGEQQRLGMARLFYHKPKFAILD 201
Cdd:PRK10261 420 VGDSIMEPLRVhgllpGKAA----AARVAWLLERVGLL-------PEHAWRYPHEFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190
....*....|....*....|....*....|....*....
gi 720069164 202 ECTSAVTTDMEERFCAKV----RAMGTSCITISHRPALV 236
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLldlqRDFGIAYLFISHDMAVV 527
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
43-205 |
1.46e-06 |
|
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: 50.89 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLV-EDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGSDLNKEIFYVPQRpy 121
Cdd:TIGR04520 1 IEVENVSFSYPESEKPAlKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 122 taVGTL----RDQLIYPlTVAE------ESEPLTQEGMV----ELLKNVDLEYLLDRyPPEKeinwgdeLSLGEQQRLGM 187
Cdd:TIGR04520 79 --VGMVfqnpDNQFVGA-TVEDdvafglENLGVPREEMRkrvdEALKLVGMEDFRDR-EPHL-------LSGGQKQRVAI 147
|
170
....*....|....*...
gi 720069164 188 ARLFYHKPKFAILDECTS 205
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATS 165
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-207 |
1.56e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 24 DKSSIQR----NGGSNYFSEANyIEFAGVKVVTPTGNvlveDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGY 99
Cdd:TIGR00957 620 EPDSIERrtikPGEGNSITVHN-ATFTWARDLPPTLN----GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 100 IFKPGigsdlnkEIFYVPQRPYTAVGTLRDQLIYPLTVAEESEPLTQEGMVELlknVDLEYLL--DRYP-PEKEINwgde 176
Cdd:TIGR00957 695 VHMKG-------SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALL---PDLEILPsgDRTEiGEKGVN---- 760
|
170 180 190
....*....|....*....|....*....|.
gi 720069164 177 LSLGEQQRLGMARLFYHKPKFAILDECTSAV 207
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
700-904 |
1.57e-06 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 50.10 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 700 ISFSEVDIITPAQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGSRCvfyvpqr 779
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAI------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 780 PYtclgtLRDQI--IYPLSQEEAELSVVkmlgtgDNSDDRAHILDTHLRSILERVRLiyLLEREGGWDASVNWEDILSLG 857
Cdd:cd03292 74 PY-----LRRKIgvVFQDFRLLPDRNVY------ENVAFALEVTGVPPREIRKRVPA--ALELVGLSHKHRALPAELSGG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 720069164 858 EQQRLGMARLFFHNPKFGILDECTN----ATSVDVEEhLYKLANEMGITVV 904
Cdd:cd03292 141 EQQRVAIARAIVNSPTILIADEPTGnldpDTTWEIMN-LLKKINKAGTTVV 190
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
718-913 |
1.63e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.78 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 718 QLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS------RCVFYVPQRPYTCLG---TLR 788
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqalrRDIQFIFQDPYASLDprqTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 789 DQIIYPLSqeeaelsvVKMLGTGDNSDDRAHILdthlrsiLERVRliylLEREGGWdasvNWEDILSLGEQQRLGMARLF 868
Cdd:PRK10261 422 DSIMEPLR--------VHGLLPGKAAAARVAWL-------LERVG----LLPEHAW----RYPHEFSGGQRQRICIARAL 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 720069164 869 FHNPKFGILDECTNATSVDVEEH----LYKLANEMGITVVTTSQRPALI 913
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSIRGQiinlLLDLQRDFGIAYLFISHDMAVV 527
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
76-207 |
1.72e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.54 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 76 GPNGSGKSSLFRVL---GGLWPLVS--------GY-IFKPGIGS-DLNKEIFYVPQRPYTAVGTLRDQLIYPLTVAEESE 142
Cdd:PRK14239 38 GPSGSGKSTLLRSInrmNDLNPEVTitgsivynGHnIYSPRTDTvDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKD 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 720069164 143 PLTQEGMVEL-LKNVDL-EYLLDRYpPEKEINwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSAV 207
Cdd:PRK14239 118 KQVLDEAVEKsLKGASIwDEVKDRL-HDSALG----LSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
60-235 |
1.80e-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: 50.34 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 60 EDLTLRVEPGSNLLITGPNGSGKSSLFRVLGG--LWPLVSGYI-FKpgiGSDLN---------KEIFYVPQRP------- 120
Cdd:TIGR01978 17 KGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTIlFK---GQDLLelepderarAGLFLAFQYPeeipgvs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 121 --------YTAVGTLRDQliYPLTVAEESEPLTQegMVELLKNVdlEYLLDRYppekeINWGdeLSLGEQQR---LGMAR 189
Cdd:TIGR01978 94 nleflrsaLNARRSARGE--EPLDLLDFEKLLKE--KLALLDMD--EEFLNRS-----VNEG--FSGGEKKRneiLQMAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 720069164 190 LfyhKPKFAILDECTSAVTTDMEERFCA---KVRAMGTSCITISHRPAL 235
Cdd:TIGR01978 161 L---EPKLAILDEIDSGLDIDALKIVAEginRLREPDRSFLIITHYQRL 206
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
55-202 |
1.86e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 51.18 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLV-EDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFkpgIGsdlNKEIFYVP--QRpytAVG-TLRDQ 130
Cdd:PRK11000 14 GDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLF---IG---EKRMNDVPpaER---GVGmVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 131 LIYP-LTVAEESE---PLTQEGMVELLKNVD-------LEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAI 199
Cdd:PRK11000 85 ALYPhLSVAENMSfglKLAGAKKEEINQRVNqvaevlqLAHLLDRKP--------KALSGGQRQRVAIGRTLVAEPSVFL 156
|
...
gi 720069164 200 LDE 202
Cdd:PRK11000 157 LDE 159
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
43-210 |
2.25e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 50.95 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVE---DLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI------GSDLNKE- 112
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsEKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 113 -----IF----YVPQRpytavgTLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPPEkeinwgdeLSLGEQQ 183
Cdd:PRK11153 82 rqigmIFqhfnLLSSR------TVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQ--------LSGGQKQ 147
|
170 180 190
....*....|....*....|....*....|
gi 720069164 184 RLGMARLFYHKPKFAILDECTSAV---TTD 210
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALdpaTTR 177
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
717-904 |
2.35e-06 |
|
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: 49.74 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLV--------KPCQNIKDVGGSRcVFYVPQrpytclgtlr 788
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgeditgLPPHEIARLGIGR-TFQIPR---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 789 dqiIYPlsqeeaELSVVKMLGTGDNSDDRAHILDTHLRS-----------ILERVRLIYLLEREGGwdasvnwedILSLG 857
Cdd:cd03219 86 ---LFP------ELTVLENVMVAAQARTGSGLLLARARReereareraeeLLERVGLADLADRPAG---------ELSYG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 720069164 858 EQQRLGMARLFFHNPKFGILDECT---NATSVDVEEHLYKLANEMGITVV 904
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVL 197
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
59-202 |
2.43e-06 |
|
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: 49.85 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIF--------KP-------GIGsdlnkeifYVPQRPYTA 123
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILldgqditkLPmhkrarlGIG--------YLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 124 VG-TLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEYLLDRYppekeinwGDELSLGEQQRLGMARLFYHKPKFAILDE 202
Cdd:cd03218 88 RKlTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSK--------ASSLSGGERRRVEIARALATNPKFLLLDE 159
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
55-266 |
2.52e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.21 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP---LVSGYIFKPGIGsdLNKEifyvpqrPYTAVGTLRdql 131
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggAPRGARVTGDVT--LNGE-------PLAAIDAPR--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 132 iypltVAEESEPLTQEGMVELLKNVDLEYLLDRYP----------PEKEINWG---------------DELSLGEQQRLG 186
Cdd:PRK13547 81 -----LARLRAVLPQAAQPAFAFSAREIVLLGRYPharragalthRDGEIAWQalalagatalvgrdvTTLSGGELARVQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 187 MARLFYH---------KPKFAILDECTSAVTTDMEERFCAKVRAMG----TSCITISHRPALVAFHDMVLSLDGEGGWKV 253
Cdd:PRK13547 156 FARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwnLGVLAIVHDPNLAARHADRIAMLADGAIVA 235
|
250
....*....|...
gi 720069164 254 HSKREDSPQPAEV 266
Cdd:PRK13547 236 HGAPADVLTPAHI 248
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
696-911 |
2.64e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.77 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 696 TEDIISFSEVDIITPAQKLLaRQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPI-----ATGRLVKPCQNI------ 764
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKAL-NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIysprtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 765 -----KDVGgsrCVFyvpQRPYTCLGTLRDQIIYPLsqeeaelsvvKMLGTGDNsddraHILDTHLRSILErvrliylle 839
Cdd:PRK14239 81 tvdlrKEIG---MVF---QQPNPFPMSIYENVVYGL----------RLKGIKDK-----QVLDEAVEKSLK--------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 840 reggwDASVnWEDI----------LSLGEQQRLGMARLFFHNPKFGILDECTNA----TSVDVEEHLYKLANEMGITVVT 905
Cdd:PRK14239 131 -----GASI-WDEVkdrlhdsalgLSGGQQQRVCIARVLATSPKIILLDEPTSAldpiSAGKIEETLLGLKDDYTMLLVT 204
|
....*.
gi 720069164 906 TSQRPA 911
Cdd:PRK14239 205 RSMQQA 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
39-249 |
2.96e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.85 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 39 EANYIEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGSD--------LN 110
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkglmkLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 111 KEIFYVPQRPytavgtlrDQLIYPLTVAEE----------SEPLTQEGMVELLKNVDLEYLLDryppeKEINWgdeLSLG 180
Cdd:PRK13636 82 ESVGMVFQDP--------DNQLFSASVYQDvsfgavnlklPEDEVRKRVDNALKRTGIEHLKD-----KPTHC---LSFG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 720069164 181 EQQRLGMARLFYHKPKFAILDECTSAV----TTDMEERFCAKVRAMGTSCITISHRPALVAFH-DMVLSLDgEG 249
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLdpmgVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYcDNVFVMK-EG 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
713-892 |
3.22e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 713 KLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRlvkpcqnikdVGGSRCVFYVPQRPYTCLGTLRDQII 792
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR----------VWAERSIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 793 YPLSQEEAELSVVKmlgtgdnsddRAHILDTHLRSilervrLIYLLEREGGwDASVNwediLSLGEQQRLGMARLFFHNP 872
Cdd:PTZ00243 743 FFDEEDAARLADAV----------RVSQLEADLAQ------LGGGLETEIG-EKGVN----LSGGQKARVSLARAVYANR 801
|
170 180
....*....|....*....|
gi 720069164 873 KFGILDECTNATSVDVEEHL 892
Cdd:PTZ00243 802 DVYLLDDPLSALDAHVGERV 821
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
57-248 |
3.38e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 57 VLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKpgigsdlNKEIFYVPQRPYTAVGTLRDQLIYplt 136
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-------ERSIAYVPQQAWIMNATVRGNILF--- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 137 VAEESEPLTQEGMVELLKNVDLEYL---LDRYPPEKEINwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSAVTTD--- 210
Cdd:PTZ00243 744 FDEEDAARLADAVRVSQLEADLAQLgggLETEIGEKGVN----LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvge 819
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 720069164 211 --MEERFCAKVRamGTSCITISHRPALVAFHDMVLSLDGE 248
Cdd:PTZ00243 820 rvVEECFLGALA--GKTRVLATHQVHVVPRADYVVALGDG 857
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
39-246 |
3.62e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 39 EANYIEFAGVKVVTPTGNVLV-EDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPG--IGS----DLNK 111
Cdd:PTZ00243 1305 QAGSLVFEGVQMRYREGLPLVlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGreIGAyglrELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 112 EIFYVPQRPYTAVGTLRDQLiypltvaeesEPLTQEGMVELLKNVDLEYLLDRYPPEKE------INWGDELSLGEQQRL 185
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNV----------DPFLEASSAEVWAALELVGLRERVASESEgidsrvLEGGSNYSVGQRQLM 1454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 720069164 186 GMARLFYHK-PKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDMVLSLD 246
Cdd:PTZ00243 1455 CMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAfsAYTVITIAHRLHTVAQYDKIIVMD 1518
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
52-231 |
3.78e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 49.66 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 52 TPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG--------SDLNKEIFYVPQRPYTA 123
Cdd:PRK13637 16 TPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitdkkvklSDIRKKVGLVFQYPEYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 124 V--GTLRDQLIYPLTVAEESEPLTQEGMVELLKNVDLEY--LLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAI 199
Cdd:PRK13637 96 LfeETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYedYKDKSP--------FELSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 720069164 200 LDECTSAVTTDMEERFCAKVRAM----GTSCITISH 231
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELhkeyNMTIILVSH 203
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
58-205 |
4.56e-06 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 48.81 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 58 LVEDLTLRVEPGSNLLITGPNGSGKSSLF-----RVLGGlwPLVSGYIFKPGIGSD---LNKEIFYVPQRPYTAVG-TLR 128
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLdaisgRVEGG--GTTSGQILFNGQPRKpdqFQKCVAYVRQDDILLPGlTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 129 DQLIY----PLTVAEESEPLTQEGMVELLKNVDLEYLLDRYPPEkeinwgdeLSLGEQQRLGMARLFYHKPKFAILDECT 204
Cdd:cd03234 100 ETLTYtailRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKG--------ISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
.
gi 720069164 205 S 205
Cdd:cd03234 172 S 172
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
58-139 |
5.70e-06 |
|
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: 47.93 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 58 LVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGL--WPLVSGYIFKPGIGSDLN---KEIFYVPQrpytavgtlRDQLI 132
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRsfrKIIGYVPQ---------DDILH 94
|
....*..
gi 720069164 133 YPLTVAE 139
Cdd:cd03213 95 PTLTVRE 101
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
51-210 |
5.74e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.87 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 51 VTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGG--LWPLVSGYIFKPGIgSDLNKE--------IFYVPQRP 120
Cdd:CHL00131 15 ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGE-SILDLEpeerahlgIFLAFQYP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 121 YTAVGT-----LRdqLIY----PLTVAEESEPLT-QEGMVELLKNVDL-EYLLDRYppekeINWGdeLSLGEQQR---LG 186
Cdd:CHL00131 94 IEIPGVsnadfLR--LAYnskrKFQGLPELDPLEfLEIINEKLKLVGMdPSFLSRN-----VNEG--FSGGEKKRneiLQ 164
|
170 180
....*....|....*....|....
gi 720069164 187 MARLfyhKPKFAILDECTSAVTTD 210
Cdd:CHL00131 165 MALL---DSELAILDETDSGLDID 185
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
711-883 |
6.06e-06 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 48.61 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 711 AQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRlvkpCQ-NIKDVGGsrcvfYVPQRPYTCLGTLRD 789
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGE----VRlNGRPLAD-----WSPAELARRRAVLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 790 Q--IIYPLSQEEaelsVVKMlGTGDNSDDRAHiLDTHLRSILERVRLIYLLEReggwdasvnweDILSL--GEQQRLGMA 865
Cdd:PRK13548 84 HssLSFPFTVEE----VVAM-GRAPHGLSRAE-DDALVAAALAQVDLAHLAGR-----------DYPQLsgGEQQRVQLA 146
|
170 180
....*....|....*....|....
gi 720069164 866 R----LFFHNPKFGI--LDECTNA 883
Cdd:PRK13548 147 RvlaqLWEPDGPPRWllLDEPTSA 170
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
717-886 |
6.09e-06 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 48.13 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGvwpiatgrLVKPCQNIKDVGGSRcVFYVPQRPYTCLGTLRDQI-IYPl 795
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAG--------LLEPDAGFATVDGFD-VVKEPAEARRRLGFVSDSTgLYD- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 796 sqeeaELSVVKMLG--------TGDNSDDRahildthLRSILERVRLIYLLEREGGWdasvnwediLSLGEQQRLGMARL 867
Cdd:cd03266 92 -----RLTARENLEyfaglyglKGDELTAR-------LEELADRLGMEELLDRRVGG---------FSTGMRQKVAIARA 150
|
170
....*....|....*....
gi 720069164 868 FFHNPKFGILDECTNATSV 886
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDV 169
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
695-905 |
6.43e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 48.89 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 695 TTEDIISFSEVDIITPAQKLLaRQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPI------ATGRLVKPCQNI---- 764
Cdd:PRK14246 6 SAEDVFNISRLYLYINDKAIL-KDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYFGKDIfqid 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 765 -----KDVGgsrCVFYVPQrPYTCLgTLRDQIIYPLsqeeaelsvvKMLGTGDNSDdrahildthLRSILERVrliylLE 839
Cdd:PRK14246 85 aiklrKEVG---MVFQQPN-PFPHL-SIYDNIAYPL----------KSHGIKEKRE---------IKKIVEEC-----LR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 720069164 840 REGGW----DASVNWEDILSLGEQQRLGMARLFFHNPKFGILDECTN----ATSVDVEEHLYKLANEMGITVVT 905
Cdd:PRK14246 136 KVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSmidiVNSQAIEKLITELKNEIAIVIVS 209
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
59-214 |
6.49e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.63 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIF------KPGIGSDLNKEIFYVPQRPYTA------VGT 126
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplHFGDYSYRSQRIRMIFQDPSTSlnprqrISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 127 LRDqliYPLTVAEESEPLTQE-GMVELLKNVDLEylldrypPEKEINWGDELSLGEQQRLGMARLFYHKPKFAILDECTS 205
Cdd:PRK15112 109 ILD---FPLRLNTDLEPEQREkQIIETLRQVGLL-------PDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
....*....
gi 720069164 206 AVttDMEER 214
Cdd:PRK15112 179 SL--DMSMR 185
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
61-217 |
7.00e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 48.56 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 61 DLTLRVEPGS-----NLLITGPNGSGKSSLFRVLGGLwplvsgyiFKPG---IGSDLNKeIFYVPQR---PYTavGTLRD 129
Cdd:cd03237 12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGV--------LKPDegdIEIELDT-VSYKPQYikaDYE--GTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 130 qLIYPLTVAEESEPLTQegmVELLKNVDLEYLLDRYPPekeinwgdELSLGEQQRLGMARLFYHKPKFAILDEcTSAvTT 209
Cdd:cd03237 81 -LLSSITKDFYTHPYFK---TEIAKPLQIEQILDREVP--------ELSGGELQRVAIAACLSKDADIYLLDE-PSA-YL 146
|
....*...
gi 720069164 210 DMEERFCA 217
Cdd:cd03237 147 DVEQRLMA 154
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
59-204 |
8.70e-06 |
|
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: 48.10 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGSDLNKEIFyvpQRPYTAVGTLRDQLIYPLTVA 138
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF---LRRIGVVFGQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 720069164 139 EESEPL-------------TQEGMVELLknvDLEYLLDRypPEKeinwgdELSLGEQQRLGMARLFYHKPKFAILDECT 204
Cdd:cd03267 114 DSFYLLaaiydlpparfkkRLDELSELL---DLEELLDT--PVR------QLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
699-913 |
8.86e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 47.95 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 699 IISFSEVDIITPAQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGSRCVFyvpq 778
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPF---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 779 rpytclgtLRDQI--IYPLSQEEAELSV-----VKMLGTGDNSDDRahildthlrsileRVRLIYLLEREGGWDASVNWE 851
Cdd:PRK10908 77 --------LRRQIgmIFQDHHLLMDRTVydnvaIPLIIAGASGDDI-------------RRRVSAALDKVGLLDKAKNFP 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 720069164 852 DILSLGEQQRLGMARLFFHNPKFGILDECTNATSVDVEEHLYKL---ANEMGITVVTTSQRPALI 913
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLfeeFNRVGVTVLMATHDIGLI 200
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
37-262 |
9.67e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 48.29 E-value: 9.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 37 FSEANYIEFAGvkvvTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP------LVSGYIFKPGIGS--- 107
Cdd:PRK13641 5 FENVDYIYSPG----TPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKpssgtiTIAGYHITPETGNknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 108 -DLNKEIFYVPQRPYTAV---GTLRDQLIYPLTVAEeSEPLTQEGMVELLKNVDL-EYLLDRYPpekeinwgDELSLGEQ 182
Cdd:PRK13641 81 kKLRKKVSLVFQFPEAQLfenTVLKDVEFGPKNFGF-SEDEAKEKALKWLKKVGLsEDLISKSP--------FELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 183 QRLGMARLFYHKPKFAILDECTSAV----TTDMEERFCAKVRAmGTSCITISHRPALVA-FHDMVLSLDgeggwkvHSK- 256
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLdpegRKEMMQLFKDYQKA-GHTVILVTHNMDDVAeYADDVLVLE-------HGKl 223
|
....*..
gi 720069164 257 -REDSPQ 262
Cdd:PRK13641 224 iKHASPK 230
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
58-248 |
1.03e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 47.26 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 58 LVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPL---VSGYIFKPGIGSDLNKEIF-----YVPQrpytavgtlRD 129
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNGIPYKEFAEKYpgeiiYVSE---------ED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 130 QLIYPLTVAEeseplTQEGMVELLknvdleylldryppekeinwGDE----LSLGEQQRLGMARLFYHKPKFAILDECT- 204
Cdd:cd03233 93 VHFPTLTVRE-----TLDFALRCK--------------------GNEfvrgISGGERKRVSIAEALVSRASVLCWDNSTr 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 720069164 205 ---SAVTTDMEERFCAKVRAMGTSCITISHRPALVAFH--DMVLSL-DGE 248
Cdd:cd03233 148 gldSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDlfDKVLVLyEGR 197
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
668-881 |
1.05e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.07 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 668 ELEELLDSAKNGVSLPEsQSMFKKDDVTtediISFSEVDIITPAQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLR 747
Cdd:PRK11174 323 SLVTFLETPLAHPQQGE-KELASNDPVT----IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 748 GVWPIaTGRLVKPCQNIKDVGGS---RCVFYVPQRPYTCLGTLRDQIiyplsqeeaelsvvkMLGtgdnsddRAHILDTH 824
Cdd:PRK11174 398 GFLPY-QGSLKINGIELRELDPEswrKHLSWVGQNPQLPHGTLRDNV---------------LLG-------NPDASDEQ 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 720069164 825 LRSILERVRLIYLLER-EGGWDASVNWEDI-LSLGEQQRLGMARLFFHNPKFGILDECT 881
Cdd:PRK11174 455 LQQALENAWVSEFLPLlPQGLDTPIGDQAAgLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
52-205 |
1.06e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.52 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 52 TPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLfrvLGGLWPLVS--GYIFKPGIGSD------LNKEIFYVPQRPYTA 123
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTL---LSALLRLLSteGEIQIDGVSWNsvtlqtWRKAFGVIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 124 VGTLRDQLiypltvaEESEPLTQEGMVELLKNVDLEYLLDRYPPEKE---INWGDELSLGEQQRLGMARLFYHKPKFAIL 200
Cdd:TIGR01271 1305 SGTFRKNL-------DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDfvlVDGGYVLSNGHKQLMCLARSILSKAKILLL 1377
|
....*
gi 720069164 201 DECTS 205
Cdd:TIGR01271 1378 DEPSA 1382
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
43-205 |
1.22e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 48.29 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVvTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIF-----KPGIGSDLNKEIFYVP 117
Cdd:PRK13536 42 IDLAGVSK-SYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpVPARARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 118 QrpytavgtlRDQLIYPLTVAEEsepLTQEGMVELLKNVDLEY----LLDRYPPEKEINWG-DELSLGEQQRLGMARLFY 192
Cdd:PRK13536 121 Q---------FDNLDLEFTVREN---LLVFGRYFGMSTREIEAvipsLLEFARLESKADARvSDLSGGMKRRLTLARALI 188
|
170
....*....|...
gi 720069164 193 HKPKFAILDECTS 205
Cdd:PRK13536 189 NDPQLLILDEPTT 201
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
713-881 |
1.24e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 48.29 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 713 KLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVkpcqnikdvggsrcVFYVPQRPYTCLGTLRDQII 792
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKIT--------------VLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 793 YPLSQEEAELSVVK-MLGTGDNSDDRAHILDTHLRSILERVRLiyllerEGGWDASVNwedILSLGEQQRLGMARLFFHN 871
Cdd:PRK13536 120 PQFDNLDLEFTVREnLLVFGRYFGMSTREIEAVIPSLLEFARL------ESKADARVS---DLSGGMKRRLTLARALIND 190
|
170
....*....|
gi 720069164 872 PKFGILDECT 881
Cdd:PRK13536 191 PQLLILDEPT 200
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
43-244 |
1.25e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 48.68 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVtptgnvlvEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGI------GSDLNKEIFYV 116
Cdd:PRK09536 11 VEFGDTTVL--------DGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 117 PQRPYTAVGTLRDQLI----YPLTVAEESEPLTQEGMVE-LLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLF 191
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVemgrTPHRSRFDTWTETDRAAVErAMERTGVAQFADRPV--------TSLSGGERQRVLLARAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 720069164 192 YHKPKFAILDECTSAVTTDMEERFCAKVRAMGTscitiSHRPALVAFHDMVLS 244
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVD-----DGKTAVAAIHDLDLA 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
45-232 |
1.65e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.51 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 45 FAGVKVVTPTgnvlveDLTLRvePGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYI---------FKPGIGSDLNkeIFY 115
Cdd:PRK15439 21 YSGVEVLKGI------DFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeiggnpcarLTPAKAHQLG--IYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 116 VPQRPytavgtlrdqLIYP-LTVAEE------SEPLTQEGMVELLKNVDLEYLLDryppekeINWGdELSLGEQQRLGMA 188
Cdd:PRK15439 91 VPQEP----------LLFPnLSVKENilfglpKRQASMQKMKQLLAALGCQLDLD-------SSAG-SLEVADRQIVEIL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 720069164 189 RLFYHKPKFAILDECTSAVTTDMEERFCAKVRAM---GTSCITISHR 232
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIRELlaqGVGIVFISHK 199
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
697-882 |
1.71e-05 |
|
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: 47.39 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 697 EDIISFSEVDIITPAQKLLaRQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKpcqnikdVGGSRcvfyv 776
Cdd:COG1119 1 DPLLELRNVTVRRGGKTIL-DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVR-------LFGER----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 777 pqrpytcLGT-----LRDQIIYpLSQE-----EAELSVVKMLGTG------------DNSDDRAhildthlRSILERVRL 834
Cdd:COG1119 68 -------RGGedvweLRKRIGL-VSPAlqlrfPRDETVLDVVLSGffdsiglyreptDEQRERA-------RELLELLGL 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 720069164 835 IYLLEReggwdasvNWEDiLSLGEQQRLGMARLFFHNPKFGILDECTN 882
Cdd:COG1119 133 AHLADR--------PFGT-LSQGEQRRVLIARALVKDPELLILDEPTA 171
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
59-206 |
2.05e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.14 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPlVSGYI-FKpgiGSDLN-----------KEIFYVPQRPYtavGT 126
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIrFD---GQDLDglsrralrplrRRMQVVFQDPF---GS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 127 L--RdqliypLTVAEE-SEPLT----------QEGMV-ELLKNVDL-EYLLDRYPpekeinwgDELSLGEQQRLGMARLF 191
Cdd:COG4172 375 LspR------MTVGQIiAEGLRvhgpglsaaeRRARVaEALEEVGLdPAARHRYP--------HEFSGGQRQRIAIARAL 440
|
170
....*....|....*
gi 720069164 192 YHKPKFAILDECTSA 206
Cdd:COG4172 441 ILEPKLLVLDEPTSA 455
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
719-907 |
2.18e-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: 48.26 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 719 LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLvkpCQNIKD----------VGGSRCVFYV----------PQ 778
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV---NVRVGDewvdmtkpgpDGRGRAKRYIgilhqeydlyPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 779 RpyTCLGTLRDQIIYPLSQEEAELSVVKMLGTGDNSDDRAhildthlRSILERvrliyllereggwdasvnWEDILSLGE 858
Cdd:TIGR03269 380 R--TVLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKA-------EEILDK------------------YPDELSEGE 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 720069164 859 QQRLGMARLFFHNPKFGILDECTNA----TSVDVEEHLYKLANEMGITVVTTS 907
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTmdpiTKVDVTHSILKAREEMEQTFIIVS 485
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
59-205 |
2.25e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.39 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGSDLNKEIFYVPQRPYTAVGTLRDQLIypLTVA 138
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPDNQIV--ATIV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 720069164 139 EES----------EPLTQEGMV-ELLKNVDL-EYllDRYPPEKeinwgdeLSLGEQQRLGMARLFYHKPKFAILDECTS 205
Cdd:PRK13633 104 EEDvafgpenlgiPPEEIRERVdESLKKVGMyEY--RRHAPHL-------LSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
54-267 |
2.52e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 54 TGNVLVE---------DLTLRVEPGSN-----LLITGPNGSGKSSLFRVLGGlwplvsgyIFKPGIGS-DLNKEIFYVPQ 118
Cdd:PRK13409 336 ERETLVEypdltkklgDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAG--------VLKPDEGEvDPELKISYKPQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 119 RPYTAV-GTLRDqLIYPLTVAEESEPLTqegmVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKF 197
Cdd:PRK13409 408 YIKPDYdGTVED-LLRSITDDLGSSYYK----SEIIKPLQLERLLDKNV--------KDLSGGELQRVAIAACLSRDADL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 198 AILDECTSAVttDMEERF-CAKV--RAM---GTSCITISHRpalVAFHDMV----LSLDGEGGwkVHSKredSPQPAEVR 267
Cdd:PRK13409 475 YLLDEPSAHL--DVEQRLaVAKAirRIAeerEATALVVDHD---IYMIDYIsdrlMVFEGEPG--KHGH---ASGPMDMR 544
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
730-879 |
2.79e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.16 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 730 LVTGPNGSGKSSIFRVLRgvWPI--ATGRLVKPCQNIKDVGGSRC----VFYVPQRPYTClgtLRDQ--IIYPLSQEEAE 801
Cdd:COG0419 27 LIVGPNGAGKSTILEAIR--YALygKARSRSKLRSDLINVGSEEAsvelEFEHGGKRYRI---ERRQgeFAEFLEAKPSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 802 L--SVVKMLGTG--DNSDDRAHILDTHLRSILERVRLIYLLEREGGWDASVNWE-DILSLGEQQRLGMA---RLFFhnpK 873
Cdd:COG0419 102 RkeALKRLLGLEiyEELKERLKELEEALESALEELAELQKLKQEILAQLSGLDPiETLSGGERLRLALAdllSLIL---D 178
|
....*.
gi 720069164 874 FGILDE 879
Cdd:COG0419 179 FGSLDE 184
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
34-231 |
3.57e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 34 SNYFSEANYIEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGSDLNKEI 113
Cdd:PRK10522 314 PQAFPDWQTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 114 FYvpQRPYTAVGT---LRDQLIYPltVAEESEP------LTQEGMVELLKNVDLEYLLDRyppekeinwgdeLSLGEQQR 184
Cdd:PRK10522 394 DY--RKLFSAVFTdfhLFDQLLGP--EGKPANPalvekwLERLKMAHKLELEDGRISNLK------------LSKGQKKR 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 720069164 185 LGMARLFYHKPKFAILDECtsAVTTD-MEERFCAKV-----RAMGTSCITISH 231
Cdd:PRK10522 458 LALLLALAEERDILLLDEW--AADQDpHFRREFYQVllpllQEMGKTIFAISH 508
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
43-246 |
3.61e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 46.52 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGS-------DLNKEIFY 115
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfsklqGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 116 VPQRPYTA-VGTlrdqliyplTVaEESEPLTQEGM----VELLKNVDL---EYLLDRYPPEKEinwgDELSLGEQQRLGM 187
Cdd:PRK13644 82 VFQNPETQfVGR---------TV-EEDLAFGPENLclppIEIRKRVDRalaEIGLEKYRHRSP----KTLSGGQGQCVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 720069164 188 ARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAM---GTSCITISHRPALVAFHDMVLSLD 246
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhekGKTIVYITHNLEELHDADRIIVMD 209
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
719-892 |
3.78e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 47.26 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 719 LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGgsrcvfyvpqrpytcLGTLRDQIIYPLsqE 798
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---------------RASLRRNIAVVF--Q 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 799 EAEL---SVVKMLGTGdnsddRAHILDTHLRSILERVR-LIYLLEREGGWDASVNWE-DILSLGEQQRLGMARLFFHNPK 873
Cdd:PRK13657 417 DAGLfnrSIEDNIRVG-----RPDATDEEMRAAAERAQaHDFIERKPDGYDTVVGERgRQLSGGERQRLAIARALLKDPP 491
|
170
....*....|....*....
gi 720069164 874 FGILDECTNATSVDVEEHL 892
Cdd:PRK13657 492 ILILDEATSALDVETEAKV 510
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
48-207 |
4.73e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.70 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 48 VKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGSDLNKEIFyvpqRPYTAVGTL 127
Cdd:TIGR01257 935 VKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV----RQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 128 RDQLIYPLTVAEESEPLTQ-EGMVELLKNVDLEYLL-DRYPPEKEINWGDELSLGEQQRLGMARLFYHKPKFAILDECTS 205
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQlKGRSWEEAQLEMEAMLeDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
..
gi 720069164 206 AV 207
Cdd:TIGR01257 1091 GV 1092
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
718-919 |
5.31e-05 |
|
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: 45.36 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 718 QLTFDiTPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVkpcqnikdVGGsrcVFYVPQRPYTCLGTLRDQIIYpLSQ 797
Cdd:cd03297 16 KIDFD-LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIV--------LNG---TVLFDSRKKINLPPQQRKIGL-VFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 798 EEA---ELSVVKMLGTGDNSDDRAHILDThLRSILERVRLIYLLEReggwdasvnWEDILSLGEQQRLGMARLFFHNPKF 874
Cdd:cd03297 83 QYAlfpHLNVRENLAFGLKRKRNREDRIS-VDELLDLLGLDHLLNR---------YPAQLSGGEKQRVALARALAAQPEL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 720069164 875 GILDECTNATSVDVEEHLYKLANEMgitvVTTSQRPALIPFHSLE 919
Cdd:cd03297 153 LLLDEPFSALDRALRLQLLPELKQI----KKNLNIPVIFVTHDLS 193
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
55-91 |
6.64e-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: 46.47 E-value: 6.64e-05
10 20 30
....*....|....*....|....*....|....*..
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGG 91
Cdd:TIGR03719 334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG 370
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
59-236 |
6.70e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.11 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG---------SDLNKEIFYVPQRPYTAVG---T 126
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDllkadpeaqKLLRQKIQIVFQNPYGSLNprkK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 127 LRDQLIYPLTV-AEESEPLTQEGMVELLKNVDL--EYLlDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDEC 203
Cdd:PRK11308 111 VGQILEEPLLInTSLSAAERREKALAMMAKVGLrpEHY-DRYP--------HMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 720069164 204 TSAVttDMEERfcAKV--------RAMGTSCITISHRPALV 236
Cdd:PRK11308 182 VSAL--DVSVQ--AQVlnlmmdlqQELGLSYVFISHDLSVV 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
700-920 |
6.93e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 46.37 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 700 ISFSEVDIITpaqkllarQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLV---KPCQNIKDVGGSRCVFYV 776
Cdd:PRK09536 11 VEFGDTTVLD--------GVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 777 PQrpytclGTlrdqiiyPLSQEEAELSVVKM--------LGTGDNSDDRAhildthLRSILERVRLIYLLEReggwdaSV 848
Cdd:PRK09536 83 PQ------DT-------SLSFEFDVRQVVEMgrtphrsrFDTWTETDRAA------VERAMERTGVAQFADR------PV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 720069164 849 nweDILSLGEQQRLGMARLFFHNPKFGILDECTnaTSVDVEEHLYKLanEMGITVVTTSqRPALIPFHSLEL 920
Cdd:PRK09536 138 ---TSLSGGERQRVLLARALAQATPVLLLDEPT--ASLDINHQVRTL--ELVRRLVDDG-KTAVAAIHDLDL 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
142-243 |
7.47e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 142 EPLTQEGMVELLKNVDLEYLLDRYPPEKEIN---WGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDME---ERF 215
Cdd:PTZ00265 1321 EDATREDVKRACKFAAIDEFIESLPNKYDTNvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEkliEKT 1400
|
90 100
....*....|....*....|....*....
gi 720069164 216 CAKVRAMG-TSCITISHRPALVAFHDMVL 243
Cdd:PTZ00265 1401 IVDIKDKAdKTIITIAHRIASIKRSDKIV 1429
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
711-883 |
7.49e-05 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 45.49 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 711 AQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLV---KPCQNIK--DVGGSRCVfyVPQRPytclg 785
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngRPLAAWSpwELARRRAV--LPQHS----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 786 tlrdQIIYPLSQEEaelsVVKM--LGTGDNSDDRAHIldthLRSILERVRLIYLLEReggwdasvnweDILSL--GEQQR 861
Cdd:COG4559 85 ----SLAFPFTVEE----VVALgrAPHGSSAAQDRQI----VREALALVGLAHLAGR-----------SYQTLsgGEQQR 141
|
170 180
....*....|....*....|....*....
gi 720069164 862 LGMARLF--FHNPKFG-----ILDECTNA 883
Cdd:COG4559 142 VQLARVLaqLWEPVDGgprwlFLDEPTSA 170
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
59-204 |
7.50e-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: 46.33 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSG-YIFKpgIGS---DLNKEIFYVPQRPYTAVGTLRDQL-IY 133
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGeVNVR--VGDewvDMTKPGPDGRGRAKRYIGILHQEYdLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 134 P-------LTVA---EESEPLTQEGMVELLKNVDL-----EYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFA 198
Cdd:TIGR03269 378 PhrtvldnLTEAiglELPDELARMKAVITLKMVGFdeekaEEILDKYP--------DELSEGERHRVALAQVLIKEPRIV 449
|
....*.
gi 720069164 199 ILDECT 204
Cdd:TIGR03269 450 ILDEPT 455
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
719-879 |
8.00e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 45.27 E-value: 8.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 719 LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIK----DVGGSRCVFYVPQRPytclgtlrdQIIYP 794
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARARRGIGYLPQEA---------SIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 795 LSQEEAELSVVKMLG--TGDNSDDRAHildthlrSILERVRLIYLLEREGgwdasvnweDILSLGEQQRLGMARLFFHNP 872
Cdd:PRK10895 93 LSVYDNLMAVLQIRDdlSAEQREDRAN-------ELMEEFHIEHLRDSMG---------QSLSGGERRRVEIARALAANP 156
|
....*..
gi 720069164 873 KFGILDE 879
Cdd:PRK10895 157 KFILLDE 163
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
43-222 |
8.15e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 45.64 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIfkPGIGSDLNKE-----IFYVP 117
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI--SILGQPTRQAlqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 118 QRP------------------YTAVGTLRdqliypltvaeESEPLTQEGMVELLKNVD-LEYlldRYppeKEINwgdELS 178
Cdd:PRK15056 85 QSEevdwsfpvlvedvvmmgrYGHMGWLR-----------RAKKRDRQIVTAALARVDmVEF---RH---RQIG---ELS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 720069164 179 LGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAM 222
Cdd:PRK15056 145 GGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL 188
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
44-231 |
8.80e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 44 EFAGVKVVtptgnvlvEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPlvsgyifkpgIGSdLNKEIFYVPQRpyTA 123
Cdd:NF040905 10 TFPGVKAL--------DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP----------HGS-YEGEILFDGEV--CR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 124 VGTLRDQ-------------LIYPLTVAEE----SEP---------LTQEGMVELLKNVDLeylldRYPPEKEInwgDEL 177
Cdd:NF040905 69 FKDIRDSealgiviihqelaLIPYLSIAENiflgNERakrgvidwnETNRRARELLAKVGL-----DESPDTLV---TDI 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 720069164 178 SLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERF---CAKVRAMGTSCITISH 231
Cdd:NF040905 141 GVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALldlLLELKAQGITSIIISH 197
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
70-207 |
9.26e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 45.18 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 70 SNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPgiGSDLNKEIFYVPQRPYTAVGTLRDQLIYPLTVAEE--------- 140
Cdd:PRK13652 31 SRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR--GEPITKENIREVRKFVGLVFQNPDDQIFSPTVEQDiafgpinlg 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 720069164 141 -SEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAV 207
Cdd:PRK13652 109 lDEETVAHRVSSALHMLGLEELRDRVP--------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
700-796 |
9.82e-05 |
|
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: 44.23 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 700 ISFSEVDIITPAQKLLARQ-LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGG--SRCVFYV 776
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKnLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKalSSLISVL 80
|
90 100
....*....|....*....|
gi 720069164 777 PQRPYTCLGTLRDQIIYPLS 796
Cdd:cd03247 81 NQRPYLFDTTLRNNLGRRFS 100
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
717-909 |
1.01e-04 |
|
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: 44.33 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS---RCVFYVPQRPYTCLGTLRdqiiy 793
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdlrSSLTIIPQDPTLFSGTIR----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 794 plsqeeaelsvvkmlgtgDNSDDRAHILDTHLRSILeRVrliylleREGGwdasvnweDILSLGEQQRLGMARLFFHNPK 873
Cdd:cd03369 100 ------------------SNLDPFDEYSDEEIYGAL-RV-------SEGG--------LNLSQGQRQLLCLARALLKRPR 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 720069164 874 FGILDECTNATSVDVEEHLYKLANEM--GITVVTTSQR 909
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEftNSTILTIAHR 183
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
60-242 |
1.12e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.93 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 60 EDLTLRVEPGS-----NLLITGPNGSGKSSLFRVLGGlwplvsgyIFKPGIGS-DLNKEIFYVPQRPYTAV-GTLRDQLI 132
Cdd:COG1245 352 GGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAG--------VLKPDEGEvDEDLKISYKPQYISPDYdGTVEEFLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 133 YPLTVAEESEPLTqegmVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDEcTSAvTTDME 212
Cdd:COG1245 424 SANTDDFGSSYYK----TEIIKPLGLEKLLDKNV--------KDLSGGELQRVAIAACLSRDADLYLLDE-PSA-HLDVE 489
|
170 180 190
....*....|....*....|....*....|....*.
gi 720069164 213 ERF-CAKV-----RAMGTSCITISHRpalVAFHDMV 242
Cdd:COG1245 490 QRLaVAKAirrfaENRGKTAMVVDHD---IYLIDYI 522
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
55-204 |
1.17e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRV-LGGLWPlVSGYIFkpgIGSDLnkEIFYVPQRpytavgtlRDQLIY 133
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQA-DSGRIH---CGTKL--EVAYFDQH--------RAELDP 396
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 720069164 134 PLTVAEESEPLTQEGMVELLKNVDLEYLLD-RYPPEKEINWGDELSLGEQQRLGMARLFYHKPKFAILDECT 204
Cdd:PRK11147 397 EKTVMDNLAEGKQEVMVNGRPRHVLGYLQDfLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPT 468
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
59-100 |
1.21e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 44.69 E-value: 1.21e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYI 100
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
52-101 |
1.24e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 44.69 E-value: 1.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 720069164 52 TPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIF 101
Cdd:COG1101 15 TVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL 64
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
708-905 |
1.91e-04 |
|
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: 45.67 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 708 ITPAQKllarQLTFDITPGKSLLVTGPNGSGKSSIFRVLrgvwpiaTGRLVKPCQNIKDVGGsrcVFYVPQRPYTCLGTL 787
Cdd:TIGR01271 438 VTPVLK----NISFKLEKGQLLAVAGSTGSGKSSLLMMI-------MGELEPSEGKIKHSGR---ISFSPQTSWIMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 788 RDQIIYPLSQEEAEL-SVVKmlgtgdnsddrAHILDTHLRSILERVRLIYLlerEGGWdasvnwedILSLGEQQRLGMAR 866
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYtSVIK-----------ACQLEEDIALFPEKDKTVLG---EGGI--------TLSGGQRARISLAR 561
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 720069164 867 LFFHNPKFGILDECTNATSVDVEEHLYK------LANEMGITVVT 905
Cdd:TIGR01271 562 AVYKDADLYLLDSPFTHLDVVTEKEIFEsclcklMSNKTRILVTS 606
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
59-207 |
2.12e-04 |
|
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: 43.86 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIF-------KPGIGSDLNKE---IFYVPQRPYTAVGTLR 128
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknesEPSFEATRSRNrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 129 DQLIYpltvaeeSEPLTQEGMVELLKNVDLEYLLDRYPPEKEINWGDE---LSLGEQQRLGMARLFYHKPKFAILDECTS 205
Cdd:cd03290 97 ENITF-------GSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERginLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
..
gi 720069164 206 AV 207
Cdd:cd03290 170 AL 171
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
854-904 |
2.33e-04 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 42.80 E-value: 2.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 720069164 854 LSLGEQQRLGMARLFFHNPKFGILDECTNATSVDVEEHLYKLANEM---GITVV 904
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraqGVAVI 136
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
711-907 |
2.36e-04 |
|
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: 42.94 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 711 AQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGSRcvfyvpqrpytclGTLRDQ 790
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDEL-------------PPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 791 IIYPLSQeeaelsvvkmlgtgdnsddraHILDTHLrSILERVRLIyllereggwdasvnwediLSLGEQQRLGMARLFFH 870
Cdd:cd03229 78 IGMVFQD---------------------FALFPHL-TVLENIALG------------------LSGGQQQRVALARALAM 117
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 720069164 871 NPKFGILDECTNA----TSVDVEEHLYKLANEMGITVVTTS 907
Cdd:cd03229 118 DPDVLLLDEPTSAldpiTRREVRALLKSLQAQLGITVVLVT 158
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
59-100 |
2.43e-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: 43.68 E-value: 2.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 720069164 59 VEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYI 100
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV 79
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
56-206 |
2.47e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.70 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 56 NVLVEDLTLRVEPGSNLLITGPNGSGKSS----LFRVL---GGLW----PLvsgYIFKPGIGSDLNKEIFYVPQRPYTAV 124
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsqGEIWfdgqPL---HNLNRRQLLPVRHRIQVVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 125 GTLRD--QLI-------YPLTVAEESEPLTQEGMVELLKNVDLEYlldRYPPEkeinwgdeLSLGEQQRLGMARLFYHKP 195
Cdd:PRK15134 376 NPRLNvlQIIeeglrvhQPTLSAAQREQQVIAVMEEVGLDPETRH---RYPAE--------FSGGQRQRIAIARALILKP 444
|
170
....*....|.
gi 720069164 196 KFAILDECTSA 206
Cdd:PRK15134 445 SLIILDEPTSS 455
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
62-100 |
2.52e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 43.30 E-value: 2.52e-04
10 20 30
....*....|....*....|....*....|....*....
gi 720069164 62 LTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYI 100
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI 68
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
719-893 |
2.60e-04 |
|
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: 44.94 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 719 LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVkpcqnikdVGGSrcVFYVPQRPYTCLGTLRDQIIYPLSQE 798
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH--------MKGS--VAYVPQQAWIQNDSLRENILFGKALN 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 799 EaelsvvkmlgtgdnsddrahildTHLRSILERVRLIYLLEREGGWDAS------VNwediLSLGEQQRLGMARLFFHNP 872
Cdd:TIGR00957 727 E-----------------------KYYQQVLEACALLPDLEILPSGDRTeigekgVN----LSGGQKQRVSLARAVYSNA 779
|
170 180
....*....|....*....|.
gi 720069164 873 KFGILDECTNATSVDVEEHLY 893
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIF 800
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
55-245 |
2.78e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 43.74 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVE---------------PGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIG------SDLNKEI 113
Cdd:cd03288 18 GEIKIHDLCVRYEnnlkpvlkhvkayikPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDisklplHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 114 FYVPQRPYTAVGTLRDQLiypltvaEESEPLTQEGMVELLKNVDLEYLLDRYPPEKE---INWGDELSLGEQQRLGMARL 190
Cdd:cd03288 98 SIILQDPILFSGSIRFNL-------DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDavvTEGGENFSVGQRQLFCLARA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 720069164 191 FYHKPKFAILDECTSAVttDM-EERFCAKVRAMG---TSCITISHRPALVAFHDMVLSL 245
Cdd:cd03288 171 FVRKSSILIMDEATASI--DMaTENILQKVVMTAfadRTVVTIAHRVSTILDADLVLVL 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
719-879 |
2.88e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 43.94 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 719 LTFDITPGK--SLLvtGPNGSGKSSIFRVLRGVwpIAT--------GRLVKPcQNIKDVGgsrcvfYVPQ-RpytclG-- 785
Cdd:COG4152 20 VSFTVPKGEifGLL--GPNGAGKTTTIRIILGI--LAPdsgevlwdGEPLDP-EDRRRIG------YLPEeR-----Gly 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 786 ---TLRDQIIY-----PLSQEEAelsvvkmlgtgdnsddrahildthlrsileRVRLIYLLER---EGGWDASVnwEDiL 854
Cdd:COG4152 84 pkmKVGEQLVYlarlkGLSKAEA------------------------------KRRADEWLERlglGDRANKKV--EE-L 130
|
170 180
....*....|....*....|....*
gi 720069164 855 SLGEQQRLGMARLFFHNPKFGILDE 879
Cdd:COG4152 131 SKGNQQKVQLIAALLHDPELLILDE 155
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
52-202 |
3.68e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 43.30 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 52 TPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPlVSGYIFKPGIGSD------LNKEIFYVPQRPYTAVG 125
Cdd:cd03289 13 TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNsvplqkWRKAFGVIPQKVFIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 126 TLRDQLiypltvaeesEPLTQEGMVELLK---NVDLEYLLDRYPPEKE---INWGDELSLGEQQRLGMARLFYHKPKFAI 199
Cdd:cd03289 92 TFRKNL----------DPYGKWSDEEIWKvaeEVGLKSVIEQFPGQLDfvlVDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
...
gi 720069164 200 LDE 202
Cdd:cd03289 162 LDE 164
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
55-100 |
4.08e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.95 E-value: 4.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYI 100
Cdd:PRK11819 336 DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
63-86 |
4.20e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.12 E-value: 4.20e-04
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
49-204 |
4.52e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.95 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 49 KVVtPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSG-YIFKPGIgsdlnkEIFYVPQRPY------ 121
Cdd:PRK11819 14 KVV-PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGI------KVGYLPQEPQldpekt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 122 ------TAVGTLRDQL-----IYpltvAEESEPLTQegMVELLK---------------NVD--LEYLLD--RYPPekei 171
Cdd:PRK11819 87 vrenveEGVAEVKAALdrfneIY----AAYAEPDAD--FDALAAeqgelqeiidaadawDLDsqLEIAMDalRCPP---- 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 720069164 172 nwGDE----LSLGEQQRLGMARLFYHKPKFAILDECT 204
Cdd:PRK11819 157 --WDAkvtkLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
719-888 |
4.66e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 719 LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS---RCVFYVPQRPYTCLGTLRDQiIYPL 795
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdlrKVLGIIPQAPVLFSGTVRFN-LDPF 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 796 SQ-EEAELSvvkmlgtgdNSDDRAHILDTHLRSILervrliylleregGWDASVNWE-DILSLGEQQRLGMARLFFHNPK 873
Cdd:PLN03130 1337 NEhNDADLW---------ESLERAHLKDVIRRNSL-------------GLDAEVSEAgENFSVGQRQLLSLARALLRRSK 1394
|
170
....*....|....*
gi 720069164 874 FGILDECTNAtsVDV 888
Cdd:PLN03130 1395 ILVLDEATAA--VDV 1407
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
61-246 |
4.72e-04 |
|
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: 44.04 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 61 DLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFkpgI-GSD--------LNKEIFYVPQRPytaV---GTLR 128
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIL---IdGQDirdvtqasLRAAIGIVPQDT---VlfnDTIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 129 DQLIYPLTVAeeseplTQEGMVELLKNVDLEYLLDRYPPEKEINWGD---ELSLGEQQRLGMARLFYHKPKFAILDECTS 205
Cdd:COG5265 450 YNIAYGRPDA------SEEEVEAAARAAQIHDFIESLPDGYDTRVGErglKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 720069164 206 AVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDMVLSLD 246
Cdd:COG5265 524 ALDSRTERAIQAALREVarGRTTLVIAHRLSTIVDADEILVLE 566
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
719-757 |
4.80e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.53 E-value: 4.80e-04
10 20 30
....*....|....*....|....*....|....*....
gi 720069164 719 LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRL 757
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI 68
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
719-905 |
5.05e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 42.69 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 719 LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGG---SRCVFYVPQRPYTCLG-TLRDQIIYP 794
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrqlARRLALLPQHHLTPEGiTVRELVAYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 795 LSqeeAELSVVKMLGTgdnsDDRAHIldthlRSILERVRLIYLLEREggwdasvnWEDiLSLGEQQRLGMARLFFHNPKF 874
Cdd:PRK11231 101 RS---PWLSLWGRLSA----EDNARV-----NQAMEQTRINHLADRR--------LTD-LSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190
....*....|....*....|....*....|....
gi 720069164 875 GILDECTNATSVDVEEHLYKLANEM---GITVVT 905
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELntqGKTVVT 193
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
40-202 |
5.59e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 42.80 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 40 ANYIEFAGVKVVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKpgIGSDLNKEIFY---- 115
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKV--MGREVNAENEKwvrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 116 ----VPQRPYTAV--GTLRDQLIY-PLTV---AEESEPLTQEGmvelLKNVDLEYLLDRYPpekeinwgDELSLGEQQRL 185
Cdd:PRK13647 80 kvglVFQDPDDQVfsSTVWDDVAFgPVNMgldKDEVERRVEEA----LKAVRMWDFRDKPP--------YHLSYGQKKRV 147
|
170
....*....|....*..
gi 720069164 186 GMARLFYHKPKFAILDE 202
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDE 164
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
700-882 |
6.65e-04 |
|
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: 40.89 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 700 ISFSEVDIITPAQKLLaRQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPcQNIKdvggsrcVFYVPQr 779
Cdd:cd03221 1 IELENLSKTYGGKLLL-KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-STVK-------IGYFEQ- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 780 pytclgtlrdqiiyplsqeeaelsvvkmlgtgdnsddrahildthlrsilervrliyllereggwdasvnwediLSLGEQ 859
Cdd:cd03221 71 --------------------------------------------------------------------------LSGGEK 76
|
170 180
....*....|....*....|...
gi 720069164 860 QRLGMARLFFHNPKFGILDECTN 882
Cdd:cd03221 77 MRLALAKLLLENPNLLLLDEPTN 99
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
74-205 |
7.49e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 42.43 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 74 ITGPNGSGKSSLFRVLGGLWPLVSGYIF------KPGIGSDLNKEIFYVPQRPYTA-VGTLrdqLIYPLTVAEESEPLTQ 146
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGIEKVKSGEIFynnqaiTDDNFEKLRKHIGIVFQNPDNQfVGSI---VKYDVAFGLENHAVPY 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 720069164 147 EGMVEL----LKNVDLeylLDRYPPEKEinwgdELSLGEQQRLGMARLFYHKPKFAILDECTS 205
Cdd:PRK13648 117 DEMHRRvseaLKQVDM---LERADYEPN-----ALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
37-205 |
7.52e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 42.42 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 37 FSEANYIEFAGvkvvTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSG--YIFKPGIGSD-LNKEI 113
Cdd:PRK13649 5 LQNVSYTYQAG----TPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGsvRVDDTLITSTsKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 114 ----------FYVPQRPYTAVGTLRDQLIYPLTVA---EESEPLTQEGMveLLKNVDlEYLLDRYPpekeinwgDELSLG 180
Cdd:PRK13649 81 kqirkkvglvFQFPESQLFEETVLKDVAFGPQNFGvsqEEAEALAREKL--ALVGIS-ESLFEKNP--------FELSGG 149
|
170 180
....*....|....*....|....*
gi 720069164 181 EQQRLGMARLFYHKPKFAILDECTS 205
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTA 174
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
61-233 |
7.63e-04 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 41.71 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 61 DLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIgsdlnkEIFYVP--QRPYTAVgtLRDQLIYP-LTV 137
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV------DVTAAPpaDRPVSML--FQENNLFAhLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 138 AE----------ESEPLTQEGMVELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAV 207
Cdd:cd03298 88 EQnvglglspglKLTAEDRQAIEVALARVGLAGLEKRLP--------GELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190
....*....|....*....|....*....|
gi 720069164 208 ----TTDMEERFCAKVRAMGTSCITISHRP 233
Cdd:cd03298 160 dpalRAEMLDLVLDLHAETKMTVLMVTHQP 189
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
51-210 |
8.40e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.09 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 51 VTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGL--WPLVSGYI-FKpgiGSDL---------NKEIFYVPQ 118
Cdd:PRK09580 9 VSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVeFK---GKDLlelspedraGEGIFMAFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 119 RPYTAVGtLRDQLIYPLTVAE-----ESEPLTQ-------EGMVELLKNVdlEYLLDRyppekEINWGdeLSLGEQQR-- 184
Cdd:PRK09580 86 YPVEIPG-VSNQFFLQTALNAvrsyrGQEPLDRfdfqdlmEEKIALLKMP--EDLLTR-----SVNVG--FSGGEKKRnd 155
|
170 180
....*....|....*....|....*..
gi 720069164 185 -LGMARLfyhKPKFAILDECTSAVTTD 210
Cdd:PRK09580 156 iLQMAVL---EPELCILDESDSGLDID 179
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
713-803 |
9.01e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 713 KLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLrGVwpIATGRLVKpcQNIKDVGGSRCvfYVPQRPYTcLGTLRDQii 792
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAI-GL--ALGGAQSA--TRRRSGVKAGC--IVAAVSAE-LIFTRLQ-- 77
|
90
....*....|.
gi 720069164 793 ypLSQEEAELS 803
Cdd:cd03227 78 --LSGGEKELS 86
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
692-748 |
9.28e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 9.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 720069164 692 DDVTTEDIISFSEVDIITPAQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRG 748
Cdd:PLN03073 501 DDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG 557
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
62-205 |
9.93e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 42.00 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 62 LTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIGS------DLNKEIFYVPQRPYTAV--GTLRDQLIY 133
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLtaenvwNLRRKIGMVFQNPDNQFvgATVEDDVAF 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 720069164 134 PLtvaeESEPLTQEgmvELLKNVDlEYLLDRYPPEKEINWGDELSLGEQQRLGMARLFYHKPKFAILDECTS 205
Cdd:PRK13642 106 GM----ENQGIPRE---EMIKRVD-EALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
43-237 |
1.19e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 42.36 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 43 IEFAGVKVVTPtgnvLVEDLTLRVEPGSNLLITGPNGSGKS----SLFRVLGGLWPLVSGYI-FKpgiGSDLNK------ 111
Cdd:COG4172 14 VAFGQGGGTVE----AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSIlFD---GQDLLGlserel 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 112 ------EIFYVPQRPYTA---VGTLRDQLIYPLTVaeeSEPLT----QEGMVELLKNV---DLEYLLDRYPpekeinwgD 175
Cdd:COG4172 87 rrirgnRIAMIFQEPMTSlnpLHTIGKQIAEVLRL---HRGLSgaaaRARALELLERVgipDPERRLDAYP--------H 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 720069164 176 ELSLGEQQR--LGMARLfyHKPKFAILDECTSA--VTT---------DMeerfcakVRAMGTSCITISHRPALVA 237
Cdd:COG4172 156 QLSGGQRQRvmIAMALA--NEPDLLIADEPTTAldVTVqaqildllkDL-------QRELGMALLLITHDLGVVR 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
719-904 |
1.21e-03 |
|
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: 41.41 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 719 LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPIATGRLVKPCQNIKDVGGS------RCVFYVPQRpYTCLG--TLRDQ 790
Cdd:cd03258 24 VSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrkarRRIGMIFQH-FNLLSsrTVFEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 791 IIYPLsqeeaelsvvKMLGTgdnsdDRAHILdthlRSILERVRLIYLLEREGGWDASvnwediLSLGEQQRLGMARLFFH 870
Cdd:cd03258 103 VALPL----------EIAGV-----PKAEIE----ERVLELLELVGLEDKADAYPAQ------LSGGQKQRVGIARALAN 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 720069164 871 NPKFGILDECTNA----TSVDVEEHLYKLANEMGITVV 904
Cdd:cd03258 158 NPKVLLCDEATSAldpeTTQSILALLRDINRELGLTIV 195
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
723-914 |
1.38e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 41.71 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 723 ITPGKS-LLVTGPNGSGKSSIFRVLRGVWPIATGRLV---KPC--QNIKDVggSRCVFYVPQRPytclgtlRDQIIYPLS 796
Cdd:PRK13652 26 IAPRNSrIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgEPItkENIREV--RKFVGLVFQNP-------DDQIFSPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 797 QEEAELSVVKMlgtGDNSDDRAHILDthlrSILERVRLIYLLEREggwdasvnwEDILSLGEQQRLGMARLFFHNPKFGI 876
Cdd:PRK13652 97 EQDIAFGPINL---GLDEETVAHRVS----SALHMLGLEELRDRV---------PHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 720069164 877 LDECTNATS----VDVEEHLYKLANEMGITVVTTSQRPALIP 914
Cdd:PRK13652 161 LDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQLDLVP 202
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
61-206 |
1.73e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.42 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 61 DLTLRVEPGSNLLITGPNGSGKSSLFR-VLGGLWPLVSGYIFKPGigsdlnkEIFYVPQRPYTAVGTLRDQLIYPLTV-- 137
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-------TVAYVPQVSWIFNATVRDNILFGSPFdp 707
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 720069164 138 -----AEESEPLTQEgmVELLKNVDLEYLLDRyppekeinwGDELSLGEQQRLGMARLFYHKPKFAILDECTSA 206
Cdd:PLN03130 708 eryerAIDVTALQHD--LDLLPGGDLTEIGER---------GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
55-212 |
1.82e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 55 GNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIfKpgiGSDlNKEIFYVPQRPYtavgtlrDQLIYP 134
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-K---WSE-NANIGYYAQDHA-------YDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 135 LTVAEESEPLTQEGMVELLKNVDLEYLLDRyppekeinwGDE-------LSLGEQQRLGMARLFYHKPKFAILDECTSAV 207
Cdd:PRK15064 399 LTLFDWMSQWRQEGDDEQAVRGTLGRLLFS---------QDDikksvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHM 469
|
....*
gi 720069164 208 ttDME 212
Cdd:PRK15064 470 --DME 472
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
713-748 |
1.96e-03 |
|
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: 41.84 E-value: 1.96e-03
10 20 30
....*....|....*....|....*....|....*.
gi 720069164 713 KLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRG 748
Cdd:TIGR03719 335 KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG 370
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
682-749 |
2.23e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 41.13 E-value: 2.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 720069164 682 LPESQSMFKKDDVttediiSFSevdiITPAQKLLARQLTFDITPGKSLLVTGPNGSGKSSIFRVLRGV 749
Cdd:PRK13632 1 IKNKSVMIKVENV------SFS----YPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGL 58
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
720-743 |
2.72e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.81 E-value: 2.72e-03
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
719-907 |
3.17e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 40.96 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 719 LTFDITPGKSLLVTGPNGSGKSSIFRVLRGVWPiatgrlvkpcqnikdvGGSRCVFYVPQRPY---TCLGTLRDQIIYpL 795
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYP----------------GKFEGNVFINGKPVdirNPAQAIRAGIAM-V 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 796 SQEEAELSVVKMLGTGDNsddrahILDTHLRSILERVRLIYLLErEGGWDASVNWEDI-----------LSLGEQQRLGM 864
Cdd:TIGR02633 342 PEDRKRHGIVPILGVGKN------ITLSVLKSFCFKMRIDAAAE-LQIIGSAIQRLKVktaspflpigrLSGGNQQKAVL 414
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 720069164 865 ARLFFHNPKFGILDECTNATSVDVEEHLYKLANEM---GITVVTTS 907
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaqeGVAIIVVS 460
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
719-742 |
3.19e-03 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 39.89 E-value: 3.19e-03
10 20
....*....|....*....|....*...
gi 720069164 719 LTFDIT---PGKSL-LVTGPNGSGKSSI 742
Cdd:cd03277 12 VTYDETefrPGPSLnMIIGPNGSGKSSI 39
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
60-86 |
4.03e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.40 E-value: 4.03e-03
10 20
....*....|....*....|....*..
gi 720069164 60 EDLTLRVEPGSNLlITGPNGSGKSSLF 86
Cdd:pfam13476 10 RDQTIDFSKGLTL-ITGPNGSGKTTIL 35
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
717-806 |
4.06e-03 |
|
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: 40.23 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLrgvwpiaTGRLVKPCQNIKDVGGsrcVFYVPQRPYTCLGTLRDQIIYPLS 796
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLI-------LGELEPSEGKIKHSGR---ISFSSQFSWIMPGTIKENIIFGVS 123
|
90
....*....|.
gi 720069164 797 QEEAE-LSVVK 806
Cdd:cd03291 124 YDEYRyKSVVK 134
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
59-120 |
4.25e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 40.37 E-value: 4.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 720069164 59 VEDLTLRVEPGSNLLItGPNGSGKSSLFRVLgglwplvsGYIFKPGIGSDLNKEIFYVPQRP 120
Cdd:COG3593 14 IKDLSIELSDDLTVLV-GENNSGKSSILEAL--------RLLLGPSSSRKFDEEDFYLGDDP 66
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
50-202 |
4.38e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 50 VVTPTGNVLVEDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPlvSGY-----IFKPGIGS-----DLNKEIFYVPQR 119
Cdd:PRK10938 267 VVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP--QGYsndltLFGRRRGSgetiwDIKKHIGYVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 120 ---PYTAVGTLRDQL---------IYPlTVAEESEPLTQE-----GMVELLKNvdleylldryPPEKEINWGdelslgeQ 182
Cdd:PRK10938 345 lhlDYRVSTSVRNVIlsgffdsigIYQ-AVSDRQQKLAQQwldilGIDKRTAD----------APFHSLSWG-------Q 406
|
170 180
....*....|....*....|.
gi 720069164 183 QRLGM-ARLFYHKPKFAILDE 202
Cdd:PRK10938 407 QRLALiVRALVKHPTLLILDE 427
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
61-101 |
4.65e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 40.55 E-value: 4.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 720069164 61 DLTLRvePGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIF 101
Cdd:COG4615 352 DLTIR--RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEIL 390
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
61-202 |
5.67e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.08 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 720069164 61 DLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLVSGYIFKPGIgsDLNKeifyvPQRPY-TAVG---------TLRDQ 130
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNC--NINN-----IAKPYcTYIGhnlglklemTVFEN 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 720069164 131 LIYPLTVAEESEplTQEGMVELLKnvdLEYLLDryppEKEINwgdeLSLGEQQRLGMARLFYHKPKFAILDE 202
Cdd:PRK13541 91 LKFWSEIYNSAE--TLYAAIHYFK---LHDLLD----EKCYS----LSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
717-748 |
6.90e-03 |
|
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: 39.03 E-value: 6.90e-03
10 20 30
....*....|....*....|....*....|..
gi 720069164 717 RQLTFDITPGKSLLVTGPNGSGKSSIFRVLRG 748
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTG 50
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| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
151-207 |
8.75e-03 |
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ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.11 E-value: 8.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 720069164 151 ELLKNVDLEYLLDRYPpekeinwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAV 207
Cdd:NF033858 380 EMLERFDLADVADALP--------DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
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