|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-681 |
0e+00 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 985.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 1 MPVLSTPRPSRVTTLKRTAVVLALTAYGVHKIYPLVRQCLTPARGPQVPAGEPTQEASGAT----ATKAGMNRVFLQRLL 76
Cdd:TIGR00954 1 MAVLSKYRLLRSTSNNKTDKQDSPAAVGMNKVIELKRERAADRRGDKSGKEELTIVGKHSTiegaKKKAHVNGVFLGKLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 77 ALLRLLFPRVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFSWQLLQWLLIALPATFINSAIRYLEG 156
Cdd:TIGR00954 81 FLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 157 QLALSFRSRLVAHAYGLYFSQQTYYRVSNMDGRLRNPDQSLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSR 236
Cdd:TIGR00954 161 ELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTALGSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 237 GAGTAWPSaiaglvVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQHSYQDLASQ 316
Cdd:TIGR00954 241 GPAGLFAY------LFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 317 INLILLERLWYVMLEQFLMKYVWSASGLLMVAVPIITATgyaesdseamKKAALEMKEEELVSErteaFTIARNLLTAAA 396
Cdd:TIGR00954 315 LNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKT----------HPAFLEMSEEELMQE----FYNNGRLLLKAA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 397 DATERIMSSYKEVTELAGYTARVYEMFQVFEDVKHCRFKRTGDLEEAQAGPGVmvQSGVHVEGplkiQGQVVDVEQGIIC 476
Cdd:TIGR00954 381 DALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREGG--RNSNLVPG----RGIVEYQDNGIKF 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 477 ENIPIITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYKPPPQRMFYIPQRPYMSVGSLRDQ 556
Cdd:TIGR00954 455 ENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 557 VIYPDSAEDMRRKGCSEQQLEAILGIVHLRHILQREGGWEAVCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVS 636
Cdd:TIGR00954 535 IIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 6671497 637 IDVEGKIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGGWKF 681
Cdd:TIGR00954 615 VDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
83-352 |
2.34e-119 |
|
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: 358.85 E-value: 2.34e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 83 FPRVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFSWQLLQWLLIALPATFINSAIRYLEGQLALSF 162
Cdd:pfam06472 6 FPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQRLALRF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 163 RSRLVAHAYGLYFSQQTYYRVSNMDGRLRNPDQSLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSRGAgtaw 242
Cdd:pfam06472 86 RTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRGP---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 243 psAIAGLVVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQHSYQDLASQINLILL 322
Cdd:pfam06472 162 --AILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILR 239
|
250 260 270
....*....|....*....|....*....|
gi 6671497 323 ERLWYVMLEQFLMKYVWSASGLLMVAVPII 352
Cdd:pfam06472 240 RRLWYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
122-688 |
1.04e-85 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 281.70 E-value: 1.04e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 122 IVRKDPRAFSWQLLQWLLIALPATFINSAIRYLEGQLALSFRSRLVAHAYGLYFSQQTYYRVSNMDGRLRNPDQSLTEDV 201
Cdd:COG4178 55 LQARDAAAFWQQLGVFALLAAISILLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 202 VAFAASVAHLYSNLtkplLDVAVT--SYT-----LLRAARSRGAGTAWpsAIAGLVVF------LTANVLrAFspKFG-- 266
Cdd:COG4178 135 RLFTETTLSLSLGL----LSSVVTliSFIgilwsLSGSLTFTLGGYSI--TIPGYMVWaaliyaIIGTLL-TH--LIGrp 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 267 --ELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQHSYQDLASQINLILLerlWYVMLEQFLmkyvwSASGL 344
Cdd:COG4178 206 liRLNFEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIANWRRLIR---RQRNLTFFT-----TGYGQ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 345 LMVAVPI-ITATGYaesdseamkkaalemkeeelvserteaftIARNL----LTAAADATERIMSS-------YKEVTEL 412
Cdd:COG4178 278 LAVIFPIlVAAPRY-----------------------------FAGEItlggLMQAASAFGQVQGAlswfvdnYQSLAEW 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 413 AGYTARVYEMFQVfedvkhcrfkrtgdLEEAQAGPGVmvqsgvhvegplkIQGQVVDVEQGIICENIPIITPTGEVVVAS 492
Cdd:COG4178 329 RATVDRLAGFEEA--------------LEAADALPEA-------------ASRIETSEDGALALEDLTLRTPDGRPLLED 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYKPPPQRMFYIPQRPYMSVGSLRDQVIYPDSAEDMrrkgcS 572
Cdd:COG4178 382 LSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTLREALLYPATAEAF-----S 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 573 EQQLEAILGIVHLRHILQReggWEAVCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDA-- 650
Cdd:COG4178 457 DAELREALEAVGLGHLAER---LDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElp 533
|
570 580 590
....*....|....*....|....*....|....*...
gi 6671497 651 GIALLSITHRPSLWKYHTHLLQFDGEGGWKFEKLDSAA 688
Cdd:COG4178 534 GTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEAPA 571
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
474-679 |
1.44e-83 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 262.09 E-value: 1.44e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 474 IICENIPIITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYKPPPQRMFYIPQRPYMSVGSL 553
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 554 RDQVIYPdsaedmrrkgcseqqleailgivhlrhilqreggweavcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:cd03223 81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6671497 634 AVSIDVEGKIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGGW 679
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
482-659 |
2.10e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.99 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 482 ITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLYK-------PPP---QRMFYIPQRPYMSV 550
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGeIYLDgkplsamPPPewrRQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 551 GSLRDQVIYPDSaedMRRKGCSEQQLEAILGIVHLRH-ILQreggweavcdwKDV--LSGGEKQRIGMARMFYHRPKYAL 627
Cdd:COG4619 88 GTVRDNLPFPFQ---LRERKFDRERALELLERLGLPPdILD-----------KPVerLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 6671497 628 LDECTSAVSID----VEGKIFQAAKDAGIALLSITH 659
Cdd:COG4619 154 LDEPTSALDPEntrrVEELLREYLAEEGRAVLWVSH 189
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
484-663 |
7.35e-24 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 98.99 E-value: 7.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 484 PTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY-------KPPP----QRMFYIPQRPYMSVGS 552
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlrDLDLeslrKNIAYVPQDPFLFSGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 553 LRDqviypdsaedmrrkgcseqqleailgivhlrhilqreggweavcdwkDVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:cd03228 92 IRE-----------------------------------------------NILSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190
....*....|....*....|....*....|...
gi 6671497 633 SAVSIDVEGKIFQA--AKDAGIALLSITHRPSL 663
Cdd:cd03228 125 SALDPETEALILEAlrALAKGKTVIVIAHRLST 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
474-663 |
8.73e-23 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 102.91 E-value: 8.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 474 IICENIPIITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVL---------YKPPP--QRMFYI 542
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdLDPASwrRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 543 PQRPYMSVGSLRDQViypdsaeDMRRKGCSEQQLEAILGIVHLRHILQR-EGGWEAVcdwkdV------LSGGEKQRIGM 615
Cdd:COG4988 417 PQNPYLFAGTIRENL-------RLGRPDASDEELEAALEAAGLDEFVAAlPDGLDTP-----LgeggrgLSGGQAQRLAL 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671497 616 ARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPSL 663
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlaKGRTVILITHRLAL 534
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
484-663 |
5.75e-20 |
|
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: 94.90 E-value: 5.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 484 PTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLY------KPPP----QRMFYIPQRPYMSVGS 552
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGrILIdgidlrQIDPaslrRQIGVVLQDVFLFSGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 553 LRDQVIypdsaedMRRKGCSEQQLEAILGIVHLRHILQR----------EGGweavcdwkDVLSGGEKQRIGMARMFYHR 622
Cdd:COG2274 565 IRENIT-------LGDPDATDEEIIEAARLAGLHDFIEAlpmgydtvvgEGG--------SNLSGGQRQRLAIARALLRN 629
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6671497 623 PKYALLDECTSAVSIDVEGKIFQA--AKDAGIALLSITHRPSL 663
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENlrRLLKGRTVIIIAHRLST 672
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
493-663 |
5.89e-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: 87.30 E-value: 5.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYkpppqrmFYIPQRPYMSVGSLRDQVIYpdsaedmrrkgcs 572
Cdd:cd00267 18 VSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL-------IDGKDIAKLPLEELRRRIGY------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 573 eqqleailgivhlrhILQreggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDA-- 650
Cdd:cd00267 78 ---------------VPQ--------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELae 128
|
170
....*....|....
gi 6671497 651 -GIALLSITHRPSL 663
Cdd:cd00267 129 eGRTVIIVTHDPEL 142
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
493-667 |
8.92e-20 |
|
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: 88.29 E-value: 8.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLYKPPP----------QRMFYIPQRPymsvgslRDQVIYPD 561
Cdd:cd03225 20 ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGeVLVDGKDltklslkelrRKVGLVFQNP-------DDQFFGPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 562 SAED----MRRKGCSEQQLEAI----LGIVHLRHILQREggweavcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:cd03225 93 VEEEvafgLENLGLPEEEIEERveeaLELVGLEGLRDRS---------PFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 6671497 634 avSIDVEG-----KIFQAAKDAGIALLSITHRPSLWKYH 667
Cdd:cd03225 164 --GLDPAGrrellELLKKLKAEGKTIIIVTHDLDLLLEL 200
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
493-633 |
2.65e-19 |
|
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: 85.01 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLY----------KPPPQRMFYIPQ----RPYMSVgslRDQV 557
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGtILLdgqdltdderKSLRKEIGYVFQdpqlFPRLTV---RENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6671497 558 IYPDSAEDMRRKGCSEQQLEAI--LGIVHLRHILQREGGweavcdwkDVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALekLGLGDLADRPVGERP--------GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
477-663 |
3.73e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 91.64 E-value: 3.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 477 ENIPIITPTGE-VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVL------YKPPPQRMF-----YIPQ 544
Cdd:TIGR01842 320 ENVTIVPPGGKkPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVrldgadLKQWDRETFgkhigYLPQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 545 RPYMSVGSLRDQViypdsaEDMRRKGCSEQQLEA-ILGIVHlRHILQREGGWE-AVCDWKDVLSGGEKQRIGMARMFYHR 622
Cdd:TIGR01842 400 DVELFPGTVAENI------ARFGENADPEKIIEAaKLAGVH-ELILRLPDGYDtVIGPGGATLSGGQRQRIALARALYGD 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6671497 623 PKYALLDECTSavSIDVEGKI-----FQAAKDAGIALLSITHRPSL 663
Cdd:TIGR01842 473 PKLVVLDEPNS--NLDEEGEQalanaIKALKARGITVVVITHRPSL 516
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
474-663 |
4.40e-19 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 85.35 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 474 IICENIPIITP-TGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVL---------YKPPPQRMF--Y 541
Cdd:cd03246 1 LEVENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisqWDPNELGDHvgY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 542 IPQRPYMSVGSLRDqviypdsaedmrrkgcseqqleailgivhlrhilqreggweavcdwkDVLSGGEKQRIGMARMFYH 621
Cdd:cd03246 81 LPQDDELFSGSIAE-----------------------------------------------NILSGGQRQRLGLARALYG 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6671497 622 RPKYALLDECTSAVSIDVEGKIFQA---AKDAGIALLSITHRPSL 663
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPET 158
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
474-666 |
4.64e-19 |
|
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: 86.39 E-value: 4.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 474 IICENIPIITPTGEVVVASL---NIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY-------KPPP------- 536
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALkgvSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdisKLSEkelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 537 -QRMFYIPQR----PYMSVgslRDQVIYPDSAEDMRRKGCsEQQLEAILGIVHLRHILQREGGWeavcdwkdvLSGGEKQ 611
Cdd:cd03255 81 rRHIGFVFQSfnllPDLTA---LENVELPLLLAGVPKKER-RERAEELLERVGLGDRLNHYPSE---------LSGGQQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6671497 612 RIGMARMFYHRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSLWKY 666
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEY 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
485-671 |
1.37e-18 |
|
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: 84.83 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 485 TGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTySGVLYKPPpqRMFYIPQRPYMSVGSLRDQVIYpDSA 563
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKL-SGSVSVPG--SIAYVSQEPWIQNGTIRENILF-GKP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 564 EDMRR-----KGCseqQLEAILGIVhlrhilqrEGGweavcDWKDV------LSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:cd03250 92 FDEERyekviKAC---ALEPDLEIL--------PDG-----DLTEIgekginLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6671497 633 SAVSIDVEGKIFQ-----AAKDAGIALLsITHRPSLWKYHTHLL 671
Cdd:cd03250 156 SAVDAHVGRHIFEncilgLLLNNKTRIL-VTHQLQLLPHADQIV 198
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
489-663 |
2.40e-18 |
|
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: 84.56 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYSGVLY------KPPP----QRMFYIPQRPYMSVGSLRDQV 557
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkPTSGSVLLdgtdirQLDPadlrRNIGYVPQDVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 558 IYPDSAEDmrrkgcSEQQLEA--ILGIVHL--RHI----LQ-REGGweavcdwkDVLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03245 99 TLGAPLAD------DERILRAaeLAGVTDFvnKHPngldLQiGERG--------RGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 6671497 629 DECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPSL 663
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQllGDKTLIIITHRPSL 201
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
486-661 |
6.63e-18 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 82.91 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLYK---------PPPQRMFYIPQRPymsvgslrd 555
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGeVLWNgepirdareDYRRRLAYLGHAD--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 556 qVIYPD-SAED-------MRRKGCSEQQLEAILGIVHLRHILQREGGweavcdwkdVLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:COG4133 85 -GLKPElTVREnlrfwaaLYGLRADREAIDEALEAVGLAGLADLPVR---------QLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 6671497 628 LDECTSAvsIDVEGK-----IFQAAKDAGIALLSITHRP 661
Cdd:COG4133 155 LDEPFTA--LDAAGVallaeLIAAHLARGGAVLLTTHQP 191
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
486-659 |
1.01e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.84 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYSGVLYK-------PPP---QRMFYIPQRPYMSVGSLR 554
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPTSGTLLFEgedistlKPEiyrQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 555 DQVIYPdsaEDMRRKGCSEQQLEAILGIVHL-RHILQREggweavcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:PRK10247 99 DNLIFP---WQIRNQQPDPAIFLDDLERFALpDTILTKN---------IAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190
....*....|....*....|....*....|
gi 6671497 634 AVS----IDVEGKIFQAAKDAGIALLSITH 659
Cdd:PRK10247 167 ALDesnkHNVNEIIHRYVREQNIAVLWVTH 196
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
486-676 |
1.72e-17 |
|
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: 81.81 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG---VLYKPP---PQRMFYIPQRPYMSVG---SLRDQ 556
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGsirVFGKPLekeRKRIGYVPQRRSIDRDfpiSVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 557 V----------IYPDSAEDMRRkgcSEQQLEAiLGIVHLRHILQREggweavcdwkdvLSGGEKQRIGMARMFYHRPKYA 626
Cdd:cd03235 91 VlmglyghkglFRRLSKADKAK---VDEALER-VGLSELADRQIGE------------LSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6671497 627 LLDECTSAVsiDVEGK-----IFQAAKDAGIALLSITH-RPSLWKYHTHLLQFDGE 676
Cdd:cd03235 155 LLDEPFAGV--DPKTQediyeLLRELRREGMTILVVTHdLGLVLEYFDRVLLLNRT 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
486-663 |
1.94e-17 |
|
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: 80.56 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYkpppqrmfyipqrpymsvgsLRDQVIYPDSAED 565
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL--------------------LDGKDLASLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 566 MRRK-GCSEQQLEAiLGIVHLRHilqreggweavcdwKDV--LSGGEKQRIGMARMFYHRPKYALLDECTSAV----SID 638
Cdd:cd03214 71 LARKiAYVPQALEL-LGLAHLAD--------------RPFneLSGGERQRVLLARALAQEPPILLLDEPTSHLdiahQIE 135
|
170 180
....*....|....*....|....*
gi 6671497 639 VEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHDLNL 160
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
486-663 |
2.15e-17 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 82.40 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY---KP----PP----QRMFYIPQRPYMSVG-SL 553
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDlaslSRrelaRRIAYVPQEPPAPFGlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 554 RDQVI---YP-------DSAEDMRRkgcSEQQLEAiLGIVHLRHilqreggweavcdwKDV--LSGGEKQRIGMARMFYH 621
Cdd:COG1120 93 RELVAlgrYPhlglfgrPSAEDREA---VEEALER-TGLEHLAD--------------RPVdeLSGGERQRVLIARALAQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6671497 622 RPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:COG1120 155 EPPLLLLDEPTSHLdlahQLEVLELLRRLARERGRTVVMVLHDLNL 200
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
484-662 |
3.77e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 85.60 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 484 PTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VL--------YKPP--PQRMFYIPQRPYMSVGS 552
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGrILidgvdirdLTLEslRRQIGVVPQDTFLFSGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 553 LRDQVIYPdsaedmrRKGCSEQQLEAILGIVHLRHILQR-EGGWEAVcdwkdV------LSGGEKQRIGMARMFYHRPKY 625
Cdd:COG1132 430 IRENIRYG-------RPDATDEEVEEAAKAAQAHEFIEAlPDGYDTV-----VgergvnLSGGQRQRIAIARALLKDPPI 497
|
170 180 190
....*....|....*....|....*....|....*....
gi 6671497 626 ALLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPS 662
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERlmKGRTTIVIAHRLS 536
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
489-659 |
1.48e-16 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 79.53 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGV------------LYKPPPQ------RMFYIPQRPYMSV 550
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegevlldgkdIYDLDVDvlelrrRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 551 GSLRDQVIYPDSAEDMRRKGCSEQQLEAILGIVHLrhilqreggWEAVCDWKDV--LSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03260 95 GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAAL---------WDEVKDRLHAlgLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190
....*....|....*....|....*....|....*
gi 6671497 629 DECTSAVSI----DVEGKIFQAAKDAGIALlsITH 659
Cdd:cd03260 166 DEPTSALDPistaKIEELIAELKKEYTIVI--VTH 198
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
486-659 |
1.59e-16 |
|
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: 79.69 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY--------KPPPQRMF-YIPQR----PYMSVgs 552
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditnLPPEKRDIsYVPQNyalfPHMTV-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 553 lrdqviYPDSAEDMRRKGCSEQQLEA----ILGIVHLRHILQREGGweavcdwkdVLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03299 89 ------YKNIAYGLKKRKVDKKEIERkvleIAEMLGIDHLLNRKPE---------TLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190
....*....|....*....|....*....|....*
gi 6671497 629 DECTSAVSIDVEGKIFQAAKDA----GIALLSITH 659
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIrkefGVTVLHVTH 188
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
489-662 |
1.66e-16 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 83.28 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGV-------LYKPPP----QRMFYIPQRPYMSVGSLRDQV 557
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSitlggvdLRDLDEddlrRRIAVVPQRPHLFDTTLRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 558 IypdsaedMRRKGCSEQQLEAILGIVHLRHILQR-EGGWEAVCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAV 635
Cdd:COG4987 430 R-------LARPDATDEELWAALERVGLGDWLAAlPDGLDTWLGEGGRrLSGGERRRLALARALLRDAPILLLDEPTEGL 502
|
170 180 190
....*....|....*....|....*....|.
gi 6671497 636 SIDVEGKI----FQAAKDAgiALLSITHRPS 662
Cdd:COG4987 503 DAATEQALladlLEALAGR--TVLLITHRLA 531
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
483-630 |
2.08e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 79.75 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 483 TPTGEV-VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY------KPPPQRMFYIPQR----PYMSVg 551
Cdd:COG1116 19 TGGGGVtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvTGPGPDRGVVFQEpallPWLTV- 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671497 552 slRDQVIYPDSAEDMRRKGCsEQQLEAILGIVHLRHILQReggweavcdWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:COG1116 98 --LDNVALGLELRGVPKAER-RERARELLELVGLAGFEDA---------YPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
488-630 |
3.87e-16 |
|
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: 77.90 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLY-----KPPPQRMFYIPQR----PYMSVgslRDQV 557
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGeVLVdgepvTGPGPDRGYVFQQdallPWLTV---LDNV 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671497 558 IYPDSAEDMRRKGcSEQQLEAILGIVHLRHILQReggweavcdWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:cd03293 95 ALGLELQGVPKAE-ARERAEELLELVGLSGFENA---------YPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
474-663 |
4.08e-16 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 81.95 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 474 IICENIPIITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGV-------LYKPPP----QRMFYI 542
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavngvpLADADAdswrDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 543 PQRPYMSVGSLRDQVIypdsaedMRRKGCSEQQLEAILGIVHLRHILQ-REGGWEAVCDWKDV-LSGGEKQRIGMARMFY 620
Cdd:TIGR02857 402 PQHPFLFAGTIAENIR-------LARPDASDAEIREALERAGLDEFVAaLPQGLDTPIGEGGAgLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6671497 621 HRPKYALLDECTSAVSIDVEGKIFQAAKDA--GIALLSITHRPSL 663
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLAL 519
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
484-663 |
8.16e-16 |
|
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: 77.37 E-value: 8.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 484 PTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLYK---PPPQRMFYIPQRpymsVGSL----RD 555
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGeVLVDgkdITKKNLRELRRK----VGLVfqnpDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 556 QVIYPDSAED----MRRKGCSEQQLEA----ILGIVHLRHILQREggweavcdwKDVLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:COG1122 87 QLFAPTVEEDvafgPENLGLPREEIRErveeALELVGLEHLADRP---------PHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6671497 628 LDECTSavSIDVEGK-----IFQAAKDAGIALLSITHRPSL 663
Cdd:COG1122 158 LDEPTA--GLDPRGRrelleLLKRLNKEGKTVIIVTHDLDL 196
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
477-659 |
1.10e-15 |
|
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: 76.14 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 477 ENIPIITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLY--KPPPQRMFYipQRPYMSVGSL 553
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGsILLngKPIKAKERR--KSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 554 RDQvIYPDSAED-----MRRKGCSEQQLEAILGIVHLrHILQREGGWEavcdwkdvLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03226 81 DYQ-LFTDSVREelllgLKELDAGNEQAETVLKDLDL-YALKERHPLS--------LSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190
....*....|....*....|....*....|....
gi 6671497 629 DECTSAV---SIDVEGKIFQAAKDAGIALLSITH 659
Cdd:cd03226 151 DEPTSGLdykNMERVGELIRELAAQGKAVIVITH 184
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
477-663 |
2.12e-15 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 79.79 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 477 ENIPIITP-TGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGV-------LYKPPPQR----MFYIPQ 544
Cdd:COG4618 334 ENLTVVPPgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSvrldgadLSQWDREElgrhIGYLPQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 545 RPYMSVGSLRD-----------QVIypDSAedmRRKGCSEQqleailgIVHLRH----ILQREGGweavcdwkdVLSGGE 609
Cdd:COG4618 414 DVELFDGTIAEniarfgdadpeKVV--AAA---KLAGVHEM-------ILRLPDgydtRIGEGGA---------RLSGGQ 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6671497 610 KQRIGMARMFYHRPKYALLDECTSavSIDVEG-----KIFQAAKDAGIALLSITHRPSL 663
Cdd:COG4618 473 RQRIGLARALYGDPRLVVLDEPNS--NLDDEGeaalaAAIRALKARGATVVVITHRPSL 529
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
484-659 |
3.35e-15 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 74.38 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 484 PTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRIL-GGLWPTYSGVLYKPPP------------QRMFYIPQRPymsv 550
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLnGLLRPQSGAVLIDGEPldysrkgllerrQRVGLVFQDP---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 551 gslRDQVIYPDSAEDM----RRKGCSEQQLEA-------ILGIVHLRHILQReggweavcdwkdVLSGGEKQRIGMARMF 619
Cdd:TIGR01166 78 ---DDQLFAADVDQDVafgpLNLGLSEAEVERrvrealtAVGASGLRERPTH------------CLSGGEKKRVAIAGAV 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6671497 620 YHRPKYALLDECTSAVsiDVEG-----KIFQAAKDAGIALLSITH 659
Cdd:TIGR01166 143 AMRPDVLLLDEPTAGL--DPAGreqmlAILRRLRAEGMTVVISTH 185
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
486-662 |
6.54e-15 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 74.57 E-value: 6.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY-----------KPPPQRMFYIPQRPYMSVGSLR 554
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgidirdisrKSLRSMIGVVLQDTFLFSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 555 DQVIY--PDSAEDmrrkgcSEQQLEAILGIVHLrhILQREGGWEA-VCDWKDVLSGGEKQRIGMARMFYHRPKYALLDEC 631
Cdd:cd03254 95 ENIRLgrPNATDE------EVIEAAKEAGAHDF--IMKLPNGYDTvLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190
....*....|....*....|....*....|....*
gi 6671497 632 TSavSIDVEG-KIFQAAKDA---GIALLSITHRPS 662
Cdd:cd03254 167 TS--NIDTETeKLIQEALEKlmkGRTSIIIAHRLS 199
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
486-662 |
1.01e-14 |
|
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: 73.71 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY-------KPPPQR-----MFyipQR----PYMS 549
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrdvtGVPPERrnigmVF---QDyalfPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 550 VgslRDQVIYPdsaedMRRKGCSEQQLEA----ILGIVHLRHILQReggweavcdWKDVLSGGEKQRIGMARMFYHRPKY 625
Cdd:cd03259 89 V---AENIAFG-----LKLRGVPKAEIRArvreLLELVGLEGLLNR---------YPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6671497 626 ALLDECTSAvsIDVE------GKIFQAAKDAGIALLSITHRPS 662
Cdd:cd03259 152 LLLDEPLSA--LDAKlreelrEELKELQRELGITTIYVTHDQE 192
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
505-662 |
1.72e-14 |
|
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: 73.10 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 505 ITGPNGCGKSSLFRILGGLWPTYSGVLY--------------KPPPQRMF-YIPQR----PYMSVgslRDQVIYpdsaeD 565
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkinLPPQQRKIgLVFQQyalfPHLNV---RENLAF-----G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 566 MRRKGCSE--QQLEAILGIVHLRHILQReggweavcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKI 643
Cdd:cd03297 100 LKRKRNREdrISVDELLDLLGLDHLLNR---------YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180
....*....|....*....|...
gi 6671497 644 F----QAAKDAGIALLSITHRPS 662
Cdd:cd03297 171 LpelkQIKKNLNIPVIFVTHDLS 193
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
484-662 |
1.86e-14 |
|
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: 73.67 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 484 PTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG---------VLYKPPPQR--MFYIPQRPYMSVGS 552
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdghdlALADPAWLRrqVGVVLQENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 553 LRDQVIYPDSAEDMRRKgcseqQLEAILGIVHlRHILQREGGWEAVCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDEC 631
Cdd:cd03252 92 IRDNIALADPGMSMERV-----IEAAKLAGAH-DFISELPEGYDTIVGEQGAgLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190
....*....|....*....|....*....|...
gi 6671497 632 TSAVSIDVEGKIFQAAKD--AGIALLSITHRPS 662
Cdd:cd03252 166 TSALDYESEHAIMRNMHDicAGRTVIIIAHRLS 198
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
486-659 |
2.32e-14 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 73.20 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG---VLYKPPPQ---RMFYIPQRPYMSVGslrdqviY 559
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGtvrLFGKPPRRarrRIGYVPQRAEVDWD-------F 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 560 PDSAEDM------RRKGC-------SEQQLEAILGIVHLRHILQReggweAVCDwkdvLSGGEKQRIGMARMFYHRPKYA 626
Cdd:COG1121 91 PITVRDVvlmgryGRRGLfrrpsraDREAVDEALERVGLEDLADR-----PIGE----LSGGQQQRVLLARALAQDPDLL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 6671497 627 LLDECTSAVsiDVEG-----KIFQAAKDAGIALLSITH 659
Cdd:COG1121 162 LLDEPFAGV--DAATeealyELLRELRREGKTILVVTH 197
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
489-659 |
2.63e-14 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 73.30 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY-----------KPPPQRMFYIPQRPYMSV---GSLR 554
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgrpvtrrrrKAFRRRVQMVFQDPYASLhprHTVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 555 DQViypdsAEDMR--RKGCSEQQLEAILGIVHL-RHILQR---EggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:COG1124 100 RIL-----AEPLRihGLPDREERIAELLEQVGLpPSFLDRyphQ------------LSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6671497 629 DECTSAVsiDVegkIFQAA---------KDAGIALLSITH 659
Cdd:COG1124 163 DEPTSAL--DV---SVQAEilnllkdlrEERGLTYLFVSH 197
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
484-663 |
3.09e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 72.77 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 484 PTGEVVVASL---NIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTySGVLY--------KPPPQR-MF------YIPQ 544
Cdd:COG1136 15 GTGEGEVTALrgvSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRPT-SGEVLidgqdissLSERELaRLrrrhigFVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 545 R----PYMSVgslRDQVIYPDSAEDMRRKGCsEQQLEAILGIVHLRHILQR---EggweavcdwkdvLSGGEKQRIGMAR 617
Cdd:COG1136 94 FfnllPELTA---LENVALPLLLAGVSRKER-RERARELLERVGLGDRLDHrpsQ------------LSGGQQQRVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671497 618 MFYHRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:COG1136 158 ALVNRPKLILADEPTGNLdsktGEEVLELLRELNRELGTTIVMVTHDPEL 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
488-659 |
9.74e-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: 69.73 E-value: 9.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEG--MHLLitGPNGCGKSSLFRILGGLWPTYSG---VLYKPPP-------QRMFYIPQRPYmsvgslrd 555
Cdd:cd03230 14 TALDDISLTVEKGeiYGLL--GPNGAGKTTLIKIILGLLKPDSGeikVLGKDIKkepeevkRRIGYLPEEPS-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 556 qvIYPD-SAEDmrrkgcseqqleailgivHLRhilqreggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSA 634
Cdd:cd03230 84 --LYENlTVRE------------------NLK------------------LSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190
....*....|....*....|....*....|
gi 6671497 635 vsIDVEG-----KIFQAAKDAGIALLSITH 659
Cdd:cd03230 126 --LDPESrrefwELLRELKKEGKTILLSSH 153
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
486-659 |
1.39e-13 |
|
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: 70.73 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG--------VLYKPPPQRMF-YIPQR----PYMSVGs 552
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGeilldgkdITNLPPHKRPVnTVFQNyalfPHLTVF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 553 lrDQVIYPdsaedMRRKGCSEQQLEA----ILGIVHLRHILQREggweavcdwKDVLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03300 91 --ENIAFG-----LRLKKLPKAEIKErvaeALDLVQLEGYANRK---------PSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 6671497 629 DECTSAV------SIDVEGKIFQaaKDAGIALLSITH 659
Cdd:cd03300 155 DEPLGALdlklrkDMQLELKRLQ--KELGITFVFVTH 189
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
488-659 |
2.24e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 70.09 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG---VLYKPPP-------QRMFYIPQR----PYMSVgsl 553
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGevrVLGEDVArdpaevrRRIGYVPQEpalyPDLTV--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 554 RDQV-----IYPDSAEDMRRKGcseQQLEAILGIVHLRHILQREggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:COG1131 91 RENLrffarLYGLPRKEARERI---DELLELFGLTDAADRKVGT------------LSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 6671497 629 DECTSAVsiDVEG-----KIFQAAKDAGIA-LLSiTH 659
Cdd:COG1131 156 DEPTSGL--DPEArrelwELLRELAAEGKTvLLS-TH 189
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
488-660 |
2.68e-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: 69.62 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVL---YKP----PPQRMFYIPQR----PYMSVgslRDQ 556
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdGKPldiaARNRIGYLPEErglyPKMKV---IDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 557 VIYPDSAEDMRRKGCSEQQLEAI--LGIVHLRHILQREggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSA 634
Cdd:cd03269 91 LVYLAQLKGLKKEEARRRIDEWLerLELSEYANKRVEE------------LSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180
....*....|....*....|....*....
gi 6671497 635 ---VSIDVEGKIFQAAKDAGIALLSITHR 660
Cdd:cd03269 159 ldpVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
486-661 |
2.79e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.52 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLYKPPPQ-------RMFYIPQR----PYMSVgsl 553
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtIKLDGGDIddpdvaeACHYLGHRnamkPALTV--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 554 rdqviypdsAEDM----RRKGCSEQQLEAILGIVHLRHILQREGGweavcdwkdVLSGGEKQRIGMAR-MFYHRPKYaLL 628
Cdd:PRK13539 91 ---------AENLefwaAFLGGEELDIAAALEAVGLAPLAHLPFG---------YLSAGQKRRVALARlLVSNRPIW-IL 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 6671497 629 DECTSAvsIDVEGK-----IFQA-AKDAGIALLSiTHRP 661
Cdd:PRK13539 152 DEPTAA--LDAAAValfaeLIRAhLAQGGIVIAA-THIP 187
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
484-660 |
4.72e-13 |
|
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: 69.06 E-value: 4.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 484 PTGEVVVASLNIRVEEGMHLLITGPNGCGKSS----LFRILgglwPTYSGVLY-------KPPP----QRMFYIPQRPYM 548
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILidgvdisKIGLhdlrSRISIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 549 SVGSLRDQvIYPDSAedmrrkgCSEQQLEAILGIVHLR-HILQREGGWEA-VCDWKDVLSGGEKQRIGMARMFYHRPKYA 626
Cdd:cd03244 90 FSGTIRSN-LDPFGE-------YSDEELWQALERVGLKeFVESLPGGLDTvVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 6671497 627 LLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHR 660
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREafKDCTVLTIAHR 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
494-630 |
5.26e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 494 NIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYKPPPQRMFYIPQRPYMSVG-SLRDQVI--YPDSAEDMRRKG 570
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDlTVLDTVLdgDAELRALEAELE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 571 CSEQQL----EAILGIVHLRHILQREGGWEA--------------VCDW-KDV--LSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:COG0488 98 ELEAKLaepdEDLERLAELQEEFEALGGWEAearaeeilsglgfpEEDLdRPVseLSGGWRRRVALARALLSEPDLLLLD 177
|
.
gi 6671497 630 E 630
Cdd:COG0488 178 E 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
375-659 |
6.13e-13 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 71.86 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 375 EELVSERTEAFTIARNLLTAAADATERIMSSYKEVTELAGYTARVYEMFQVFEDVKHCRFKRTGDLEEAQAGPGVMVQSG 454
Cdd:COG1123 186 RELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRN 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 455 VHVEGPLKIQGQVVdveqgiicenipiitptgevVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLY- 532
Cdd:COG1123 266 LSKRYPVRGKGGVR--------------------AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGsILFd 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 533 ------------KPPPQRMFYIPQRPY------MSVGslrDQVIYPDSAEDMRRKGCSEQQLEAILGIVHL------RHI 588
Cdd:COG1123 326 gkdltklsrrslRELRRRVQMVFQDPYsslnprMTVG---DIIAEPLRLHGLLSRAERRERVAELLERVGLppdladRYP 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 589 LQreggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSA--VSIdvegkifQA---------AKDAGIALLSI 657
Cdd:COG1123 403 HE--------------LSGGQRQRVAIARALALEPKLLILDEPTSAldVSV-------QAqilnllrdlQRELGLTYLFI 461
|
..
gi 6671497 658 TH 659
Cdd:COG1123 462 SH 463
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
489-659 |
6.26e-13 |
|
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: 68.69 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLYK-----PPPQRMF--------YIPQRPY------M 548
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGsIIFDgkdllKLSRRLRkirrkeiqMVFQDPMsslnprM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 549 SVGslrDQViypdsAEDMRRKGC-SEQQLEAILGIVHLRHILQREggweavcDWKDV----LSGGEKQRIGMARMFYHRP 623
Cdd:cd03257 100 TIG---EQI-----AEPLRIHGKlSKKEARKEAVLLLLVGVGLPE-------EVLNRypheLSGGQRQRVAIARALALNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6671497 624 KYALLDECTSAVSIDVEGKIFQAAKDA----GIALLSITH 659
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKKLqeelGLTLLFITH 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
474-662 |
8.70e-13 |
|
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: 68.41 E-value: 8.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 474 IICENIPIITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYkpppqrmfyIPQRPYMSV--G 551
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIL---------IDGQDIREVtlD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 552 SLR--------DQVIYPDSAEDMRRKGC---SEQQLE--AILGIVHLRhILQREGGWEAVCDWKDV-LSGGEKQRIGMAR 617
Cdd:cd03253 72 SLRraigvvpqDTVLFNDTIGYNIRYGRpdaTDEEVIeaAKAAQIHDK-IMRFPDGYDTIVGERGLkLSGGEKQRVAIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6671497 618 MFYHRPKYALLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPS 662
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDvsKGRTTIVIAHRLS 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
474-664 |
9.64e-13 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 71.09 E-value: 9.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 474 IICENIPIITPTGEV-VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP---TYSG--------VLYKPPPQR--- 538
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGevlldgrdLLELSEALRgrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 539 MFYIPQRPYMSVGSLR--DQVIYPDSAEDMRRKGCSEQQLEAiLGIVHLRHILQReggweavcdWKDVLSGGEKQRIGMA 616
Cdd:COG1123 85 IGMVFQDPMTQLNPVTvgDQIAEALENLGLSRAEARARVLEL-LEAVGLERRLDR---------YPHQLSGGQRQRVAIA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6671497 617 RMFYHRPKYALLDECTSA----VSIDVEGKIFQAAKDAGIALLSITHRPSLW 664
Cdd:COG1123 155 MALALDPDLLIADEPTTAldvtTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
486-630 |
2.01e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.29 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVAS-LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYKpPPQRMFYIP--QRpymSVGSL-RDQVIYP- 560
Cdd:PRK11000 14 GDVVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRMNDVPpaER---GVGMVfQSYALYPh 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671497 561 -DSAEDMR--------RKGCSEQQLEAILGIVHLRHILQREGgweavcdwKDvLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:PRK11000 90 lSVAENMSfglklagaKKEEINQRVNQVAEVLQLAHLLDRKP--------KA-LSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
493-659 |
2.09e-12 |
|
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: 67.49 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYSGVLYK------PPPQRMFYIPQR---PYMSVgslRDQV-IYPD 561
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEgkqitePGPDRMVVFQNYsllPWLTV---RENIaLAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 562 SAEDMRRKGCSEQQLEAILGIVHLRHilqreggweAVCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSI---- 637
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEHIALVGLTE---------AADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrg 151
|
170 180
....*....|....*....|..
gi 6671497 638 DVEGKIFQAAKDAGIALLSITH 659
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTH 173
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
488-660 |
2.64e-12 |
|
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: 67.08 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEG-MHLLItGPNGCGKSSLFRILGGLWPTYSG-VLYK-------PPPQ-------RMFYIPqRPY--MS 549
Cdd:cd03219 14 VALDDVSFSVRPGeIHGLI-GPNGAGKTTLFNLISGFLRPTSGsVLFDgeditglPPHEiarlgigRTFQIP-RLFpeLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 550 V------GSLRDQVIYPDSAEDMRRKGCSEQQLEAILGIVHLRHILQREGGweavcdwkdVLSGGEKQRIGMARMFYHRP 623
Cdd:cd03219 92 VlenvmvAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAG---------ELSYGQQRRLEIARALATDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6671497 624 KYALLDECTSAVS---IDVEGKIFQAAKDAGIALLSITHR 660
Cdd:cd03219 163 KLLLLDEPAAGLNpeeTEELAELIRELRERGITVLLVEHD 202
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
486-660 |
2.77e-12 |
|
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: 65.14 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYkpppqrmfyipqrpymsvgsLRDQVIYPDSAED 565
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL--------------------VDGKEVSFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 566 MRRKGcseqqleaiLGIVHlrhilQreggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVS---IDVEGK 642
Cdd:cd03216 72 ARRAG---------IAMVY-----Q--------------LSVGERQMVEIARALARNARLLILDEPTAALTpaeVERLFK 123
|
170
....*....|....*...
gi 6671497 643 IFQAAKDAGIALLSITHR 660
Cdd:cd03216 124 VIRRLRAQGVAVIFISHR 141
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
461-678 |
3.64e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.01 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 461 LKIQGQVVDVEQGIICENIPIITPTGEVVVaslnirveegmhllITGPNGCGKSSLFRILGGLwPTY---SG-VLYK--- 533
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHA--------------IMGPNGSGKSTLAKVLMGH-PKYevtSGsILLDged 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 534 ----PPPQR----MFYIPQRP------------YMSVGSLRDQVIypdSAEDMRRKgcseqqLEAILGIVHL-RHILQR- 591
Cdd:COG0396 66 ilelSPDERaragIFLAFQYPveipgvsvsnflRTALNARRGEEL---SAREFLKL------LKEKMKELGLdEDFLDRy 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 592 --EGgweavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID---VEGKIFQAAKDAGIALLSITHRPSLWKY 666
Cdd:COG0396 137 vnEG-----------FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDalrIVAEGVNKLRSPDRGILIITHYQRILDY 205
|
250 260
....*....|....*....|
gi 6671497 667 ----HTHLLqFDG----EGG 678
Cdd:COG0396 206 ikpdFVHVL-VDGrivkSGG 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
489-655 |
3.85e-12 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 66.30 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLY-------KPPPQR----MFYIPQR----PYMSVG- 551
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsIRFdgrditgLPPHERaragIGYVPEGrrifPELTVEe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 552 SLRdqviypdSAEDMRRKGCSEQQLEAILGIV-HLRHILQREGGweavcdwkdVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:cd03224 95 NLL-------LGAYARRRAKRKARLERVYELFpRLKERRKQLAG---------TLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180
....*....|....*....|....*...
gi 6671497 631 CTSAVSIDVEGKIFQAA---KDAGIALL 655
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIrelRDEGVTIL 186
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
493-662 |
3.87e-12 |
|
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: 66.79 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVL---------YKPPPQR--MFYIPQRPYMSVGSLRDQVIY-- 559
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdLNLRWLRsqIGLVSQEPVLFDGTIAENIRYgk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 560 PDSAEDMRRKGCSEQQLEAIlgIVHLRHilqregGWEAVCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSID 638
Cdd:cd03249 102 PDATDEEVEEAAKKANIHDF--IMSLPD------GYDTLVGERGSqLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180
....*....|....*....|....*..
gi 6671497 639 VEgKIFQAAKD---AGIALLSITHRPS 662
Cdd:cd03249 174 SE-KLVQEALDramKGRTTIVIAHRLS 199
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
482-659 |
3.89e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 65.97 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 482 ITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWP--TYSGVLY--------KPPPQR-MFYIPQR---- 545
Cdd:COG4136 9 ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPafSASGEVLlngrrltaLPAEQRrIGILFQDdllf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 546 PYMSVG-----SLrdqviyPDSAEDMRRKGCSEQQLEAI-LGIVHLRHILQreggweavcdwkdvLSGGEKQRIGMARMF 619
Cdd:COG4136 89 PHLSVGenlafAL------PPTIGRAQRRARVEQALEEAgLAGFADRDPAT--------------LSGGQRARVALLRAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6671497 620 YHRPKYALLDECTS----AVSIDVEGKIFQAAKDAGIALLSITH 659
Cdd:COG4136 149 LAEPRALLLDEPFSkldaALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
505-675 |
3.96e-12 |
|
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: 66.34 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 505 ITGPNGCGKSSLFRILGGLWPTYSGVLY---KPPPQ--------RMFYIPQRPYMSVGSLRDQVIYPDSAEDMRRKGCSE 573
Cdd:cd03248 45 LVGPSGSGKSTVVALLENFYQPQGGQVLldgKPISQyehkylhsKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 574 QQLEAILGIVHLRHilqreGGWEAVCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKD--AG 651
Cdd:cd03248 125 QKAHAHSFISELAS-----GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDwpER 199
|
170 180
....*....|....*....|....
gi 6671497 652 IALLSITHRPSLWKYHTHLLQFDG 675
Cdd:cd03248 200 RTVLVIAHRLSTVERADQILVLDG 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
486-634 |
4.03e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 68.44 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY--------KPPPQR----------MFyipqrPY 547
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMldgqdithVPAENRhvntvfqsyaLF-----PH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 548 MSVgslRDQViypdsAEDMRRKGCSEQQ-----LEAiLGIVHLRHILQREggweavcdwKDVLSGGEKQRIGMARMFYHR 622
Cdd:PRK09452 101 MTV---FENV-----AFGLRMQKTPAAEitprvMEA-LRMVQLEEFAQRK---------PHQLSGGQQQRVAIARAVVNK 162
|
170
....*....|..
gi 6671497 623 PKYALLDECTSA 634
Cdd:PRK09452 163 PKVLLLDESLSA 174
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
488-643 |
4.93e-12 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 65.68 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEGMHLLItGPNGCGKSSLFRILGGLWPTYSGVLY----KPPPQRMF------YIPQR----PYMSVgsl 553
Cdd:cd03264 14 RALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRidgqDVLKQPQKlrrrigYLPQEfgvyPNFTV--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 554 RDQVIYPDSAEDMRRKGCsEQQLEAILGIVHLRHILQREGGweavcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTs 633
Cdd:cd03264 90 REFLDYIAWLKGIPSKEV-KARVDEVLELVNLGDRAKKKIG---------SLSGGMRRRVGIAQALVGDPSILIVDEPT- 158
|
170
....*....|
gi 6671497 634 aVSIDVEGKI 643
Cdd:cd03264 159 -AGLDPEERI 167
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
486-661 |
5.68e-12 |
|
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: 66.26 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYSGVLY----KPPPQRMFYIpqRPYMSV--GSLRDQVI 558
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRlfgeRRGGEDVWEL--RKRIGLvsPALQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 559 YPDSAEDM----------RRKGCSEQQLE---AILGIVHLRHILQREGGweavcdwkdVLSGGEKQRIGMARMFYHRPKY 625
Cdd:COG1119 93 RDETVLDVvlsgffdsigLYREPTDEQRErarELLELLGLAHLADRPFG---------TLSQGEQRRVLIARALVKDPEL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6671497 626 ALLDECTSavSIDVEGK------IFQAAKDAGIALLSITHRP 661
Cdd:COG1119 164 LILDEPTA--GLDLGARelllalLDKLAAEGAPTLVLVTHHV 203
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
486-630 |
5.86e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 67.79 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG--------VLYKPPPQRMF-YIPQR----PYMSVgs 552
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGeiliggrdVTDLPPKDRNIaMVFQSyalyPHMTV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 553 lRDQVIYPdsaedMRRKGCS----EQQLEAILGIVHLRHILQR---EggweavcdwkdvLSGGEKQRIGMARMFYHRPKY 625
Cdd:COG3839 93 -YENIAFP-----LKLRKVPkaeiDRRVREAAELLGLEDLLDRkpkQ------------LSGGQRQRVALGRALVREPKV 154
|
....*
gi 6671497 626 ALLDE 630
Cdd:COG3839 155 FLLDE 159
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
489-660 |
6.66e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.70 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY---KPPP--------QRMFYIPQRPYMSVGSLRDQV 557
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlngQPIAdyseaalrQAISVVSQRVHLFSATLRDNL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 558 IypdsaedMRRKGCSEQQLEAILGIVHLRHILQREGGWEAvcdW----KDVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:PRK11160 435 L-------LAAPNASDEALIEVLQQVGLEKLLEDDKGLNA---WlgegGRQLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180
....*....|....*....|....*....
gi 6671497 634 AVSIDVEGKIFQAAKD--AGIALLSITHR 660
Cdd:PRK11160 505 GLDAETERQILELLAEhaQNKTVLMITHR 533
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
489-659 |
6.83e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 6.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYKPPPQRMFYIPQRPYMsvgslrDQVIYPDSAEDMR- 567
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYL------DTTLPLTVNRFLRl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 568 RKGCSEQQLEAILGIVHLRHILQREggweavcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVsiDVEGK----- 642
Cdd:PRK09544 93 RPGTKKEDILPALKRVQAGHLIDAP---------MQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV--DVNGQvalyd 161
|
170
....*....|....*...
gi 6671497 643 -IFQAAKDAGIALLSITH 659
Cdd:PRK09544 162 lIDQLRRELDCAVLMVSH 179
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
486-666 |
7.32e-12 |
|
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: 64.86 E-value: 7.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLwPTYS----GVLYKpppqrmfyipqrpymsvgslrDQVIYPD 561
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEvtegEILFK---------------------GEDITDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 562 SAEDMRRKGC--SEQQLEAILGiVHLRHILQ--REGgweavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVSI 637
Cdd:cd03217 70 PPEERARLGIflAFQYPPEIPG-VKNADFLRyvNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190
....*....|....*....|....*....|..
gi 6671497 638 D---VEGKIFQAAKDAGIALLSITHRPSLWKY 666
Cdd:cd03217 138 DalrLVAEVINKLREEGKSVLIITHYQRLLDY 169
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
486-659 |
7.91e-12 |
|
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: 66.03 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLY------KPPP---QRMFYIPQRPYMSVG-SLR 554
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGsILIdgedvrKEPRearRQIGVLPDERGLYDRlTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 555 DQV-----IYPDSAEDMRRKgcsEQQLEAILGIVHLRHILQREggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:COG4555 93 ENIryfaeLYGLFDEELKKR---IEELIELLGLEEFLDRRVGE------------LSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190
....*....|....*....|....*....|....*
gi 6671497 630 ECTSAvsIDVEG-----KIFQAAKDAGIALLSITH 659
Cdd:COG4555 158 EPTNG--LDVMArrllrEILRALKKEGKTVLFSSH 190
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
486-630 |
1.35e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.78 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVL--------YKPPPQR----MFyipQR----PYMS 549
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlsHVPPYQRpinmMF---QSyalfPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 550 VgslrDQVIYPDSAEDMRRKGCSEQQLEAILGIVHLRHILQREggweavcdwKDVLSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:PRK11607 108 V----EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRK---------PHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
.
gi 6671497 630 E 630
Cdd:PRK11607 175 E 175
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
488-630 |
1.57e-11 |
|
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: 64.20 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY--------KPPPQR---MFYipQR----PYMSVgs 552
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdLPPKDRdiaMVF--QNyalyPHMTV-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 553 lRDQVIYPDSAEDMRRKGCSEQQLEA--ILGIVHLRHILQREggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:cd03301 90 -YDNIAFGLKLRKVPKDEIDERVREVaeLLQIEHLLDRKPKQ------------LSGGQRQRVALGRAIVREPKVFLMDE 156
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
484-661 |
2.00e-11 |
|
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: 67.00 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 484 PTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG--VLYKPPPQ---------RMFYIPQRPYMSVGS 552
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGevTLDGVPVSsldqdevrrRVSVCAQDAHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 553 LRDQVIypdsaedMRRKGCSEQQLEAILGIVHL-RHILQREGGWEAVC-DWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:TIGR02868 425 VRENLR-------LARPDATDEELWAALERVGLaDWLRALPDGLDTVLgEGGARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|...
gi 6671497 631 CTSAVSIDVEGKIFQ--AAKDAGIALLSITHRP 661
Cdd:TIGR02868 498 PTEHLDAETADELLEdlLAALSGRTVVLITHHL 530
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
489-659 |
2.72e-11 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 63.39 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGV--LYKPPPQRMFYIPQRpymsVGSLRD-QVIYPD-SA- 563
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEitFDGKSYQKNIEALRR----IGALIEaPGFYPNlTAr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 564 EDMRRKGC----SEQQLEAILGIVHLRHILQREGGweavcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAvsIDV 639
Cdd:cd03268 91 ENLRLLARllgiRKKRIDEVLDVVGLKDSAKKKVK---------GFSLGMKQRLGIALALLGNPDLLILDEPTNG--LDP 159
|
170 180
....*....|....*....|....*
gi 6671497 640 EG-----KIFQAAKDAGIALLSITH 659
Cdd:cd03268 160 DGikelrELILSLRDQGITVLISSH 184
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
489-663 |
4.57e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.28 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYSGVLYKPPPQRMF---YI-------PQRPYMSVGSLRDQV 557
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPTGGQVLLDGVPLVQYdhhYLhrqvalvGQEPVLFSGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 558 IYpdsaedmrrkGCSEQQLEAILGIVHLRH----ILQREGGWEAVCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:TIGR00958 576 AY----------GLTDTPDEEIMAAAKAANahdfIMEFPNGYDTEVGEKGSqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190
....*....|....*....|....*....|.
gi 6671497 633 SAVSIDVEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:TIGR00958 646 SALDAECEQLLQESRSRASRTVLLIAHRLST 676
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
486-659 |
4.62e-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: 65.12 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG--------VLYKPPPQRMF-YIPQR----PYMSVgs 552
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGrilldgrdVTGLPPEKRNVgMVFQDyalfPHLTV-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 553 lRDQVIYPdsaedMRRKGCSEQQLEA----ILGIVHLRHILQR---EggweavcdwkdvLSGGEKQRIGMARMFYHRPKY 625
Cdd:COG3842 95 -AENVAFG-----LRMRGVPKAEIRArvaeLLELVGLEGLADRyphQ------------LSGGQQQRVALARALAPEPRV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6671497 626 ALLDECTSAvsIDVEGK------IFQAAKDAGIALLSITH 659
Cdd:COG3842 157 LLLDEPLSA--LDAKLReemreeLRRLQRELGITFIYVTH 194
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
482-646 |
1.48e-10 |
|
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: 64.93 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 482 ITPtgevVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYSGVLYKpppQRMFYIPQRPYMSVGSLRDQVIYP 560
Cdd:TIGR01271 438 VTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPSEGKIKHS---GRISFSPQTSWIMPGTIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 561 DSAEDMRR----KGCseqQLEAILGIVHLR-HILQREGGWeavcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAV 635
Cdd:TIGR01271 511 LSYDEYRYtsviKAC---QLEEDIALFPEKdKTVLGEGGI--------TLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170
....*....|.
gi 6671497 636 SIDVEGKIFQA 646
Cdd:TIGR01271 580 DVVTEKEIFES 590
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
486-661 |
1.64e-10 |
|
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: 60.97 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLYKPPP---------QRMFYIPQRPYMSvGSLrd 555
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGrVLLNGGPldfqrdsiaRGLLYLGHAPGIK-TTL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 556 qviypDSAEDMR--RKGCSEQQLEAILGIVHLRHILQREGGWeavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:cd03231 89 -----SVLENLRfwHADHSDEQVEEALARVGLNGFEDRPVAQ---------LSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|..
gi 6671497 634 AVSIDVEGKIFQA----AKDAGIALLSiTHRP 661
Cdd:cd03231 155 ALDKAGVARFAEAmaghCARGGMVVLT-THQD 185
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
487-663 |
3.97e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.36 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 487 EVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLwptysgvLYKPPPQRMFYIPQRPYMSVGSLRDQViypDSAEDM 566
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA-------LKGTPVAGCVDVPDNQFGREASLIDAI---GRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 567 rrkgcseqqLEAIlgivhlrHILQREGGWEAVCdWK---DVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID----V 639
Cdd:COG2401 113 ---------KDAV-------ELLNAVGLSDAVL-WLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtakrV 175
|
170 180
....*....|....*....|....
gi 6671497 640 EGKIFQAAKDAGIALLSITHRPSL 663
Cdd:COG2401 176 ARNLQKLARRAGITLVVATHHYDV 199
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
487-660 |
6.05e-10 |
|
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: 58.86 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 487 EVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY---KPPP-------QRMFYIPQRPYMSVGSLRDQ 556
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITldgVPVSdlekalsSLISVLNQRPYLFDTTLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 557 ViypdsaedMRRkgcseqqleailgivhlrhilqreggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTsaVS 636
Cdd:cd03247 95 L--------GRR------------------------------------FSGGERQRLALARILLQDAPIVLLDEPT--VG 128
|
170 180 190
....*....|....*....|....*....|
gi 6671497 637 IDVEGK------IFQAAKDAgiALLSITHR 660
Cdd:cd03247 129 LDPITErqllslIFEVLKDK--TLIWITHH 156
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
489-646 |
8.12e-10 |
|
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: 60.64 E-value: 8.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPT-----YSGvlykpppqRMFYIPQRPYMSVGSLRDQVIYPDS 562
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEPSegkikHSG--------RISFSSQFSWIMPGTIKENIIFGVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 563 AEDMRRKGCSE--QQLEAILGIVHLRHILQREGGWeavcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVE 640
Cdd:cd03291 124 YDEYRYKSVVKacQLEEDITKFPEKDNTVLGEGGI--------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
....*.
gi 6671497 641 GKIFQA 646
Cdd:cd03291 196 KEIFES 201
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
486-659 |
9.28e-10 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 59.08 E-value: 9.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-------VLYKPPP------QRMFYIPQR----PYM 548
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtiiidglKLTDDKKninelrQKVGMVFQQfnlfPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 549 SVgsLRDQVIYPdsaedMRRKGCSEQQLEAILgivhlRHILQREGGWEAVCDWKDVLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03262 92 TV--LENITLAP-----IKVKGMSKAEAEERA-----LELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190
....*....|....*....|....*....|....*
gi 6671497 629 DECTSA----VSIDVEGKIFQAAKDaGIALLSITH 659
Cdd:cd03262 160 DEPTSAldpeLVGEVLDVMKDLAEE-GMTMVVVTH 193
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
486-643 |
9.59e-10 |
|
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: 62.06 E-value: 9.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLYKPPP----------QRMFYIPQRPYMSVGSLR 554
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGeILLNGFSlkdidrhtlrQFINYLPQEPYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 555 DQVIYPDsaedmrRKGCSEQQLEAILGIVHLR-HILQREGGWEA-VCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:TIGR01193 566 ENLLLGA------KENVSQDEIWAACEIAEIKdDIENMPLGYQTeLSEEGSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170
....*....|.
gi 6671497 633 SAVSIDVEGKI 643
Cdd:TIGR01193 640 SNLDTITEKKI 650
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
490-669 |
1.04e-09 |
|
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: 59.27 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 490 VASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY---KPPPQRMF------------YIPQRPYMSVGSLR 554
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnKNESEPSFeatrsrnrysvaYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 555 DQVIYPDSAEDMRRK----GCSEQQleailGIVHLRHILQREGGWEAVCdwkdvLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:cd03290 97 ENITFGSPFNKQRYKavtdACSLQP-----DIDLLPFGDQTEIGERGIN-----LSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6671497 631 CTSAVSIDVEGKIFQAA-----KDAGIALLSITHRpslWKYHTH 669
Cdd:cd03290 167 PFSALDIHLSDHLMQEGilkflQDDKRTLVLVTHK---LQYLPH 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
474-663 |
1.26e-09 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 58.91 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 474 IICENIPIITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTySGVLY-------KPPPQRMFYIPQR 545
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKlLYGEERPT-SGQVLvngqdlsRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 546 -----------PYMSVG-----SLRdqVIYPDSAEDMRRkgcseqqLEAILGIVHLRHILQR---EggweavcdwkdvLS 606
Cdd:COG2884 81 igvvfqdfrllPDRTVYenvalPLR--VTGKSRKEIRRR-------VREVLDLVGLSDKAKAlphE------------LS 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671497 607 GGEKQRIGMARMFYHRPKYALLDECT----SAVSIDVEgKIFQAAKDAGIALLSITHRPSL 663
Cdd:COG2884 140 GGEQQRVAIARALVNRPELLLADEPTgnldPETSWEIM-ELLEEINRRGTTVLIATHDLEL 199
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
488-659 |
1.68e-09 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 58.60 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGlwpTY---SG-VLY----------KPPPQRMFYIPQRP--YMS-- 549
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG---NYlpdSGsILVrhdggwvdlaQASPREILALRRRTigYVSqf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 550 ------VGSLrDQViypdsAEDMRRKGCSEQQLEAILgivhlRHILQR----EGGWEavcdwkdvL-----SGGEKQRIG 614
Cdd:COG4778 102 lrviprVSAL-DVV-----AEPLLERGVDREEARARA-----RELLARlnlpERLWD--------LppatfSGGEQQRVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671497 615 MARMFYHRPKYALLDECTSavSIDVEGK-----IFQAAKDAGIALLSITH 659
Cdd:COG4778 163 IARGFIADPPLLLLDEPTA--SLDAANRavvveLIEEAKARGTAIIGIFH 210
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
474-660 |
2.10e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.63 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 474 IICENIPIITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPtYSGVL--------------YKpppQRM 539
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLkingielreldpesWR---KHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 540 FYIPQRPYMSVGSLRDQVIypdsaedMRRKGCSEQQLEAILGIVHLRHILQR-EGGWE-AVCDWKDVLSGGEKQRIGMAR 617
Cdd:PRK11174 426 SWVGQNPQLPHGTLRDNVL-------LGNPDASDEQLQQALENAWVSEFLPLlPQGLDtPIGDQAAGLSVGQAQRLALAR 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6671497 618 MFYHRPKYALLDECTSAVSIDVEGKIFQAAKDA--GIALLSITHR 660
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQ 543
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
489-659 |
2.63e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.54 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYK---PPPQ-----RMFYIPQR--PYMSV-------- 550
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAgtaPLAEaredtRLMFQDARllPWKKVidnvglgl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 551 -GSLRDQviypdsaedmrrkgcSEQQLEAIlgivhlrhilqreGGWEAVCDWKDVLSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:PRK11247 107 kGQWRDA---------------ALQALAAV-------------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190
....*....|....*....|....*....|....
gi 6671497 630 ECTSAVS----IDVEGKIFQAAKDAGIALLSITH 659
Cdd:PRK11247 159 EPLGALDaltrIEMQDLIESLWQQHGFTVLLVTH 192
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
486-659 |
2.64e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 58.37 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGV------------LYKPPPQRMFYIPQRP------- 546
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddedisllpLHARARRGIGYLPQEAsifrrls 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 547 ----YMSVGSLRDQViypdSAEdmRRKGCSEQQLEAiLGIVHLRHILQREggweavcdwkdvLSGGEKQRIGMARMFYHR 622
Cdd:PRK10895 95 vydnLMAVLQIRDDL----SAE--QREDRANELMEE-FHIEHLRDSMGQS------------LSGGERRRVEIARALAAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6671497 623 PKYALLDECTSAVS----IDVEgKIFQAAKDAGIALLSITH 659
Cdd:PRK10895 156 PKFILLDEPFAGVDpisvIDIK-RIIEHLRDSGLGVLITDH 195
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
492-645 |
3.50e-09 |
|
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: 60.34 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 492 SLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLYKpppQRMFYIPQRPYMSVGSLRDQVIYPDSAEDMRRKg 570
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGhVHMK---GSVAYVPQQAWIQNDSLRENILFGKALNEKYYQ- 731
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671497 571 cseQQLEAILGIVHLRhIL----QREGGWEAVCdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQ 645
Cdd:TIGR00957 732 ---QVLEACALLPDLE-ILpsgdRTEIGEKGVN-----LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
486-661 |
3.53e-09 |
|
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: 56.98 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGV----------LYKPPPQRMFYIPQRPYMSvGSLrd 555
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEvrwngtplaeQRDEPHENILYLGHLPGLK-PEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 556 qviypDSAEDMR---RKGCSEQQ-LEAILGIVHLRHILQREGGWeavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDEC 631
Cdd:TIGR01189 89 -----SALENLHfwaAIHGGAQRtIEDALAAVGLTGFEDLPAAQ---------LSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 6671497 632 TsaVSIDVEG-KIFQAAKDA-----GIALLSiTHRP 661
Cdd:TIGR01189 155 T--TALDKAGvALLAGLLRAhlargGIVLLT-THQD 187
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
486-659 |
4.61e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 55.53 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYKPPPQRMFYIPQrpymsvgslrdqviypdsaed 565
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 566 mrrkgcseqqleailgivhlrhilqreggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSavSIDVEGKIF- 644
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN--HLDLESIEAl 109
|
170
....*....|....*.
gi 6671497 645 -QAAKDAGIALLSITH 659
Cdd:cd03221 110 eEALKEYPGTVILVSH 125
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
486-671 |
4.73e-09 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 56.47 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYKPPPQRMFYIPQR-------PY-----MSVGSL 553
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRsevpdslPLtvrdlVAMGRW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 554 RDQVIY-PDSAEDMRRkgcSEQQLEAiLGIVHLRHILQREggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:NF040873 84 ARRGLWrRLTRDDRAA---VDDALER-VGLADLAGRQLGE------------LSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6671497 633 SAVSIDVEGKIFQ---AAKDAGIALLSITHRPSLWKYHTHLL 671
Cdd:NF040873 148 TGLDAESRERIIAllaEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
486-659 |
6.37e-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: 56.04 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYSGVLY------------KPPPQRMFYIPQR----PYM 548
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLeEPDSGSILIdgedltdledelPPLRRRIGMVFQDfalfPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 549 SVgslRDQVIYPdsaedmrrkgcseqqleailgivhlrhilqreggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03229 92 TV---LENIALG--------------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190
....*....|....*....|....*....|....*
gi 6671497 629 DECTSA----VSIDVEGKIFQAAKDAGIALLSITH 659
Cdd:cd03229 125 DEPTSAldpiTRREVRALLKSLQAQLGITVVLVTH 159
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
493-661 |
7.39e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLYKPPP---------QRMFYIPQRPymsvGslrdqvIYPD- 561
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGeVLWQGEPirrqrdeyhQDLLYLGHQP----G------IKTEl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 562 SAED-----MRRKGC-SEQQLEAILGIVHLRhilQREggwEAVCdwkDVLSGGEKQRIGMARMFYHRPKYALLDECTSAv 635
Cdd:PRK13538 90 TALEnlrfyQRLHGPgDDEALWEALAQVGLA---GFE---DVPV---RQLSAGQQRRVALARLWLTRAPLWILDEPFTA- 159
|
170 180 190
....*....|....*....|....*....|..
gi 6671497 636 sIDVEG-KIFQA-----AKDAGIALLSiTHRP 661
Cdd:PRK13538 160 -IDKQGvARLEAllaqhAEQGGMVILT-THQD 189
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
489-659 |
7.54e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 57.05 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLY--KP----PPQRMFYI----PQRPYMSVGSLRDQV 557
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGeVRLngRPlaawSPWELARRravlPQHSSLAFPFTVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 558 I----YPDSAEDMRRKGCSEQQLEAiLGIVHLRHILQREggweavcdwkdvLSGGEKQRIGMAR-------MFYHRPKYA 626
Cdd:COG4559 96 ValgrAPHGSSAAQDRQIVREALAL-VGLAHLAGRSYQT------------LSGGEQQRVQLARvlaqlwePVDGGPRWL 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 6671497 627 LLDECTSAVSIDVEGKIFQAAKD---AGIALLSITH 659
Cdd:COG4559 163 FLDEPTSALDLAHQHAVLRLARQlarRGGGVVAVLH 198
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
489-660 |
1.10e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 56.40 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY--------KPPPQR----MFYIPQRPY----MSVG- 551
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILldgqditkLPMHKRarlgIGYLPQEASifrkLTVEe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 552 --SLRDQVIYPDSAEDMRRkgcseqqLEAILGIVHLRHILQREGgweavcdwkDVLSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:cd03218 95 niLAVLEIRGLSKKEREEK-------LEELLEEFHITHLRKSKA---------SSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6671497 630 ECTSAVS----IDVEgKIFQAAKDAGI----------ALLSITHR 660
Cdd:cd03218 159 EPFAGVDpiavQDIQ-KIIKILKDRGIgvlitdhnvrETLSITDR 202
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
505-662 |
1.39e-08 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 57.43 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 505 ITGPNGCGKSSLFRILGGLWPTYSGVLY--------------KPPPQRMF-YIPQR----PYMSVgslRDQVIYPDSAED 565
Cdd:TIGR02142 28 IFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtlfdsrkgifLPPEKRRIgYVFQEarlfPHLSV---RGNLRYGMKRAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 566 MRRKGCSEQQLEAILGIVHLrhiLQREGGweavcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIF- 644
Cdd:TIGR02142 105 PSERRISFERVIELLGIGHL---LGRLPG---------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILp 172
|
170 180
....*....|....*....|.
gi 6671497 645 ---QAAKDAGIALLSITHRPS 662
Cdd:TIGR02142 173 yleRLHAEFGIPILYVSHSLQ 193
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
483-662 |
1.98e-08 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 55.70 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 483 TPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVL---------YKPPPQR--MFYIPQRPYMSVG 551
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlidghdvrdYTLASLRrqIGLVSQDVFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 552 SLRDQVIYPdsaedmrRKGCSEQQLEAILGIVHLrH--ILQREGGWEAVCDWKDV-LSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03251 91 TVAENIAYG-------RPGATREEVEEAARAANA-HefIMELPEGYDTVIGERGVkLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 6671497 629 DECTSAVSIDVEgKIFQAAKD---AGIALLSITHRPS 662
Cdd:cd03251 163 DEATSALDTESE-RLVQAALErlmKNRTTFVIAHRLS 198
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
488-642 |
2.26e-08 |
|
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: 55.20 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY----------KPPPQRMFYIPQrpymsvgslrDQV 557
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYingysirtdrKAARQSLGYCPQ----------FDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 558 IYPD-SAEDM-----RRKGCSEQQLEAILgivhlrHILQREGGWEAVCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:cd03263 86 LFDElTVREHlrfyaRLKGLPKSEIKEEV------ELLLRVLGLTDKANKRARtLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170
....*....|..
gi 6671497 631 CTSavSIDVEGK 642
Cdd:cd03263 160 PTS--GLDPASR 169
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
480-643 |
5.90e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.41 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 480 PIIT--------PTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTySGVLYKPPPQRMFYIPQRPYMSV 550
Cdd:PLN03073 507 PIISfsdasfgyPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGeLQPS-SGTVFRSAKVRMAVFSQHHVDGL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 551 GSLRDQVIYpdsaedMRR--KGCSEQQLEAILGIVHLRHILQREGGWeavcdwkdVLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:PLN03073 586 DLSSNPLLY------MMRcfPGVPEQKLRAHLGSFGVTGNLALQPMY--------TLSGGQKSRVAFAKITFKKPHILLL 651
|
170
....*....|....*.
gi 6671497 629 DECTSAVSID-VEGKI 643
Cdd:PLN03073 652 DEPSNHLDLDaVEALI 667
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
487-661 |
7.01e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 54.28 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 487 EVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-------VLY-------------KPPPQRMFYIPQR- 545
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSkikvdgkVLYfgkdifqidaiklRKEVGMVFQQPNPf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 546 PYMSVgslRDQVIYPDSAEDMRRKgcseQQLEAILgivhlRHILQREGGWEAVCDWKDV----LSGGEKQRIGMARMFYH 621
Cdd:PRK14246 103 PHLSI---YDNIAYPLKSHGIKEK----REIKKIV-----EECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6671497 622 RPKYALLDECTSAVSI----DVEGKIFQAAKDAGIALLSitHRP 661
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIvnsqAIEKLITELKNEIAIVIVS--HNP 212
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
489-660 |
8.61e-08 |
|
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: 53.18 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSL----FRIL----GGLwpTYSGVLYKPPP-----QRMFYIPQRPYMSVGSLRD 555
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLilalFRFLeaeeGKI--EIDGIDISTIPledlrSSLTIIPQDPTLFSGTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 556 QViypdSAEDMRrkgcSEQQLEAILGIvhlrhilqREGGweavcdwkDVLSGGEKQRIGMARMFYHRPKYALLDECTSAV 635
Cdd:cd03369 101 NL----DPFDEY----SDEEIYGALRV--------SEGG--------LNLSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180
....*....|....*....|....*..
gi 6671497 636 SIDVEGKIFQAAKD--AGIALLSITHR 660
Cdd:cd03369 157 DYATDALIQKTIREefTNSTILTIAHR 183
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
497-659 |
8.87e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 54.25 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 497 VEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLykpppqRMFYIP-----------------QRP-YMSVGS-LRDQV 557
Cdd:PRK13635 30 VYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI------TVGGMVlseetvwdvrrqvgmvfQNPdNQFVGAtVQDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 558 IYPDSAEDMRRKGCSEQQLEAiLGIVHLRHILQREggweavcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVS- 636
Cdd:PRK13635 104 AFGLENIGVPREEMVERVDQA-LRQVGMEDFLNRE---------PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDp 173
|
170 180
....*....|....*....|....*.
gi 6671497 637 ---IDVEGKIFQAAKDAGIALLSITH 659
Cdd:PRK13635 174 rgrREVLETVRQLKEQKGITVLSITH 199
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
488-659 |
9.44e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 54.73 E-value: 9.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGlwptysgvLYKPPPQRMFY---------IPQR------------P 546
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAG--------LEKPTEGQIFIdgedvthrsIQQRdicmvfqsyalfP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 547 YMSVGslrDQVIYpdsAEDMRRKGCSE--QQLEAILGIVHLrhilqreGGWEAvcDWKDVLSGGEKQRIGMARMFYHRPK 624
Cdd:PRK11432 92 HMSLG---ENVGY---GLKMLGVPKEErkQRVKEALELVDL-------AGFED--RYVDQISGGQQQRVALARALILKPK 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 6671497 625 YALLDECTSAVSIDV----EGKIFQAAKDAGIALLSITH 659
Cdd:PRK11432 157 VLLFDEPLSNLDANLrrsmREKIRELQQQFNITSLYVTH 195
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
488-659 |
1.08e-07 |
|
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: 53.50 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEG-MHLLItGPNGCGKSSLFRILGGLWPTYSG-VLYK-------PPPQ-------RMFYIPQ-RPYMSV 550
Cdd:COG0411 18 VAVDDVSLEVERGeIVGLI-GPNGAGKTTLFNLITGFYRPTSGrILFDgrditglPPHRiarlgiaRTFQNPRlFPELTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 551 -------------GSLRDQVIYPDSAEDMRRKgcSEQQLEAILGIVHLRHILQREGGweavcdwkdVLSGGEKQRIGMAR 617
Cdd:COG0411 97 lenvlvaaharlgRGLLAALLRLPRARREERE--ARERAEELLERVGLADRADEPAG---------NLSYGQQRRLEIAR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6671497 618 MFYHRPKYALLDECTSAVSI----DVEGKIFQAAKDAGIALLSITH 659
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPeeteELAELIRRLRDERGITILLIEH 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
505-632 |
1.43e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.94 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 505 ITGPNGCGKSSLFRILGGLWPTYSGVLYKPPPQRMFYIPQRPY------------MSVGSLRDQV--------IYPDSAE 564
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQldptktvrenveEGVAEIKDALdrfneisaKYAEPDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 565 DMRRKGCSEQQLEAilgivhlrhILQREGGWE----------AV-C---DWK-DVLSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:TIGR03719 116 DFDKLAAEQAELQE---------IIDAADAWDldsqleiamdALrCppwDADvTKLSGGERRRVALCRLLLSKPDMLLLD 186
|
...
gi 6671497 630 ECT 632
Cdd:TIGR03719 187 EPT 189
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
489-666 |
2.14e-07 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 52.89 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYSGVLYKPPPQRMFYIPQRPYMSvgslRD-QVIYPDS---- 562
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEkPAQGTVSFRGQDLYQLDRKQRRAFR----RDvQLVFQDSpsav 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 563 ----------AEDMR---RKGCSEQQ--LEAILGIVHLR-HILQReggweavcdWKDVLSGGEKQRIGMARMFYHRPKYA 626
Cdd:TIGR02769 102 nprmtvrqiiGEPLRhltSLDESEQKarIAELLDMVGLRsEDADK---------LPRQLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6671497 627 LLDECTSAVSIDVEGKIFQAAKD----AGIALLSITHRPSLWKY 666
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKlqqaFGTAYLFITHDLRLVQS 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
484-659 |
2.70e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.77 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 484 PTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYSGVLYKPPP------------QRMFYIPQRPymsv 550
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPTSGEVLIKGEPikydkksllevrKTVGIVFQNP---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 551 gslRDQVIYPDSAEDMR----RKGCSEQQLEAilgivHLRHILQREG--GWEAVCDWKdvLSGGEKQRIGMARMFYHRPK 624
Cdd:PRK13639 88 ---DDQLFAPTVEEDVAfgplNLGLSKEEVEK-----RVKEALKAVGmeGFENKPPHH--LSGGQKKRVAIAGILAMKPE 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 6671497 625 YALLDECTSAVSIDVEGKIFQAAKD---AGIALLSITH 659
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDlnkEGITIIISTH 195
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
474-669 |
3.78e-07 |
|
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: 51.64 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 474 IICENIPIITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYSGVLYKPPPQRMFYIPQRPYM--SV 550
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKlIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 551 GS-------LRDQVIYPDSAEDMRRKGCSEQQLE----AILGIVHLRHILQreggweavcDWKDVLSGGEKQRIGMARMF 619
Cdd:cd03292 81 GVvfqdfrlLPDRNVYENVAFALEVTGVPPREIRkrvpAALELVGLSHKHR---------ALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6671497 620 YHRPKYALLDECTSAVSIDVEGKI---FQAAKDAGIALLSITHRPSLWKYHTH 669
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEImnlLKKINKAGTTVVVATHAKELVDTTRH 204
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
461-671 |
3.86e-07 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 51.88 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 461 LKIQGQVVDVEQGIICENIPIITPTGEVVVaslnirveegmhllITGPNGCGKSSLFRILGGlWPTY---SG-VLYK--- 533
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHA--------------IMGPNGSGKSTLSKTIAG-HPSYevtSGtILFKgqd 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 534 ----PPPQR----MFYIPQRPYMSVG-SLRDqviYPDSAEDMRRKGCSEQQLEAILGIVHLRHILQREGGWEAVCDwKDV 604
Cdd:TIGR01978 66 llelEPDERaragLFLAFQYPEEIPGvSNLE---FLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLN-RSV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671497 605 ---LSGGEKQRIGMARMFYHRPKYALLDECTSAVSID-----VEGkiFQAAKDAGIALLSITHRPSLWKY----HTHLL 671
Cdd:TIGR01978 142 negFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDalkivAEG--INRLREPDRSFLIITHYQRLLNYikpdYVHVL 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
489-630 |
4.66e-07 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 52.46 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTySGVLY---------KPPPQR-MFYIPQR----PYMSVgsl 553
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLeTPD-SGRIVlngrdlftnLPPRERrVGFVFQHyalfPHMTV--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 554 RDQViypdsAEDMRRKGCSEQQLEAI----LGIVHLRHILQR---EggweavcdwkdvLSGGEKQRIGMARMFYHRPKYA 626
Cdd:COG1118 93 AENI-----AFGLRVRPPSKAEIRARveelLELVQLEGLADRypsQ------------LSGGQRQRVALARALAVEPEVL 155
|
....
gi 6671497 627 LLDE 630
Cdd:COG1118 156 LLDE 159
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
497-659 |
4.75e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.04 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 497 VEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY----KPPPQRMFYIPQRPYMSVGSLRDQ----VIYPDSAEDMRR 568
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIidgdLLTEENVWDIRHKIGMVFQNPDNQfvgaTVEDDVAFGLEN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 569 KGCSEQQL-----EAiLGIVHLRHILQREGGweavcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAvsIDVEGK- 642
Cdd:PRK13650 110 KGIPHEEMkervnEA-LELVGMQDFKEREPA---------RLSGGQKQRVAIAGAVAMRPKIIILDEATSM--LDPEGRl 177
|
170 180
....*....|....*....|..
gi 6671497 643 -----IFQAAKDAGIALLSITH 659
Cdd:PRK13650 178 eliktIKGIRDDYQMTVISITH 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
486-630 |
6.62e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 52.76 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYKPPPQRMFYIPQ-RPYMSVG-SLRDQVIypDSA 563
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQhQEELDPDkTVLDELR--DGA 404
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6671497 564 EDMRRKgcseqqleailgivHLRHILQR-----EGGWEAVcdwkDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:COG0488 405 PGGTEQ--------------EVRGYLGRflfsgDDAFKPV----GVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
488-659 |
9.61e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 50.48 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY------KPPPQRMFYIPQR-----------PYMSv 550
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkvNDPKVDERLIRQEagmvfqqfylfPHLT- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 551 gSLRDQVIYPdsaedMRRKGCSEQQLEAILgivhlRHILQREGGWEAVCDWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:PRK09493 94 -ALENVMFGP-----LRVRGASKEEAEKQA-----RELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190
....*....|....*....|....*....|....
gi 6671497 631 CTSAvsIDVE-----GKIFQAAKDAGIALLSITH 659
Cdd:PRK09493 163 PTSA--LDPElrhevLKVMQDLAEEGMTMVIVTH 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
488-676 |
9.78e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.76 E-value: 9.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY-----------KPPPQRMFYIPQRPY----MSVGS 552
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWldgehiqhyasKEVARRIGLLAQNATtpgdITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 553 LRDQVIYPDSAEDMRRKGCSEQQLEAIL---GIVHLRHilqreggwEAVcdwkDVLSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:PRK10253 101 LVARGRYPHQPLFTRWRKEDEEAVTKAMqatGITHLAD--------QSV----DTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6671497 630 ECTSAV----SIDVEGKIFQAAKDAGIALLSITHR-PSLWKYHTHLLQF-DGE 676
Cdd:PRK10253 169 EPTTWLdishQIDLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALrEGK 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
486-634 |
1.24e-06 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 50.54 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLY--KP----PPQRMFYI----PQRPYMSVGSLR 554
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGeVRLngRPladwSPAELARRravlPQHSSLSFPFTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 555 DQVI----YPDSAEDMRRKGCSEQQLEAiLGIVHLRHILQREggweavcdwkdvLSGGEKQRIGMARMF------YHRPK 624
Cdd:PRK13548 94 EEVVamgrAPHGLSRAEDDALVAAALAQ-VDLAHLAGRDYPQ------------LSGGEQQRVQLARVLaqlwepDGPPR 160
|
170
....*....|
gi 6671497 625 YALLDECTSA 634
Cdd:PRK13548 161 WLLLDEPTSA 170
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
489-661 |
1.36e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.30 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTY-----SGVLY--------------KPPPQRMFYIPQR-PYM 548
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYldgqdifkmdvielRRRVQMVFQIPNPiPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 549 SvgslrdqvIYPDSAEDMR--RKGCSEQQLEAilgivHLRHILQREGGWEAVCDWKDV----LSGGEKQRIGMARMFYHR 622
Cdd:PRK14247 98 S--------IFENVALGLKlnRLVKSKKELQE-----RVRWALEKAQLWDEVKDRLDApagkLSGGQQQRLCIARALAFQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6671497 623 PKYALLDECTSAV----SIDVEGKIFQAAKDAGIALlsITHRP 661
Cdd:PRK14247 165 PEVLLADEPTANLdpenTAKIESLFLELKKDMTIVL--VTHFP 205
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
460-646 |
1.41e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 460 PLKIQGQVVDVEQGIICENIPIITPTgevvVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTY-SGVLYKpppQ 537
Cdd:PLN03232 607 PLQPGAPAISIKNGYFSWDSKTSKPT----LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAEtSSVVIR---G 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 538 RMFYIPQRPYMSVGSLRDQVIYPDSAEdmrrkgcSEQQLEAIlGIVHLRHILQREGGWE--AVCDWKDVLSGGEKQRIGM 615
Cdd:PLN03232 680 SVAYVPQVSWIFNATVRENILFGSDFE-------SERYWRAI-DVTALQHDLDLLPGRDltEIGERGVNISGGQKQRVSM 751
|
170 180 190
....*....|....*....|....*....|.
gi 6671497 616 ARMFYHRPKYALLDECTSAVSIDVEGKIFQA 646
Cdd:PLN03232 752 ARAVYSNSDIYIFDDPLSALDAHVAHQVFDS 782
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
489-659 |
1.42e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.20 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYSGVLYKPPPqrmfyIPQRPYMSVGSLRDQ---VIY----- 559
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQP-----MSKLSSAAKAELRNQklgFIYqfhhl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 560 -PD--SAED---------MRRKGCSEQQLE--AILGIVHLRHILQREggweavcdwkdvLSGGEKQRIGMARMFYHRPKY 625
Cdd:PRK11629 99 lPDftALENvamplligkKKPAEINSRALEmlAAVGLEHRANHRPSE------------LSGGERQRVAIARALVNNPRL 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 6671497 626 ALLDECTSAVSIDVEGKIFQAAKD----AGIALLSITH 659
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGElnrlQGTAFLVVTH 204
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
507-630 |
1.48e-06 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 50.87 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 507 GPNGCGKSSLFRILGGLWPTYSG-------VLYK-------PPPQRMF-YIPQ--R--PYMSV-GSLRDqviypdsAEDM 566
Cdd:COG4148 32 GPSGSGKTTLLRAIAGLERPDSGrirlggeVLQDsargiflPPHRRRIgYVFQeaRlfPHLSVrGNLLY-------GRKR 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6671497 567 RRKGCSEQQLEAI---LGIVHL--RHILQreggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:COG4148 105 APRAERRISFDEVvelLGIGHLldRRPAT--------------LSGGERQRVAIGRALLSSPRLLLMDE 159
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
474-663 |
2.46e-06 |
|
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: 49.49 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 474 IICENIPIITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYkpppqrmFYIPQRPYMSVGSL 553
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL-------IDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 554 RDQviypdsaedmRRK-GCSEQQLEAI-------------LGIVHL----------------RHILQREGGWEAVCDWKD 603
Cdd:cd03256 74 RQL----------RRQiGMIFQQFNLIerlsvlenvlsgrLGRRSTwrslfglfpkeekqraLAALERVGLLDKAYQRAD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6671497 604 VLSGGEKQRIGMARMFYHRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLHQVDL 207
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
505-635 |
3.24e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 49.24 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 505 ITGPNGCGKSSLFRILGGLW-PTYSGVLYKPPP----QRMFYIPQRPYMSVGSLRDQVIY-----PDSAEDMRRKGCSEQ 574
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKPldysKRGLLALRQQVATVFQDPEQQIFytdidSDIAFSLRNLGVPEA 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6671497 575 QL----EAILGIVHLRHILQREggweavcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAV 635
Cdd:PRK13638 112 EItrrvDEALTLVDAQHFRHQP---------IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
507-643 |
3.45e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.00 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 507 GPNGCGKSSLFRIL---GGLWPT--------YSGV-LYKPPP------QRMFYIPQRPYMSVGSLRDQVIYpdsaeDMRR 568
Cdd:PRK14239 38 GPSGSGKSTLLRSInrmNDLNPEvtitgsivYNGHnIYSPRTdtvdlrKEIGMVFQQPNPFPMSIYENVVY-----GLRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 569 KGCSEQQL--EAIlgivhlRHILQREGGWEAVcdwKDVL-------SGGEKQRIGMARMFYHRPKYALLDECTSAVSIDV 639
Cdd:PRK14239 113 KGIKDKQVldEAV------EKSLKGASIWDEV---KDRLhdsalglSGGQQQRVCIARVLATSPKIILLDEPTSALDPIS 183
|
....
gi 6671497 640 EGKI 643
Cdd:PRK14239 184 AGKI 187
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
507-659 |
3.89e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.02 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 507 GPNGCGKSSLFRILGGLWPTYSG-VLYKPPP----------QRMFYIPQR-PYMSVGSLRDQVI---YPDSAEDMRRKGC 571
Cdd:PRK10575 44 GHNGSGKSTLLKMLGRHQPPSEGeILLDAQPleswsskafaRKVAYLPQQlPAAEGMTVRELVAigrYPWHGALGRFGAA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 572 SEQQLEAILGIVHLRHILQReggweavcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSI----DVEGKIFQAA 647
Cdd:PRK10575 124 DREKVEEAISLVGLKPLAHR---------LVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLS 194
|
170
....*....|..
gi 6671497 648 KDAGIALLSITH 659
Cdd:PRK10575 195 QERGLTVIAVLH 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
488-660 |
4.10e-06 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 48.52 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGV-------LYKPP---PQRMFYIPQR----PYMSVgsl 553
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFatvdgfdVVKEPaeaRRRLGFVSDStglyDRLTA--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 554 RDQVIYPDSAEDMRRKGcSEQQLEAILGIVHLRHILQREGGweavcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:cd03266 96 RENLEYFAGLYGLKGDE-LTARLEELADRLGMEELLDRRVG---------GFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190
....*....|....*....|....*....|
gi 6671497 634 AVSIDVEGKIF---QAAKDAGIALLSITHR 660
Cdd:cd03266 166 GLDVMATRALRefiRQLRALGKCILFSTHI 195
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
490-666 |
4.46e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 49.32 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 490 VASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLY----------------KPPPQRMFYIPQ---RPYMS 549
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGeVAWlgkdllgmkddewravRSDIQMIFQDPLaslNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 550 VGS-----LRdqVIYPD-SAEDMRRKgcseqqLEAILGIVHLR-HILQReggweavcdWKDVLSGGEKQRIGMARMFYHR 622
Cdd:PRK15079 117 IGEiiaepLR--TYHPKlSRQEVKDR------VKAMMLKVGLLpNLINR---------YPHEFSGGQCQRIGIARALILE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6671497 623 PKYALLDECTSAVSIDVEGKIF----QAAKDAGIALLSITHRPSLWKY 666
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVnllqQLQREMGLSLIFIAHDLAVVKH 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
486-633 |
4.50e-06 |
|
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: 48.65 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY--------------KPPPQRMFYIPQRPY---- 547
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedisglseaelYRLRRRMGMLFQSGAlfds 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 548 MSVGslrDQVIYPdsaedMRRKG-CSEQQLEAI----LGIVHLRHILQReggweavcdWKDVLSGGEKQRIGMARMFYHR 622
Cdd:cd03261 92 LTVF---ENVAFP-----LREHTrLSEEEIREIvlekLEAVGLRGAEDL---------YPAELSGGMKKRVALARALALD 154
|
170
....*....|.
gi 6671497 623 PKYALLDECTS 633
Cdd:cd03261 155 PELLLYDEPTA 165
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
493-659 |
5.88e-06 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 48.58 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY-----KPPPQRMFYIPQRPYMS--------VGSL-RDQVI 558
Cdd:TIGR04520 21 VSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTvdgldTLDEENLWEIRKKVGMVfqnpdnqfVGATvEDDVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 559 Y-PD----SAEDMRRKgcseqqLEAILGIVHLRHILQREggweavcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:TIGR04520 101 FgLEnlgvPREEMRKR------VDEALKLVGMEDFRDRE---------PHLLSGGQKQRVAIAGVLAMRPDIIILDEATS 165
|
170 180 190
....*....|....*....|....*....|..
gi 6671497 634 AvsIDVEGK------IFQAAKDAGIALLSITH 659
Cdd:TIGR04520 166 M--LDPKGRkevletIRKLNKEEGITVISITH 195
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
493-659 |
9.90e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.06 E-value: 9.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYkpppqrMFYIpQRPYMSVGSLRDQV--IY--PD------S 562
Cdd:PRK13632 28 VSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIK------IDGI-TISKENLKEIRKKIgiIFqnPDnqfigaT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 563 AED-----MRRKGCSEQQLEAIlgIVHLRH------ILQREggweavcdwKDVLSGGEKQRIGMARMFYHRPKYALLDEC 631
Cdd:PRK13632 101 VEDdiafgLENKKVPPKKMKDI--IDDLAKkvgmedYLDKE---------PQNLSGGQKQRVAIASVLALNPEIIIFDES 169
|
170 180 190
....*....|....*....|....*....|....
gi 6671497 632 TSAvsIDVEGK------IFQAAKDAGIALLSITH 659
Cdd:PRK13632 170 TSM--LDPKGKreikkiMVDLRKTRKKTLISITH 201
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
505-681 |
1.32e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.39 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 505 ITGPNGCGKSSLFRILGGLWPTYSGVLYKPPPQRMFYIPQrpymSVGSLRD-----QVIypDSAEDMRRKGCSEQQLEAI 579
Cdd:TIGR03719 353 VIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQ----SRDALDPnktvwEEI--SGGLDIIKLGKREIPSRAY 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 580 LGIVHLRHILQReggweavcdwKDV--LSGGEKQRIGMARMFYHRPKYALLDECTSavSIDVEgkIFQAAKDA-----GI 652
Cdd:TIGR03719 427 VGRFNFKGSDQQ----------KKVgqLSGGERNRVHLAKTLKSGGNVLLLDEPTN--DLDVE--TLRALEEAllnfaGC 492
|
170 180 190
....*....|....*....|....*....|
gi 6671497 653 ALLsITH-RPSLWKYHTHLLQFDGEGGWKF 681
Cdd:TIGR03719 493 AVV-ISHdRWFLDRIATHILAFEGDSHVEW 521
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
493-662 |
1.51e-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: 48.28 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 493 LNIRVEEGMHLLITGPNGCGKSSLFRILgglwptysgvlYKpppqrmFYIPQRPYMSVG----------SLR-------- 554
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLL-----------FR------FYDVTSGRILIDgqdirdvtqaSLRaaigivpq 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 555 DQVIYPDS-AEDMR--RKGCSEQQLEAILGIVHLRH-ILQREGGWEAVcdwkdV------LSGGEKQRIGMARMFYHRPK 624
Cdd:COG5265 440 DTVLFNDTiAYNIAygRPDASEEEVEAAARAAQIHDfIESLPDGYDTR-----VgerglkLSGGEKQRVAIARTLLKNPP 514
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6671497 625 YALLDECTSAVSIDVEGKIFQAAKDA--GIALLSITHRPS 662
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVarGRTTLVIAHRLS 554
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
485-659 |
1.56e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.49 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 485 TGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWP--------TYSGVlyKPPPQRMFYIPQRPYMSVGSLRD 555
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPddnpnskiTVDGI--TLTAKTVWDIREKVGIVFQNPDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 556 Q----VIYPDSAEDMRRKGCSEQQLEAILgivhlRHILQREGGWEAVCDWKDVLSGGEKQRIGMARMFYHRPKYALLDEC 631
Cdd:PRK13640 96 QfvgaTVGDDVAFGLENRAVPRPEMIKIV-----RDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190
....*....|....*....|....*....|....
gi 6671497 632 TSAvsIDVEGK------IFQAAKDAGIALLSITH 659
Cdd:PRK13640 171 TSM--LDPAGKeqilklIRKLKKKNNLTVISITH 202
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
493-630 |
2.15e-05 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 46.51 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLYK-------PPPQR----MFYIPQR----PYMSV------ 550
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsIRFDgeditglPPHRIarlgIGYVPEGrrifPSLTVeenlll 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 551 -GSLRdqviypdsaedmRRKGCSEQQLEAILGIV-HLRHILQREGGweavcdwkdVLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:COG0410 102 gAYAR------------RDRAEVRADLERVYELFpRLKERRRQRAG---------TLSGGEQQMLAIGRALMSRPKLLLL 160
|
..
gi 6671497 629 DE 630
Cdd:COG0410 161 DE 162
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
484-662 |
2.37e-05 |
|
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: 47.79 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 484 PTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILgglwPTYsgvlYKPPPQRMFY--IPQRPYmSVGSLRDQV---- 557
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI----PRF----YEPDSGQILLdgHDLADY-TLASLRRQValvs 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 558 ----IYPDS-AEDM---RRKGCSEQQLEAILGIVHLRHILQR--EGGWEAVCDWKDVLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:TIGR02203 413 qdvvLFNDTiANNIaygRTEQADRAEIERALAAAYAQDFVDKlpLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILI 492
|
170 180 190
....*....|....*....|....*....|....*...
gi 6671497 628 LDECTSAVSIDVEGKIfQAAKDA---GIALLSITHRPS 662
Cdd:TIGR02203 493 LDEATSALDNESERLV-QAALERlmqGRTTLVIAHRLS 529
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
488-645 |
2.40e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYKpppQRMF-YIPQRPYMSVGSLRDQVIYPDSaEDM 566
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA---ERSIaYVPQQAWIMNATVRGNILFFDE-EDA 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 567 RR--KGCSEQQLEAILGivhlrhilQREGGWEAVCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKI 643
Cdd:PTZ00243 750 ARlaDAVRVSQLEADLA--------QLGGGLETEIGEKGVnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV 821
|
..
gi 6671497 644 FQ 645
Cdd:PTZ00243 822 VE 823
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
484-634 |
2.56e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 46.14 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 484 PTGEVVVaslnirveegmhllITGPNGCGKSSLFRILGGLWP------TYSGVLYKPPPQRMFYIPQR-----------P 546
Cdd:COG1126 25 EKGEVVV--------------IIGPSGSGKSTLLRCINLLEEpdsgtiTVDGEDLTDSKKDINKLRRKvgmvfqqfnlfP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 547 YMSVgslRDQVIYPDsaedMRRKGCSEQQLEAI----LGIVHLRhilqreggweavcDWKDV----LSGGEKQRIGMAR- 617
Cdd:COG1126 91 HLTV---LENVTLAP----IKVKKMSKAEAEERamelLERVGLA-------------DKADAypaqLSGGQQQRVAIARa 150
|
170
....*....|....*....
gi 6671497 618 --MfyhRPKYALLDECTSA 634
Cdd:COG1126 151 laM---EPKVMLFDEPTSA 166
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
489-662 |
2.78e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 46.37 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL---------------------WPTYSGVLYKPPPQRMFYIPQR-P 546
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneearvegevrlfgrniySPDVDPIEVRREVGMVFQYPNPfP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 547 YMSvgslrdqvIYPDSAEDMRRKGC--SEQQLEAILgivhlRHILQREGGWEAV----CDWKDVLSGGEKQRIGMARMFY 620
Cdd:PRK14267 99 HLT--------IYDNVAIGVKLNGLvkSKKELDERV-----EWALKKAALWDEVkdrlNDYPSNLSGGQRQRLVIARALA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6671497 621 HRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALlsITHRPS 662
Cdd:PRK14267 166 MKPKILLMDEPTANIdpvgTAKIEELLFELKKEYTIVL--VTHSPA 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
483-659 |
2.81e-05 |
|
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: 46.97 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 483 TPTGEV-VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTY---SG-VLYK-------PPPQ-------RMFYIP 543
Cdd:COG0444 13 TRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGeILFDgedllklSEKElrkirgrEIQMIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 544 QRPY------MSVGslrDQViypdsAEDMRR-KGCSEQQLEA----ILGIVHLRHILQR------EggweavcdwkdvLS 606
Cdd:COG0444 93 QDPMtslnpvMTVG---DQI-----AEPLRIhGGLSKAEAREraieLLERVGLPDPERRldryphE------------LS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6671497 607 GGEKQRIGMARMFYHRPKYALLDECTSA--VSIdvegkifQA---------AKDAGIALLSITH 659
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTAldVTI-------QAqilnllkdlQRELGLAILFITH 209
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
493-671 |
4.14e-05 |
|
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: 45.34 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 493 LNIRVEEGMHLLITGPNGCGKSSLF-----RILGGlwPTYSGVLY---KPP-----PQRMFYIPQR----PYMSV----- 550
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLdaisgRVEGG--GTTSGQILfngQPRkpdqfQKCVAYVRQDdillPGLTVretlt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 551 --GSLRDQVIYPDSAEDMRrkgcSEQQLEAILGIVHLRHILQREggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03234 104 ytAILRLPRKSSDAIRKKR----VEDVLLRDLALTRIGGNLVKG------------ISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6671497 629 DECTSAV----SIDVEGKIFQAAKDAGIALLSItH--RPSLWKYHTHLL 671
Cdd:cd03234 168 DEPTSGLdsftALNLVSTLSQLARRNRIVILTI-HqpRSDLFRLFDRIL 215
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
605-660 |
4.26e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 4.26e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 605 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSID----VEGKIFQAAKDAGIALLSITHR 660
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHR 1418
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
488-659 |
4.28e-05 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 45.65 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYSGVLY-------------KPPPQRMFYIPQR-PYMSVGS 552
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTSGSVLVdgtdltllsgkelRKARRRIGMIFQHfNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 553 LRDQVIYPDSAEDMRRKGCSEQQLE--AILGIVHLRHILQREggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:cd03258 99 VFENVALPLEIAGVPKAEIEERVLEllELVGLEDKADAYPAQ------------LSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190
....*....|....*....|....*....|...
gi 6671497 631 CTSAVSIDVEGKIFQAAKDA----GIALLSITH 659
Cdd:cd03258 167 ATSALDPETTQSILALLRDInrelGLTIVLITH 199
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
489-659 |
4.46e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.62 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKS----SLFRIL---------GGLWPTYSGVLYKPPPQ-------RMFYIPQRPYM 548
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypsGDIRFHGESLLHASEQTlrgvrgnKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 549 SVGSLrdQVIYPDSAE------DMRRKGCSEQQLEAiLGIVHLRHILQReggweaVCDWKDVLSGGEKQRIGMARMFYHR 622
Cdd:PRK15134 104 SLNPL--HTLEKQLYEvlslhrGMRREAARGEILNC-LDRVGIRQAAKR------LTDYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6671497 623 PKYALLDECTSAVSIDVEGKIFQAAKD----AGIALLSITH 659
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRElqqeLNMGLLFITH 215
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
471-659 |
4.49e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 471 EQGIICENIPIITPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG---VLYKPPPQRM-----FYI 542
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGkisILGQPTRQALqknlvAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 543 PQRPYM--SVGSLRDQVIYPDSAEDM----RRKGCSEQQLEAILGIVHLRHILQREGGweavcdwkdVLSGGEKQRIGMA 616
Cdd:PRK15056 84 PQSEEVdwSFPVLVEDVVMMGRYGHMgwlrRAKKRDRQIVTAALARVDMVEFRHRQIG---------ELSGGQKKRVFLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6671497 617 RMFYHRPKYALLDECTSAVSIDVEGKI---FQAAKDAGIALLSITH 659
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIislLRELRDEGKTMLVSTH 200
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
487-675 |
6.51e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.84 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 487 EVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY---KPPP--QRMFYIpqrPYMS-VGSLRDQViyp 560
Cdd:PRK13543 24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQidgKTATrgDRSRFM---AYLGhLPGLKADL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 561 DSAEDMR----RKGCSEQQLE----AILGIVHLRHILQREggweavcdwkdvLSGGEKQRIGMARMFYHRPKYALLDEct 632
Cdd:PRK13543 98 STLENLHflcgLHGRRAKQMPgsalAIVGLAGYEDTLVRQ------------LSAGQKKRLALARLWLSPAPLWLLDE-- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6671497 633 SAVSIDVEG-----KIFQAAKDAGIALLSITH--RPSLwKYHTHLLQFDG 675
Cdd:PRK13543 164 PYANLDLEGitlvnRMISAHLRGGGAALVTTHgaYAAP-PVRTRMLTLEA 212
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
500-659 |
7.62e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 500 GMHLLITGPNGCGKSSLFRILGGLWPTYSGVL------------YKPPPQR--MFYIPQRPYMSVG---SLRDQVIYPDS 562
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIifngqridtlspGKLQALRrdIQFIFQDPYASLDprqTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 563 AEDMRRKGCSEQQLEAILGIVHLRhilqREGGWEavcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGK 642
Cdd:PRK10261 430 VHGLLPGKAAAARVAWLLERVGLL----PEHAWR----YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ 501
|
170 180
....*....|....*....|.
gi 6671497 643 I----FQAAKDAGIALLSITH 659
Cdd:PRK10261 502 IinllLDLQRDFGIAYLFISH 522
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
488-660 |
1.50e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 44.33 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEG--MHLLitGPNGCGKSSLFRILGGLWPTYSG-VLYK-----PPPQRMF-YIPQ----RPYMSVGslr 554
Cdd:COG4152 15 TAVDDVSFTVPKGeiFGLL--GPNGAGKTTTIRIILGILAPDSGeVLWDgepldPEDRRRIgYLPEerglYPKMKVG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 555 DQVIYpdsaedM-RRKGCSEQQLEAilgivHLRHILQREGgweaVCDWKDV----LSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:COG4152 90 EQLVY------LaRLKGLSKAEAKR-----RADEWLERLG----LGDRANKkveeLSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 6671497 630 ECTS---AVSIDV-EGKIF-QAAKDAGIaLLSiTHR 660
Cdd:COG4152 155 EPFSgldPVNVELlKDVIReLAAKGTTV-IFS-SHQ 188
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
605-705 |
1.56e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 44.19 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 605 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEG---KIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGgwKF 681
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG--KI 230
|
90 100
....*....|....*....|....
gi 6671497 682 EKLDSAARLSLTEEKQRLEQQLAG 705
Cdd:PRK10619 231 EEEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
489-630 |
1.64e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.45 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY--------KPPPQR---M------FYipqrPYMSVg 551
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWiggrvvneLEPADRdiaMvfqnyaLY----PHMSV- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 552 slrdqviypdsAEDM------RR--KGCSEQQLEAILGIVHLRHILQR---EggweavcdwkdvLSGGEKQRIGMARMFY 620
Cdd:PRK11650 94 -----------RENMayglkiRGmpKAEIEERVAEAARILELEPLLDRkprE------------LSGGQRQRVAMGRAIV 150
|
170
....*....|
gi 6671497 621 HRPKYALLDE 630
Cdd:PRK11650 151 REPAVFLFDE 160
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
491-669 |
1.90e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 43.91 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 491 ASLNIRVEEGMHLLitGPNGCGKSSLFRILGGL-WPTYSGVLYKPPPQRMFYIPQRPYMSvgslRD-QVIYPDS------ 562
Cdd:PRK10419 31 VSLSLKSGETVALL--GRSGCGKSTLARLLVGLeSPSQGNVSWRGEPLAKLNRAQRKAFR----RDiQMVFQDSisavnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 563 --------AEDMRR-----KGCSEQQLEAILGIVHLR-HILQREGGWeavcdwkdvLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:PRK10419 105 rktvreiiREPLRHllsldKAERLARASEMLRAVDLDdSVLDKRPPQ---------LSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6671497 629 DECTSAVSIDVEGKIFQAAKD----AGIALLSITHRPSLWKYHTH 669
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKlqqqFGTACLFITHDLRLVERFCQ 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
483-659 |
2.62e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 43.57 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 483 TPTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVL---------------YKPPPQRMFYIPQRPY 547
Cdd:PRK13643 15 SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvsstskqkeIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 548 msvGSLRDQVIYPDSAEDMRRKGCSEQQLEAI----LGIVHLRHILQREGGWEavcdwkdvLSGGEKQRIGMARMFYHRP 623
Cdd:PRK13643 95 ---SQLFEETVLKDVAFGPQNFGIPKEKAEKIaaekLEMVGLADEFWEKSPFE--------LSGGQMRRVAIAGILAMEP 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 6671497 624 KYALLDECTSAVSIDVE---GKIFQAAKDAGIALLSITH 659
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARiemMQLFESIHQSGQTVVLVTH 202
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
485-662 |
2.83e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 44.32 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 485 TGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGlwptysgvlYKPPPQRMFYIPQRPY--MSVGSLR-------- 554
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG---------YYPLTEGEIRLDGRPLssLSHSVLRqgvamvqq 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 555 DQVIYPDSAEDMRRKG--CSEQQLEAILGIVHLRHILQR--EGGWEAVCDWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:PRK10790 423 DPVVLADTFLANVTLGrdISEEQVWQALETVQLAELARSlpDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190
....*....|....*....|....*....|....
gi 6671497 631 CTSAVSIDVEGKIFQA--AKDAGIALLSITHRPS 662
Cdd:PRK10790 503 ATANIDSGTEQAIQQAlaAVREHTTLVVIAHRLS 536
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
488-659 |
3.09e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 43.15 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY-----KPPPQRMFYIPQRPYMSVGSLRDQVIYPDS 562
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYvdgldTSDEENLWDIRNKAGMVFQNPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 563 AEDMrrkgcseqqleAI----LGI----VHLR--HILQREGGWEavcdWKD----VLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:PRK13633 104 EEDV-----------AFgpenLGIppeeIRERvdESLKKVGMYE----YRRhaphLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190
....*....|....*....|....*....|....*
gi 6671497 629 DECTSAVS----IDVEGKIFQAAKDAGIALLSITH 659
Cdd:PRK13633 169 DEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
588-674 |
3.27e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.18 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 588 ILQREGGWEAVCDWK-DVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIfQAAKDA---GIALLSITHRPSL 663
Cdd:PRK13657 454 IERKPDGYDTVVGERgRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV-KAALDElmkGRTTFIIAHRLST 532
|
90
....*....|.
gi 6671497 664 WKYHTHLLQFD 674
Cdd:PRK13657 533 VRNADRILVFD 543
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
605-634 |
3.64e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 43.25 E-value: 3.64e-04
10 20 30
....*....|....*....|....*....|
gi 6671497 605 LSGGEKQRIGMARMFYHRPKYALLDECTSA 634
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSA 170
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
605-663 |
4.36e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.46 E-value: 4.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6671497 605 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKI----FQAAKDAGIALLSITHRPSL 663
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIadllFSLNREHGTTLILVTHDLQL 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
605-634 |
4.80e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 43.14 E-value: 4.80e-04
10 20 30
....*....|....*....|....*....|
gi 6671497 605 LSGGEKQRIGMARMFYHRPKYALLDECTSA 634
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
484-659 |
6.83e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 42.14 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 484 PTGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLYKPPP-----QRMFYIPQRPYMSVGSLRDQV 557
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGrILFDGKPidysrKGLMKLRESVGMVFQDPDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 558 ----IYPDSAEDMRRKGCSEQQLEAilgivHLRHILQREGgweaVCDWKD----VLSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:PRK13636 96 fsasVYQDVSFGAVNLKLPEDEVRK-----RVDNALKRTG----IEHLKDkpthCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 6671497 630 ECTSAvsIDVEGK------IFQAAKDAGIALLSITH 659
Cdd:PRK13636 167 EPTAG--LDPMGVseimklLVEMQKELGLTIIIATH 200
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
488-659 |
7.75e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLYKPPPQRMFYIPQR----------PYMSVGSLRDQV 557
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHqleflradesPLQHLARLAPQE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 558 iypdsaedmrrkgcSEQQLEAILGIVHLRHilqreggwEAVCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSI 637
Cdd:PRK10636 406 --------------LEQKLRDYLGGFGFQG--------DKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
|
170 180
....*....|....*....|..
gi 6671497 638 DVEGKIFQAAKDAGIALLSITH 659
Cdd:PRK10636 464 DMRQALTEALIDFEGALVVVSH 485
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
493-529 |
8.64e-04 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 41.36 E-value: 8.64e-04
10 20 30
....*....|....*....|....*....|....*..
gi 6671497 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG 529
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG 77
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
489-659 |
9.74e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 41.54 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLYKPPP----------QRMFYIPQRPYMSVG-SLRDQ 556
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGtVFLGDKPismlssrqlaRRLALLPQHHLTPEGiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 557 VIYPDS----------AEDmrrkgcsEQQLEAILGIVHLRHILQReggweAVCDwkdvLSGGEKQRIGMARMFYHRPKYA 626
Cdd:PRK11231 97 VAYGRSpwlslwgrlsAED-------NARVNQAMEQTRINHLADR-----RLTD----LSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 6671497 627 LLDECTSAVSID--VE-GKIFQAAKDAGIALLSITH 659
Cdd:PRK11231 161 LLDEPTTYLDINhqVElMRLMRELNTQGKTVVTVLH 196
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
605-662 |
1.52e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 41.93 E-value: 1.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6671497 605 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIfQAAKDA---GIALLSITHRPS 662
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI-QAALDElqkNRTSLVIAHRLS 540
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
486-643 |
1.92e-03 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 40.50 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYSGVLY---------KPPPQRMFYIPQrpymsvgsLRDQ 556
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtaRSLSQQKGLIRQ--------LRQH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 557 V--------IYPDSA--EDMRR-----KGCSEQQLEAiLGivhlRHILQREG--GWEAVcdWKDVLSGGEKQRIGMARMF 619
Cdd:PRK11264 87 VgfvfqnfnLFPHRTvlENIIEgpvivKGEPKEEATA-RA----RELLAKVGlaGKETS--YPRRLSGGQQQRVAIARAL 159
|
170 180
....*....|....*....|....
gi 6671497 620 YHRPKYALLDECTSAVSIDVEGKI 643
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEV 183
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
492-637 |
2.32e-03 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 40.87 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 492 SLNIRveEGMHLLITGPNGCGKSSLFRILGGLWPTYSG-VLY-------------KPPPQRMFYIPQRPY------MSVG 551
Cdd:COG4608 38 SFDIR--RGETLGLVGESGCGKSTLGRLLLRLEEPTSGeILFdgqditglsgrelRPLRRRMQMVFQDPYaslnprMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 552 S-----LRDQVIYPdsAEDMRRKgcseqqLEAILGIVHLR--HiLQR---EggweavcdwkdvLSGGEKQRIGMARMFYH 621
Cdd:COG4608 116 DiiaepLRIHGLAS--KAERRER------VAELLELVGLRpeH-ADRyphE------------FSGGQRQRIGIARALAL 174
|
170
....*....|....*...
gi 6671497 622 RPKYALLDECTSA--VSI 637
Cdd:COG4608 175 NPKLIVCDEPVSAldVSI 192
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
486-663 |
2.56e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 40.24 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLwptysgvlYKPPPQRMFY----IPQRPYMSVGSLRDQV--IY 559
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI--------ERPSAGKIWFsghdITRLKNREVPFLRRQIgmIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 560 PDSAEDMRRKGCSEQQLEAILGIVHLRHI-------LQREGGWEAVCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:PRK10908 86 QDHHLLMDRTVYDNVAIPLIIAGASGDDIrrrvsaaLDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190
....*....|....*....|....*....|....*
gi 6671497 633 ----SAVSIDVEgKIFQAAKDAGIALLSITHRPSL 663
Cdd:PRK10908 166 gnldDALSEGIL-RLFEEFNRVGVTVLMATHDIGL 199
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
605-635 |
3.08e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 3.08e-03
10 20 30
....*....|....*....|....*....|.
gi 6671497 605 LSGGEKQRIGMARMFYHRPKYALLDECTSAV 635
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
542-660 |
3.17e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.11 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 542 IPQRPYMSVGSLRDQvIYPDSAEDmrrkgcsEQQLEAILGIVHLRHILQREG-GWEA-VCDWKDVLSGGEKQRIGMARMF 619
Cdd:PLN03232 1315 IPQSPVLFSGTVRFN-IDPFSEHN-------DADLWEALERAHIKDVIDRNPfGLDAeVSEGGENFSVGQRQLLSLARAL 1386
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 6671497 620 YHRPKYALLDECTSAVSIDVEGKIFQAAKDA--GIALLSITHR 660
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREEfkSCTMLVIAHR 1429
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
489-662 |
4.40e-03 |
|
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: 39.51 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 489 VVASLNIRVEEGMHLLITGPNGCGKSSL----FRIL----GGLwpTYSGV-LYKPPPQ----RMFYIPQRPYMSVGSLRD 555
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVdifdGKI--VIDGIdISKLPLHtlrsRLSIILQDPILFSGSIRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 556 QViypdsaeDMRRKgCSEQQLEAILGIVHLRHILQR-EGGWEA-VCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:cd03288 114 NL-------DPECK-CTDDRLWEALEIAQLKNMVKSlPGGLDAvVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190
....*....|....*....|....*....|..
gi 6671497 634 AVSIDVEgKIFQAAKDAGIA---LLSITHRPS 662
Cdd:cd03288 186 SIDMATE-NILQKVVMTAFAdrtVVTIAHRVS 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
487-660 |
6.23e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 38.78 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 487 EVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLwptysgvlYKPPPQRMFYIPQRPYMSVGSLRDQVIYPDSAEDM 566
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGL--------LNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671497 567 R-----RKGC--------SEQQLEAILGIVHLRHILQREGGweavcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:PRK13540 86 NpyltlRENClydihfspGAVGITELCRLFSLEHLIDYPCG---------LLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|
gi 6671497 634 AV---SIDVEGKIFQAAKDAGIALLSITHR 660
Cdd:PRK13540 157 ALdelSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
483-523 |
8.97e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 38.52 E-value: 8.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6671497 483 TPTGEVVVAS-LNIRVEEGMHLLITGPNGCGKSSLFRILGGL 523
Cdd:COG1134 34 TRREEFWALKdVSFEVERGESVGIIGRNGAGKSTLLKLIAGI 75
|
|
| |
