|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
325-916 |
1.54e-143 |
|
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: 441.11 E-value: 1.54e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 325 RVAAMCKVLVPTVLDKQGAQLLTVAFLVVARTWVSDRIASLNGTTVKFVLEQDKASFIRLIGLSVLQSAASSFIAPSIRH 404
Cdd:TIGR00954 78 KLDFLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 405 LRARLALGWRIRLTQHLLKNYLRNNSFYKVFHMASKNIDADQRITHDLEKLTTDLSGLVTGMVKPSVDILWFTWRMKLLT 484
Cdd:TIGR00954 158 LLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTAL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 485 GQRGVAILYAYMLLGLGFLRTVTPDFGDLISQEQQLEGTFRFMHERLCTHAESVAFFGGGTREKTMVESRFRELLSHSNY 564
Cdd:TIGR00954 238 GSVGPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 565 LLKKKWLFGILDDFITKQLPHNVTWLLSLLYAMEHKGDRASISTQGELAHAL----RFLASVVSqsflAFGDILELHRKF 640
Cdd:TIGR00954 318 IIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFLEMSEEELMQEFynngRLLLKAAD----ALGRLMLAGRDM 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 641 VELSGGINRIFELEELLDAAQS-------VDSINGSITPSMRDY---------YAKDAISFSKVDIVTPAQKMLARELTC 704
Cdd:TIGR00954 394 TRLAGFTARVDTLLQVLDDVKSgnfkrprVEEIESGREGGRNSNlvpgrgiveYQDNGIKFENIPLVTPNGDVLIESLSF 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 705 DIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEdvdqeagsgCGIFYVPQRPYTCLGTLRDQIIYPLSREEa 784
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK---------GKLFYVPQRPYMTLGTLRDQIIYPDSSED- 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 785 efralkMYGKGekhadprkLLDTHLQIILENVRLNYLLERdNRGWDANLNWEDTLSLGEQQRLGMARLFFHRPKYGILDE 864
Cdd:TIGR00954 544 ------MKRRG--------LSDKDLEQILDNVQLTHILER-EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1654042132 865 CTNATSVDVEEHLYGLANKMGITVVTSSQRPALIPYHSMELRlIDGEGNWEL 916
Cdd:TIGR00954 609 CTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLY-MDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
331-597 |
3.32e-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: 295.29 E-value: 3.32e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 331 KVLVPTVLDKQGAQLLTVAFLVVARTWVSDRIASLNGTTVKFVLEQDKASFIRLIGLSVLQSAASSFIAPSIRHLRARLA 410
Cdd:pfam06472 3 KILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 411 LGWRIRLTQHLLKNYLRNNSFYKVFHMASKNIDADQRITHDLEKLTTDLSGLVTGMVKPSVDILWFTWRMKLLTGQRGVA 490
Cdd:pfam06472 83 LRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRGPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 491 ILYAYMLLGLGFLRTVTPDFGDLISQEQQLEGTFRFMHERLCTHAESVAFFGGGTREKTMVESRFRELLSHSNYLLKKKW 570
Cdd:pfam06472 163 ILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILRRRL 242
|
250 260
....*....|....*....|....*..
gi 1654042132 571 LFGILDDFITKQLPHNVTWLLSLLYAM 597
Cdd:pfam06472 243 WYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
345-921 |
2.10e-83 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 279.38 E-value: 2.10e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 345 LLTVAFLVVARTWVSDRIASLNGTtvkF--VLEQ-DKASFIRLIGLSVLQSAASSFIAPSIRHLRARLALGWRIRLTQHL 421
Cdd:COG4178 27 LALLLLLTLASVGLNVLLNFWNRD---FydALQArDAAAFWQQLGVFALLAAISILLAVYQTYLRQRLQIRWREWLTERL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 422 LKNYLRNNSFYKVfHMASKNID-ADQRITHDLEKLTTDLSGLVTGMVKPSVD------ILW-------FTWRMKLLTGQR 487
Cdd:COG4178 104 LDRWLSNRAYYRL-QLSGGEIDnPDQRIAEDIRLFTETTLSLSLGLLSSVVTlisfigILWslsgsltFTLGGYSITIPG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 488 G-VAILYAYMLLG--LGFLrtvtpdFG----DLISQEQQLEGTFRF--MHERlcTHAESVAFFGGGTREKTMVESRFREL 558
Cdd:COG4178 183 YmVWAALIYAIIGtlLTHL------IGrpliRLNFEQQRREADFRFalVRVR--ENAESIALYRGEAAERRRLRRRFDAV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 559 LShsNYLLKKKWLFGIldDFITK---QLPHNVTWLLSllyamehkgdrasistqgelahALRFLAS-----VVSQSFLAF 630
Cdd:COG4178 255 IA--NWRRLIRRQRNL--TFFTTgygQLAVIFPILVA----------------------APRYFAGeitlgGLMQAASAF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 631 GDILE-L------HRKFVELSGGINRIFELEELLDAAQSVDSINGSITPSmrdyyAKDAISFSKVDIVTPAQKMLARELT 703
Cdd:COG4178 309 GQVQGaLswfvdnYQSLAEWRATVDRLAGFEEALEAADALPEAASRIETS-----EDGALALEDLTLRTPDGRPLLEDLS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 704 CDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDvdqeagsgcGIFYVPQRPYTCLGTLRDQIIYPlsree 783
Cdd:COG4178 384 LSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA---------RVLFLPQRPYLPLGTLREALLYP----- 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 784 aefralkmygkgekhADPRKLLDTHLQIILENVRLNYLLERDnrgwDANLNWEDTLSLGEQQRLGMARLFFHRPKYGILD 863
Cdd:COG4178 450 ---------------ATAEAFSDAELREALEAVGLGHLAERL----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLD 510
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 864 ECTNATSVDVEEHLYGLANKM--GITVVTSSQRPALIPYHSMELRLiDGEGNWELRSIKQ 921
Cdd:COG4178 511 EATSALDEENEAALYQLLREElpGTTVISVGHRSTLAAFHDRVLEL-TGDGSWQLLPAEA 569
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
31-239 |
3.38e-80 |
|
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: 256.70 E-value: 3.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGigsdlNKEIFYVPQRPYT 110
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----GEDLLFLPQRPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 111 AVGTLRDQLIYPltadqeveqltdrgmvellknvdleylldryppekevnWGDELSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:cd03223 76 PLGTLREQLIYP--------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1654042132 191 CTSAVTTDMEERFCAKVRAMGTSCITISHRPALVAFHDVVLSLDGEGGW 239
Cdd:cd03223 118 ATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
2-239 |
1.26e-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: 266.23 E-value: 1.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 2 AVSRELSMVDEKSSLQRK-GSRNCISEANYIEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGL 80
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVpGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 81 WPLISGHIVKPGIGSdlnkeIFYVPQRPYTAVGTLRDQLIYPLTADQEVEQ-LTDRGMVELLKNVDLEYLLDRYPPEKEV 159
Cdd:TIGR00954 502 WPVYGGRLTKPAKGK-----LFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRgLSDKDLEQILDNVQLTHILEREGGWSAV 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 160 -NWGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAMGTSCITISHRPALVAFHDVVLSLDGEGG 238
Cdd:TIGR00954 577 qDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGG 656
|
.
gi 1654042132 239 W 239
Cdd:TIGR00954 657 Y 657
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
10-242 |
2.14e-69 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 241.25 E-value: 2.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 10 VDEKSSLQRKGSRNCISEANYIEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV 89
Cdd:COG4178 342 LEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 90 KPGigsdlNKEIFYVPQRPYTAVGTLRDQLIYPLTADqeveQLTDRGMVELLKNVDLEYLLDRYppEKEVNWGDELSLGE 169
Cdd:COG4178 422 RPA-----GARVLFLPQRPYLPLGTLREALLYPATAE----AFSDAELREALEAVGLGHLAERL--DEEADWDQVLSLGE 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654042132 170 QQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLDGEGGWSVH 242
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGHRSTLAAFHDRVLELTGDGSWQLL 565
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
683-914 |
3.43e-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: 205.08 E-value: 3.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 683 ISFSKVDIVTPAQKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPsedvdqeagSGCGIFYVPQ 762
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP---------EGEDLLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 763 RPYTCLGTLRDQIIYPlsreeaefralkmygkgekhadprklldthlqiilenvrlnyllerdnrgwdanlnWEDTLSLG 842
Cdd:cd03223 72 RPYLPLGTLREQLIYP--------------------------------------------------------WDDVLSGG 95
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654042132 843 EQQRLGMARLFFHRPKYGILDECTNATSVDVEEHLYGLANKMGITVVTSSQRPALIPYHSMELRLiDGEGNW 914
Cdd:cd03223 96 EQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDL-DGEGGW 166
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
31-235 |
5.74e-28 |
|
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: 119.86 E-value: 5.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGI------GSDLNKEIFYV 104
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 105 PQRPYTAVGTLRDQLiypLTADQEVeqlTDRGMVELLKNVDLEYLLDRYP--PEKEVnwGDE---LSLGEQQRLGMARLF 179
Cdd:COG4988 417 PQNPYLFAGTIRENL---RLGRPDA---SDEELEAALEAAGLDEFVAALPdgLDTPL--GEGgrgLSGGQAQRLALARAL 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1654042132 180 YHKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLDG 235
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQADRILVLDD 546
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
31-235 |
1.54e-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: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLV-DDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGI------GSDLNKEIFY 103
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 104 VPQRPYTAVGTLRDqliypltadqeveqltdrgmvellkNVdleylldryppekevnwgdeLSLGEQQRLGMARLFYHKP 183
Cdd:cd03228 81 VPQDPFLFSGTIRE-------------------------NI--------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1654042132 184 KFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLDG 235
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALakGKTVIVIAHRLSTIRDADRIIVLDD 169
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
39-225 |
9.29e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 108.75 E-value: 9.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 39 VTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI------VKPGIGSDLNKEIFYVPQRPYTAV 112
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkpLSAMPPPEWRRQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 113 GTLRDQLIYPLTADQEveQLTDRGMVELLKNVDL-EYLLDryppeKEVnwgDELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:COG4619 88 GTVRDNLPFPFQLRER--KFDRERALELLERLGLpPDILD-----KPV---ERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1654042132 192 TSAVTTDMEERFCAKVRAM----GTSCITISHRPALVA 225
Cdd:COG4619 158 TSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIE 195
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
31-226 |
3.07e-24 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 102.20 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGN---VLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI---------VKPGIGSDLN 98
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllkLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 99 KEIFYVPQRPYTAVG---TLRDQLIYPLTA--DQEVEQLTDRGMVELLKNVDL-EYLLDRYPpekevnwgDELSLGEQQR 172
Cdd:cd03257 82 KEIQMVFQDPMSSLNprmTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGVGLpEEVLNRYP--------HELSGGQRQR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654042132 173 LGMARLFYHKPKFAILDECTSA--VTT---------DMEERFcakvramGTSCITISHRPALVAF 226
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSAldVSVqaqildllkKLQEEL-------GLTLLFITHDLGVVAK 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
31-235 |
1.37e-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: 99.97 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTP-TGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG------SDLNKEIFY 103
Cdd:cd03245 3 IEFRNVSFSYPnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDirqldpADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 104 VPQRPYTAVGTLRDQLI--YPLTADQEVEQLTDRGMVELLKNvDLEYLLDRYPPEKevnwGDELSLGEQQRLGMARLFYH 181
Cdd:cd03245 83 VPQDVTLFYGTLRDNITlgAPLADDERILRAAELAGVTDFVN-KHPNGLDLQIGER----GRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1654042132 182 KPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLDG 235
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLLDLVDRIIVMDS 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
31-235 |
4.22e-23 |
|
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: 98.84 E-value: 4.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGI-GSDLNKE-----IFYV 104
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdIRDISRKslrsmIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 105 PQRPYTAVGTLRDQLIY--PLTADQEVEQLTDR-GMVELLKNvdLEYLLDRYPPEKevnwGDELSLGEQQRLGMARLFYH 181
Cdd:cd03254 83 LQDTFLFSGTIMENIRLgrPNATDEEVIEAAKEaGAHDFIMK--LPNGYDTVLGEN----GGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1654042132 182 KPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLDG 235
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAHRLSTIKNADKILVLDD 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
47-193 |
5.18e-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: 96.18 E-value: 5.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI------VKPGIGSDLNKEIFYVPQRP-----YTAVGTL 115
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdLTDDERKSLRKEIGYVFQDPqlfprLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 116 RD----QLIYPLTADQEVEqltdrgmvELLKNVDLEYLLDRYPPEKevnwGDELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:pfam00005 81 RLglllKGLSKREKDARAE--------EALEKLGLGDLADRPVGER----PGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 1654042132 192 TS 193
Cdd:pfam00005 149 TA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
43-230 |
6.42e-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: 97.55 E-value: 6.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG-----SDLNKEIFYVPQRPytavgtlrd 117
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirdarEDYRRRLAYLGHAD--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 118 qLIYP-LTADQEVE--------QLTDRGMVELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:COG4133 85 -GLKPeLTVRENLRfwaalyglRADREAIDEALEAVGLAGLADLPV--------RQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1654042132 189 DECTSAVTTDMEERFCAKVRAM---GTSCITISHRPALVAFHDVV 230
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAARVL 200
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
41-235 |
1.43e-22 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 103.76 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 41 PTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI---------VKPgigSDLNKEIFYVPQRPYTA 111
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqIDP---ASLRRQIGVVLQDVFLF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 112 VGTLRDQLIYpltADQEVeqlTDRGMVELLKNVDLEYLLDRYP-------PEKevnwGDELSLGEQQRLGMARLFYHKPK 184
Cdd:COG2274 562 SGTIRENITL---GDPDA---TDEEIIEAARLAGLHDFIEALPmgydtvvGEG----GSNLSGGQRQRLAIARALLRNPR 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654042132 185 FAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLDG 235
Cdd:COG2274 632 ILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRLADRIIVLDK 684
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
31-233 |
3.22e-22 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 94.59 E-value: 3.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTP-TGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG------SDLNKEIFY 103
Cdd:cd03246 1 LEVENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADisqwdpNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 104 VPQRPYTAVGTLRDqliypltadqeveqltdrgmvellkNVdleylldryppekevnwgdeLSLGEQQRLGMARLFYHKP 183
Cdd:cd03246 81 LPQDDELFSGSIAE-------------------------NI--------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654042132 184 KFAILDECTSAVTTDMEERFCAKVRAM---GTSCITISHRPALVAFHDVVLSL 233
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALkaaGATRIVIAHRPETLASADRILVL 168
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
32-225 |
3.40e-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: 95.61 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 32 EFYDVKVVTPTGNVLV-DDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI------VKPGIGSDLNKEIFYV 104
Cdd:cd03225 1 ELKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 105 PQRPytavgtlRDQLIYPlTADQEV----EQL------TDRGMVELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLG 174
Cdd:cd03225 81 FQNP-------DDQFFGP-TVEEEVafglENLglpeeeIEERVEEALELVGLEGLRDRSP--------FTLSGGQKQRVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1654042132 175 MARLFYHKPKFAILDECTSAV----TTDMEERFcAKVRAMGTSCITISHRPALVA 225
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLdpagRRELLELL-KKLKAEGKTIIIVTHDLDLLL 198
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
31-233 |
3.49e-22 |
|
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: 101.59 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG------SDLNKEIFYV 104
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadaDSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 105 PQRPYTAVGTLRD--QLIYPLTADQEVEQ-LTDRGMVELLKnvDLEYLLDRYPPEKevnwGDELSLGEQQRLGMARLFYH 181
Cdd:TIGR02857 402 PQHPFLFAGTIAEniRLARPDASDAEIREaLERAGLDEFVA--ALPQGLDTPIGEG----GAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1654042132 182 KPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSL 233
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLALAALADRIVVL 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
31-225 |
4.41e-22 |
|
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: 101.13 E-value: 4.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNV-LVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP---LISGHIVKPGI------GSDLNKE 100
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRdllelsEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 101 IFYVPQRPYTAV--GTLRDQLIYPLTADQEVEQLTDRGMVELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARL 178
Cdd:COG1123 85 IGMVFQDPMTQLnpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYP--------HQLSGGQRQRVAIAMA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1654042132 179 FYHKPKFAILDECTSA--VTTDME--ERFCAKVRAMGTSCITISHRPALVA 225
Cdd:COG1123 157 LALDPDLLIADEPTTAldVTTQAEilDLLRELQRERGTTVLLITHDLGVVA 207
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
31-236 |
1.37e-21 |
|
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: 94.09 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLV---DDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGI----------GSDL 97
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 98 NKEIFYVPQRpYTAVGTL--RDQLIYPLTADQEVEQLTDRGMVELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGM 175
Cdd:cd03255 81 RRHIGFVFQS-FNLLPDLtaLENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYP--------SELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654042132 176 ARLFYHKPKFAILDECTSAVTTDMEER----FCAKVRAMGTSCITISHRPALVAFHDVVLSL-DGE 236
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEvmelLRELNKEAGTTIVVVTHDPELAEYADRIIELrDGK 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
32-236 |
2.94e-21 |
|
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: 92.98 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 32 EFYDVkVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI-VKPGIGSDLNKEIFYVPQR--- 107
Cdd:cd03235 1 EVEDL-TVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrVFGKPLEKERKRIGYVPQRrsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 108 ----PYTA---VGTLRDQLIYPL-TADQEVEQLTDrgmvELLKNVDLEYLLDRyppekevNWGdELSLGEQQRLGMARLF 179
Cdd:cd03235 80 drdfPISVrdvVLMGLYGHKGLFrRLSKADKAKVD----EALERVGLSELADR-------QIG-ELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654042132 180 YHKPKFAILDECTSAVTTDMEERF---CAKVRAMGTSCITISHRPALV-AFHDVVLSLDGE 236
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIyelLRELRREGMTILVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
43-234 |
1.19e-20 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 89.61 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI------VKPGIGSDLNKEIFYVPQrpytavgtlr 116
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIlidgkdIAKLPLEELRRRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 117 dqliypltadqeveqltdrgmvellknvdleylldryppekevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSAVT 196
Cdd:cd00267 81 ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1654042132 197 TDMEERFCAKVRAM---GTSCITISHRPALVAFH-DVVLSLD 234
Cdd:cd00267 113 PASRERLLELLRELaeeGRTVIIVTHDPELAELAaDRVIVLK 154
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
31-225 |
2.30e-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: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI------VKPGIGSDLNKEIFYV 104
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdgkdITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 105 PQRPytavgtlRDQLIYPLTAD-------------QEVEQLTDrgmvELLKNVDLEYLLDRYPpekevnwgDELSLGEQQ 171
Cdd:COG1122 81 FQNP-------DDQLFAPTVEEdvafgpenlglprEEIRERVE----EALELVGLEHLADRPP--------HELSGGQKQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1654042132 172 RLGMARLFYHKPKFAILDECTSAV----TTDMEERFcAKVRAMGTSCITISHRPALVA 225
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLdprgRRELLELL-KRLNKEGKTVIIVTHDLDLVA 198
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
47-230 |
1.12e-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: 93.43 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI---------VKPGIGSDLNKEIFYVPQRPYTAV---GT 114
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltkLSRRSLRELRRRVQMVFQDPYSSLnprMT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 115 LRDQLIYPLTADQEV--EQLTDRgMVELLKNVDLEY-LLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:COG1123 361 VGDIIAEPLRLHGLLsrAERRER-VAELLERVGLPPdLADRYP--------HELSGGQRQRVAIARALALEPKLLILDEP 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1654042132 192 TSA----VTTDMEERFCAKVRAMGTSCITISHRPALVAF--HDVV 230
Cdd:COG1123 432 TSAldvsVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiaDRVA 476
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
43-194 |
4.30e-19 |
|
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: 87.79 E-value: 4.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV---KPgIGS----DLNKEIFYVPQRPYTAVG-T 114
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRD-LASlsrrELARRIAYVPQEPPAPFGlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 115 LRDqLI----YPLTADQEVEQLTDRGMV-ELLKNVDLEYLLDRYppekeVnwgDELSLGEQQRLGMARLFYHKPKFAILD 189
Cdd:COG1120 92 VRE-LValgrYPHLGLFGRPSAEDREAVeEALERTGLEHLADRP-----V---DELSGGERQRVLIARALAQEPPLLLLD 162
|
....*
gi 1654042132 190 ECTSA 194
Cdd:COG1120 163 EPTSH 167
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
35-225 |
4.91e-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: 86.54 E-value: 4.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 35 DVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV---KPGIGSDLNKEIFYVPQRPYTA 111
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngKPIKAKERRKSIGYVMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 112 VG--TLRDQLIYPLTADQEVEQLTDrgmvELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILD 189
Cdd:cd03226 84 LFtdSVREELLLGLKELDAGNEQAE----TVLKDLDLYALKERHP--------LSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 1654042132 190 ECTSAVTTDMEERFCAKVR---AMGTSCITISHRPALVA 225
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRelaAQGKAVIVITHDYEFLA 190
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
43-231 |
1.02e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 86.68 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI-VKPGIGSDLNKEIFYVPQRpyTAVGtlRDqliY 121
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrLFGKPPRRARRRIGYVPQR--AEVD--WD---F 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 122 PLTadqeVEQL-----------------TDRGMV-ELLKNVDLEYLLDRYppekeVNwgdELSLGEQQRLGMARLFYHKP 183
Cdd:COG1121 91 PIT----VRDVvlmgrygrrglfrrpsrADREAVdEALERVGLEDLADRP-----IG---ELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654042132 184 KFAILDECTSAVTTDMEERFCA---KVRAMGTSCITISHRPALVA--FHDVVL 231
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYEllrELRREGKTILVVTHDLGAVReyFDRVLL 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
43-225 |
1.32e-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: 84.41 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI------VKPGIGSDLNKEIFYVPQrpytavgtlr 116
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlldgkdLASLSPKELARKIAYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 117 dqliypltadqeveqltdrgmveLLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAVt 196
Cdd:cd03214 81 -----------------------ALELLGLAHLADRPF--------NELSGGERQRVLLARALAQEPPILLLDEPTSHL- 128
|
170 180 190
....*....|....*....|....*....|....*
gi 1654042132 197 tDME------ERFCAKVRAMGTSCITISHRPALVA 225
Cdd:cd03214 129 -DIAhqiellELLRRLARERGKTVVMVLHDLNLAA 162
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
31-235 |
7.00e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 83.56 E-value: 7.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVkpgI-GSDLNK----EIFYVP 105
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVL---VnGQDLSRlkrrEIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 106 QRpytaVG------------TLRDQLIYPLTA----DQEVEQLTDrgmvELLKNVDLEYLLDRYPPekevnwgdELSLGE 169
Cdd:COG2884 79 RR----IGvvfqdfrllpdrTVYENVALPLRVtgksRKEIRRRVR----EVLDLVGLSDKAKALPH--------ELSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654042132 170 QQRLGMARLFYHKPKFAILDECTSAVTTDMEER----FcAKVRAMGTSCITISHRPALV-AFHDVVLSLDG 235
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETSWEimelL-EEINRRGTTVLIATHDLELVdRMPKRVLELED 212
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
43-195 |
8.88e-18 |
|
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: 83.75 E-value: 8.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGSD-----LNKEIFYVPQRPY-TAVGTLR 116
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkepreARRQIGVLPDERGlYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 117 DQL-----IYPLTaDQEVEQLTDrgmvELLKNVDLEYLLDRyppekevNWGdELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:COG4555 93 ENIryfaeLYGLF-DEELKKRIE----ELIELLGLEEFLDR-------RVG-ELSTGMKKKVALARALVHDPKVLLLDEP 159
|
....
gi 1654042132 192 TSAV 195
Cdd:COG4555 160 TNGL 163
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-235 |
9.73e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 87.91 E-value: 9.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 11 DEKSSLQRKGSRNCISEANY-IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV 89
Cdd:COG1132 319 DEPPEIPDPPGAVPLPPVRGeIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 90 kpgIG---------SDLNKEIFYVPQRPYTAVGTLRDQLIY--PLTADQEVEqltdrgmvELLKNVDLEYLLDRYPP--- 155
Cdd:COG1132 399 ---IDgvdirdltlESLRRQIGVVPQDTFLFSGTIRENIRYgrPDATDEEVE--------EAAKAAQAHEFIEALPDgyd 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 156 ----EKevnwGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEerfcAKV-RAM-----GTSCITISHRPALVA 225
Cdd:COG1132 468 tvvgER----GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETE----ALIqEALerlmkGRTTIVIAHRLSTIR 539
|
250
....*....|
gi 1654042132 226 FHDVVLSLDG 235
Cdd:COG1132 540 NADRILVLDD 549
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
43-222 |
1.94e-17 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 81.80 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVkpgIGsdlNKEIFYVP--QRPytaVG------- 113
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIL---ID---GRDVTGVPpeRRN---IGmvfqdya 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 114 -----TLRDQLIYPLTADQEVEQLTDRGMVELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:cd03259 83 lfphlTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYP--------HELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1654042132 189 DECTSAVTTDMEERFCAKVRAM----GTSCITISHRPA 222
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqrelGITTIYVTHDQE 192
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
30-221 |
5.70e-17 |
|
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: 85.10 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 30 YIEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGI------GSDLNKEIFY 103
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 104 VPQRPYTAVGTLRDQLiypLTADQEVeqlTDRGMVELLKNVDLEYLLDRYPPEKEVNWGDE---LSLGEQQRLGMARLFY 180
Cdd:TIGR02868 414 CAQDAHLFDTTVRENL---RLARPDA---TDEELWAALERVGLADWLRALPDGLDTVLGEGgarLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1654042132 181 HKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRP 221
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLAAlsGRTVVLITHHL 530
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
691-889 |
8.02e-17 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 79.86 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 691 VTPAQKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGL---SRPSEDVD-----QEagsgcgIFYVPQ 762
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldGKPLSAMPppewrRQ------VAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 763 RPYTCLGTLRDQIIYPLSreeaeFRalkmygkgEKHADPRKLLDthlqiilenvrlnyLLERDNRGwDANLNWE-DTLSL 841
Cdd:COG4619 82 EPALWGGTVRDNLPFPFQ-----LR--------ERKFDRERALE--------------LLERLGLP-PDILDKPvERLSG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1654042132 842 GEQQRLGMARLFFHRPKYGILDECTNA----TSVDVEEHLYGLANKMGITVV 889
Cdd:COG4619 134 GERQRLALIRALLLQPDVLLLDEPTSAldpeNTRRVEELLREYLAEEGRAVL 185
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
31-234 |
1.00e-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: 80.23 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKV-VTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG------SDLNKEIFY 103
Cdd:cd03244 3 IEFKNVSLrYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskiglHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 104 VPQRPYTAVGTLRDQL-IYPLTADQEVEQLTDR-GMVELLKNvdLEYLLDryppEKEVNWGDELSLGEQQRLGMARLFYH 181
Cdd:cd03244 83 IPQDPVLFSGTIRSNLdPFGEYSDEELWQALERvGLKEFVES--LPGGLD----TVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1654042132 182 KPKFAILDECTSAVTTDMEERFCAKVRAMGTSC--ITISHRPALVAFHDVVLSLD 234
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCtvLTIAHRLDTIIDSDRILVLD 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
44-220 |
1.41e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.11 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 44 NVLvDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG------SDLNKEIFYVPQRPYTAVGTLRD 117
Cdd:PRK11160 354 PVL-KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiadyseAALRQAISVVSQRVHLFSATLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 118 QLiypLTADqevEQLTDRGMVELLKNVDLEYLLDRyppEKEVN-W----GDELSLGEQQRLGMARLFYHKPKFAILDECT 192
Cdd:PRK11160 433 NL---LLAA---PNASDEALIEVLQQVGLEKLLED---DKGLNaWlgegGRQLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
170 180 190
....*....|....*....|....*....|
gi 1654042132 193 SAVTTDMEERFCAKVR--AMGTSCITISHR 220
Cdd:PRK11160 504 EGLDAETERQILELLAehAQNKTVLMITHR 533
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
43-233 |
1.92e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.43 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGigsdlNKEIFYVPQR-------PYTAVGTL 115
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----GARVAYVPQRsevpdslPLTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 116 ------RDQLIYPLTADqeveqltDRGMVE-LLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:NF040873 79 amgrwaRRGLWRRLTRD-------DRAAVDdALERVGLADLAGRQL--------GELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1654042132 189 DECTSAVTTDMEERFCAKVR---AMGTSCITISHRPALVAFHDVVLSL 233
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAeehARGATVVVVTHDLELVRRADPCVLL 191
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
652-898 |
2.99e-16 |
|
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: 82.88 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 652 ELEELLDAAQSVDSINGSITPSMRDyyakDAISFSKVDIVTPAQKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRG 731
Cdd:COG4988 310 KIFALLDAPEPAAPAGTAPLPAAGP----PSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 732 LWPIASGGLS---RPSEDVDQEAGSGCgIFYVPQRPYTCLGTLRDQIIypLSREEAEfralkmygkgekhadprkllDTH 808
Cdd:COG4988 386 FLPPYSGSILingVDLSDLDPASWRRQ-IAWVPQNPYLFAGTIRENLR--LGRPDAS--------------------DEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 809 LQIILENVRLNYLLERDNRGWDANLNwED--TLSLGEQQRLGMARLFFHRPKYGILDECTnaTSVDVE------EHLYGL 880
Cdd:COG4988 443 LEAALEAAGLDEFVAALPDGLDTPLG-EGgrGLSGGQAQRLALARALLRDAPLLLLDEPT--AHLDAEteaeilQALRRL 519
|
250
....*....|....*...
gi 1654042132 881 ANkmGITVVTSSQRPALI 898
Cdd:COG4988 520 AK--GRTVILITHRLALL 535
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
41-235 |
3.07e-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: 79.07 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 41 PTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP------LISGHIVKPGIGSDLNKEIFYVPQRPYTAVGT 114
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVpengrvLVDGHDLALADPAWLRRQVGVVLQENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 115 LRDQLiypltadqeveQLTDRGM-----VELLKNVDLEYLLDRYPPEKEVNWGDE---LSLGEQQRLGMARLFYHKPKFA 186
Cdd:cd03252 92 IRDNI-----------ALADPGMsmervIEAAKLAGAHDFISELPEGYDTIVGEQgagLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1654042132 187 ILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLDG 235
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADRIIVMEK 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
31-234 |
4.31e-16 |
|
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: 78.81 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG------SDLNKEIFYV 104
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDirevtlDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 105 PQRPYTAVGTLRDQLIY-PLTAdqeveqlTDRGMVELLKNVDLEYLLDRYPPEKEVNWGD---ELSLGEQQRLGMARLFY 180
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYgRPDA-------TDEEVIEAAKAAQIHDKIMRFPDGYDTIVGErglKLSGGEKQRVAIARAIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1654042132 181 HKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLD 234
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLSTIVNADKIIVLK 209
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
42-235 |
1.20e-15 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 76.35 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 42 TGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVkpgigsdLNKEIFYVPQRPYTAVGTLRDQLIY 121
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS-------VPGSIAYVSQEPWIQNGTIRENILF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 122 PLTADQE--------------VEQLTDRGMVELlknvdleylldrypPEKEVNwgdeLSLGEQQRLGMARLFYHKPKFAI 187
Cdd:cd03250 89 GKPFDEEryekvikacalepdLEILPDGDLTEI--------------GEKGIN----LSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1654042132 188 LDECTSAVTTDMEERFCAKV----RAMGTSCITISHRPALVAFHDVVLSLDG 235
Cdd:cd03250 151 LDDPLSAVDAHVGRHIFENCilglLLNNKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
31-221 |
2.06e-15 |
|
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: 77.05 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTpTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGG-LWPLISGHI--------------VKPGIG- 94
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVrlfgerrggedvweLRKRIGl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 95 --SDLnKEIFYVPQRPYTAVGT-LRDQLIYPLTADQEVEQLTDrgmvELLKNVDLEYLLDRYppekevnWGdELSLGEQQ 171
Cdd:COG1119 83 vsPAL-QLRFPRDETVLDVVLSgFFDSIGLYREPTDEQRERAR----ELLELLGLAHLADRP-------FG-TLSQGEQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1654042132 172 RLGMARLFYHKPKFAILDECTSAVttDME--ERFCAKVRAM----GTSCITISHRP 221
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGL--DLGarELLLALLDKLaaegAPTLVLVTHHV 203
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
47-195 |
2.52e-15 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 76.26 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSnllIT---GPNGSGKSSLFRVLGGLWPLISGHIVkpgI-GSDLNKE-------IFYVPQRP--YTAVg 113
Cdd:COG1131 16 LDGVSLTVEPGE---IFgllGPNGAGKTTTIRMLLGLLRPTSGEVR---VlGEDVARDpaevrrrIGYVPQEPalYPDL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 114 TLRDQL-----IYPLTADqEVEQLTDrgmvELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:COG1131 89 TVRENLrffarLYGLPRK-EARERID----ELLELFGLTDAADRKV--------GTLSGGMKQRLGLALALLHDPELLIL 155
|
....*..
gi 1654042132 189 DECTSAV 195
Cdd:COG1131 156 DEPTSGL 162
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
31-235 |
3.82e-15 |
|
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: 75.59 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPT---GNVLvDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV---KPGIGSD---LNKEI 101
Cdd:cd03248 12 VKFQNVTFAYPTrpdTLVL-QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPISQYEhkyLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 102 FYVPQRPYTAVGTLRDQLIYPLT--ADQEVEQLTDRG-----MVELLKNVDLEYlldrypPEKevnwGDELSLGEQQRLG 174
Cdd:cd03248 91 SLVGQEPVLFARSLQDNIAYGLQscSFECVKEAAQKAhahsfISELASGYDTEV------GEK----GSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654042132 175 MARLFYHKPKFAILDECTSAVTTDMEERFCAKVRA--MGTSCITISHRPALVAFHDVVLSLDG 235
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDwpERRTVLVIAHRLSTVERADQILVLDG 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
31-220 |
4.07e-15 |
|
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: 75.65 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPT--GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG-SDLN-----KEIF 102
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDiRDLNlrwlrSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 103 YVPQRPYTAVGTLRDQLIY---PLTADQEVEQLTDRGMVELLKNvdleyLLDRYppEKEV-NWGDELSLGEQQRLGMARL 178
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYgkpDATDEEVEEAAKKANIHDFIMS-----LPDGY--DTLVgERGSQLSGGQKQRIAIARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1654042132 179 FYHKPKFAILDECTSAVTTDMEERFCAKV-RAM-GTSCITISHR 220
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALdRAMkGRTTIVIAHR 197
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
700-911 |
5.67e-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: 74.88 E-value: 5.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 700 RELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSgcgIFYVPQRpytcLGTLRDqiiYPL 779
Cdd:cd03235 16 EDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR---IGYVPQR----RSIDRD---FPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 780 SREeaEFRALKMYGKGE-----KHADPRKLLDthlqiILENVRLNYLLERdnrgwdaNLnweDTLSLGEQQRLGMARLFF 854
Cdd:cd03235 86 SVR--DVVLMGLYGHKGlfrrlSKADKAKVDE-----ALERVGLSELADR-------QI---GELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654042132 855 HRPKYGILDECTnaTSVDV--EEHLYGLANKM---GITVVTSSQRPALIPYHSMELRLIDGE 911
Cdd:cd03235 149 QDPDLLLLDEPF--AGVDPktQEDIYELLRELrreGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
43-194 |
6.30e-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: 74.97 E-value: 6.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGigsdlnKEIFYVP--QRPYTAVG------- 113
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG------KDITNLPphKRPVNTVFqnyalfp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 114 --TLRDQLIYPLTADQEVEQLTDRGMVELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:cd03300 86 hlTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKP--------SQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
...
gi 1654042132 192 TSA 194
Cdd:cd03300 158 LGA 160
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
40-190 |
7.42e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 75.51 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 40 TPTGNVLV-DDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPG-IGSDLNKEIFYVPQRPytavgTL-- 115
Cdd:COG1116 19 TGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkPVTGPGPDRGVVFQEP-----ALlp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 116 ----RDQLIYPL-TADQEVEQLTDRGMvELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:COG1116 94 wltvLDNVALGLeLRGVPKAERRERAR-ELLELVGLAGFEDAYP--------HQLSGGMRQRVAIARALANDPEVLLMDE 164
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
47-219 |
1.66e-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: 72.43 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGI-----GSDLNKEIFYVPQRPYtavgtlrdqlIY 121
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKdikkePEEVKRRIGYLPEEPS----------LY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 122 P-LTAdqeveqltdrgmvellknvdLEYLldryppekevnwgdELSLGEQQRLGMARLFYHKPKFAILDECTSAVttDME 200
Cdd:cd03230 86 EnLTV--------------------RENL--------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL--DPE 129
|
170 180
....*....|....*....|....
gi 1654042132 201 ER-----FCAKVRAMGTSCITISH 219
Cdd:cd03230 130 SRrefweLLRELKKEGKTILLSSH 153
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
31-190 |
1.69e-14 |
|
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: 73.66 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGN---VLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV---KPGIGSdlNKEIFYV 104
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgEPVTGP--GPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 105 PQRPY-----TAvgtlRDQLIYPLTAdQEV--EQLTDRGMvELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMAR 177
Cdd:cd03293 79 FQQDAllpwlTV----LDNVALGLEL-QGVpkAEARERAE-ELLELVGLSGFENAYP--------HQLSGGMRQRVALAR 144
|
170
....*....|...
gi 1654042132 178 LFYHKPKFAILDE 190
Cdd:cd03293 145 ALAVDPDVLLLDE 157
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
343-898 |
1.87e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 77.51 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 343 AQLLTVAFLVVARTWVSDRIASLNGTTVKFVLeqdkasfIRLIGLSVLQSAASSFIAPSIRHLRARLALGWRIRLTQHLL 422
Cdd:COG1132 33 SALLELLLPLLLGRIIDALLAGGDLSALLLLL-------LLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 423 K---NYLRNNSFYKVFhmasknidadQRITHDLEKLTTDLSGLVTGMVKPSVDI-------LWFTWRMKLLTgqrgVAIL 492
Cdd:COG1132 106 RlplSFFDRRRTGDLL----------SRLTNDVDAVEQFLAHGLPQLVRSVVTLigalvvlFVIDWRLALIV----LLVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 493 YAYMLLGLGFLRTVTPDFGDlisQEQQLEGTFRFMHERLcTHAESVAFFGGGTREKTMVESRFRELLSHSNYLLKKKWLF 572
Cdd:COG1132 172 PLLLLVLRLFGRRLRKLFRR---VQEALAELNGRLQESL-SGIRVVKAFGREERELERFREANEELRRANLRAARLSALF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 573 GILDDFITkqlphNVTWLLSLLYAMeHKGDRASISTqGELAhALRFLASVVSQSFLAFGDILELhrkFVELSGGINRIFE 652
Cdd:COG1132 248 FPLMELLG-----NLGLALVLLVGG-LLVLSGSLTV-GDLV-AFILYLLRLFGPLRQLANVLNQ---LQRALASAERIFE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 653 LeelLDAAQSVDSINGSITPSMrdyyAKDAISFSKVDIVTPAQKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGL 732
Cdd:COG1132 317 L---LDEPPEIPDPPGAVPLPP----VRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 733 WPIASG-----GlsRPSEDVDQEA-----GsgcgifYVPQRPYtcL--GTLRDQIIY---PLSREEAEfRALKMygkgeK 797
Cdd:COG1132 390 YDPTSGrilidG--VDIRDLTLESlrrqiG------VVPQDTF--LfsGTIRENIRYgrpDATDEEVE-EAAKA-----A 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 798 HADP--RKL---LDTHLQiilenvrlnyllERDNRgwdanlnwedtLSLGEQQRLGMARLFFHRPKYGILDECTNATSVD 872
Cdd:COG1132 454 QAHEfiEALpdgYDTVVG------------ERGVN-----------LSGGQRQRIAIARALLKDPPILILDEATSALDTE 510
|
570 580
....*....|....*....|....*...
gi 1654042132 873 VEEHLY-GLANKM-GITVVTSSQRPALI 898
Cdd:COG1132 511 TEALIQeALERLMkGRTTIVIAHRLSTI 538
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
47-201 |
2.14e-14 |
|
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: 73.37 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISG------------HIVKPGIG-SDLNKEIFYVPQRPYTAVG 113
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdegevlldgkDIYDLDVDvLELRRRVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 114 TLRDQLIYPLTADQEVEQLTDRGMVE-LLKNVDL-EYLLDRYPpekevnwGDELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:cd03260 96 SIYDNVAYGLRLHGIKLKEELDERVEeALRKAALwDEVKDRLH-------ALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170
....*....|....
gi 1654042132 192 TSAV----TTDMEE 201
Cdd:cd03260 169 TSALdpisTAKIEE 182
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
46-243 |
2.16e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.45 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 46 LVDDLTLRVEPGSNLLITGPNGSGKSSLFRVlggLWPLISGhivKPGIGSdlnkeiFYVPQRPYTAVGTLRDQLIYPLTA 125
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRL---LAGALKG---TPVAGC------VDVPDNQFGREASLIDAIGRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 126 DQEVEQLTDRGMVEllknvdlEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCA 205
Cdd:COG2401 113 KDAVELLNAVGLSD-------AVLWLRRF--------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1654042132 206 KV----RAMGTSCITISHRPALVAF--HDVVLSLDGEGGWSVHY 243
Cdd:COG2401 178 NLqklaRRAGITLVVATHHYDVIDDlqPDLLIFVGYGGVPEEKR 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-253 |
2.24e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.45 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 2 AVSRELSMVDEKSSLQRKGSRNCISEANYIEFYDVKVVTPT-GNVLV-DDLTLRVEPGSNLLITGPNGSGKSSLFRVLGG 79
Cdd:TIGR00958 450 ASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNrPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQN 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 80 LWPLISGHIV---KPGIGSD---LNKEIFYVPQRPYTAVGTLRDQLIYPLTaDQEVEQLTDRGMVELLKN--VDLEYLLD 151
Cdd:TIGR00958 530 LYQPTGGQVLldgVPLVQYDhhyLHRQVALVGQEPVLFSGSVRENIAYGLT-DTPDEEIMAAAKAANAHDfiMEFPNGYD 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 152 RYPPEKevnwGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAMGTSCITISHRPALVAFHDVVL 231
Cdd:TIGR00958 609 TEVGEK----GSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQIL 684
|
250 260
....*....|....*....|..
gi 1654042132 232 SLdgeggwsvhykREGSSTEMG 253
Cdd:TIGR00958 685 VL-----------KKGSVVEMG 695
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
698-905 |
3.09e-14 |
|
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: 72.51 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 698 LARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSGCG-IFYVPQRPytclgtlrdqII 776
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYLGHAD----------GL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 777 YP-LS-REEAEFrALKMYGKGEKHADPRKLLDThlqiilenVRLNYLLERDNRgwdanlnwedTLSLGEQQRLGMARLFF 854
Cdd:COG4133 87 KPeLTvRENLRF-WAALYGLRADREAIDEALEA--------VGLAGLADLPVR----------QLSAGQKRRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1654042132 855 HRPKYGILDECTNA---TSVD-VEEHLYGLANKMGITVVTSSQRPALIPYHSMEL 905
Cdd:COG4133 148 SPAPLWLLDEPFTAldaAGVAlLAELIAAHLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
705-867 |
3.49e-14 |
|
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: 70.75 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 705 DIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSR--PSEDVDQEAGSGCGIFYVPQrpYTCLG---TLRDQIIYPL 779
Cdd:pfam00005 7 TLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgQDLTDDERKSLRKEIGYVFQ--DPQLFprlTVRENLRLGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 780 SreeaefraLKMYGKGEKhadprkllDTHLQIILENVRLNYLLER--DNRGwdanlnweDTLSLGEQQRLGMARLFFHRP 857
Cdd:pfam00005 85 L--------LKGLSKREK--------DARAEEALEKLGLGDLADRpvGERP--------GTLSGGQRQRVAIARALLTKP 140
|
170
....*....|
gi 1654042132 858 KYGILDECTN 867
Cdd:pfam00005 141 KLLLLDEPTA 150
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
43-221 |
3.82e-14 |
|
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: 72.14 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGSD-----LNKEIFYVPQRP-----YTAV 112
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDfqrdsIARGLLYLGHAPgikttLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 113 GTLRdqLIYPLTADQEVEQLTDRgmvellknVDLEYLLDRyppekEVNwgdELSLGEQQRLGMARLFYHKPKFAILDECT 192
Cdd:cd03231 92 ENLR--FWHADHSDEQVEEALAR--------VGLNGFEDR-----PVA---QLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|..
gi 1654042132 193 SAVTTDMEERFCAKVR---AMGTSCITISHRP 221
Cdd:cd03231 154 TALDKAGVARFAEAMAghcARGGMVVLTTHQD 185
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
47-234 |
5.06e-14 |
|
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: 72.06 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG------SDLNKEIFYVPQRPYTAVGTLRDQLi 120
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDistiplEDLRSSLTIIPQDPTLFSGTIRSNL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 121 ypltaDQEVEQlTDRGMVELLKnvdleylldryppEKEvnWGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDME 200
Cdd:cd03369 103 -----DPFDEY-SDEEIYGALR-------------VSE--GGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATD 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1654042132 201 ERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLD 234
Cdd:cd03369 162 ALIQKTIREEftNSTILTIAHRLRTIIDYDKILVMD 197
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
45-202 |
5.63e-14 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 71.84 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 45 VLVDDLTLRVEPG-SNLLitGPNGSGKSSLFRVLGGLWPLISGHIVKPGI-----GSDLNKEIFYVPQ--RPYTAVgTLR 116
Cdd:cd03264 14 RALDGVSLTLGPGmYGLL--GPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqPQKLRRRIGYLPQefGVYPNF-TVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 117 DQLIY--------PLTADQEVEqltdrgmvELLKNVDLEyllDRYppEKEVNwgdELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:cd03264 91 EFLDYiawlkgipSKEVKARVD--------EVLELVNLG---DRA--KKKIG---SLSGGMRRRVGIAQALVGDPSILIV 154
|
170
....*....|....
gi 1654042132 189 DECTsaVTTDMEER 202
Cdd:cd03264 155 DEPT--AGLDPEER 166
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
43-209 |
5.77e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.83 E-value: 5.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGSDLNKeifYVPQRPYtaVGTlRDQLIYP 122
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---VAEACHY--LGH-RNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 123 LTAdqeVEQLT---------DRGMVELLKNVDLEYLLDRypPEKevnwgdELSLGEQQRLGMARLF-YHKPKFaILDECT 192
Cdd:PRK13539 88 LTV---AENLEfwaaflggeELDIAAALEAVGLAPLAHL--PFG------YLSAGQKRRVALARLLvSNRPIW-ILDEPT 155
|
170
....*....|....*..
gi 1654042132 193 SAVTTDMEERFCAKVRA 209
Cdd:PRK13539 156 AALDAAAVALFAELIRA 172
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
659-899 |
7.43e-14 |
|
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: 75.40 E-value: 7.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 659 AAQSVDSINGSITPSMRDYYAKDA--ISFSKVDIVTPAQKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIA 736
Cdd:TIGR02857 296 ALFAVLDAAPRPLAGKAPVTAAPAssLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 737 SGGLS---RPSEDVDqEAGSGCGIFYVPQRPYTCLGTLRDQIIypLSREEAE----FRALKMYGKGEKHADPRKLLDThl 809
Cdd:TIGR02857 376 EGSIAvngVPLADAD-ADSWRDQIAWVPQHPFLFAGTIAENIR--LARPDASdaeiREALERAGLDEFVAALPQGLDT-- 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 810 qiilenvrlnyLLERDNRGwdanlnwedtLSLGEQQRLGMARLFFHRPKYGILDECT----NATSVDVEEHLYGLANkmG 885
Cdd:TIGR02857 451 -----------PIGEGGAG----------LSGGQAQRLALARAFLRDAPLLLLDEPTahldAETEAEVLEALRALAQ--G 507
|
250
....*....|....
gi 1654042132 886 ITVVTSSQRPALIP 899
Cdd:TIGR02857 508 RTVLLVTHRLALAA 521
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
31-220 |
1.47e-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: 71.11 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKV-VTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG------SDLNKEIFY 103
Cdd:cd03251 1 VEFKNVTFrYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDvrdytlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 104 VPQRPYTAVGTLRDQLIY--PLTADQEVEqltdrgmvELLKNVDLEYLLDRYPPEKEVNWGD---ELSLGEQQRLGMARL 178
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYgrPGATREEVE--------EAARAANAHEFIMELPEGYDTVIGErgvKLSGGQRQRIAIARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1654042132 179 FYHKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHR 220
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAHR 196
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-234 |
1.77e-13 |
|
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: 74.39 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 6 ELSMVDekSSLQRKGSRNCISEANY-IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLI 84
Cdd:TIGR01193 450 EVYLVD--SEFINKKKRTELNNLNGdIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 85 SGHIVKPGIGSD------LNKEIFYVPQRPYTAVGTLRDQLIY---PLTADQEVEQLTDrgMVELLKnvDLEYLLDRYPP 155
Cdd:TIGR01193 528 SGEILLNGFSLKdidrhtLRQFINYLPQEPYIFSGSILENLLLgakENVSQDEIWAACE--IAEIKD--DIENMPLGYQT 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 156 EKEVNwGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAMG-TSCITISHRPALVAFHDVVLSLD 234
Cdd:TIGR01193 604 ELSEE-GSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQdKTIIFVAHRLSVAKQSDKIIVLD 682
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
35-219 |
1.77e-13 |
|
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: 72.39 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 35 DVKVV--TPTGNV-LVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP---LISGHIV-KpgiGSDLN--------- 98
Cdd:COG0444 6 NLKVYfpTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILfD---GEDLLklsekelrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 99 ---KEIFYVPQRPYTA---VGTLRDQLIYPLTADQEV--EQLTDRgMVELLKNVDL---EYLLDRYPpekevnwgDELSL 167
Cdd:COG0444 83 irgREIQMIFQDPMTSlnpVMTVGDQIAEPLRIHGGLskAEARER-AIELLERVGLpdpERRLDRYP--------HELSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654042132 168 GEQQRLGMARLFYHKPKFAILDECTSA--VTT---------DMEERFcakvramGTSCITISH 219
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTAldVTIqaqilnllkDLQREL-------GLAILFITH 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
31-195 |
2.71e-13 |
|
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: 70.41 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGI------GSDLNKEIFYV 104
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdireqdPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 105 PQRpytaVG-----TLRDQLIYPLTADQEVEQLTDRGMVELLKNVDLE--YLLDRYPpekevnwgDELSLGEQQRLGMAR 177
Cdd:cd03295 81 IQQ----IGlfphmTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYP--------HELSGGQQQRVGVAR 148
|
170
....*....|....*...
gi 1654042132 178 LFYHKPKFAILDECTSAV 195
Cdd:cd03295 149 ALAADPPLLLMDEPFGAL 166
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
47-224 |
3.96e-13 |
|
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: 69.23 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGSDLNKE--IFYVPQ-RPYTAVGTLRDQLIYpl 123
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARnrIGYLPEeRGLYPKMKVIDQLVY-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 124 tadqeVEQLTDRGMVELLKNVDleYLLDRYP-PEKEVNWGDELSLGEQQRLGMARLFYHKPKFAILDECTSA---VTTDM 199
Cdd:cd03269 94 -----LAQLKGLKKEEARRRID--EWLERLElSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGldpVNVEL 166
|
170 180
....*....|....*....|....*
gi 1654042132 200 EERFCAKVRAMGTSCITISHRPALV 224
Cdd:cd03269 167 LKDVIRELARAGKTVILSTHQMELV 191
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
705-901 |
4.26e-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: 69.42 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 705 DIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSGCG--IFYVPQRPytclgtlRDQIIYPLSRE 782
Cdd:cd03225 23 TIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLVFQNP-------DDQFFGPTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 783 EAEFrALKMYGKGEKHADPRklldthLQIILENVRLNYLLERDnrgwdanlnwEDTLSLGEQQRLGMARLFFHRPKYGIL 862
Cdd:cd03225 96 EVAF-GLENLGLPEEEIEER------VEEALELVGLEGLRDRS----------PFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1654042132 863 DECTN----ATSVDVEEHLYGLaNKMGITVVTSSQRPALIPYH 901
Cdd:cd03225 159 DEPTAgldpAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLEL 200
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
43-209 |
4.74e-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: 68.92 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGSDLNKEIfyvPQRPYTAVGTlRDQLIYP 122
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE---PHENILYLGH-LPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 123 LTAD------QEVEQLTDRGMVELLKNVDLEYLLDRypPEKevnwgdELSLGEQQRLGMARLFYHKPKFAILDECTSAVT 196
Cdd:TIGR01189 88 LSALenlhfwAAIHGGAQRTIEDALAAVGLTGFEDL--PAA------QLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170
....*....|...
gi 1654042132 197 TDMEERFCAKVRA 209
Cdd:TIGR01189 160 KAGVALLAGLLRA 172
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
47-224 |
5.85e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.89 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVkpGIGSDL-----------NKEIFYVPQRPYTAVG-- 113
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVA--WLGKDLlgmkddewravRSDIQMIFQDPLASLNpr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 114 -TLRD------QLIYPLTADQEVEQLTDRGM--VELLKNvdleyLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPK 184
Cdd:PRK15079 115 mTIGEiiaeplRTYHPKLSRQEVKDRVKAMMlkVGLLPN-----LINRYP--------HEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1654042132 185 FAILDECTSAVTTDMEerfcAKV--------RAMGTSCITISHRPALV 224
Cdd:PRK15079 182 LIICDEPVSALDVSIQ----AQVvnllqqlqREMGLSLIFIAHDLAVV 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
47-224 |
7.67e-13 |
|
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: 69.00 E-value: 7.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV---------KP------GIGsdlnkEIFYVPqRPY-- 109
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgeditglPPheiarlGIG-----RTFQIP-RLFpe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 110 --------TAVGTLRDQLIYPLTADQEVEQLTDRGMvELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYH 181
Cdd:cd03219 90 ltvlenvmVAAQARTGSGLLLARARREEREARERAE-ELLERVGLADLADRPA--------GELSYGQQRRLEIARALAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1654042132 182 KPKFAILDECTSAVTTDMEERFCA---KVRAMGTSCITISHRPALV 224
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAElirELRERGITVLLVEHDMDVV 206
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
31-202 |
8.29e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.97 E-value: 8.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDV-KVVTPTgnVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGI----GSDLNKEI---- 101
Cdd:PRK09493 2 IEFKNVsKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvndPKVDERLIrqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 102 ------FYV-PQrpYTAvgtLRDQLIYPL----TADQEVEQLTDrgmvELLKNVDLEYLLDRYPpekevnwgDELSLGEQ 170
Cdd:PRK09493 80 gmvfqqFYLfPH--LTA---LENVMFGPLrvrgASKEEAEKQAR----ELLAKVGLAERAHHYP--------SELSGGQQ 142
|
170 180 190
....*....|....*....|....*....|..
gi 1654042132 171 QRLGMARLFYHKPKFAILDECTSAVttDMEER 202
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSAL--DPELR 172
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
43-190 |
8.37e-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: 68.44 E-value: 8.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVkpgIGS-DLNK------EIFYVPQR----PYTA 111
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY---IGGrDVTDlppkdrDIAMVFQNyalyPHMT 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654042132 112 VgtlRDQLIYPLTADQEVEQLTDRGMVELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:cd03301 89 V---YDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKP--------KQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
31-195 |
9.52e-13 |
|
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: 68.75 E-value: 9.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIgsDLNKEIFYVPQRPYT 110
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT--DINKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 111 AVGTLRDQ--LIYPLTADQEV------EQLTDRGMVELLKNVDLE---YLLDRYP-PEKEVNWGDELSLGEQQRLGMARL 178
Cdd:cd03256 79 QIGMIFQQfnLIERLSVLENVlsgrlgRRSTWRSLFGLFPKEEKQralAALERVGlLDKAYQRADQLSGGQQQRVAIARA 158
|
170
....*....|....*..
gi 1654042132 179 FYHKPKFAILDECTSAV 195
Cdd:cd03256 159 LMQQPKLILADEPVASL 175
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
31-227 |
1.16e-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: 68.20 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG-SDL-NKEIFYVPQRP 108
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvSDLrGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 109 YTAVGTLR--------DQLIYPLTADQEVEQLTDRGMVELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFY 180
Cdd:cd03292 81 GVVFQDFRllpdrnvyENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALP--------AELSGGEQQRVAIARAIV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1654042132 181 HKPKFAILDECTSAVTTDMEERFC---AKVRAMGTSCITISHRPALVAFH 227
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMnllKKINKAGTTVVVATHAKELVDTT 202
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-220 |
1.33e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.41 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 27 EANYIEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLiSGHIVKPGIG-SDLN-----KE 100
Cdd:PRK11174 346 DPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIElRELDpeswrKH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 101 IFYVPQRPYTAVGTLRDQLIY--PLTADQEVEQLTDRGMV-ELLKnvDLEYLLDRypPEKEVNWGdeLSLGEQQRLGMAR 177
Cdd:PRK11174 425 LSWVGQNPQLPHGTLRDNVLLgnPDASDEQLQQALENAWVsEFLP--LLPQGLDT--PIGDQAAG--LSVGQAQRLALAR 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1654042132 178 LFYHKPKFAILDECTSAVTTDMEERFC-AKVRAM-GTSCITISHR 220
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLDAHSEQLVMqALNAASrRQTTLMVTHQ 543
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
43-219 |
1.38e-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: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG-SDLNKE---IFYVPQR----PYTAVGT 114
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDiTNLPPEkrdISYVPQNyalfPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 115 -----LRDQLIYPLTADQEVEQLTdrgmvELLKnvdLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILD 189
Cdd:cd03299 91 niaygLKKRKVDKKEIERKVLEIA-----EMLG---IDHLLNRKP--------ETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190
....*....|....*....|....*....|....
gi 1654042132 190 ECTSAVTTDMEERFCAKV----RAMGTSCITISH 219
Cdd:cd03299 155 EPFSALDVRTKEKLREELkkirKEFGVTVLHVTH 188
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
38-219 |
2.26e-12 |
|
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: 68.44 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 38 VVTPTGNVL-VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVkpgI-GSDLN------------KEIFY 103
Cdd:cd03294 30 ILKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVL---IdGQDIAamsrkelrelrrKKISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 104 V-------PQRpytavgTLRDQLIYPLTADQEVEQLTDRGMVELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMA 176
Cdd:cd03294 107 VfqsfallPHR------TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYP--------DELSGGMQQRVGLA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1654042132 177 RLFYHKPKFAILDECTSA----VTTDMEERFCAKVRAMGTSCITISH 219
Cdd:cd03294 173 RALAVDPDILLMDEAFSAldplIRREMQDELLRLQAELQKTIVFITH 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
47-190 |
2.84e-12 |
|
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: 66.86 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGSDLNKEifyvpqrPYTAVGTLRD-QLIYP-LT 124
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-------ALRRIGALIEaPGFYPnLT 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654042132 125 AdqeVEQLTDRGMVELLKNVDLEYLLDryppekEVNWGDE-------LSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:cd03268 89 A---RENLRLLARLLGIRKKRIDEVLD------VVGLKDSakkkvkgFSLGMKQRLGIALALLGNPDLLILDE 152
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
48-221 |
3.70e-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: 66.55 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 48 DDLTLRVE---PGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPG-IGSDLNKEIFYVPQRpyTAVGTLRDQL-IYP 122
Cdd:cd03297 11 PDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtVLFDSRKKINLPPQQ--RKIGLVFQQYaLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 123 -LTADQEVE-------QLTDRGMV-ELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTS 193
Cdd:cd03297 89 hLNVRENLAfglkrkrNREDRISVdELLDLLGLDHLLNRYP--------AQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190
....*....|....*....|....*....|..
gi 1654042132 194 AVTTDMEERFCAKVRAMGTS----CITISHRP 221
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNlnipVIFVTHDL 192
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
43-194 |
6.47e-12 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 66.01 E-value: 6.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGSDLNKeifyvpqrpyTAVGTLRDQL--- 119
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK----------KNINELRQKVgmv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 120 -----IYP-LTADQEV------------EQLTDRGMvELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYH 181
Cdd:cd03262 82 fqqfnLFPhLTVLENItlapikvkgmskAEAEERAL-ELLEKVGLADKADAYP--------AQLSGGQQQRVAIARALAM 152
|
170
....*....|...
gi 1654042132 182 KPKFAILDECTSA 194
Cdd:cd03262 153 NPKVMLFDEPTSA 165
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
47-255 |
7.13e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.96 E-value: 7.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGS------DLNKEIFYVPQRPYTA-VG-TLRDQ 118
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLseetvwDVRRQVGMVFQNPDNQfVGaTVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 119 LIYPLtADQEVEQLTdrgMVE----LLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSA 194
Cdd:PRK13635 103 VAFGL-ENIGVPREE---MVErvdqALRQVGMEDFLNREP--------HRLSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 195 VTTDMEERFCAKVRAM----GTSCITISHRPALVAFHDVVLSLDG-----EGGWSVHYKREGSSTEMGID 255
Cdd:PRK13635 171 LDPRGRREVLETVRQLkeqkGITVLSITHDLDEAAQADRVIVMNKgeileEGTPEEIFKSGHMLQEIGLD 240
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
43-194 |
7.95e-12 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 66.29 E-value: 7.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV---------KPGigsDLNKEIFYVPQR-----P 108
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngrplaawSPW---ELARRRAVLPQHsslafP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 109 YTA---VGTLRdqliYP-LTADQEVEQLTDRGMVEllknVDLEYLLDR-YPpekevnwgdELSLGEQQRLGMARLF---- 179
Cdd:COG4559 90 FTVeevVALGR----APhGSSAAQDRQIVREALAL----VGLAHLAGRsYQ---------TLSGGEQQRVQLARVLaqlw 152
|
170
....*....|....*...
gi 1654042132 180 ---YHKPKFAILDECTSA 194
Cdd:COG4559 153 epvDGGPRWLFLDEPTSA 170
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
31-198 |
8.59e-12 |
|
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: 66.07 E-value: 8.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDV-KVVTPTGN--VLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGL-WP-----LISGHIVKPGIGSDL---N 98
Cdd:cd03258 2 IELKNVsKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPtsgsvLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 99 KEIFYVPQ-------RpytavgTLRDQLIYPL----TADQEVEQLTDrgmvELLKNVDLEYLLDRYPpekevnwgDELSL 167
Cdd:cd03258 82 RRIGMIFQhfnllssR------TVFENVALPLeiagVPKAEIEERVL----ELLELVGLEDKADAYP--------AQLSG 143
|
170 180 190
....*....|....*....|....*....|....
gi 1654042132 168 GEQQRLGMARLFYHKPKFAILDECTSAV---TTD 198
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALdpeTTQ 177
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
47-208 |
9.56e-12 |
|
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: 65.82 E-value: 9.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGI-GSDLN---KEIFYVPQRpYTAVG--TLRDQLI 120
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdATDVPvqeRNVGFVFQH-YALFRhmTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 121 YPL----TADQEVEQLTDRGMVELLKNVDLEYLLDRYPPEkevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSAVT 196
Cdd:cd03296 97 FGLrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQ--------LSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170
....*....|..
gi 1654042132 197 tdmeerfcAKVR 208
Cdd:cd03296 169 --------AKVR 172
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
43-190 |
9.66e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.55 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVkpgIGSDLnkEIFYVPQRpytavgtlRDQLIYP 122
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK---LGETV--KIGYFDQH--------QEELDPD 393
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654042132 123 LTADQEVEQLTDRGMVELLKNVdLEYLLdrYPPE---KEVNwgdELSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:COG0488 394 KTVLDELRDGAPGGTEQEVRGY-LGRFL--FSGDdafKPVG---VLSGGEKARLALAKLLLSPPNVLLLDE 458
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
47-194 |
1.36e-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: 67.05 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVkpgIGsdlNKEIFYVP--QRPytaVG----------- 113
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL---LD---GRDVTGLPpeKRN---VGmvfqdyalfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 114 -TLRDQLIYPLTAD----QEVEQLTDrgmvELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:COG3842 92 lTVAENVAFGLRMRgvpkAEIRARVA----ELLELVGLEGLADRYP--------HQLSGGQQQRVALARALAPEPRVLLL 159
|
....*.
gi 1654042132 189 DECTSA 194
Cdd:COG3842 160 DEPLSA 165
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
43-220 |
1.41e-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: 63.60 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLV-DDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGigsdlnkeifyvpqrpytavgtlrdqliy 121
Cdd:cd03216 11 GGVKAlDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG----------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 122 pltadQEVEQLTDR-------GMVellknvdleylldrYppekevnwgdELSLGEQQRLGMARLFYHKPKFAILDECTSA 194
Cdd:cd03216 62 -----KEVSFASPRdarragiAMV--------------Y----------QLSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180
....*....|....*....|....*....
gi 1654042132 195 VTTDMEERFCA---KVRAMGTSCITISHR 220
Cdd:cd03216 113 LTPAEVERLFKvirRLRAQGVAVIFISHR 141
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
683-898 |
1.41e-11 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 63.77 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 683 ISFSKVDIVTP-AQKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSGCG--IFY 759
Cdd:cd03246 1 LEVENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 760 VPQRPYTCLGTLRDQIiyplsreeaefralkmygkgekhadprklldthlqiilenvrlnyllerdnrgwdanlnwedtL 839
Cdd:cd03246 81 LPQDDELFSGSIAENI---------------------------------------------------------------L 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654042132 840 SLGEQQRLGMARLFFHRPKYGILDECTNATSVDVEEHLYGL---ANKMGITVVTSSQRPALI 898
Cdd:cd03246 98 SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPETL 159
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
43-194 |
1.70e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.74 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG-SDLNKEIF-----YVPQRPYTAVGTLR 116
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDiSTLKPEIYrqqvsYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654042132 117 DQLIYPLTADQEVEQltdrgMVELLKnvDLEYL-LDRYPPEKEVNwgdELSLGEQQRLGMARLFYHKPKFAILDECTSA 194
Cdd:PRK10247 99 DNLIFPWQIRNQQPD-----PAIFLD--DLERFaLPDTILTKNIA---ELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
700-874 |
1.70e-11 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 64.94 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 700 RELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGL---SRPSEDVDqEAGSGCGIFYVPQRPYTCLGTLRDQII 776
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidGIDIRDIS-RKSLRSMIGVVLQDTFLFSGTIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 777 Y--PLSREEAEFRALKMygkgekhadprklldthlqiilenVRLNYLLERDNRGWDANLNWE-DTLSLGEQQRLGMARLF 853
Cdd:cd03254 99 LgrPNATDEEVIEAAKE------------------------AGAHDFIMKLPNGYDTVLGENgGNLSQGERQLLAIARAM 154
|
170 180
....*....|....*....|.
gi 1654042132 854 FHRPKYGILDECTnaTSVDVE 874
Cdd:cd03254 155 LRDPKILILDEAT--SNIDTE 173
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
39-190 |
1.94e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 65.09 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 39 VTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGlwplISGHIVKPG-I---GSDL---------NKEIFYVP 105
Cdd:COG0396 8 VSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG----HPKYEVTSGsIlldGEDIlelspderaRAGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 106 QRP------------YTAVGTLRDQLIYPLTADQEVEqltdrgmvELLKNVDL-EYLLDRYppekeVNWGdeLSLGEQQR 172
Cdd:COG0396 84 QYPveipgvsvsnflRTALNARRGEELSAREFLKLLK--------EKMKELGLdEDFLDRY-----VNEG--FSGGEKKR 148
|
170 180
....*....|....*....|.
gi 1654042132 173 ---LGMARLfyhKPKFAILDE 190
Cdd:COG0396 149 neiLQMLLL---EPKLAILDE 166
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
47-219 |
2.15e-11 |
|
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: 65.06 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI---------------VKPGIG---------SDL----N 98
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlfdgrditglpphriARLGIArtfqnprlfPELtvleN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 99 keiFYVPQRPYTAVGTLRDQLIYPLTADQEvEQLTDRGMvELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARL 178
Cdd:COG0411 100 ---VLVAAHARLGRGLLAALLRLPRARREE-REARERAE-ELLERVGLADRADEPA--------GNLSYGQQRRLEIARA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1654042132 179 FYHKPKFAILDECTSAVTTDMEERFCAKVRA----MGTSCITISH 219
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPEETEELAELIRRlrdeRGITILLIEH 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
699-907 |
2.62e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 63.67 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 699 ARELTCD-------------IELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSgcgifyvPQRPY 765
Cdd:cd03231 3 ADELTCErdgralfsglsftLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-------IARGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 766 TCLGtlrdqiiyplsreeaefralkmygkgekHADPRKLLDThlqiILENVRLNYLLERDNRGWDA----NLN-WED--- 837
Cdd:cd03231 76 LYLG----------------------------HAPGIKTTLS----VLENLRFWHADHSDEQVEEAlarvGLNgFEDrpv 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654042132 838 -TLSLGEQQRLGMARLFFHRPKYGILDECTNA---TSVD-VEEHLYGLANKMGITVVTSSQRPALIPYHSMELRL 907
Cdd:cd03231 124 aQLSAGQQRRVALARLLLSGRPLWILDEPTTAldkAGVArFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
45-220 |
3.73e-11 |
|
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: 63.93 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 45 VLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIgsDLNKEIFYVPQRpytaVGTLRDQL-IYP- 122
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF--DVVKEPAEARRR----LGFVSDSTgLYDr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 123 LTADQEVE-----------QLTDRgMVELLKNVDLEYLLDRYppekevnwGDELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:cd03266 93 LTARENLEyfaglyglkgdELTAR-LEELADRLGMEELLDRR--------VGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190
....*....|....*....|....*....|..
gi 1654042132 192 TSA---VTTDMEERFCAKVRAMGTSCITISHR 220
Cdd:cd03266 164 TTGldvMATRALREFIRQLRALGKCILFSTHI 195
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
31-234 |
5.57e-11 |
|
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: 66.28 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTP-TGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG------SDLNKEIFY 103
Cdd:TIGR02203 331 VEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDladytlASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 104 VPQRPYTAVGTLRDQLIYPLTADQEVEQLTDrgmveLLKNVDLEYLLDRYPPEKEVNWGDE---LSLGEQQRLGMARLFY 180
Cdd:TIGR02203 411 VSQDVVLFNDTIANNIAYGRTEQADRAEIER-----ALAAAYAQDFVDKLPLGLDTPIGENgvlLSGGQRQRLAIARALL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1654042132 181 HKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLD 234
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLmqGRTTLVIAHRLSTIEKADRIVVMD 541
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
683-905 |
7.31e-11 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 63.12 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 683 ISFSKVDIVTPAQKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASG-----GLSRPSEDVD---QEAGsg 754
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGevlvdGKDITKKNLRelrRKVG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 755 cgifYVPQRPytclgtlRDQIIYPLSREEAEFrALKMYGKGEKHADPRklldthLQIILENVRLNYLLERDnrgwdanln 834
Cdd:COG1122 79 ----LVFQNP-------DDQLFAPTVEEDVAF-GPENLGLPREEIRER------VEEALELVGLEHLADRP--------- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654042132 835 wEDTLSLGEQQRLGMARLFFHRPKYGILDECTN----ATSVDVEEHLYGLaNKMGITVVTSSqrpalipyHSMEL 905
Cdd:COG1122 132 -PHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAgldpRGRRELLELLKRL-NKEGKTVIIVT--------HDLDL 196
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
608-898 |
8.75e-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: 65.63 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 608 TQGELAhALRFLASVVSQSFLAFGDILElhrKFVELSGGINRIFEL------EELLDAAQSVDSINGSITpsMRDyyakd 681
Cdd:COG2274 410 TLGQLI-AFNILSGRFLAPVAQLIGLLQ---RFQDAKIALERLDDIldlppeREEGRSKLSLPRLKGDIE--LEN----- 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 682 aISFSkvdiVTPAQKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLS---RPSEDVDQEA-GSGCGi 757
Cdd:COG2274 479 -VSFR----YPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgIDLRQIDPASlRRQIG- 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 758 fYVPQRPYTCLGTLRDQIIypLSREEAEF----RALKMYGkgeKHADPRKL---LDThlqIILENVRlnyllerdnrgwd 830
Cdd:COG2274 553 -VVLQDVFLFSGTIRENIT--LGDPDATDeeiiEAARLAG---LHDFIEALpmgYDT---VVGEGGS------------- 610
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654042132 831 anlnwedTLSLGEQQRLGMARLFFHRPKYGILDECTNATSVDVEEHLygLAN----KMGITVVTSSQRPALI 898
Cdd:COG2274 611 -------NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAII--LENlrrlLKGRTVIIIAHRLSTI 673
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
700-909 |
8.77e-11 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 62.95 E-value: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 700 RELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASG-------GLSRPSEDVDQEagsgcgIFYVPQRPYTCLG-TL 771
Cdd:COG4555 18 KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGsilidgeDVRKEPREARRQ------IGVLPDERGLYDRlTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 772 RDQI-----IYPLSREEAEFRAlkmygkgekhadprklldthlQIILENVRLNYLLERdnrgwdanlNWEdTLSLGEQQR 846
Cdd:COG4555 92 RENIryfaeLYGLFDEELKKRI---------------------EELIELLGLEEFLDR---------RVG-ELSTGMKKK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654042132 847 LGMARLFFHRPKYGILDECTNAtsVDVE------EHLYGLANKmGITVVTSSqrpalipyHSMEL--RLID 909
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNG--LDVMarrllrEILRALKKE-GKTVLFSS--------HIMQEveALCD 200
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
680-898 |
9.34e-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: 65.31 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 680 KDAISFSKVDIVTPAQKMLA-RELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIA---SGGLSRPSEDVDQ--EAGS 753
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAvDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLElsEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 754 GCGIFYVPQRPYTCL--GTLRDQIIYPL-----SREEAEFRALKMygkgekhadprklldthlqiiLENVRLNYLLERDn 826
Cdd:COG1123 82 GRRIGMVFQDPMTQLnpVTVGDQIAEALenlglSRAEARARVLEL---------------------LEAVGLERRLDRY- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654042132 827 rgwdanlnwEDTLSLGEQQRLGMARLFFHRPKYGILDECTNA----TSVDVEEHLYGLANKMGITVVTSSQRPALI 898
Cdd:COG1123 140 ---------PHQLSGGQRQRVAIAMALALDPDLLIADEPTTAldvtTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
681-898 |
1.09e-10 |
|
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: 62.22 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 681 DAISFSKVDIVTPAQKMLA-RELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQ----EAGSGC 755
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAlDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQldpaDLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 756 GifYVPQRPYTCLGTLRDQII--YPLSREEAEFRALKMYGkgekhadprklldthlqiilenvrLNYLLERDNRGWDANL 833
Cdd:cd03245 81 G--YVPQDVTLFYGTLRDNITlgAPLADDERILRAAELAG------------------------VTDFVNKHPNGLDLQI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654042132 834 NwE--DTLSLGEQQRLGMARLFFHRPKYGILDECTNATSVDVEEHLYGLANKM--GITVVTSSQRPALI 898
Cdd:cd03245 135 G-ErgRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLL 202
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
43-219 |
1.12e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.47 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIgsDLNkeifYVP--QRPYTAVgtLRDQLI 120
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV--DLS----HVPpyQRPINMM--FQSYAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 121 YP-LTADQEV-----------EQLTDRgMVELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:PRK11607 103 FPhMTVEQNIafglkqdklpkAEIASR-VNEMLGLVHMQEFAKRKP--------HQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190
....*....|....*....|....*....|....*
gi 1654042132 189 DECTSAVTTDMEERFCAKV----RAMGTSCITISH 219
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVvdilERVGVTCVMVTH 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
43-194 |
1.42e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 62.87 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIvkpgigsDLNkeifyvpQRPYT-----------A 111
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV-------RLN-------GRPLAdwspaelarrrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 112 VgtLRDQ--LIYPLTA--------------DQEVEQLTDRGMVEllknVDLEYLLDR-YPpekevnwgdELSLGEQQRLG 174
Cdd:PRK13548 80 V--LPQHssLSFPFTVeevvamgraphglsRAEDDALVAAALAQ----VDLAHLAGRdYP---------QLSGGEQQRVQ 144
|
170 180
....*....|....*....|....*.
gi 1654042132 175 MARLF------YHKPKFAILDECTSA 194
Cdd:PRK13548 145 LARVLaqlwepDGPPRWLLLDEPTSA 170
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
697-907 |
1.50e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 61.61 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 697 MLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSgcgifyvPQRPYTCLGTlRDQII 776
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-------PHENILYLGH-LPGLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 777 YPLS-REEAEFRAlkmygkgEKHADPRKLLDThlqiILENVRLNYLLERDNRgwdanlnwedTLSLGEQQRLGMARLFFH 855
Cdd:TIGR01189 86 PELSaLENLHFWA-------AIHGGAQRTIED----ALAAVGLTGFEDLPAA----------QLSAGQQRRLALARLWLS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1654042132 856 RPKYGILDECTnaTSVDVE------EHLYGLANKMGITVVTSSQrpALIPYHSMELRL 907
Cdd:TIGR01189 145 RRPLWILDEPT--TALDKAgvallaGLLRAHLARGGIVLLTTHQ--DLGLVEARELRL 198
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
700-898 |
1.99e-10 |
|
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: 60.47 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 700 RELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLS---RPSEDVDQEAGSGCgIFYVPQRPYtcL--GTLRDQ 774
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgVDLRDLDLESLRKN-IAYVPQDPF--LfsGTIREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 775 IiyplsreeaefralkmygkgekhadprklldthlqiilenvrlnyllerdnrgwdanlnwedtLSLGEQQRLGMARLFF 854
Cdd:cd03228 96 I---------------------------------------------------------------LSGGQRQRIAIARALL 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1654042132 855 HRPKYGILDECT----NATSVDVEEHLYGLANkmGITVVTSSQRPALI 898
Cdd:cd03228 113 RDPPILILDEATsaldPETEALILEALRALAK--GKTVIVIAHRLSTI 158
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-234 |
3.14e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.58 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 1 MAVSR--ELSMVDEKSSLQRKGSR--NCISEANYIEFYDVKV-VTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSS--- 72
Cdd:TIGR00957 1251 VAVERlkEYSETEKEAPWQIQETAppSGWPPRGRVEFRNYCLrYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltl 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 73 -LFRVLGGlwplISGHIVKPGIG------SDLNKEIFYVPQRPYTAVGTLRDQLiYPLTADQEVEQLTDRGMVELLKNVD 145
Cdd:TIGR00957 1331 gLFRINES----AEGEIIIDGLNiakiglHDLRFKITIIPQDPVLFSGSLRMNL-DPFSQYSDEEVWWALELAHLKTFVS 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 146 -LEYLLDRYPPEKevnwGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAMGTSC--ITISHRPA 222
Cdd:TIGR00957 1406 aLPDKLDHECAEG----GENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCtvLTIAHRLN 1481
|
250
....*....|..
gi 1654042132 223 LVAFHDVVLSLD 234
Cdd:TIGR00957 1482 TIMDYTRVIVLD 1493
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
43-190 |
3.23e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.59 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPgiGSDLNKeifyvpQRPytavgTLRDQLIY- 121
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ--GEPIRR------QRD-----EYHQDLLYl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 122 --------PLTAD------QEVEQLTDR-GMVELLKNVDL---EYLLDRYppekevnwgdeLSLGEQQRLGMARLFYHKP 183
Cdd:PRK13538 80 ghqpgiktELTALenlrfyQRLHGPGDDeALWEALAQVGLagfEDVPVRQ-----------LSAGQQRRVALARLWLTRA 148
|
....*..
gi 1654042132 184 KFAILDE 190
Cdd:PRK13538 149 PLWILDE 155
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
43-194 |
4.05e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 62.66 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGigsdlnKEIFYVP--QRPYTAV-------- 112
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG------QDITHVPaeNRHVNTVfqsyalfp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 113 -GTLRDQLIYPL----TADQEVEQltdRGMvELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAI 187
Cdd:PRK09452 100 hMTVFENVAFGLrmqkTPAAEITP---RVM-EALRMVQLEEFAQRKP--------HQLSGGQQQRVAIARAVVNKPKVLL 167
|
....*..
gi 1654042132 188 LDECTSA 194
Cdd:PRK09452 168 LDESLSA 174
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
716-904 |
4.51e-10 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 60.85 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 716 GPNGSGKSSIFRVLrglwpiasGGLSRPS--------EDVDQEAGSGCG-IFYVPQRPYtclgtlrdqiIYP-LS-REEA 784
Cdd:COG1131 33 GPNGAGKTTTIRML--------LGLLRPTsgevrvlgEDVARDPAEVRRrIGYVPQEPA----------LYPdLTvRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 785 EFRAlKMYGKGEKHADPRklldthLQIILENVRLNYLLERDNRgwdanlnwedTLSLGEQQRLGMARLFFHRPKYGILDE 864
Cdd:COG1131 95 RFFA-RLYGLPRKEARER------IDELLELFGLTDAADRKVG----------TLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1654042132 865 CTNAtsVDVE------EHLYGLANKmGITVVTSSqrpalipyHSME 904
Cdd:COG1131 158 PTSG--LDPEarrelwELLRELAAE-GKTVLLST--------HYLE 192
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
43-190 |
5.52e-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: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGigsdlNKEIFYVPQRPYTAVG-TLRDQLiy 121
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----GLRIGYLPQEPPLDDDlTVLDTV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 122 pLTADQEVEQLTDRgMVELL-KNVDLEYLLDRY-------------------------------PPEKEVNwgdELSLGE 169
Cdd:COG0488 83 -LDGDAELRALEAE-LEELEaKLAEPDEDLERLaelqeefealggweaearaeeilsglgfpeeDLDRPVS---ELSGGW 157
|
170 180
....*....|....*....|.
gi 1654042132 170 QQRLGMARLFYHKPKFAILDE 190
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDE 178
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
47-190 |
5.56e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 61.66 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSnllIT---GPNGSGKSSLFRVLGGLWPLISGHI-VKpgiGSDLNKE----IFYVPQ-RpytavG---- 113
Cdd:COG4152 17 VDDVSFTVPKGE---IFgllGPNGAGKTTTIRIILGILAPDSGEVlWD---GEPLDPEdrrrIGYLPEeR-----Glypk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 114 -TLRDQLIYpltadqeVEQLtdRGM--VELLKNVDleYLLDRYppEKEVNWGD---ELSLGEQQRLGMARLFYHKPKFAI 187
Cdd:COG4152 86 mKVGEQLVY-------LARL--KGLskAEAKRRAD--EWLERL--GLGDRANKkveELSKGNQQKVQLIAALLHDPELLI 152
|
...
gi 1654042132 188 LDE 190
Cdd:COG4152 153 LDE 155
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
700-907 |
5.69e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 59.55 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 700 RELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRpsedvdqeaGSGCGIFYVPQR---PYTCLGTLRDQII 776
Cdd:NF040873 9 HGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR---------AGGARVAYVPQRsevPDSLPLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 777 YPLSREEAEFRALKmygkgekhADPRKLLDThlqiILENVRLNYLLERDnrgwdanlnwEDTLSLGEQQRLGMARLFFHR 856
Cdd:NF040873 80 MGRWARRGLWRRLT--------RDDRAAVDD----ALERVGLADLAGRQ----------LGELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1654042132 857 PKYGILDECTNATSVDVEEHLYGL---ANKMGITVVTSSQRPALIPYHSMELRL 907
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALlaeEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
705-889 |
6.17e-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: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 705 DIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSGCGIF-----YVPQRPYTCL---GTLRDQII 776
Cdd:COG1123 287 TLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELrrrvqMVFQDPYSSLnprMTVGDIIA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 777 YPLsreeaefRALKMYGKGEKHADPRKLLDThlqiilenVRLNY-LLERDNRgwdanlnwedTLSLGEQQRLGMARLFFH 855
Cdd:COG1123 367 EPL-------RLHGLLSRAERRERVAELLER--------VGLPPdLADRYPH----------ELSGGQRQRVAIARALAL 421
|
170 180 190
....*....|....*....|....*....|....*...
gi 1654042132 856 RPKYGILDECTNA--TSV--DVEEHLYGLANKMGITVV 889
Cdd:COG1123 422 EPKLLILDEPTSAldVSVqaQILNLLRDLQRELGLTYL 459
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
49-195 |
6.32e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 49 DLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGigsdlNKEIFYVPQRPYTAVgTLrdqliyPLTADQE 128
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----KLRIGYVPQKLYLDT-TL------PLTVNRF 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 129 VE---QLTDRGMVELLKNVDLEYLLDrYPPEKevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSAV 195
Cdd:PRK09544 90 LRlrpGTKKEDILPALKRVQAGHLID-APMQK-------LSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-234 |
6.36e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKV-VTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV-------KPGIgSDLNKEIF 102
Cdd:PLN03232 1235 IKFEDVHLrYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMiddcdvaKFGL-TDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 103 YVPQRPYTAVGTLRDQlIYPLTadqeveQLTDRGMVELLKNVDLEYLLDRYP--PEKEVNWGDE-LSLGEQQRLGMARLF 179
Cdd:PLN03232 1314 IIPQSPVLFSGTVRFN-IDPFS------EHNDADLWEALERAHIKDVIDRNPfgLDAEVSEGGEnFSVGQRQLLSLARAL 1386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1654042132 180 YHKPKFAILDECTSAVTTDMEERFCAKVRAMGTSC--ITISHRPALVAFHDVVLSLD 234
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCtmLVIAHRLNTIIDCDKILVLS 1443
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
47-190 |
1.00e-09 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 59.76 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISG---------------HIVKPGIGsdlnkeifYVPQ-RPYT 110
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsirfdgrditglpphERARAGIG--------YVPEgRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 111 AVGTLRDQL---IYPLTADQEVEqltdrgmvellknvDLEYLLDRYP--PEKEVNWGDELSLGEQQRLGMARLFYHKPKF 185
Cdd:cd03224 88 PELTVEENLllgAYARRRAKRKA--------------RLERVYELFPrlKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
....*
gi 1654042132 186 AILDE 190
Cdd:cd03224 154 LLLDE 158
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
700-904 |
1.15e-09 |
|
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: 59.50 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 700 RELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGglSRPSEDVDQEAGSGCGIFYVP-----------QRPYTCL 768
Cdd:cd03260 17 KDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPG--APDEGEVLLDGKDIYDLDVDVlelrrrvgmvfQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 769 GTLRDQIIYPLsreeaefRALKMYGKGEKHADPRKLLdthlqiilenvRLNYLLERDNRGWDAnlnweDTLSLGEQQRLG 848
Cdd:cd03260 95 GSIYDNVAYGL-------RLHGIKLKEELDERVEEAL-----------RKAALWDEVKDRLHA-----LGLSGGQQQRLC 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 849 MARLFFHRPKYGILDECTNA----TSVDVEEHLYGLANKMGITVVTssqrpalipyHSME 904
Cdd:cd03260 152 LARALANEPEVLLLDEPTSAldpiSTAKIEELIAELKKEYTIVIVT----------HNMQ 201
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
43-190 |
1.39e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.52 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV---------------KPGIGsdlnkeifYVPQR 107
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplharaRRGIG--------YLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 108 P-----------YTAVGTLRDqliypltaDQEVEQLTDRGmVELLKNVDLEYLLDryppekevNWGDELSLGEQQRLGMA 176
Cdd:PRK10895 87 AsifrrlsvydnLMAVLQIRD--------DLSAEQREDRA-NELMEEFHIEHLRD--------SMGQSLSGGERRRVEIA 149
|
170
....*....|....
gi 1654042132 177 RLFYHKPKFAILDE 190
Cdd:PRK10895 150 RALAANPKFILLDE 163
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
43-192 |
2.26e-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: 56.69 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGigsdlNKEIFYVPQrpytavgtlrdqliyp 122
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----TVKIGYFEQ---------------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 123 ltadqeveqltdrgmvellknvdleylldryppekevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECT 192
Cdd:cd03221 71 ------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
46-225 |
2.37e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.29 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 46 LVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPG----IGSD--------LNKEIFYVPQRPYTAVG 113
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlyFGKDifqidaikLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 114 -TLRDQLIYPLTA-----DQEVEQLtdrgMVELLKNVDL-EYLLDRYPPEkevnwGDELSLGEQQRLGMARLFYHKPKFA 186
Cdd:PRK14246 105 lSIYDNIAYPLKShgikeKREIKKI----VEECLRKVGLwKEVYDRLNSP-----ASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1654042132 187 ILDECTSAV----TTDMEERFCAKVRAMgtSCITISHRPALVA 225
Cdd:PRK14246 176 LMDEPTSMIdivnSQAIEKLITELKNEI--AIVIVSHNPQQVA 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
44-190 |
2.42e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.12 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 44 NVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVkpgI-GSDL------NKEIFYVPQR----PYTAV 112
Cdd:PRK11432 19 NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF---IdGEDVthrsiqQRDICMVFQSyalfPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 113 GtlrDQLIYPL----TADQEVEQLTDrgmvELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:PRK11432 96 G---ENVGYGLkmlgVPKEERKQRVK----EALELVDLAGFEDRYV--------DQISGGQQQRVALARALILKPKVLLF 160
|
..
gi 1654042132 189 DE 190
Cdd:PRK11432 161 DE 162
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
682-866 |
2.44e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.99 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 682 AISFSKVDIVTPAQKMLA-RELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLS---RPSEDVDQEAGSGCgI 757
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVlKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlngQPIADYSEAALRQA-I 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 758 FYVPQRPYTCLGTLRDQiiyplsreeaefraLKMygkgekhADPrKLLDTHLQIILENVRLNYLLErDNRGWDAnlnW-- 835
Cdd:PRK11160 417 SVVSQRVHLFSATLRDN--------------LLL-------AAP-NASDEALIEVLQQVGLEKLLE-DDKGLNA---Wlg 470
|
170 180 190
....*....|....*....|....*....|...
gi 1654042132 836 --EDTLSLGEQQRLGMARLFFHRPKYGILDECT 866
Cdd:PRK11160 471 egGRQLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
43-219 |
2.66e-09 |
|
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: 57.58 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIgsDLNKEIFYVPQRPyTAVGTL-RDQLIY 121
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE--DLTDLEDELPPLR-RRIGMVfQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 122 P-LTAdqeveqltdrgmvelLKNVdleylldRYPpekevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSA---VTT 197
Cdd:cd03229 89 PhLTV---------------LENI-------ALG----------LSGGQQQRVALARALAMDPDVLLLDEPTSAldpITR 136
|
170 180
....*....|....*....|...
gi 1654042132 198 DMEERFCAKVRAM-GTSCITISH 219
Cdd:cd03229 137 REVRALLKSLQAQlGITVVLVTH 159
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
31-219 |
3.31e-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: 58.28 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVkVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP------LISGHIVKPGIGSDLN---KEI 101
Cdd:cd03261 1 IELRGL-TKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpdsgevLIDGEDISGLSEAELYrlrRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 102 FYVPQRP--YTAVgTLRDQLIYPL---TADQEvEQLTDRGMvELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMA 176
Cdd:cd03261 80 GMLFQSGalFDSL-TVFENVAFPLrehTRLSE-EEIREIVL-EKLEAVGLRGAEDLYP--------AELSGGMKKRVALA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1654042132 177 R--------LFYHKPkFAILDECTSAVTTDMEERFcakVRAMGTSCITISH 219
Cdd:cd03261 149 RalaldpelLLYDEP-TAGLDPIASGVIDDLIRSL---KKELGLTSIMVTH 195
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
716-892 |
3.42e-09 |
|
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: 57.61 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 716 GPNGSGKSSIFRVLRGLwpiasgglSRPSEDVDQEAGSGcgifyvPQRPYTCL---GTLRD-QIIYP-LSREEAEFRALK 790
Cdd:cd03268 33 GPNGAGKTTTMKIILGL--------IKPDSGEITFDGKS------YQKNIEALrriGALIEaPGFYPnLTARENLRLLAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 791 MYGKGEKHADprKLLDThlqIILENVrlnyllERDNRGwdanlnwedTLSLGEQQRLGMARLFFHRPKYGILDECTNATS 870
Cdd:cd03268 99 LLGIRKKRID--EVLDV---VGLKDS------AKKKVK---------GFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180
....*....|....*....|....*.
gi 1654042132 871 VD----VEEHLYGLANKmGITVVTSS 892
Cdd:cd03268 159 PDgikeLRELILSLRDQ-GITVLISS 183
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
700-892 |
3.86e-09 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 58.18 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 700 RELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSgcgIFYVPQRpytclGTL-RDqiiYP 778
Cdd:COG1121 23 EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR---IGYVPQR-----AEVdWD---FP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 779 LSREE-------AEFRALKMYGKGEKhadpRKLLDthlqiILENVRLNYLLERdnrgwdaNLNwedTLSLGEQQRLGMAR 851
Cdd:COG1121 92 ITVRDvvlmgryGRRGLFRRPSRADR----EAVDE-----ALERVGLEDLADR-------PIG---ELSGGQQQRVLLAR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1654042132 852 LFFHRPKYGILDECTnaTSVDV--EEHLYGL---ANKMGITVVTSS 892
Cdd:COG1121 153 ALAQDPDLLLLDEPF--AGVDAatEEALYELlreLRREGKTILVVT 196
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
45-234 |
3.96e-09 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 56.94 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 45 VLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPG-----IGSDLNKEIFYVPQRPYTAVGTLRDql 119
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdLEKALSSLISVLNQRPYLFDTTLRN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 120 iypltadqeveqltdrgmvellknvdleylldryppekevNWGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDM 199
Cdd:cd03247 94 ----------------------------------------NLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190
....*....|....*....|....*....|....*..
gi 1654042132 200 EERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLD 234
Cdd:cd03247 134 ERQLLSLIFEVlkDKTLIWITHHLTGIEHMDKILFLE 170
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
49-194 |
4.27e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.10 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 49 DLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI------------VKPGIGSDLNKEIFYVPQR----PYTav 112
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdfsktPSDKAIRELRRNVGMVFQQynlwPHL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 113 gTLRDQLIyplTADQEV-----EQLTDRGMvELLKNVDLEYLLDRYPPEkevnwgdeLSLGEQQRLGMARLFYHKPKFAI 187
Cdd:PRK11124 98 -TVQQNLI---EAPCRVlglskDQALARAE-KLLERLRLKPYADRFPLH--------LSGGQQQRVAIARALMMEPQVLL 164
|
....*..
gi 1654042132 188 LDECTSA 194
Cdd:PRK11124 165 FDEPTAA 171
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
696-907 |
5.90e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.12 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 696 KMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLrglwpiasGGLSRPsedvdqEAGSgcgIFYvpqrpytclgtlRDQi 775
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRIL--------AGLARP------DAGE---VLW------------QGE- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 776 iyPLSREEAEFRALKMY-GkgekHADPRKLLDThlqiILENVRLNYLLE---RDNRGWDA----NL-NWED----TLSLG 842
Cdd:PRK13538 64 --PIRRQRDEYHQDLLYlG----HQPGIKTELT----ALENLRFYQRLHgpgDDEALWEAlaqvGLaGFEDvpvrQLSAG 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654042132 843 EQQRLGMARLFFHRPKYGILDECTNA---TSVDV-EEHLYGLANKMGITVVTSSQRPALIPYHSMELRL 907
Cdd:PRK13538 134 QQRRVALARLWLTRAPLWILDEPFTAidkQGVARlEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRL 202
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
350-898 |
6.15e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 59.74 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 350 FLVVARTWVSdrIASLNGTTVKFV-------LEQDKA--SFIRLIGLSVLQSAASSFIAP----SIRHLRARLALGWRIR 416
Cdd:TIGR00958 162 WLISAFVFLT--LSSLGEMFIPFYtgrvidtLGGDKGppALASAIFFMCLLSIASSVSAGlrggSFNYTMARINLRIRED 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 417 LTQHLLKNYLRnnsfykvFHMASKNIDADQRITHDL----EKLTTDLSGLVTGMVKPSVDI---LWFTWRMKLLTgqrgv 489
Cdd:TIGR00958 240 LFRSLLRQDLG-------FFDENKTGELTSRLSSDTqtmsRSLSLNVNVLLRNLVMLLGLLgfmLWLSPRLTMVT----- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 490 ailyaymLLGLGFLRTVTPDFG---DLISQEQQ--LEGTFRFMHERLCThAESVAFFGGGTREKtmveSRFRELLSHSNY 564
Cdd:TIGR00958 308 -------LINLPLVFLAEKVFGkryQLLSEELQeaVAKANQVAEEALSG-MRTVRSFAAEEGEA----SRFKEALEETLQ 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 565 LLKKKWLFGILDdFITKQLPHNVTWLLSLLYA----MEHKGDRASIST----QGELAHALRFLASVvsqsflaFGDILEL 636
Cdd:TIGR00958 376 LNKRKALAYAGY-LWTTSVLGMLIQVLVLYYGgqlvLTGKVSSGNLVSfllyQEQLGEAVRVLSYV-------YSGMMQA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 637 hrkfvelSGGINRIFELeelLDAAQSVdSINGSITPSmrdyYAKDAISFSKVDIVTPAQ--KMLARELTCDIELGRSLLV 714
Cdd:TIGR00958 448 -------VGASEKVFEY---LDRKPNI-PLTGTLAPL----NLEGLIEFQDVSFSYPNRpdVPVLKGLTFTLHPGEVVAL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 715 TGPNGSGKSSIFRVLRGLWPIASGGL---SRPSEDVD-----QEAGSgcgifyVPQRPYTCLGTLRDQIIYPLSR-EEAE 785
Cdd:TIGR00958 513 VGPSGSGKSTVAALLQNLYQPTGGQVlldGVPLVQYDhhylhRQVAL------VGQEPVLFSGSVRENIAYGLTDtPDEE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 786 FRALKMygkgEKHADprklldthlqiilenvrlNYLLERDNrGWDANLNWEDT-LSLGEQQRLGMARLFFHRPKYGILDE 864
Cdd:TIGR00958 587 IMAAAK----AANAH------------------DFIMEFPN-GYDTEVGEKGSqLSGGQKQRIAIARALVRKPRVLILDE 643
|
570 580 590
....*....|....*....|....*....|....
gi 1654042132 865 CTNATSVDVEEHLYGLANKMGITVVTSSQRPALI 898
Cdd:TIGR00958 644 ATSALDAECEQLLQESRSRASRTVLLIAHRLSTV 677
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-192 |
6.55e-09 |
|
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: 59.56 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 37 KVVTPTGNVLvDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV-KPGIgsdlnkEIFYVPQRPY------ 109
Cdd:TIGR03719 12 KVVPPKKEIL-KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARpQPGI------KVGYLPQEPQldptkt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 110 ------TAVGTLRDQL-----IYPLTA--DQEVEQLTDRgMVELLKNVD----------LEYLLD--RYPP-EKEVNwgd 163
Cdd:TIGR03719 85 vrenveEGVAEIKDALdrfneISAKYAepDADFDKLAAE-QAELQEIIDaadawdldsqLEIAMDalRCPPwDADVT--- 160
|
170 180
....*....|....*....|....*....
gi 1654042132 164 ELSLGEQQRLGMARLFYHKPKFAILDECT 192
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
653-895 |
7.31e-09 |
|
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: 59.30 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 653 LEELLDAAQSVDSINGsitPSMRDYYAKDA-ISFSKVDIVTPAQKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRG 731
Cdd:TIGR02868 307 IVEVLDAAGPVAEGSA---PAAGAVGLGKPtLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 732 LWPIASGGLS---RPSEDVDQEAGSGCgIFYVPQRPYTCLGTLRDQIiyplsreeaefralkMYGKGEkhADPRKLLDth 808
Cdd:TIGR02868 384 LLDPLQGEVTldgVPVSSLDQDEVRRR-VSVCAQDAHLFDTTVRENL---------------RLARPD--ATDEELWA-- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 809 lqiILENVRLNYLLERDNRGWDANLNwED--TLSLGEQQRLGMARLFFHRPKYGILDECTNATSVDVEEHLYG--LANKM 884
Cdd:TIGR02868 444 ---ALERVGLADWLRALPDGLDTVLG-EGgaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEdlLAALS 519
|
250
....*....|.
gi 1654042132 885 GITVVTSSQRP 895
Cdd:TIGR02868 520 GRTVVLITHHL 530
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
47-190 |
9.13e-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: 56.91 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI---------------VKPGIGsdlnkeifYVPQrpyta 111
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIrfdgeditglpphriARLGIG--------YVPE----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 112 vG-------TLRDQLI---YPLTADQEVEQltdrgmvellknvDLEYLLDRYPP--EKEVNWGDELSLGEQQRLGMARLF 179
Cdd:COG0410 86 -GrrifpslTVEENLLlgaYARRDRAEVRA-------------DLERVYELFPRlkERRRQRAGTLSGGEQQMLAIGRAL 151
|
170
....*....|.
gi 1654042132 180 YHKPKFAILDE 190
Cdd:COG0410 152 MSRPKLLLLDE 162
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
43-192 |
9.58e-09 |
|
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: 56.61 E-value: 9.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP------LISGH-IVKPGIgsDLNKEIFYVPQRPytavgTL 115
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKptsgraTVAGHdVVREPR--EVRRRIGIVFQDL-----SV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 116 RDQliypLTADQEVE----------QLTDRGMVELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKF 185
Cdd:cd03265 85 DDE----LTGWENLYiharlygvpgAERRERIDELLDFVGLLEAADRLV--------KTYSGGMRRRLEIARSLVHRPEV 152
|
....*..
gi 1654042132 186 AILDECT 192
Cdd:cd03265 153 LFLDEPT 159
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
705-902 |
1.11e-08 |
|
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: 54.94 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 705 DIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSGC--GIFYVPQrpytclgtlrdqiiyplsre 782
Cdd:cd00267 21 TLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELrrRIGYVPQ-------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 783 eaefralkmygkgekhadprklldthlqiilenvrlnyllerdnrgwdanlnwedtLSLGEQQRLGMARLFFHRPKYGIL 862
Cdd:cd00267 81 --------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1654042132 863 DECTNATSVD----VEEHLYGLANKmGITVVTSSQRPALIPYHS 902
Cdd:cd00267 105 DEPTSGLDPAsrerLLELLRELAEE-GRTVIIVTHDPELAELAA 147
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
705-889 |
1.17e-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: 56.29 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 705 DIELGRSLLVT--GPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVD---QEAGSGCGIFYVPQrpytclgtlRDQIIYPL 779
Cdd:cd03224 20 SLTVPEGEIVAllGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglpPHERARAGIGYVPE---------GRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 780 SREEaefrALKMYGKGEKHADPRKLLDthlqIILEnvRLNYLLER-DNRGwdanlnweDTLSLGEQQRLGMARLFFHRPK 858
Cdd:cd03224 91 TVEE----NLLLGAYARRRAKRKARLE----RVYE--LFPRLKERrKQLA--------GTLSGGEQQMLAIARALMSRPK 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1654042132 859 YGILDECTNATS---VD-VEEHLYGLaNKMGITVV 889
Cdd:cd03224 153 LLLLDEPSEGLApkiVEeIFEAIREL-RDEGVTIL 186
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
705-911 |
1.36e-08 |
|
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: 55.96 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 705 DIELGRSLLVTGPNGSGKSSIFRVLrglwpiasGGLSRPSE--------DVDQEAGSGCGIF------YVPQRpYTCLGT 770
Cdd:cd03255 26 SIEKGEFVAIVGPSGSGKSTLLNIL--------GGLDRPTSgevrvdgtDISKLSEKELAAFrrrhigFVFQS-FNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 771 L--RDQIIYPL-----SREEAEFRALKMygkgekhadprklldthlqiiLENVRLNYLLERdnrgwdanlnWEDTLSLGE 843
Cdd:cd03255 97 LtaLENVELPLllagvPKKERRERAEEL---------------------LERVGLGDRLNH----------YPSELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654042132 844 QQRLGMARLFFHRPKYGILDECTNA----TSVDVEEHLYGLANKMGITVVTSSQRPALIPYHSMELRLIDGE 911
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNldseTGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
31-233 |
1.59e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.19 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPG------IGSDLNKEIFYV 104
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 105 PQRPYTAVGTLRDQLIypLTADQEVEQLTdrgmvELLKNVDLEYLLDRYPPEKEVNWGDE---LSLGEQQRLGMARLFYH 181
Cdd:PRK10790 421 QQDPVVLADTFLANVT--LGRDISEEQVW-----QALETVQLAELARSLPDGLYTPLGEQgnnLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1654042132 182 KPKFAILDECTSAVTTDMEE---RFCAKVRAMgTSCITISHRPALVAFHDVVLSL 233
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQaiqQALAAVREH-TTLVVIAHRLSTIVEADTILVL 547
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
47-235 |
1.90e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 56.62 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG-SDLNKE--------IFYVPQRPYTAVG---T 114
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlAKLNRAqrkafrrdIQMVFQDSISAVNprkT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 115 LRDQLIYP---LTADQEVEQLTDRGmvELLKNVDL-EYLLDRYPPekevnwgdELSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:PRK10419 108 VREIIREPlrhLLSLDKAERLARAS--EMLRAVDLdDSVLDKRPP--------QLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1654042132 191 CTS-----------AVTTDMEERFcakvramGTSCITISHRPALVA-FHDVVLSLDG 235
Cdd:PRK10419 178 AVSnldlvlqagviRLLKKLQQQF-------GTACLFITHDLRLVErFCQRVMVMDN 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
39-304 |
2.08e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.38 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 39 VTPtgnvLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGigsdlnkEIFYVPQRPYTAVGTLRDQ 118
Cdd:TIGR01271 438 VTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 119 LIYPLTADQeveqltdRGMVELLKNVDLEYLLDRYPPEKEVNWGD---ELSLGEQQRLGMARLFYHKPKFAILDECTSA- 194
Cdd:TIGR01271 507 IIFGLSYDE-------YRYTSVIKACQLEEDIALFPEKDKTVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFTHl 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 195 -VTTDME--ERFCAKVRAMGTSCITISHRPALVAFHDVVLSLDGE----GGWS--VHYKREGSSTEMGIDTMKA-SETKR 264
Cdd:TIGR01271 580 dVVTEKEifESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVcyfyGTFSelQAKRPDFSSLLLGLEAFDNfSAERR 659
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1654042132 265 QSDAKAVQRAFAMSKKDSAFS--NTKAQSY------FAEVISSSPSMN 304
Cdd:TIGR01271 660 NSILTETLRRVSIDGDSTVFSgpETIKQSFkqpppeFAEKRKQSIILN 707
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
43-226 |
2.14e-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: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGL--WPLISGHIvkpgigsdlnkeifyvpqrpytavgTLRDQLI 120
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEI-------------------------LFKGEDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 121 ypltADQEVEQLTDRGMvellknvdleYLLDRYPPE----------KEVNWGdeLSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:cd03217 67 ----TDLPPEERARLGI----------FLAFQYPPEipgvknadflRYVNEG--FSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190
....*....|....*....|....*....|....*....
gi 1654042132 191 CTSAVTTD---MEERFCAKVRAMGTSCITISHRPALVAF 226
Cdd:cd03217 131 PDSGLDIDalrLVAEVINKLREEGKSVLIITHYQRLLDY 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
47-220 |
2.78e-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: 57.53 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP--------------LISGHIV---KPGIgSDLNKEIFYVPQRPY 109
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtwdgeiywsgspLKASNIRdteRAGI-VIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 110 TAVGTLRDQLIYP--LTADQEveqltdrgMVELLKNVDLEYLLDRYPPEKEVNwgdELSLGEQQRLGMARLFYHKPKFAI 187
Cdd:TIGR02633 96 AENIFLGNEITLPggRMAYNA--------MYLRAKNLLRELQLDADNVTRPVG---DYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1654042132 188 LDECTSAVTTDMEERFCAKVR---AMGTSCITISHR 220
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRdlkAHGVACVYISHK 200
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
716-891 |
2.94e-08 |
|
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: 54.36 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 716 GPNGSGKSSIFRVLRGLWPIASGglsrpseDVdqeagsgcgifyvpqrpytclgTLRDQIIYPLSREE-AEFRALkmygk 794
Cdd:cd03214 32 GPNGAGKSTLLKTLAGLLKPSSG-------EI----------------------LLDGKDLASLSPKElARKIAY----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 795 gekhadprklldthLQIILENVRLNYLLERDnrgwdanlnwEDTLSLGEQQRLGMARLFFHRPKYGILDECTNA----TS 870
Cdd:cd03214 78 --------------VPQALELLGLAHLADRP----------FNELSGGERQRVLLARALAQEPPILLLDEPTSHldiaHQ 133
|
170 180
....*....|....*....|.
gi 1654042132 871 VDVEEHLYGLANKMGITVVTS 891
Cdd:cd03214 134 IELLELLRRLARERGKTVVMV 154
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
31-234 |
3.39e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 57.28 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG------SDLNKEIFYV 104
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDirtvtrASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 105 PQRPYTAVGTLRDQLiypltadqEV--EQLTDRGMVELLKNVDLEYLLDRYPPEKEVNWGD---ELSLGEQQRLGMARLF 179
Cdd:PRK13657 415 FQDAGLFNRSIEDNI--------RVgrPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGErgrQLSGGERQRLAIARAL 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1654042132 180 YHKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLD 234
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELmkGRTTFIIAHRLSTVRNADRILVFD 543
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
43-210 |
3.61e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.53 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGSDLNKEIfyVPQRpyTAVGTLRDQLIY- 121
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSL--SQQK--GLIRQLRQHVGFv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 122 -------------------PLTADQEV-EQLTDRGMvELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYH 181
Cdd:PRK11264 91 fqnfnlfphrtvleniiegPVIVKGEPkEEATARAR-ELLAKVGLAGKETSYP--------RRLSGGQQQRVAIARALAM 161
|
170 180
....*....|....*....|....*....
gi 1654042132 182 KPKFAILDECTSAVTTDMEERFCAKVRAM 210
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQL 190
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
34-195 |
4.12e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 34 YDVKVVTPTgnvlVDDLTLRVEPGSNLLITGPNGSGKSSLFR-VLGGLWPLISGHIVKPGigsdlnkEIFYVPQRPYTAV 112
Cdd:PLN03232 624 WDSKTSKPT----LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-------SVAYVPQVSWIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 113 GTLRDQLIYplTADQEVEQLTdrgmvellKNVD---LEYLLDRYPPEKEVNWGDE---LSLGEQQRLGMARLFYHKPKFA 186
Cdd:PLN03232 693 ATVRENILF--GSDFESERYW--------RAIDvtaLQHDLDLLPGRDLTEIGERgvnISGGQKQRVSMARAVYSNSDIY 762
|
....*....
gi 1654042132 187 ILDECTSAV 195
Cdd:PLN03232 763 IFDDPLSAL 771
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
47-231 |
4.30e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.51 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGS------DLNKEIFYVPQRPYTA-VG-TLRDQ 118
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteenvwDIRHKIGMVFQNPDNQfVGaTVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 119 LIYPL-TADQEVEQLTDRgMVELLKNVDLEYLLDRYPPekevnwgdELSLGEQQRLGMARLFYHKPKFAILDECTSAVTT 197
Cdd:PRK13650 103 VAFGLeNKGIPHEEMKER-VNEALELVGMQDFKEREPA--------RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1654042132 198 DMEERFCAKVRAM----GTSCITISHRPALVAFHDVVL 231
Cdd:PRK13650 174 EGRLELIKTIKGIrddyQMTVISITHDLDEVALSDRVL 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
716-904 |
4.93e-08 |
|
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: 53.56 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 716 GPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSGCG-IFYVPQRPYtclgtlrdqiiyplsreeaefralkmygk 794
Cdd:cd03230 33 GPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLPEEPS----------------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 795 gekhadprklLDTHLQIIlENVRLnyllerdnrgwdanlnwedtlSLGEQQRLGMARLFFHRPKYGILDECTNA----TS 870
Cdd:cd03230 84 ----------LYENLTVR-ENLKL---------------------SGGMKQRLALAQALLHDPELLILDEPTSGldpeSR 131
|
170 180 190
....*....|....*....|....*....|....
gi 1654042132 871 VDVEEHLYGLANKmGITVVTSSqrpalipyHSME 904
Cdd:cd03230 132 REFWELLRELKKE-GKTILLSS--------HILE 156
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
46-220 |
5.50e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 46 LVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV--KPGIGSDL---NKEIFYVPQR----PYTavgTLR 116
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILfeRQSIKKDLctyQKQLCFVGHRsginPYL---TLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 117 DQLIYPLTADQeveqlTDRGMVELLKNVDLEYLLDrYPpekevnwGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVT 196
Cdd:PRK13540 93 ENCLYDIHFSP-----GAVGITELCRLFSLEHLID-YP-------CGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180
....*....|....*....|....*..
gi 1654042132 197 TDMEERFCAKV---RAMGTSCITISHR 220
Cdd:PRK13540 160 ELSLLTIITKIqehRAKGGAVLLTSHQ 186
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
705-868 |
6.83e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 53.72 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 705 DIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAgsgcgifYVPQRPYtcLGTlRDQIIYPLS-REE 783
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD-------VAEACHY--LGH-RNAMKPALTvAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 784 AEFRAlKMYGKGEKHADPrklldthlqiILENVRLNYLLERDNRgwdanlnwedTLSLGEQQRLGMARLF-FHRPKYgIL 862
Cdd:PRK13539 94 LEFWA-AFLGGEELDIAA----------ALEAVGLAPLAHLPFG----------YLSAGQKRRVALARLLvSNRPIW-IL 151
|
....*.
gi 1654042132 863 DECTNA 868
Cdd:PRK13539 152 DEPTAA 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
695-891 |
7.99e-08 |
|
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: 54.28 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 695 QKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGL--------SRPSEDVDQEAGsgcgifYVPQRPYT 766
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaSLSRRELARRIA------YVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 767 CLG-TLRDQIIypLSReeaeFRALKMYGkGEKHADprklldthLQII---LENVRLNYLLERDnrgWdanlnweDTLSLG 842
Cdd:COG1120 87 PFGlTVRELVA--LGR----YPHLGLFG-RPSAED--------REAVeeaLERTGLEHLADRP---V-------DELSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654042132 843 EQQRLGMARLFFHRPKYGILDECTNA----TSVDVEEHLYGLANKMGITVVTS 891
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHldlaHQLEVLELLRRLARERGRTVVMV 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
43-220 |
8.31e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.79 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGlwplisghIVKPGIGsdlnkEIFY--VPQRPYTAvgtlRD--- 117
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSG--------VYQPDSG-----EILLdgEPVRFRSP----RDaqa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 118 ---QLIYpltadQE---VEQLT------------DRGMV----------ELLKNVDLEylLDrypPEKEVnwgDELSLGE 169
Cdd:COG1129 79 agiAIIH-----QElnlVPNLSvaeniflgreprRGGLIdwramrrrarELLARLGLD--ID---PDTPV---GDLSVAQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1654042132 170 QQRLGMARLFYHKPKFAILDECTSAVTTDMEERF---CAKVRAMGTSCITISHR 220
Cdd:COG1129 146 QQLVEIARALSRDARVLILDEPTASLTEREVERLfriIRRLKAQGVAIIYISHR 199
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
40-219 |
8.91e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 54.67 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 40 TPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG--------SDLNKEIFYVPQRP-YT 110
Cdd:PRK13637 16 TPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitdkkvklSDIRKKVGLVFQYPeYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 111 avgtLRDQLIYPLTA---------DQEVEQLTDRGMvELLKnVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYH 181
Cdd:PRK13637 96 ----LFEETIEKDIAfgpinlglsEEEIENRVKRAM-NIVG-LDYEDYKDKSP--------FELSGGQKRRVAIAGVVAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1654042132 182 KPKFAILDECTSAVTTDMEERFCAKVRAM----GTSCITISH 219
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELhkeyNMTIILVSH 203
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
31-193 |
9.40e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 54.31 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPG--IGSDlNKEIFYVPQRp 108
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYD-KKSLLEVRKT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 109 ytaVGTL----RDQLIYPlTADQEV-----------EQLTDRGMvELLKNVDLEYlLDRYPPEkevnwgdELSLGEQQRL 173
Cdd:PRK13639 80 ---VGIVfqnpDDQLFAP-TVEEDVafgplnlglskEEVEKRVK-EALKAVGMEG-FENKPPH-------HLSGGQKKRV 146
|
170 180
....*....|....*....|
gi 1654042132 174 GMARLFYHKPKFAILDECTS 193
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTS 166
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
681-884 |
1.20e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 681 DAISFSKVDiVTPAQKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPsedvdqeagSGCGIFYV 760
Cdd:PRK09544 3 SLVSLENVS-VSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN---------GKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 761 PQRpytclgtLRDQIIYPLSREeaEFRALKmygKGEKHADprklldthLQIILENVRLNYLLERDNRgwdanlnwedTLS 840
Cdd:PRK09544 73 PQK-------LYLDTTLPLTVN--RFLRLR---PGTKKED--------ILPALKRVQAGHLIDAPMQ----------KLS 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1654042132 841 LGEQQRLGMARLFFHRPKYGILDECTNATSVDVEEHLYGLANKM 884
Cdd:PRK09544 123 GGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQL 166
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
52-236 |
1.26e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.63 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 52 LRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKpgIGSDLN------------KEIFYVPQRpYTAVGTL--RD 117
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL--VGQPLHqmdeearaklraKHVGFVFQS-FMLIPTLnaLE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 118 QLIYPLTADQEVEQLTDRGMVELLKNVDLEYLLDRYPPEkevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSAVTT 197
Cdd:PRK10584 108 NVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ--------LSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1654042132 198 DMEERFCAKV----RAMGTSCITISHRPALVAFHDVVLSL-DGE 236
Cdd:PRK10584 180 QTGDKIADLLfslnREHGTTLILVTHDLQLAARCDRRLRLvNGQ 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
31-193 |
1.29e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 53.84 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKV-VTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIgsDLNKE--------- 100
Cdd:PRK13632 8 IKVENVSFsYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI--TISKEnlkeirkki 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 101 --IFYVPQRPYtaVG-TLRDQLIYPLTADQEVEQLTDRGMVELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMAR 177
Cdd:PRK13632 86 giIFQNPDNQF--IGaTVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEP--------QNLSGGQKQRVAIAS 155
|
170
....*....|....*.
gi 1654042132 178 LFYHKPKFAILDECTS 193
Cdd:PRK13632 156 VLALNPEIIIFDESTS 171
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
714-867 |
1.70e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.07 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 714 VTGPNGSGKSSIFRVLRGLWPIASGGLSRPsedvdqeagSGCGIFYVPQRPYTCLG-TLRDQIIY---PLSREEAEFRAL 789
Cdd:COG0488 29 LVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGLRIGYLPQEPPLDDDlTVLDTVLDgdaELRALEAELEEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 790 kmygkGEKHADPRKLLD--THLQIILENV-------RLNYLLER---DNRGWDANLNwedTLSLGEQQRLGMARLFFHRP 857
Cdd:COG0488 100 -----EAKLAEPDEDLErlAELQEEFEALggweaeaRAEEILSGlgfPEEDLDRPVS---ELSGGWRRRVALARALLSEP 171
|
170
....*....|
gi 1654042132 858 KYGILDECTN 867
Cdd:COG0488 172 DLLLLDEPTN 181
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
48-220 |
1.93e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.65 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 48 DDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP------LISGHIVKP---------GIGsdlnkeifYVPQRPytav 112
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQpdsgeiLIDGKPVRIrsprdaialGIG--------MVHQHF---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 113 gtlrdQLIYPLT---------------------ADQEVEQLTDR-GMvellkNVDleylldrypPEKEVnwgDELSLGEQ 170
Cdd:COG3845 90 -----MLVPNLTvaenivlgleptkggrldrkaARARIRELSERyGL-----DVD---------PDAKV---EDLSVGEQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1654042132 171 QRLGMARLFYHKPKFAILDECTsAVTTDME-ERF---CAKVRAMGTSCITISHR 220
Cdd:COG3845 148 QRVEILKALYRGARILILDEPT-AVLTPQEaDELfeiLRRLAAEGKSIIFITHK 200
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
31-236 |
2.02e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 54.73 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGN---VLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG-SDLNKEIFYVPQ 106
Cdd:PRK10535 5 LELKDIRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 107 RPYTAVGTLRDQLIYPLTADQEVE-----------QLTDRGmVELLKNVDLEYLLDrYPPekevnwgDELSLGEQQRLGM 175
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEvpavyaglerkQRLLRA-QELLQRLGLEDRVE-YQP-------SQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654042132 176 ARLFYHKPKFAILDECTSAVTTDMEERFCA---KVRAMGTSCITISHRPALVAFHDVVLSL-DGE 236
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAilhQLRDRGHTVIIVTHDPQVAAQAERVIEIrDGE 220
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
48-223 |
2.18e-07 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 53.03 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 48 DDLTLRVEPGSNLLITGPNGSGKSSLFRVLGG--LWPLISGHI-VKpgiGSDLN---------KEIFYVPQRP------- 108
Cdd:TIGR01978 17 KGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTIlFK---GQDLLelepderarAGLFLAFQYPeeipgvs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 109 --------YTAVGTLRDQliYPLTADQEVEQLTDrgMVELLKNVdlEYLLDRYppekeVNWGdeLSLGEQQR---LGMAR 177
Cdd:TIGR01978 94 nleflrsaLNARRSARGE--EPLDLLDFEKLLKE--KLALLDMD--EEFLNRS-----VNEG--FSGGEKKRneiLQMAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1654042132 178 LfyhKPKFAILDECTSAVTTDMEERFCA---KVRAMGTSCITISHRPAL 223
Cdd:TIGR01978 161 L---EPKLAILDEIDSGLDIDALKIVAEginRLREPDRSFLIITHYQRL 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
40-193 |
2.58e-07 |
|
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: 54.92 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 40 TPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLfrvLGGLWPLIS--GHIVKPGIGSD------LNKEIFYVPQRPYTA 111
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTL---LSALLRLLSteGEIQIDGVSWNsvtlqtWRKAFGVIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 112 VGTLRDQL-IYPLTADQEVEQLTDRgmvellknVDLEYLLDRYPPEKE---VNWGDELSLGEQQRLGMARLFYHKPKFAI 187
Cdd:TIGR01271 1305 SGTFRKNLdPYEQWSDEEIWKVAEE--------VGLKSVIEQFPDKLDfvlVDGGYVLSNGHKQLMCLARSILSKAKILL 1376
|
....*.
gi 1654042132 188 LDECTS 193
Cdd:TIGR01271 1377 LDEPSA 1382
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
31-232 |
2.80e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 54.08 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVtptgnvlvDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGI------GSDLNKEIFYV 104
Cdd:PRK09536 11 VEFGDTTVL--------DGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 105 PQrpytavGTlrdqliyPLTADQEVEQLTDRGMVELLKNVDLEYLLDRYPPEKEVNWGD----------ELSLGEQQRLG 174
Cdd:PRK09536 83 PQ------DT-------SLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGvaqfadrpvtSLSGGERQRVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1654042132 175 MARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAMGTscitiSHRPALVAFHDVVLS 232
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVD-----DGKTAVAAIHDLDLA 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
32-220 |
2.95e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 32 EFYDVKVVtptgnvlvDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP--------LISGHIVKP---------GIg 94
Cdd:PRK13549 14 TFGGVKAL--------DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtyegeiIFEGEELQAsnirdteraGI- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 95 SDLNKEIFYVPQ----------RPYTAVGTLRDQLIYpltadQEVEqltdrgmvELLKNVDLEylldrYPPEKEVNwgdE 164
Cdd:PRK13549 85 AIIHQELALVKElsvleniflgNEITPGGIMDYDAMY-----LRAQ--------KLLAQLKLD-----INPATPVG---N 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1654042132 165 LSLGEQQRLGMARLFYHKPKFAILDECTSAVT---TDMEERFCAKVRAMGTSCITISHR 220
Cdd:PRK13549 144 LGLGQQQLVEIAKALNKQARLLILDEPTASLTeseTAVLLDIIRDLKAHGIACIYISHK 202
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
700-897 |
3.30e-07 |
|
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: 52.14 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 700 RELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSGCGIFYVPQRP--YTCLgTLRDQIIY 777
Cdd:cd03259 17 DDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQDYalFPHL-TVAENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 778 PLsreeaefralKMYGKGEKHADPRKLLdthlqiILENVRLNYLLERdnrgwdanlnWEDTLSLGEQQRLGMARLFFHRP 857
Cdd:cd03259 96 GL----------KLRGVPKAEIRARVRE------LLELVGLEGLLNR----------YPHELSGGQQQRVALARALAREP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1654042132 858 KYGILDECTNAtsVDVE------EHLYGLANKMGITV--VTSSQRPAL 897
Cdd:cd03259 150 SLLLLDEPLSA--LDAKlreelrEELKELQRELGITTiyVTHDQEEAL 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
48-220 |
3.54e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.85 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 48 DDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV---KP------------GIGSdLNKEIFYVPQ------ 106
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILylgKEvtfngpkssqeaGIGI-IHQELNLIPQltiaen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 107 -----RPYTAVGTLRDQLIYPlTADQeveqltdrgmveLLKNVDLeylldRYPPEKEVNwgdELSLGEQQRLGMARLFYH 181
Cdd:PRK10762 100 iflgrEFVNRFGRIDWKKMYA-EADK------------LLARLNL-----RFSSDKLVG---ELSIGEQQMVEIAKVLSF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1654042132 182 KPKFAILDECTSAVT-TDMEERFcaKV----RAMGTSCITISHR 220
Cdd:PRK10762 159 ESKVIIMDEPTDALTdTETESLF--RVirelKSQGRGIVYISHR 200
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
705-868 |
3.64e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 52.40 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 705 DIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASG-----GLSRPSEDVD-----QEAGSGCGIFYV-PQrpytcLGTLRD 773
Cdd:PRK09493 23 NIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdGLKVNDPKVDerlirQEAGMVFQQFYLfPH-----LTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 774 QIIYPL-----SREEAEFRALKMYGK-GekhadprklldthlqiilenvrlnyLLERDNrgwdanlNWEDTLSLGEQQRL 847
Cdd:PRK09493 98 VMFGPLrvrgaSKEEAEKQARELLAKvG-------------------------LAERAH-------HYPSELSGGQQQRV 145
|
170 180
....*....|....*....|.
gi 1654042132 848 GMARLFFHRPKYGILDECTNA 868
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSA 166
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
50-234 |
4.46e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.97 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 50 LTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG------SDLNKEIFYVPQRPYTAVGTLRDQLiypl 123
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDiskfglMDLRKVLGIIPQAPVLFSGTVRFNL---- 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 124 taDQEVEQlTDRGMVELLKNVDLEYLLDRYPP--EKEVNWGDE-LSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDME 200
Cdd:PLN03130 1334 --DPFNEH-NDADLWESLERAHLKDVIRRNSLglDAEVSEAGEnFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTD 1410
|
170 180 190
....*....|....*....|....*....|....*.
gi 1654042132 201 ERFCAKVRAMGTSC--ITISHRPALVAFHDVVLSLD 234
Cdd:PLN03130 1411 ALIQKTIREEFKSCtmLIIAHRLNTIIDCDRILVLD 1446
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
46-193 |
4.66e-07 |
|
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: 51.89 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 46 LVDDLTLRVEPGSNLLITGPNGSGKSSLF-----RVLGGlwPLISGHIVKPGIGSD---LNKEIFYVPQRPYTAVG-TLR 116
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLdaisgRVEGG--GTTSGQILFNGQPRKpdqFQKCVAYVRQDDILLPGlTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 117 DQLIY----PLTADQEVEQLTDRGMVELLKNVDLEYLLDRYPPEkevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECT 192
Cdd:cd03234 100 ETLTYtailRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKG--------ISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
.
gi 1654042132 193 S 193
Cdd:cd03234 172 S 172
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
700-909 |
5.20e-07 |
|
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: 51.51 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 700 RELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSGCGifYVPQ-RPYTCLGTLRDQIIYp 778
Cdd:cd03269 17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIG--YLPEeRGLYPKMKVIDQLVY- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 779 lsreeaeFRALkmygKGEKHADPRKlldthlqiilenvRLNYLLERDNRGWDANLNWEdTLSLGEQQRLGMARLFFHRPK 858
Cdd:cd03269 94 -------LAQL----KGLKKEEARR-------------RIDEWLERLELSEYANKRVE-ELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1654042132 859 YGILDECTNA---TSVDV-EEHLYGLANKmGITVVTSSqrpalipyHSMEL--RLID 909
Cdd:cd03269 149 LLILDEPFSGldpVNVELlKDVIRELARA-GKTVILST--------HQMELveELCD 196
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
700-877 |
5.62e-07 |
|
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: 51.57 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 700 RELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSGCGIFYVPQrpytclgtlrDQIIYP- 778
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQ----------NYALFPh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 779 LSREEAEFRALKMYgKGEKHADPRKLLDthlqiILENVRLNYLLERDNRgwdanlnwedTLSLGEQQRLGMARLFFHRPK 858
Cdd:cd03299 86 MTVYKNIAYGLKKR-KVDKKEIERKVLE-----IAEMLGIDHLLNRKPE----------TLSGGEQQRVAIARALVVNPK 149
|
170
....*....|....*....
gi 1654042132 859 YGILDECTNATSVDVEEHL 877
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKL 168
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
43-192 |
5.70e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 51.74 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVD---DLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPG---------IGSDL-NKEIFYVPQ--- 106
Cdd:PRK11629 18 GSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaAKAELrNQKLGFIYQfhh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 107 --RPYTAVgtlrDQLIYPLTADQEVEQLTDRGMVELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPK 184
Cdd:PRK11629 98 llPDFTAL----ENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRP--------SELSGGERQRVAIARALVNNPR 165
|
....*...
gi 1654042132 185 FAILDECT 192
Cdd:PRK11629 166 LVLADEPT 173
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
46-236 |
5.74e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.11 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 46 LVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPL---ISGHIVKPGIGSDLNKEIFyvpqrpytavgtlRDQLIYP 122
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNGIPYKEFAEKY-------------PGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 123 LTADQEVEQLTDRgmvELLKNVdleyLLDRyppekevnwGDE----LSLGEQQRLGMARLFYHKPKFAILDECT----SA 194
Cdd:cd03233 89 SEEDVHFPTLTVR---ETLDFA----LRCK---------GNEfvrgISGGERKRVSIAEALVSRASVLCWDNSTrgldSS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1654042132 195 VTTDMEERFCAKVRAMGTSCITISHRPALVAFH---DVVLSLDGE 236
Cdd:cd03233 153 TALEILKCIRTMADVLKTTTFVSLYQASDEIYDlfdKVLVLYEGR 197
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
10-236 |
7.22e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.24 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 10 VDEKSSLQRKGSRNCISEANyiEFYDVKvvtptGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV 89
Cdd:PTZ00243 646 GHEATPTSERSAKTPKMKTD--DFFELE-----PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 90 KpgigsdlNKEIFYVPQRPYTAVGTLRDQLIYpltADQE-VEQLTDRGMVELLKnVDLEYL---LDRYPPEKEVNwgdeL 165
Cdd:PTZ00243 719 A-------ERSIAYVPQQAWIMNATVRGNILF---FDEEdAARLADAVRVSQLE-ADLAQLgggLETEIGEKGVN----L 783
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654042132 166 SLGEQQRLGMARLFYHKPKFAILDECTSAVTTD-----MEERFCAKVRamGTSCITISHRPALVAFHDVVLSLDGE 236
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHvgervVEECFLGALA--GKTRVLATHQVHVVPRADYVVALGDG 857
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
31-193 |
7.62e-07 |
|
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: 51.66 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLV-DDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGSDLNKEIFYVPQRpy 109
Cdd:TIGR04520 1 IEVENVSFSYPESEKPAlKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 110 taVGTL----RDQLIYPLTAD-------------QEVEQLTDrgmvELLKNVDLEYLLDRyPPEKevnwgdeLSLGEQQR 172
Cdd:TIGR04520 79 --VGMVfqnpDNQFVGATVEDdvafglenlgvprEEMRKRVD----EALKLVGMEDFRDR-EPHL-------LSGGQKQR 144
|
170 180
....*....|....*....|.
gi 1654042132 173 LGMARLFYHKPKFAILDECTS 193
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATS 165
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-253 |
8.19e-07 |
|
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: 53.41 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 12 EKSSLQRK----GSRNCISEANyIEFYDVKVVTPTGNvlvdDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGH 87
Cdd:TIGR00957 620 EPDSIERRtikpGEGNSITVHN-ATFTWARDLPPTLN----GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 88 IVKPGigsdlnkEIFYVPQRPYTAVGTLRDQLIYPLTADQEVEQLTDRGMVELlknVDLEYLL--DRYP-PEKEVNwgde 164
Cdd:TIGR00957 695 VHMKG-------SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALL---PDLEILPsgDRTEiGEKGVN---- 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 165 LSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRA-----MGTSCITISHRPALVAFHDVVLSLDGeggw 239
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGpegvlKNKTRILVTHGISYLPQVDVIIVMSG---- 836
|
250
....*....|....
gi 1654042132 240 svhykreGSSTEMG 253
Cdd:TIGR00957 837 -------GKISEMG 843
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
31-198 |
9.42e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 52.00 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGN---VLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVkpgI-GSDLN-------- 98
Cdd:COG1135 2 IELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVL---VdGVDLTalserelr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 99 ---KEIFYVPQ-------RpytavgTLRDQLIYPL----TADQEVEQLTDrgmvELLKNVDLEYLLDRYPpekevnwgDE 164
Cdd:COG1135 79 aarRKIGMIFQhfnllssR------TVAENVALPLeiagVPKAEIRKRVA----ELLELVGLSDKADAYP--------SQ 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 1654042132 165 LSLGEQQRLGMARLFYHKPKfaIL--DECTSAV---TTD 198
Cdd:COG1135 141 LSGGQKQRVGIARALANNPK--VLlcDEATSALdpeTTR 177
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
48-238 |
1.04e-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: 50.87 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 48 DDLTLRVEPGS-----NLLITGPNGSGKSSLFRVLGGLwplisghiVKPG---IGSDLNKeIFYVPQRpytavgtlrdql 119
Cdd:cd03237 11 GEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGV--------LKPDegdIEIELDT-VSYKPQY------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 120 iypLTADQE--VEQL---TDRGM-------VELLKNVDLEYLLDRyppekEVNwgdELSLGEQQRLGMARLFYHKPKFAI 187
Cdd:cd03237 70 ---IKADYEgtVRDLlssITKDFythpyfkTEIAKPLQIEQILDR-----EVP---ELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654042132 188 LDEcTSAvTTDMEERFcakvraMGTSCIT--ISH--RPALVAFHDV---------VLSLDGEGG 238
Cdd:cd03237 139 LDE-PSA-YLDVEQRL------MASKVIRrfAENneKTAFVVEHDIimidyladrLIVFEGEPS 194
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-189 |
1.08e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.40 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 17 QRKGSRNCISEANYIEFYDVKVVtptGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFR-VLGGLWPlISGHIVKPGigs 95
Cdd:cd03291 26 QENNDRKHSSDDNNLFFSNLCLV---GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEP-SEGKIKHSG--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 96 dlnkEIFYVPQRPYTAVGTLRDQLIYPLTADQEVEQltdrgmvELLKNVDLEYLLDRYPPEKEVNWGD---ELSLGEQQR 172
Cdd:cd03291 99 ----RISFSSQFSWIMPGTIKENIIFGVSYDEYRYK-------SVVKACQLEEDITKFPEKDNTVLGEggiTLSGGQRAR 167
|
170
....*....|....*..
gi 1654042132 173 LGMARLFYHKPKFAILD 189
Cdd:cd03291 168 ISLARAVYKDADLYLLD 184
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
705-911 |
1.17e-06 |
|
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: 50.16 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 705 DIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSedvdqeagsgcGIFYVPQRPYTCLGTLRDQIIYplsreea 784
Cdd:cd03250 27 EVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQEPWIQNGTIRENILF------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 785 efralkmygkGEKHaDPRKL--------LDTHLQIilenvrlnyLLERDN-----RGWdanlnwedTLSLGEQQRLGMAR 851
Cdd:cd03250 89 ----------GKPF-DEERYekvikacaLEPDLEI---------LPDGDLteigeKGI--------NLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654042132 852 LFFHRPKYGILDECTNATSVDVEEHLY-------GLANKmgiTVVTSSQRPALIPYHSMELRLIDGE 911
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIFencilglLLNNK---TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
47-202 |
1.30e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.94 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP------LISGHIVKPGIGSDLNKEIFYVPQRPYTA------VGT 114
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEptsgelLIDDHPLHFGDYSYRSQRIRMIFQDPSTSlnprqrISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 115 LRDqliYPLTADQEVE-QLTDRGMVELLKNVDLEylldrypPEKEVNWGDELSLGEQQRLGMARLFYHKPKFAILDECTS 193
Cdd:PRK15112 109 ILD---FPLRLNTDLEpEQREKQIIETLRQVGLL-------PDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
....*....
gi 1654042132 194 AVttDMEER 202
Cdd:PRK15112 179 SL--DMSMR 185
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
27-237 |
1.32e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.00 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 27 EANYIEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGSD--------LN 98
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkglmkLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 99 KEIFYVPQRP---------YTAV--GTLRDQLiypltADQEVEQLTDRGMvellKNVDLEYLLDryppeKEVNWgdeLSL 167
Cdd:PRK13636 82 ESVGMVFQDPdnqlfsasvYQDVsfGAVNLKL-----PEDEVRKRVDNAL----KRTGIEHLKD-----KPTHC---LSF 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654042132 168 GEQQRLGMARLFYHKPKFAILDECTSAV----TTDMEERFCAKVRAMGTSCITISHRPALVAFH-DVVLSLDgEG 237
Cdd:PRK13636 145 GQKKRVAIAGVLVMEPKVLVLDEPTAGLdpmgVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYcDNVFVMK-EG 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
37-199 |
1.35e-06 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 50.20 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 37 KVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP------LISGHIVKPGIgSDLNKEIFYVPQRPyT 110
Cdd:cd03263 8 KTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRptsgtaYINGYSIRTDR-KAARQSLGYCPQFD-A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 111 AVGTL--RDQL--------IYPLTADQEVEQltdrgmveLLKNVDLEYLLDRyppekEVNwgdELSLGEQQRLGMARLFY 180
Cdd:cd03263 86 LFDELtvREHLrfyarlkgLPKSEIKEEVEL--------LLRVLGLTDKANK-----RAR---TLSGGMKRKLSLAIALI 149
|
170
....*....|....*....
gi 1654042132 181 HKPKFAILDEctsaVTTDM 199
Cdd:cd03263 150 GGPSVLLLDE----PTSGL 164
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
31-234 |
1.70e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 50.76 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGS-------DLNKEIFY 103
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfsklqGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 104 VPQRPYTA-VG-TLRDQLIY-------PLTadqEVEQLTDRGMVEllknVDLEYLLDRYPpekevnwgDELSLGEQQRLG 174
Cdd:PRK13644 82 VFQNPETQfVGrTVEEDLAFgpenlclPPI---EIRKRVDRALAE----IGLEKYRHRSP--------KTLSGGQGQCVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654042132 175 MARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAM---GTSCITISHRPALVAFHDVVLSLD 234
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhekGKTIVYITHNLEELHDADRIIVMD 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
48-231 |
2.95e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 48 DDLTLRVEPGS-----NLLITGPNGSGKSSLFRVLGGlwplisghIVKPGIGS-DLNKEIFYVPQRpytavgtLRDQliY 121
Cdd:PRK13409 351 GDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAG--------VLKPDEGEvDPELKISYKPQY-------IKPD--Y 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 122 PLTADQEVEQLTDRGM-----VELLKNVDLEYLLDRYppekeVNwgdELSLGEQQRLGMARLFYHKPKFAILDECTSAVt 196
Cdd:PRK13409 414 DGTVEDLLRSITDDLGssyykSEIIKPLQLERLLDKN-----VK---DLSGGELQRVAIAACLSRDADLYLLDEPSAHL- 484
|
170 180 190
....*....|....*....|....*....|....*...
gi 1654042132 197 tDMEERF-CAKV--RAMGTSCITishrpALVAFHDVVL 231
Cdd:PRK13409 485 -DVEQRLaVAKAirRIAEEREAT-----ALVVDHDIYM 516
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
31-198 |
3.03e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 50.18 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGN---VLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGI------GSDLNKE- 100
Cdd:PRK11153 2 IELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsEKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 101 -----IF----YVPQRpytavgTLRDQLIYPLTADQEVEQLTDRGMVELLKNVDLEYLLDRYPPEkevnwgdeLSLGEQQ 171
Cdd:PRK11153 82 rqigmIFqhfnLLSSR------TVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQ--------LSGGQKQ 147
|
170 180 190
....*....|....*....|....*....|
gi 1654042132 172 RLGMARLFYHKPKFAILDECTSAV---TTD 198
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALdpaTTR 177
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
31-225 |
3.21e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.10 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPG--IGSDLNKEIFYVPQRp 108
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdITRLKNREVPFLRRQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 109 ytaVG------------TLRDQLIYPLTADQEVEQLTDRGMVELLKNVDLeylLDryppeKEVNWGDELSLGEQQRLGMA 176
Cdd:PRK10908 81 ---IGmifqdhhllmdrTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGL---LD-----KAKNFPIQLSGGEQQRVGIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1654042132 177 RLFYHKPKFAILDECTSAVTTDMEE---RFCAKVRAMGTSCITISHRPALVA 225
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEgilRLFEEFNRVGVTVLMATHDIGLIS 201
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
34-194 |
3.49e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.28 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 34 YDVKVVTPTgnvlVDDLTLRVEPGSNLLITGPNGSGKSSLFR-VLGGLWPLISGHIVKPGigsdlnkEIFYVPQRPYTAV 112
Cdd:PLN03130 624 WDSKAERPT----LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-------TVAYVPQVSWIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 113 GTLRDQLIYPLTADQE-VEQLTD----RGMVELLKNVDLEYLLDRyppekevnwGDELSLGEQQRLGMARLFYHKPKFAI 187
Cdd:PLN03130 693 ATVRDNILFGSPFDPErYERAIDvtalQHDLDLLPGGDLTEIGER---------GVNISGGQKQRVSMARAVYSNSDVYI 763
|
....*..
gi 1654042132 188 LDECTSA 194
Cdd:PLN03130 764 FDDPLSA 770
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
47-192 |
3.51e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 50.57 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHiVKPGIGS---DLNKEIFYVPQRPYTAVGTLRDQL-IYP 122
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE-VNVRVGDewvDMTKPGPDGRGRAKRYIGILHQEYdLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 123 -------LTADQEVE---QLTDRGMVELLKNVDL-----EYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAI 187
Cdd:TIGR03269 379 hrtvldnLTEAIGLElpdELARMKAVITLKMVGFdeekaEEILDKYP--------DELSEGERHRVALAQVLIKEPRIVI 450
|
....*
gi 1654042132 188 LDECT 192
Cdd:TIGR03269 451 LDEPT 455
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
47-224 |
3.57e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGSD---------LNKEIFYVPQRPYTAVG---T 114
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspgklqaLRRDIQFIFQDPYASLDprqT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 115 LRDQLIYPLTADQEVE-QLTDRGMVELLKNVDLEylldrypPEKEVNWGDELSLGEQQRLGMARLFYHKPKFAILDECTS 193
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLL-------PEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190
....*....|....*....|....*....|....*
gi 1654042132 194 AVTTDMEERFCAKV----RAMGTSCITISHRPALV 224
Cdd:PRK10261 493 ALDVSIRGQIINLLldlqRDFGIAYLFISHDMAVV 527
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
28-190 |
3.70e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 49.73 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 28 ANYIEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPL------ISGHIVKPGIGSDLNKEI 101
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPqrgrvkVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 102 FYVPQRPYTAV--GTLRDQLIY-PLTADQEVEQLTDRgMVELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARL 178
Cdd:PRK13647 82 GLVFQDPDDQVfsSTVWDDVAFgPVNMGLDKDEVERR-VEEALKAVRMWDFRDKPP--------YHLSYGQKKRVAIAGV 152
|
170
....*....|..
gi 1654042132 179 FYHKPKFAILDE 190
Cdd:PRK13647 153 LAMDPDVIVLDE 164
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
33-224 |
4.19e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.96 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 33 FYDVK--VVTPTGNV-LVDDLTLRVEPGSNLLITGPNGSGKSSLFRVL--------GGLwpLISGH-IVKPGIG--SDLN 98
Cdd:PRK11308 14 HYPVKrgLFKPERLVkALDGVSFTLERGKTLAVVGESGCGKSTLARLLtmietptgGEL--YYQGQdLLKADPEaqKLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 99 KEIFYVPQRPYTAVG---TLRDQLIYPL------TADQEVEQltdrgMVELLKNVDL--EYlLDRYPpekevnwgDELSL 167
Cdd:PRK11308 92 QKIQIVFQNPYGSLNprkKVGQILEEPLlintslSAAERREK-----ALAMMAKVGLrpEH-YDRYP--------HMFSG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654042132 168 GEQQRLGMARLFYHKPKFAILDECTSAVttDMEERfcAKV--------RAMGTSCITISHRPALV 224
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSAL--DVSVQ--AQVlnlmmdlqQELGLSYVFISHDLSVV 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
700-874 |
4.29e-06 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 48.64 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 700 RELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSrpsedVDQEAGSGCGIFY-------VPQRPYTCLGTLR 772
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIL-----IDGVDISKIGLHDlrsrisiIPQDPVLFSGTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 773 DQIIyPLSR--EEAEFRALKMYGKGEKHADPRKLLDTHlqiILENvrlnyllerdnrgwdanlnwEDTLSLGEQQRLGMA 850
Cdd:cd03244 96 SNLD-PFGEysDEELWQALERVGLKEFVESLPGGLDTV---VEEG--------------------GENLSVGQRQLLCLA 151
|
170 180
....*....|....*....|....
gi 1654042132 851 RLFFHRPKYGILDECTnaTSVDVE 874
Cdd:cd03244 152 RALLRKSKILVLDEAT--ASVDPE 173
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
54-233 |
5.15e-06 |
|
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: 49.14 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 54 VEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG------SDLNKEIFYVPQRPYTAVGTLRDQLiypltaDQ 127
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDisklplHTLRSRLSIILQDPILFSGSIRFNL------DP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 128 EvEQLTDRGMVELLKNVDLEYLLDRYPPEKE---VNWGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVttDM-EERF 203
Cdd:cd03288 118 E-CKCTDDRLWEALEIAQLKNMVKSLPGGLDavvTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI--DMaTENI 194
|
170 180 190
....*....|....*....|....*....|...
gi 1654042132 204 CAKVRAMG---TSCITISHRPALVAFHDVVLSL 233
Cdd:cd03288 195 LQKVVMTAfadRTVVTIAHRVSTILDADLVLVL 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
47-194 |
5.54e-06 |
|
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: 50.07 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPlISGHIVKpgIGSDLN-----------KEIFYVPQRPYTA---- 111
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRF--DGQDLDglsrralrplrRRMQVVFQDPFGSlspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 112 --VGtlrdQLI-------YPLTADQEVEQLtdrgMVELLKNVDL-EYLLDRYPpekevnwgDELSLGEQQRLGMARLFYH 181
Cdd:COG4172 379 mtVG----QIIaeglrvhGPGLSAAERRAR----VAEALEEVGLdPAARHRYP--------HEFSGGQRQRIAIARALIL 442
|
170
....*....|...
gi 1654042132 182 KPKFAILDECTSA 194
Cdd:COG4172 443 EPKLLVLDEPTSA 455
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
39-198 |
5.69e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.87 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 39 VTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGG--LWPLISGHIVKPGIgSDLNKE--------IFYVPQRP 108
Cdd:CHL00131 15 ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGE-SILDLEpeerahlgIFLAFQYP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 109 YTAVG-TLRDQLIYPLTADQEVEQLTDRG-------MVELLKNVDL-EYLLDRYppekeVNWGdeLSLGEQQR---LGMA 176
Cdd:CHL00131 94 IEIPGvSNADFLRLAYNSKRKFQGLPELDplefleiINEKLKLVGMdPSFLSRN-----VNEG--FSGGEKKRneiLQMA 166
|
170 180
....*....|....*....|..
gi 1654042132 177 RLfyhKPKFAILDECTSAVTTD 198
Cdd:CHL00131 167 LL---DSELAILDETDSGLDID 185
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
58-195 |
5.75e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.03 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 58 SNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPgiGSDLNKEIFYVPQRPYTAVGTLRDQLIYPLTADQEV-------- 129
Cdd:PRK13652 31 SRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR--GEPITKENIREVRKFVGLVFQNPDDQIFSPTVEQDIafgpinlg 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1654042132 130 --EQLTDRGMVELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAV 195
Cdd:PRK13652 109 ldEETVAHRVSSALHMLGLEELRDRVP--------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-192 |
6.46e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.73 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 37 KVVtPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV-KPGIgsdlnkEIFYVPQRPY------ 109
Cdd:PRK11819 14 KVV-PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARpAPGI------KVGYLPQEPQldpekt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 110 ------TAVGTLRDQL-----IYPLTA--DQEVEQLTDRgMVEL--------LKNVD--LEYLLD--RYPPekevnwGDE 164
Cdd:PRK11819 87 vrenveEGVAEVKAALdrfneIYAAYAepDADFDALAAE-QGELqeiidaadAWDLDsqLEIAMDalRCPP------WDA 159
|
170 180 190
....*....|....*....|....*....|..
gi 1654042132 165 ----LSLGEQQRLGMARLFYHKPKFAILDECT 192
Cdd:PRK11819 160 kvtkLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
43-195 |
7.20e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 48.63 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPG--IGSDLNK----EIFYVPQRPYTAVGTLR 116
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpLESWSSKafarKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 117 DQLI----YPLTADQEVEQLTDRGMV-ELLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:PRK10575 103 RELVaigrYPWHGALGRFGAADREKVeEAISLVGLKPLAHRLV--------DSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
....
gi 1654042132 192 TSAV 195
Cdd:PRK10575 175 TSAL 178
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-253 |
8.93e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.78 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 27 EANYIEFYDVKVVTPTGNVLV-DDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPG--IGS----DLNK 99
Cdd:PTZ00243 1305 QAGSLVFEGVQMRYREGLPLVlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGreIGAyglrELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 100 EIFYVPQRPYTAVGTLRdqliypltadQEVEQLTDRGMVELLKNVDLEYLLDRYPPEKE------VNWGDELSLGEQQRL 173
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVR----------QNVDPFLEASSAEVWAALELVGLRERVASESEgidsrvLEGGSNYSVGQRQLM 1454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 174 GMARLFYHK-PKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLDgeggwsvhykrEGSST 250
Cdd:PTZ00243 1455 CMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAfsAYTVITIAHRLHTVAQYDKIIVMD-----------HGAVA 1523
|
...
gi 1654042132 251 EMG 253
Cdd:PTZ00243 1524 EMG 1526
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
47-192 |
9.27e-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: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGSDLNKEIFyvpQRPYTAVGTLRDQL------- 119
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF---LRRIGVVFGQKTQLwwdlpvi 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 120 --------IYPLTADQEVEQLtdRGMVELLknvDLEYLLDRypPEKevnwgdELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:cd03267 114 dsfyllaaIYDLPPARFKKRL--DELSELL---DLEELLDT--PVR------QLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
.
gi 1654042132 192 T 192
Cdd:cd03267 181 T 181
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
43-193 |
9.27e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 48.67 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV-----KPGIGSDLNKEIFYVPQ-----RPYTAv 112
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpVPARARLARARIGVVPQfdnldLEFTV- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 113 gtlRDQLI----YPLTADQEVEQLtdrgMVELLKNVDLEYLLDryppeKEVNwgdELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:PRK13536 132 ---RENLLvfgrYFGMSTREIEAV----IPSLLEFARLESKAD-----ARVS---DLSGGMKRRLTLARALINDPQLLIL 196
|
....*
gi 1654042132 189 DECTS 193
Cdd:PRK13536 197 DEPTT 201
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
47-88 |
1.28e-05 |
|
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: 47.53 E-value: 1.28e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI 88
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV 79
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
40-89 |
1.44e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 47.77 E-value: 1.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1654042132 40 TPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV 89
Cdd:COG1101 15 TVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL 64
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
714-866 |
1.47e-05 |
|
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: 46.87 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 714 VTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSGCgIFYVPQRPYTCLG--TLRDQIIYplsreeaefralkm 791
Cdd:cd03226 31 LTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS-IGYVMQDVDYQLFtdSVREELLL-------------- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654042132 792 yGKGEKHADPRKLldthlQIILENVRLNYLLERDNRgwdanlnwedTLSLGEQQRLGMARLFFHRPKYGILDECT 866
Cdd:cd03226 96 -GLKELDAGNEQA-----ETVLKDLDLYALKERHPL----------SLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
50-190 |
1.54e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.15 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 50 LTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI---VKPGIGSDLNKEIFYVPQRP--YTAVGTLrDQLIYPLT 124
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidGKTATRGDRSRFMAYLGHLPglKADLSTL-ENLHFLCG 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654042132 125 ADQEVEQLTDRGMVELLKNVDLEYLLDRyppekevnwgdELSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:PRK13543 109 LHGRRAKQMPGSALAIVGLAGYEDTLVR-----------QLSAGQKKRLALARLWLSPAPLWLLDE 163
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
47-88 |
1.85e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 47.00 E-value: 1.85e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI 88
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
40-190 |
1.93e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 47.54 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 40 TPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPlISGHIVKPGIGSD------LNKEIFYVPQRPYTAVG 113
Cdd:cd03289 13 TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNsvplqkWRKAFGVIPQKVFIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 114 TLRDQL-IYPLTADQEVEQLTDRgmvellknVDLEYLLDRYPPEKE---VNWGDELSLGEQQRLGMARLFYHKPKFAILD 189
Cdd:cd03289 92 TFRKNLdPYGKWSDEEIWKVAEE--------VGLKSVIEQFPGQLDfvlVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163
|
.
gi 1654042132 190 E 190
Cdd:cd03289 164 E 164
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
43-236 |
2.81e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.74 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP---LISGHIVKPGIGsdLNKEifyvpqrPYTAVGTLR--- 116
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggAPRGARVTGDVT--LNGE-------PLAAIDAPRlar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 117 --------DQLIYPLTADQEVeqltdrgmvellknvdleyLLDRYP----------PEKEVNWG---------------D 163
Cdd:PRK13547 84 lravlpqaAQPAFAFSAREIV-------------------LLGRYPharragalthRDGEIAWQalalagatalvgrdvT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 164 ELSLGEQQRLGMARLFYH---------KPKFAILDECTSAVTTDMEERFCAKVRAMG----TSCITISHRPALVAFH--D 228
Cdd:PRK13547 145 TLSGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwnLGVLAIVHDPNLAARHadR 224
|
....*...
gi 1654042132 229 VVLSLDGE 236
Cdd:PRK13547 225 IAMLADGA 232
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
43-192 |
2.84e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRV-LGGLWPlISGHIvkpGIGSDLnkEIFYVPQrpYTAV----GTLRD 117
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQA-DSGRI---HCGTKL--EVAYFDQ--HRAEldpeKTVMD 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1654042132 118 QLiypltAD--QEVeqltdrgMVELLKNVDLEYLLD-RYPPEKEVNWGDELSLGEQQRLGMARLFYHKPKFAILDECT 192
Cdd:PRK11147 403 NL-----AEgkQEV-------MVNGRPRHVLGYLQDfLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPT 468
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
54-205 |
3.22e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 46.59 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 54 VEPGSNLLITGPNGSGKSSLFRVLGG-LWPLISGH--------IVKPGIGSDL--------NKEIF------YVPQRPYT 110
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGkLKPNLGKFddppdwdeILDEFRGSELqnyftkllEGDVKvivkpqYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 111 AVGTLRDQLiypltadqevEQLTDRGMV-ELLKNVDLEYLLDRyppekEVnwgDELSLGEQQRLGMARLFYHKPKFAILD 189
Cdd:cd03236 103 VKGKVGELL----------KKKDERGKLdELVDQLELRHVLDR-----NI---DQLSGGELQRVAIAAALARDADFYFFD 164
|
170
....*....|....*.
gi 1654042132 190 ECTSAVttDMEERFCA 205
Cdd:cd03236 165 EPSSYL--DIKQRLNA 178
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
31-234 |
3.28e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 46.75 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVV----TPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI------VKPGIGS----D 96
Cdd:PRK13641 3 IKFENVDYIyspgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyhITPETGNknlkK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 97 LNKEIFYVPQRPYTAV---GTLRDQLIYPLT---ADQEVEQltdrGMVELLKNVDL-EYLLDRYPpekevnwgDELSLGE 169
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLfenTVLKDVEFGPKNfgfSEDEAKE----KALKWLKKVGLsEDLISKSP--------FELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 170 QQRLGMARLFYHKPKFAILDECTSAV----TTDMEERFCAKVRAmGTSCITISHRPALVA-FHDVVLSLD 234
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLdpegRKEMMQLFKDYQKA-GHTVILVTHNMDDVAeYADDVLVLE 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
35-225 |
3.33e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.03 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 35 DVKVVTPTGNVL-VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLwpLISGHIVKpgiGSDL--NKEIFYVPQR---- 107
Cdd:PRK09473 19 RVTFSTPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL--LAANGRIG---GSATfnGREILNLPEKelnk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 108 ------------------PYTAVGtlrDQLIypltadqEVEQLtDRGM---------VELLKNVDLEYLLDR---YPpek 157
Cdd:PRK09473 94 lraeqismifqdpmtslnPYMRVG---EQLM-------EVLML-HKGMskaeafeesVRMLDAVKMPEARKRmkmYP--- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654042132 158 evnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSA--VT------TDMEErfcAKvRAMGTSCITISHRPALVA 225
Cdd:PRK09473 160 -----HEFSGGMRQRVMIAMALLCRPKLLIADEPTTAldVTvqaqimTLLNE---LK-REFNTAIIMITHDLGVVA 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
839-896 |
3.54e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 46.31 E-value: 3.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654042132 839 LSLGEQQRLGMARLFFHRPKYGILDECTNA----TSVDVEEHLYGLANKMGITVVTSSQRPA 896
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSAldpiSAGKIEETLLGLKDDYTMLLVTRSMQQA 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
47-190 |
3.80e-05 |
|
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: 46.00 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV--------KP-------GIGsdlnkeifYVPQRPYTA 111
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILldgqditkLPmhkrarlGIG--------YLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 112 VG-TLRDQLIYPL-TADQEVEQLTDRgMVELLKNVDLEYLLDRYppekevnwGDELSLGEQQRLGMARLFYHKPKFAILD 189
Cdd:cd03218 88 RKlTVEENILAVLeIRGLSKKEREEK-LEELLEEFHITHLRKSK--------ASSLSGGERRRVEIARALATNPKFLLLD 158
|
.
gi 1654042132 190 E 190
Cdd:cd03218 159 E 159
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
679-896 |
3.92e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 46.19 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 679 AKDAISFSKVDIVTPAQKMLaRELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPI------ASGGLSRPSEDVDQ--- 749
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAIL-KDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYFGKDIFQida 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 750 -EAGSGCGIFYVPQRPYTCLgTLRDQIIYPlsreeaefraLKMYGKGEKHaDPRKLLDTHLQiilenvRLNYLLERDNRg 828
Cdd:PRK14246 86 iKLRKEVGMVFQQPNPFPHL-SIYDNIAYP----------LKSHGIKEKR-EIKKIVEECLR------KVGLWKEVYDR- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654042132 829 wdanLNWEDT-LSLGEQQRLGMARLFFHRPKYGILDECTN----ATSVDVEEHLYGLANKMGITVVTSSQRPA 896
Cdd:PRK14246 147 ----LNSPASqLSGGQQQRLTIARALALKPKVLLMDEPTSmidiVNSQAIEKLITELKNEIAIVIVSHNPQQV 215
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
695-899 |
3.99e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 45.72 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 695 QKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLwpiasgglsrpsedvdQEAGSGCGIFYVPQRPYTCLGTLRDQ 774
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA----------------LKGTPVAGCVDVPDNQFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 775 IiYPLSREEAEFRALKMYGKGEkhadprklldthlqiilenvrlNYLLERDnrgwdanlnwEDTLSLGEQQRLGMARLFF 854
Cdd:COG2401 106 I-GRKGDFKDAVELLNAVGLSD----------------------AVLWLRR----------FKELSTGQKFRFRLALLLA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654042132 855 HRPKYGILDECTNA----TSVDVEEHLYGLANKMGITVVTSSQRP----ALIP 899
Cdd:COG2401 153 ERPKLLVIDEFCSHldrqTAKRVARNLQKLARRAGITLVVATHHYdvidDLQP 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
681-789 |
4.15e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.60 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 681 DAISFSKVDI-VTPAQKmlarELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWpiasgglsRPSEDVDQEAGSgcgIFY 759
Cdd:TIGR01271 427 DGLFFSNFSLyVTPVLK----NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGEL--------EPSEGKIKHSGR---ISF 491
|
90 100 110
....*....|....*....|....*....|
gi 1654042132 760 VPQRPYTCLGTLRDQIIYPLSREEAEFRAL 789
Cdd:TIGR01271 492 SPQTSWIMPGTIKDNIIFGLSYDEYRYTSV 521
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
43-79 |
4.82e-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: 46.85 E-value: 4.82e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGG 79
Cdd:TIGR03719 334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG 370
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
49-220 |
5.03e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.97 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 49 DLTLRvePGSNLLITGPNGSGKSSLFRVLGGLWP------LISGHIV---KPGIGSDLNkeIFYVPQRPytavgtlrdqL 119
Cdd:PRK15439 31 DFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPpdsgtlEIGGNPCarlTPAKAHQLG--IYLVPQEP----------L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 120 IYP-LTADQEV------EQLTDRGMVELLKNVDLEYLLDryppekeVNWGdELSLGEQQRLGMARLFYHKPKFAILDECT 192
Cdd:PRK15439 97 LFPnLSVKENIlfglpkRQASMQKMKQLLAALGCQLDLD-------SSAG-SLEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190
....*....|....*....|....*....|.
gi 1654042132 193 SAVTTDMEERFCAKVRAM---GTSCITISHR 220
Cdd:PRK15439 169 ASLTPAETERLFSRIRELlaqGVGIVFISHK 199
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
49-221 |
5.06e-05 |
|
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: 45.56 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 49 DLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIgsdlnkEIFYVP--QRPYTAVgtLRDQLIYP-LTA 125
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV------DVTAAPpaDRPVSML--FQENNLFAhLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 126 DQEVE-------QLT--DRGMVE-LLKNVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAV 195
Cdd:cd03298 88 EQNVGlglspglKLTaeDRQAIEvALARVGLAGLEKRLP--------GELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190
....*....|....*....|....*....|
gi 1654042132 196 ----TTDMEERFCAKVRAMGTSCITISHRP 221
Cdd:cd03298 160 dpalRAEMLDLVLDLHAETKMTVLMVTHQP 189
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
35-210 |
5.06e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 35 DVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGSD--LNKE-IFYVPQRP--- 108
Cdd:PRK15056 11 DVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqaLQKNlVAYVPQSEevd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 109 ---------------YTAVGTLRdqliYPLTADQEVeqltdrgMVELLKNVD-LEYlldRYppeKEVNwgdELSLGEQQR 172
Cdd:PRK15056 91 wsfpvlvedvvmmgrYGHMGWLR----RAKKRDRQI-------VTAALARVDmVEF---RH---RQIG---ELSGGQKKR 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 1654042132 173 LGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAM 210
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL 188
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
48-220 |
5.09e-05 |
|
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: 47.12 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 48 DDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI---------VKPgigSDLNKEIFYVPQRPytaV---GTL 115
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdirdVTQ---ASLRAAIGIVPQDT---VlfnDTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 116 RDQLIY--PLTADQEVE------QLTDrgMVELLKnvdleyllDRYppEKEVnwGD---ELSLGEQQRLGMARLFYHKPK 184
Cdd:COG5265 449 AYNIAYgrPDASEEEVEaaaraaQIHD--FIESLP--------DGY--DTRV--GErglKLSGGEKQRVAIARTLLKNPP 514
|
170 180 190
....*....|....*....|....*....|....*...
gi 1654042132 185 FAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHR 220
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVarGRTTLVIAHR 552
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
46-193 |
5.67e-05 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 44.85 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 46 LVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGL--WPLISGHIVKPGIGSDLN---KEIFYVPQrpytavgtlRDQLI 120
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRsfrKIIGYVPQ---------DDILH 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654042132 121 YPLTADQEVEqltdrgMVELLKNvdleylldryppekevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECTS 193
Cdd:cd03213 95 PTLTVRETLM------FAAKLRG---------------------LSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
36-195 |
5.73e-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: 47.32 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 36 VKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGSDLNKEIFyvpqRPYTAVGTL 115
Cdd:TIGR01257 935 VKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV----RQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 116 RDQLIYPLTADQEV---EQLTDRGMVEllKNVDLEYLL-DRYPPEKEVNWGDELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:TIGR01257 1011 HNILFHHLTVAEHIlfyAQLKGRSWEE--AQLEMEAMLeDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
....
gi 1654042132 192 TSAV 195
Cdd:TIGR01257 1089 TSGV 1092
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
48-74 |
6.76e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 41.43 E-value: 6.76e-05
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
716-864 |
9.59e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.88 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 716 GPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVD---QEAGSGCGIFYVPQrpytclgtlrdqiiyplsrEEAEFRALKMY 792
Cdd:PRK10895 36 GPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllpLHARARRGIGYLPQ-------------------EASIFRRLSVY 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654042132 793 GKGEKHADPRKLLDTHLQiileNVRLNYLLE-------RDNRGwdanlnweDTLSLGEQQRLGMARLFFHRPKYGILDE 864
Cdd:PRK10895 97 DNLMAVLQIRDDLSAEQR----EDRANELMEefhiehlRDSMG--------QSLSGGERRRVEIARALAANPKFILLDE 163
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-176 |
1.06e-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: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFyDVKVVT--PTGNVLV---------DDLTLRVEPGS-----NLLITGPNGSGKSSLFRVLGGlwplisghIVKPGIG 94
Cdd:COG1245 325 IEF-EVHAPRreKEEETLVeypdltksyGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAG--------VLKPDEG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 95 S-DLNKEIFYVPQRpytavgtlrdqliypLTADQE--VEQLTDRGM----------VELLKNVDLEYLLDryppeKEVnw 161
Cdd:COG1245 396 EvDEDLKISYKPQY---------------ISPDYDgtVEEFLRSANtddfgssyykTEIIKPLGLEKLLD-----KNV-- 453
|
170
....*....|....*
gi 1654042132 162 gDELSLGEQQRLGMA 176
Cdd:COG1245 454 -KDLSGGELQRVAIA 467
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
43-89 |
1.10e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 1.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIV 89
Cdd:PRK11819 336 DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK 382
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
700-904 |
1.14e-04 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 44.28 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 700 RELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGS-GCGIFYVPQRPytclgTLRDQIIyp 778
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQDL-----SVDDELT-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 779 lSREEAEFRAlKMYGKGEKHADPRklldthlqiILENVRLNYLLERDNRgwdanlnWEDTLSLGEQQRLGMARLFFHRPK 858
Cdd:cd03265 90 -GWENLYIHA-RLYGVPGAERRER---------IDELLDFVGLLEAADR-------LVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1654042132 859 YGILDECTNATSVDVEEHLYGLANKM----GITVvtssqrpaLIPYHSME 904
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLkeefGMTI--------LLTTHYME 193
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
704-742 |
1.20e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 45.31 E-value: 1.20e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1654042132 704 CDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSR 742
Cdd:COG4637 16 LELPLGPLTVLIGANGSGKSNLLDALRFLSDAARGGLQD 54
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
683-874 |
1.26e-04 |
|
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: 44.40 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 683 ISFSKVDI-VTPAQKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSED---VDQEAGSGcGIF 758
Cdd:cd03252 1 ITFEHVRFrYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlalADPAWLRR-QVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 759 YVPQRPYTCLGTLRDQIIYP---LSREEAEFRAlKMYGKgekHADPRKLLDTHLQIILEnvrlnyllerdnRGwdanlnw 835
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALAdpgMSMERVIEAA-KLAGA---HDFISELPEGYDTIVGE------------QG------- 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 1654042132 836 eDTLSLGEQQRLGMARLFFHRPKYGILDECTNATSVDVE 874
Cdd:cd03252 137 -AGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
716-871 |
1.64e-04 |
|
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: 43.90 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 716 GPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQ---EAGSGCGIFYVPQRPYTCLgTLRDQIIYplsreeaeFRALkmY 792
Cdd:cd03266 38 GPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepaEARRRLGFVSDSTGLYDRL-TARENLEY--------FAGL--Y 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 793 G-KG-EKHADPRKLLDThlqiilenVRLNYLLERDNRGwdanlnwedtLSLGEQQRLGMARLFFHRPKYGILDECTNATS 870
Cdd:cd03266 107 GlKGdELTARLEELADR--------LGMEELLDRRVGG----------FSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
.
gi 1654042132 871 V 871
Cdd:cd03266 169 V 169
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
706-853 |
1.73e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.85 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 706 IELGRSL-LVTGPNGSGKSSIFRVLR-GLWpiasGGLSRPSEDVDQEAGSGCGIFYVpqrpytCLGTLRDQIIYPLSREE 783
Cdd:COG0419 19 IDFDDGLnLIVGPNGAGKSTILEAIRyALY----GKARSRSKLRSDLINVGSEEASV------ELEFEHGGKRYRIERRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 784 AEFRALKMYGKGEKHADPRKLLDTH-LQIILENVR-LNYLLERDNRGWDANLNWE-------------DTLSLGEQQRLG 848
Cdd:COG0419 89 GEFAEFLEAKPSERKEALKRLLGLEiYEELKERLKeLEEALESALEELAELQKLKqeilaqlsgldpiETLSGGERLRLA 168
|
....*
gi 1654042132 849 MARLF 853
Cdd:COG0419 169 LADLL 173
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
44-194 |
2.09e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 44 NVLVDDLTLRVEPGSNLLITGPNGSGKSS----LFRVL---GGLW----PLisgHIVKPGIGSDLNKEIFYVPQRPYTAV 112
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsqGEIWfdgqPL---HNLNRRQLLPVRHRIQVVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 113 GTLRD--QLI-------YPLTADQEVEQLTDRGMVELLKNVDLEYlldRYPPEkevnwgdeLSLGEQQRLGMARLFYHKP 183
Cdd:PRK15134 376 NPRLNvlQIIeeglrvhQPTLSAAQREQQVIAVMEEVGLDPETRH---RYPAE--------FSGGQRQRIAIARALILKP 444
|
170
....*....|.
gi 1654042132 184 KFAILDECTSA 194
Cdd:PRK15134 445 SLIILDEPTSS 455
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
43-172 |
2.25e-04 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 43.92 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSnllIT---GPNGSGKSSLFRVLGGLWPLISGHIVKPGI------GSDLNKEIFYVPQRPYTAVG 113
Cdd:COG4604 13 GKVVLDDVSLTIPKGG---ITaliGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattpSRELAKRLAILRQENHINSR 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 114 -TLRDqLI----YP-----LTADqeveqltDRGMV-ELLKNVDLEYLLDRYPpekevnwgDELSLGEQQR 172
Cdd:COG4604 90 lTVRE-LVafgrFPyskgrLTAE-------DREIIdEAIAYLDLEDLADRYL--------DELSGGQRQR 143
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
62-190 |
2.86e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.09 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 62 ITGPNGSGKSSLFRVLGGLWPLISGHIVKPG-IGSDLNKEIF---------YVPQ--R--P-YTAVGTLRdqliYPLtAD 126
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGIClppekrrigYVFQdaRlfPhYKVRGNLR----YGM-AK 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654042132 127 QEVEQLTDrgMVELLknvDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:PRK11144 104 SMVAQFDK--IVALL---GIEPLLDRYP--------GSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
43-200 |
2.95e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGhIVKpgiGSDlNKEIFYVPQRPYTAVG---TLRD-- 117
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG-TVK---WSE-NANIGYYAQDHAYDFEndlTLFDwm 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 118 -QLIYPLTADQEVeqltdRGMV-ELLKNVDleylldryPPEKEVNwgdELSLGEQQRLGMARLFYHKPKFAILDECTSAV 195
Cdd:PRK15064 406 sQWRQEGDDEQAV-----RGTLgRLLFSQD--------DIKKSVK---VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHM 469
|
....*
gi 1654042132 196 ttDME 200
Cdd:PRK15064 470 --DME 472
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
146-252 |
3.06e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 146 LEYLLDRYPPEKEVN---WGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDME---ERFCAKVRAMG-TSCITIS 218
Cdd:PTZ00265 1337 IDEFIESLPNKYDTNvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEkliEKTIVDIKDKAdKTIITIA 1416
|
90 100 110
....*....|....*....|....*....|....
gi 1654042132 219 HRPALVAFHDVVLSLDGEGGWSVHYKREGSSTEM 252
Cdd:PTZ00265 1417 HRIASIKRSDKIVVFNNPDRTGSFVQAHGTHEEL 1450
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-255 |
3.09e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 43.59 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 27 EANYIEFYDVKVVTPTGNVL-VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI------VKPGIGSDLNK 99
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 100 EIFYVPQRPYTA-VGTLrdqLIYPLTADQEVEQLTDRGMV----ELLKNVDleyLLDRYPPEKEvnwgdELSLGEQQRLG 174
Cdd:PRK13648 84 HIGIVFQNPDNQfVGSI---VKYDVAFGLENHAVPYDEMHrrvsEALKQVD---MLERADYEPN-----ALSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 175 MARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAM----GTSCITISH--RPALVAFHDVVLSlDG----EGGWSVHYK 244
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITHdlSEAMEADHVIVMN-KGtvykEGTPTEIFD 231
|
250
....*....|.
gi 1654042132 245 REGSSTEMGID 255
Cdd:PRK13648 232 HAEELTRIGLD 242
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
47-193 |
3.35e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 43.54 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGhIVKPGiGSDLNKEIFYVPQRPYTAVGTLRDQLIYPLTAD 126
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG-KVKID-GELLTAENVWNLRRKIGMVFQNPDNQFVGATVE 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 127 QEVE-QLTDRGMV--ELLKNVDlEYLLDRYPPEKEVNWGDELSLGEQQRLGMARLFYHKPKFAILDECTS 193
Cdd:PRK13642 101 DDVAfGMENQGIPreEMIKRVD-EALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
415-878 |
3.44e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.58 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 415 IRLTQHLLKNYLRNnsfyKVFHMASKNIDADQRITHDLEKLTTDLSGLVTGMVkpsvdilwftwrmkLLTGQRGVAILYA 494
Cdd:PLN03232 385 LRLTHEARKNFASG----KVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMV--------------LLYQQLGVASLFG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 495 YMLLGLgflrtVTPDFGDLISQEQQL--EGTFR------FMHERLCThAESVAFFGGgtrEKTMvESRFRELLSHSNYLL 566
Cdd:PLN03232 447 SLILFL-----LIPLQTLIVRKMRKLtkEGLQWtdkrvgIINEILAS-MDTVKCYAW---EKSF-ESRIQGIRNEELSWF 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 567 KKKWLFGILDDFITKQLPHNVTwLLSLLYAMEHKGD----RA--SISTQGELAHALRFLASVVSQSFLAFgdiLELHRkf 640
Cdd:PLN03232 517 RKAQLLSAFNSFILNSIPVVVT-LVSFGVFVLLGGDltpaRAftSLSLFAVLRSPLNMLPNLLSQVVNAN---VSLQR-- 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 641 velsgginrifeLEELLDAAQSVDSINGSITPSMRDYYAKDAiSFSkVDIVTpaQKMLARELTCDIELGRSLLVTGPNGS 720
Cdd:PLN03232 591 ------------IEELLLSEERILAQNPPLQPGAPAISIKNG-YFS-WDSKT--SKPTLSDINLEIPVGSLVAIVGGTGE 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 721 GKSSIFRVLRGLWPiasgglsrPSEDVDQEA-GSgcgIFYVPQRPYTCLGTLRDQIIYPlSREEAEfralkMYGKGekha 799
Cdd:PLN03232 655 GKTSLISAMLGELS--------HAETSSVVIrGS---VAYVPQVSWIFNATVRENILFG-SDFESE-----RYWRA---- 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 800 dprklLD-THLQIILENVRLNYLLERDNRGWDanlnwedtLSLGEQQRLGMARLFFHRPKYGILDECTNATSVDVEEHLY 878
Cdd:PLN03232 714 -----IDvTALQHDLDLLPGRDLTEIGERGVN--------ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
683-908 |
3.58e-04 |
|
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: 42.78 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 683 ISFSKVDIVTPAQKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSgcgifyvpQ 762
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGR--------A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 763 RPY--TCLGTLRDQIIYPLSREEAEFRALKMYGKGEKHADPRKlldtHLQIILENVRLNyllerdnrgwDANLNWEDTLS 840
Cdd:cd03292 73 IPYlrRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRK----RVPAALELVGLS----------HKHRALPAELS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654042132 841 LGEQQRLGMARLFFHRPKYGILDECTN----ATSVDVEEHLYGLaNKMGITVVTSSQRPALipYHSMELRLI 908
Cdd:cd03292 139 GGEQQRVAIARAIVNSPTILIADEPTGnldpDTTWEIMNLLKKI-NKAGTTVVVATHAKEL--VDTTRHRVI 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
47-225 |
3.86e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 43.90 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKS----SLFRVLGGLWPLISGHIVKPGI------GSDLNK----EIFYVPQRPYTA- 111
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQdllglsERELRRirgnRIAMIFQEPMTSl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 112 --VGTLRDQLIYPLTADQEV--EQLTDRgMVELLKNV---DLEYLLDRYPpekevnwgDELSLGEQQR--LGMARLfyHK 182
Cdd:COG4172 106 npLHTIGKQIAEVLRLHRGLsgAAARAR-ALELLERVgipDPERRLDAYP--------HQLSGGQRQRvmIAMALA--NE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1654042132 183 PKFAILDECTSA--VTT---------DMeerfcakVRAMGTSCITISHRPALVA 225
Cdd:COG4172 175 PDLLIADEPTTAldVTVqaqildllkDL-------QRELGMALLLITHDLGVVR 221
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
698-864 |
4.39e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 43.48 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 698 LARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSGCGIFYVPQRpYTclgtlrdqiIY 777
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQS-YA---------LY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 778 P-LSREEAEFRALKMYGKGEKHADPRklldthLQIILENVRLNYLLERDNRgwdanlnwedTLSLGEQQRLGMARLFFHR 856
Cdd:PRK11000 88 PhLSVAENMSFGLKLAGAKKEEINQR------VNQVAEVLQLAHLLDRKPK----------ALSGGQRQRVAIGRTLVAE 151
|
....*...
gi 1654042132 857 PKYGILDE 864
Cdd:PRK11000 152 PSVFLLDE 159
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
713-893 |
4.56e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 42.78 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 713 LVTGPNGSGKSSIFRVLRGLWPIASGGL--------SRPSEDVDQEagsgcgIFYVPQRPYTCLGTLRDQIIYPlsreea 784
Cdd:PRK10247 37 LITGPSGCGKSTLLKIVASLISPTSGTLlfegedisTLKPEIYRQQ------VSYCAQTPTLFGDTVYDNLIFP------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 785 efralkmYGKGEKHADPRKLLDTHLQIILENVRLnyllerdnrgwDANLNwedTLSLGEQQRLGMARLFFHRPKYGILDE 864
Cdd:PRK10247 105 -------WQIRNQQPDPAIFLDDLERFALPDTIL-----------TKNIA---ELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1654042132 865 CTNATSVD----VEEHLYGLANKMGITV--VTSSQ 893
Cdd:PRK10247 164 ITSALDESnkhnVNEIIHRYVREQNIAVlwVTHDK 198
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
705-864 |
6.04e-04 |
|
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: 42.28 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 705 DIELGRSLLVT--GPNGSGKSSIFRVLRGLWPIASG-----G---LSRPSEDVdqeagSGCGIFYVPQrpytclgtlRDQ 774
Cdd:COG0410 23 SLEVEEGEIVAllGRNGAGKTTLLKAISGLLPPRSGsirfdGediTGLPPHRI-----ARLGIGYVPE---------GRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 775 IIYPLSREEaefrALKMygkGEKHADPRKLLDTHLQIILEnvrlnY---LLER-DNRGWdanlnwedTLSLGEQQRLGMA 850
Cdd:COG0410 89 IFPSLTVEE----NLLL---GAYARRDRAEVRADLERVYE-----LfprLKERrRQRAG--------TLSGGEQQMLAIG 148
|
170
....*....|....
gi 1654042132 851 RLFFHRPKYGILDE 864
Cdd:COG0410 149 RALMSRPKLLLLDE 162
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
31-219 |
7.73e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.04 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 31 IEFYDVKVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIGSDLNKEIFYvpQRPYT 110
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY--RKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 111 AVGT---LRDQLIYP---LTADQEVEQLTDR-GMVELLKNVDLEYLLDRyppekevnwgdeLSLGEQQRLGMARLFYHKP 183
Cdd:PRK10522 401 AVFTdfhLFDQLLGPegkPANPALVEKWLERlKMAHKLELEDGRISNLK------------LSKGQKKRLALLLALAEER 468
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1654042132 184 KFAILDECtsAVTTD-MEERFCAKV-----RAMGTSCITISH 219
Cdd:PRK10522 469 DILLLDEW--AADQDpHFRREFYQVllpllQEMGKTIFAISH 508
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-190 |
9.39e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 26 SEANYIEFYDVkVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPL-ISGHIV----KPGIGS---DL 97
Cdd:PRK10938 256 ANEPRIVLNNG-VVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQgYSNDLTlfgrRRGSGEtiwDI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 98 NKEIFYVPQR---PYTAVGTLRDQL---------IYPLTADQEvEQLTDR-----GMVELLKNvdleylldryPPEKEVN 160
Cdd:PRK10938 335 KKHIGYVSSSlhlDYRVSTSVRNVIlsgffdsigIYQAVSDRQ-QKLAQQwldilGIDKRTAD----------APFHSLS 403
|
170 180 190
....*....|....*....|....*....|.
gi 1654042132 161 WGdelslgeQQRLGM-ARLFYHKPKFAILDE 190
Cdd:PRK10938 404 WG-------QQRLALiVRALVKHPTLLILDE 427
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
45-193 |
1.06e-03 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 42.10 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 45 VLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGlwplisghIVKPGIGS-DLNKEIfyVPQRPYTA---VG------- 113
Cdd:PRK13537 21 LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLG--------LTHPDAGSiSLCGEP--VPSRARHArqrVGvvpqfdn 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 114 -----TLRDQLI-----YPLTADQEveqltdRGMVELLknvdLEYLLDRYPPEKEVNwgdELSLGEQQRLGMARLFYHKP 183
Cdd:PRK13537 91 ldpdfTVRENLLvfgryFGLSAAAA------RALVPPL----LEFAKLENKADAKVG---ELSGGMKRRLTLARALVNDP 157
|
170
....*....|
gi 1654042132 184 KFAILDECTS 193
Cdd:PRK13537 158 DVLVLDEPTT 167
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
709-895 |
1.15e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.68 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 709 GRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLS---RPSEDVDQEAGSGCGIFYVPQ-RPytclgtlRDQIIYPLS-REE 783
Cdd:PRK10762 278 GEILGVSGLMGAGRTELMKVLYGALPRTSGYVTldgHEVVTRSPQDGLANGIVYISEdRK-------RDGLVLGMSvKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 784 AEFRALKMYGKGE---KHADPRKLLDTHlqIILENVRlnylleRDNRGWDANLnwedtLSLGEQQRLGMARLFFHRPKYG 860
Cdd:PRK10762 351 MSLTALRYFSRAGgslKHADEQQAVSDF--IRLFNIK------TPSMEQAIGL-----LSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1654042132 861 ILDECTNATSVDVEEHLYGLANK-----MGITVVtSSQRP 895
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQfkaegLSIILV-SSEMP 456
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
47-195 |
1.26e-03 |
|
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: 41.16 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI-------VKPGIGSDLNKE---IFYVPQRPYTAVGTLR 116
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkneSEPSFEATRSRNrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 117 DQLIY--PLTaDQEVEQLTDrgMVELLKNVDLEYLLDRYP-PEKEVNwgdeLSLGEQQRLGMARLFYHKPKFAILDECTS 193
Cdd:cd03290 97 ENITFgsPFN-KQRYKAVTD--ACSLQPDIDLLPFGDQTEiGERGIN----LSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
..
gi 1654042132 194 AV 195
Cdd:cd03290 170 AL 171
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-195 |
1.43e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 42.69 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 37 KVVTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGIG-----SDLNKEIFYVPQrpYTA 111
Cdd:TIGR01257 1945 KVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltniSDVHQNMGYCPQ--FDA 2022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 112 VGTL---RDQL-IYPL---TADQEVEQLTDRGMVELLKNVDLEYLLDRYppekevnwgdelSLGEQQRLGMARLFYHKPK 184
Cdd:TIGR01257 2023 IDDLltgREHLyLYARlrgVPAEEIEKVANWSIQSLGLSLYADRLAGTY------------SGGNKRKLSTAIALIGCPP 2090
|
170
....*....|.
gi 1654042132 185 FAILDECTSAV 195
Cdd:TIGR01257 2091 LVLLDEPTTGM 2101
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-225 |
1.46e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 41.62 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 43 GNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI----VKPGIGSDLN--------KEIFYVPQRPYT 110
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRysgdVLLGGRSIFNyrdvlefrRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 111 AVGTLRDQLIYPLTADQEVEQLTDRGMVEL-LKNVDL-EYLLDRYPPEKEvnwgdELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:PRK14271 113 FPMSIMDNVLAGVRAHKLVPRKEFRGVAQArLTEVGLwDAVKDRLSDSPF-----RLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 1654042132 189 DECTSAVTTDMEERFCAKVRAMGT--SCITISHRPALVA 225
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAA 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
694-889 |
1.47e-03 |
|
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: 40.63 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 694 AQKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSgcgifyvpqrpytcLGTLRD 773
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE--------------LPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 774 QIIYplsreeaefralkMYGKGEkhadprklLDTHLQiILENVRLnyllerdnrgwdanlnwedTLSLGEQQRLGMARLF 853
Cdd:cd03229 77 RIGM-------------VFQDFA--------LFPHLT-VLENIAL-------------------GLSGGQQQRVALARAL 115
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1654042132 854 FHRPKYGILDECTNA----TSVDVEEHLYGLANKMGITVV 889
Cdd:cd03229 116 AMDPDVLLLDEPTSAldpiTRREVRALLKSLQAQLGITVV 155
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
47-195 |
1.92e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.03 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP------LISGHIVKPGigsDLN--KEIFYVPQ--RPYTAVgTLR 116
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPasegeaWLFGQPVDAG---DIAtrRRVGYMSQafSLYGEL-TVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 117 DQL-----IYPLTADQ---EVEQLTDRgmvellknVDLEYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:NF033858 358 QNLelharLFHLPAAEiaaRVAEMLER--------FDLADVADALP--------DSLPLGIRQRLSLAVAVIHKPELLIL 421
|
....*..
gi 1654042132 189 DECTSAV 195
Cdd:NF033858 422 DEPTSGV 428
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
716-864 |
1.98e-03 |
|
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: 40.99 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 716 GPNGSGKSSIFRVLRGLWPIASGGLSRPSEDV-----DQEAGSGCGifYVPQRPytclgtlrdQIIYPLSREEAEFRALk 790
Cdd:cd03218 33 GPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItklpmHKRARLGIG--YLPQEA---------SIFRKLTVEENILAVL- 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654042132 791 mygkgEKHADPRKLLDTHLQIILENVRLNYLleRDNRGwdanlnweDTLSLGEQQRLGMARLFFHRPKYGILDE 864
Cdd:cd03218 101 -----EIRGLSKKEREEKLEELLEEFHITHL--RKSKA--------SSLSGGERRRVEIARALATNPKFLLLDE 159
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
49-88 |
2.15e-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: 41.71 E-value: 2.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1654042132 49 DLTLRvePGSNLLITGPNGSGKSSLFRVLGGLWPLISGHI 88
Cdd:COG4615 352 DLTIR--RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
39-198 |
2.42e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.54 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 39 VTPTGNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVLGGL--WPLISGHIVKPgiGSDL---------NKEIFYVPQR 107
Cdd:PRK09580 9 VSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFK--GKDLlelspedraGEGIFMAFQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 108 PYTAVGtLRDQLiYPLTADQEVEQLTDRgmvELLKNVDLEYLLD------RYPPE---KEVNWGdeLSLGEQQR---LGM 175
Cdd:PRK09580 87 PVEIPG-VSNQF-FLQTALNAVRSYRGQ---EPLDRFDFQDLMEekiallKMPEDlltRSVNVG--FSGGEKKRndiLQM 159
|
170 180
....*....|....*....|...
gi 1654042132 176 ARLfyhKPKFAILDECTSAVTTD 198
Cdd:PRK09580 160 AVL---EPELCILDESDSGLDID 179
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
47-225 |
2.55e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.88 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 47 VDDLTLRVEPGSNLLITGPNGSGKS--SLfrvlgglwpLISGHIVKPGI---------GSDLNK------------EIFY 103
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSvsSL---------AIMGLIDYPGRvmaeklefnGQDLQRisekerrnlvgaEVAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 104 VPQRPYTAVG---TLRDQLIYPLTADQEVEQLTDRG-MVELLKNV---DLEYLLDRYPpekevnwgDELSLGEQQRLGMA 176
Cdd:PRK11022 94 IFQDPMTSLNpcyTVGFQIMEAIKVHQGGNKKTRRQrAIDLLNQVgipDPASRLDVYP--------HQLSGGMSQRVMIA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654042132 177 RLFYHKPKFAILDECTSA--VTTDME--ERFCAKVRAMGTSCITISHRPALVA 225
Cdd:PRK11022 166 MAIACRPKLLIADEPTTAldVTIQAQiiELLLELQQKENMALVLITHDLALVA 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
813-911 |
2.58e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 40.53 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 813 LENVRLNYLL----ERDNRGWDANL-----------NWEDTLSLGEQQRLGMARLFFHRPKYGILDECTN----ATSVDV 873
Cdd:PRK10584 106 LENVELPALLrgesSRQSRNGAKALleqlglgkrldHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGnldrQTGDKI 185
|
90 100 110
....*....|....*....|....*....|....*...
gi 1654042132 874 EEHLYGLANKMGITVVTSSQRPALIPYHSMELRLIDGE 911
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQ 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
123-269 |
2.94e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.55 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 123 LTADQEVEQLTDRGMVELLKNVDLEYLLDRYPPEKEVNWGD---ELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDM 199
Cdd:PTZ00265 535 IEMRKNYQTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1654042132 200 EERFCAKVRAMGTS----CITISHRPALVAFHDVVLSLDgeggwsvhyKREGSSTE----MGIDTMKASETKRQSDAK 269
Cdd:PTZ00265 615 EYLVQKTINNLKGNenriTIIIAHRLSTIRYANTIFVLS---------NRERGSTVdvdiIGEDPTKDNKENNNKNNK 683
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
694-868 |
3.42e-03 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 40.10 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 694 AQKMLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLS---RPSEDVDQEAGSGC-GIfyVPQR-----P 764
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngRPLAAWSPWELARRrAV--LPQHsslafP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 765 YTCLgtlrdQII----YPLSREEAEFRALkmygkgekhadprklldthLQIILENVRLNYLLERDNRgwdanlnwedTLS 840
Cdd:COG4559 90 FTVE-----EVValgrAPHGSSAAQDRQI-------------------VREALALVGLAHLAGRSYQ----------TLS 135
|
170 180 190
....*....|....*....|....*....|....*
gi 1654042132 841 LGEQQRLGMARLF-------FHRPKYGILDECTNA 868
Cdd:COG4559 136 GGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSA 170
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
655-789 |
3.58e-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: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 655 ELLDAAQSvdSINGSITPSmrdyyAKDAISFSKVDI-VTPaqkmLARELTCDIELGRSLLVTGPNGSGKSSIFRVLRGLW 733
Cdd:cd03291 19 ELLEKAKQ--ENNDRKHSS-----DDNNLFFSNLCLvGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGEL 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1654042132 734 piasgglsRPSEDVDQEAGSgcgIFYVPQRPYTCLGTLRDQIIYPLSREEAEFRAL 789
Cdd:cd03291 88 --------EPSEGKIKHSGR---ISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
54-207 |
3.60e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 54 VEPGSNLLITGPNGSGKSSLFRVL-GGLWPLISGHIVKPGI--------GSDL--------NKEIF------YVPQRPYT 110
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsGELIPNLGDYEEEPSWdevlkrfrGTELqnyfkklyNGEIKvvhkpqYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 111 AVGTLRDQLiypltadqevEQLTDRGMV-ELLKNVDLEYLLDRyppekEVnwgDELSLGEQQRLGMARLFYHKPKFAILD 189
Cdd:PRK13409 176 FKGKVRELL----------KKVDERGKLdEVVERLGLENILDR-----DI---SELSGGELQRVAIAAALLRDADFYFFD 237
|
170
....*....|....*....
gi 1654042132 190 ECTSAVttDMEERF-CAKV 207
Cdd:PRK13409 238 EPTSYL--DIRQRLnVARL 254
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
706-889 |
5.21e-03 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 39.37 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 706 IELGRSLLVTGPNGSGKSSIFRVLRGLWPIASGGLSRPSEDVDQEAGSGCGIFyvpqRPYTCLG--TLRDQIIYPLSRee 783
Cdd:TIGR01184 8 IQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVF----QNYSLLPwlTVRENIALAVDR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 784 aefrALKMYGKGEKhadpRKLLDTHLQIIleNVRlnyllerdnrgwDANLNWEDTLSLGEQQRLGMARLFFHRPKYGILD 863
Cdd:TIGR01184 82 ----VLPDLSKSER----RAIVEEHIALV--GLT------------EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190
....*....|....*....|....*....|
gi 1654042132 864 ECTNA----TSVDVEEHLYGLANKMGITVV 889
Cdd:TIGR01184 140 EPFGAldalTRGNLQEELMQIWEEHRVTVL 169
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
48-74 |
5.31e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.02 E-value: 5.31e-03
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
49-193 |
6.47e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 39.73 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 49 DLTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWPLISGHIVKPGI---GSDLNKEI----------FYVPQRPYTAVGTL 115
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitSTSKNKDIkqirkkvglvFQFPESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 116 RDQLIYPLT---ADQEVEQLTDrgmvELLKNVDL-EYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:PRK13649 105 KDVAFGPQNfgvSQEEAEALAR----EKLALVGIsESLFEKNP--------FELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
..
gi 1654042132 192 TS 193
Cdd:PRK13649 173 TA 174
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
34-243 |
6.89e-03 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 38.76 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 34 YDVKVVTPTgNVLVDDLTLRVEPGSNLLITGPNGSGKSSLFRVL-----GGlwpLISGHIVKPG--IGSDLNKEIFYVPQ 106
Cdd:cd03232 11 YTVPVKGGK-RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAG---VITGEILINGrpLDKNFQRSTGYVEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 107 RP-YTAVGTLRDQLIYplTADQeveqltdRGmvellknvdleylldryppekevnwgdeLSLGEQQRLGMARLFYHKPKF 185
Cdd:cd03232 87 QDvHSPNLTVREALRF--SALL-------RG----------------------------LSVEQRKRLTIGVELAAKPSI 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654042132 186 AILDECTS---AVTTDMEERFCAKVRAMGTSCITISHRPALVAFH--DVVLSLDgEGGWSVHY 243
Cdd:cd03232 130 LFLDEPTSgldSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEkfDRLLLLK-RGGKTVYF 191
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
839-889 |
7.34e-03 |
|
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: 38.18 E-value: 7.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1654042132 839 LSLGEQQRLGMARLFFHRPKYGILDECTNATSVDVEEHLYGLANKM---GITVV 889
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraqGVAVI 136
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
50-179 |
9.20e-03 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 39.05 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654042132 50 LTLRVEPGSNLLITGPNGSGKSSLFRVLGGLWP-----LISGHIVKPGIGSDLNKEIFYVPQRPYTAVGTLRDQLI---- 120
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPgqgeiLLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLalhq 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1654042132 121 YPLTADQEVEQLtdrgMVELLKNVDLEYLLDRyppekEVNwgdELSLGEQQRLGMARLF 179
Cdd:COG4138 95 PAGASSEAVEQL----LAQLAEALGLEDKLSR-----PLT---QLSGGEWQRVRLAAVL 141
|
|
| |
