|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
326-900 |
1.38e-148 |
|
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: 453.82 E-value: 1.38e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 326 RVAAMLKILVPRLFDKQGGQLLAVAVLVFSRTWISDRIASLNGTTVKFVLEQDKDAFIRLIGVSILQSGANSFVAPSLRT 405
Cdd:TIGR00954 78 KLDFLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 406 LTAKLALGWRIRMTNHMLRYYLKRNAFYKVFNMSGKSIDADQRLTLDVDKLTTDLAGLVTGMVKPLVDILWFTWRMKLLS 485
Cdd:TIGR00954 158 LLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTAL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 486 GRRGVAILYAYMLLGLGFLRAISPDFGHLSGQEQELEGTFRFMHSRLRTHAESIAFFGGGSREKAMVEAKFVKLINHSKI 565
Cdd:TIGR00954 238 GSVGPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 566 LLRKQWLYGIVDDFVTKqlphnVTWGLSLLYA-----LEHKGDRALTSTQGELAHAL----RFLASVVSqsfiAFGDILE 636
Cdd:TIGR00954 318 IIKFRFSYGFLDNIVAK-----YTWSAVGLVAvsipiFDKTHPAFLEMSEEELMQEFynngRLLLKAAD----ALGRLML 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 637 LHKKFLELSGGINRIFEL--------------------EEFTRFAQRNTVVSPNAISAASKETISFHEVDIVTPSQKLLA 696
Cdd:TIGR00954 389 AGRDMTRLAGFTARVDTLlqvlddvksgnfkrprveeiESGREGGRNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDVLI 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 697 RKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKPSEG-MFHVPQRPYTSLGTLRDQIIYPLSREEAKIKV 775
Cdd:TIGR00954 469 ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGkLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRG 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 776 LSlhrsgnnssasmllDDHLKTILENVRLVYLLERE-GWDSTPNWEDVLSLGEQQRLGMARLFFHHPKFGILDECTNATS 854
Cdd:TIGR00954 549 LS--------------DKDLEQILDNVQLTHILEREgGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1142837572 855 VDVEEHLYRLATSMGITVITSSQRPALIPFHALELKlIDGEGNWEL 900
Cdd:TIGR00954 615 VDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLY-MDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
330-598 |
6.83e-97 |
|
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: 304.92 E-value: 6.83e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 330 MLKILVPRLFDKQGGQLLAVAVLVFSRTWISDRIASLNGTTVKFVLEQDKDAFIRLIGVSILQSGANSFVAPSLRTLTAK 409
Cdd:pfam06472 1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 410 LALGWRIRMTNHMLRYYLKRNAFYKVFNMSGKSIDADQRLTLDVDKLTTDLAGLVTGMVKPLVDILWFTWRMKLLSGRRG 489
Cdd:pfam06472 81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 490 VAILYAYMLLGLGFLRAISPDFGHLSGQEQELEGTFRFMHSRLRTHAESIAFFGGGSREKAMVEAKFVKLINHSKILLRK 569
Cdd:pfam06472 161 PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILRR 240
|
250 260
....*....|....*....|....*....
gi 1142837572 570 QWLYGIVDDFVTKQLPHNVTWGLSLLYAL 598
Cdd:pfam06472 241 RLWYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
344-905 |
1.16e-81 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 274.38 E-value: 1.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 344 GQLLAVAVLVFSRTWISDRIASLNGTtvkF--VLEQ-DKDAFIRLIGVSILQSGANSFVAPSLRTLTAKLALGWRIRMTN 420
Cdd:COG4178 25 GLLALLLLLTLASVGLNVLLNFWNRD---FydALQArDAAAFWQQLGVFALLAAISILLAVYQTYLRQRLQIRWREWLTE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 421 HMLRYYLKRNAFYKVfNMSGKSID-ADQRLTLDVDKLTTDLAGLVTGMVKPLVD------ILW-------FTWRMKLLSG 486
Cdd:COG4178 102 RLLDRWLSNRAYYRL-QLSGGEIDnPDQRIAEDIRLFTETTLSLSLGLLSSVVTlisfigILWslsgsltFTLGGYSITI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 487 RRG-VAILYAYMLLGLGFLRAIspdfGH----LSGQEQELEGTFRFMHSRLRTHAESIAFFGGGSREKAMVEAKFVKLIN 561
Cdd:COG4178 181 PGYmVWAALIYAIIGTLLTHLI----GRplirLNFEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 562 HSKILLRKQWLYGIVddfvtkQLPHNVtwgLSLLYALehkgdraltstqgeLAHALRFLAS-----VVSQSFIAFGDILE 636
Cdd:COG4178 257 NWRRLIRRQRNLTFF------TTGYGQ---LAVIFPI--------------LVAAPRYFAGeitlgGLMQAASAFGQVQG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 637 -L------HKKFLELSGGINRIFELEEFTRFAQRNTVVSPnAISAASKETISFHEVDIVTPSQKLLARKLSCDVVQGKSL 709
Cdd:COG4178 314 aLswfvdnYQSLAEWRATVDRLAGFEEALEAADALPEAAS-RIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 710 LLTGPNGSGKSSIFRVLRDLWPTFSGRVTKPS-EGMFHVPQRPYTSLGTLRDQIIYPLSREEAKikvlslhrsgnnssas 788
Cdd:COG4178 393 LITGPSGSGKSTLLRAIAGLWPYGSGRIARPAgARVLFLPQRPYLPLGTLREALLYPATAEAFS---------------- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 789 mllDDHLKTILENVRLVYLLERegWDSTPNWEDVLSLGEQQRLGMARLFFHHPKFGILDECTNATSVDVEEHLYRL--AT 866
Cdd:COG4178 457 ---DAELREALEAVGLGHLAER--LDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLlrEE 531
|
570 580 590
....*....|....*....|....*....|....*....
gi 1142837572 867 SMGITVITSSQRPALIPFHALELKLiDGEGNWELCAIQQ 905
Cdd:COG4178 532 LPGTTVISVGHRSTLAAFHDRVLEL-TGDGSWQLLPAEA 569
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
30-238 |
1.39e-79 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 254.77 E-value: 1.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGsdlnkEIFYVPQRPYT 109
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----DLLFLPQRPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 110 AVGTLREQLIYPltadqgiepltydgmvdllknvdleyllerypldkevnWGDELSLGEQQRLGMARLFYHKPKFAILDE 189
Cdd:cd03223 76 PLGTLREQLIYP--------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1142837572 190 CTSAVTTDMEERFCKKVRAMGTSCITISHRPALVAFHDIVLSLDGEGGW 238
Cdd:cd03223 118 ATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-238 |
5.46e-77 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 264.30 E-value: 5.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 21 GNYVSEANHIEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSdlnkeI 100
Cdd:TIGR00954 443 GIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGK-----L 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 101 FYVPQRPYTAVGTLREQLIYPLTADQGIEPLTYDG-MVDLLKNVDLEYLLER-YPLDKEVNWGDELSLGEQQRLGMARLF 178
Cdd:TIGR00954 518 FYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKdLEQILDNVQLTHILEReGGWSAVQDWMDVLSGGEKQRIAMARLF 597
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 179 YHKPKFAILDECTSAVTTDMEERFCKKVRAMGTSCITISHRPALVAFHDIVLSLDGEGGW 238
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGY 657
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-238 |
2.05e-68 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 238.17 E-value: 2.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 13 RSLDHSSPGNYVSEANHIEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGv 92
Cdd:COG4178 346 DALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 93 gsdlNKEIFYVPQRPYTAVGTLREQLIYPLTADQgiepLTYDGMVDLLKNVDLEYLLERypLDKEVNWGDELSLGEQQRL 172
Cdd:COG4178 425 ----GARVLFLPQRPYLPLGTLREALLYPATAEA----FSDAELREALEAVGLGHLAER--LDEEADWDQVLSLGEQQRL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 173 GMARLFYHKPKFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRPALVAFHDIVLSLDGEGGW 238
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGHRSTLAAFHDRVLELTGDGSW 562
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
680-898 |
4.73e-60 |
|
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: 201.61 E-value: 4.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 680 ISFHEVDIVTPSQKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKP-SEGMFHVPQRPYTSLGTL 758
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPeGEDLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 759 RDQIIYPlsreeakikvlslhrsgnnssasmllddhlktilenvrlvylleregwdstpnWEDVLSLGEQQRLGMARLFF 838
Cdd:cd03223 81 REQLIYP-----------------------------------------------------WDDVLSGGEQQRLAFARLLL 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 839 HHPKFGILDECTNATSVDVEEHLYRLATSMGITVITSSQRPALIPFHALELKLiDGEGNW 898
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDL-DGEGGW 166
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
25-234 |
4.73e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 119.86 E-value: 4.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 25 SEANHIEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV------GSDLNK 98
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 99 EIFYVPQRPYTAVGTLREQL-IYPLTADQgiepltyDGMVDLLKNVDLEYLLERYP--LDKEVnwGDE---LSLGEQQRL 172
Cdd:COG4988 412 QIAWVPQNPYLFAGTIRENLrLGRPDASD-------EELEAALEAAGLDEFVAALPdgLDTPL--GEGgrgLSGGQAQRL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142837572 173 GMARLFYHKPKFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRPALVAFHDIVLSLDG 234
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQADRILVLDD 546
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
30-234 |
2.37e-27 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 109.01 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLV-DDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV------GSDLNKEIFY 102
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 103 VPQRPYTAVGTLREqliypltadqgiepltydgmvdllkNVdleyllerypldkevnwgdeLSLGEQQRLGMARLFYHKP 182
Cdd:cd03228 81 VPQDPFLFSGTIRE-------------------------NI--------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1142837572 183 KFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRPALVAFHDIVLSLDG 234
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALakGKTVIVIAHRLSTIRDADRIIVLDD 169
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
30-234 |
5.11e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.52 E-value: 5.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVvTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGSDLNKEIFYV 103
Cdd:COG4619 1 LELEGLSF-RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkpLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 104 PQRPYTAVGTLREQLIYPLTADQgiEPLTYDGMVDLLKNVDLEYLLerypLDKEVnwgDELSLGEQQRLGMARLFYHKPK 183
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLRE--RKFDRERALELLERLGLPPDI----LDKPV---ERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142837572 184 FAILDECTSAVTTDMEERFCKKVRAM----GTSCITISHRPALVAFH-DIVLSLDG 234
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVaDRVLTLEA 206
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
29-234 |
5.58e-23 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 104.92 E-value: 5.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 29 HIEFSDVK-VVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI---------VKPgvgSDLNK 98
Cdd:COG2274 473 DIELENVSfRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqIDP---ASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 99 EIFYVPQRPYTAVGTLREQLIYpltADQGIeplTYDGMVDLLKNVDLEYLLERYP--LDKEV-NWGDELSLGEQQRLGMA 175
Cdd:COG2274 550 QIGVVLQDVFLFSGTIRENITL---GDPDA---TDEEIIEAARLAGLHDFIEALPmgYDTVVgEGGSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142837572 176 RLFYHKPKFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRPALVAFHDIVLSLDG 234
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRLADRIIVLDK 684
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
30-234 |
5.74e-23 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 98.05 E-value: 5.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAG-NVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFY 102
Cdd:cd03245 3 IEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDirqldpADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 103 VPQRPYTAVGTLREQLI--YPLTADQGI-EPLTYDGMVDLLKN----VDLEyLLERypldkevnwGDELSLGEQQRLGMA 175
Cdd:cd03245 83 VPQDVTLFYGTLRDNITlgAPLADDERIlRAAELAGVTDFVNKhpngLDLQ-IGER---------GRGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142837572 176 RLFYHKPKFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRPALVAFHDIVLSLDG 234
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLLDLVDRIIVMDS 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
30-235 |
2.54e-22 |
|
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: 96.40 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLV---DDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV----------GSDL 96
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 97 NKEIFYVPQRPYtavgtlreqLIYPLTADQGIE-PLTYDGMV---------DLLKNVDLEYLLERYPldkevnwgDELSL 166
Cdd:cd03255 81 RRHIGFVFQSFN---------LLPDLTALENVElPLLLAGVPkkerreraeELLERVGLGDRLNHYP--------SELSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142837572 167 GEQQRLGMARLFYHKPKFAILDECTSAVTTDMEER----FCKKVRAMGTSCITISHRPALVAFHDIVLSL-DGE 235
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEvmelLRELNKEAGTTIVVVTHDPELAEYADRIIELrDGK 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
30-232 |
3.79e-22 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 94.21 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTP-AGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFY 102
Cdd:cd03246 1 LEVENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADisqwdpNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 103 VPQRPYTAVGTLREqliypltadqgiepltydgmvdllkNVdleyllerypldkevnwgdeLSLGEQQRLGMARLFYHKP 182
Cdd:cd03246 81 LPQDDELFSGSIAE-------------------------NI--------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1142837572 183 KFAILDECTSAVTTDMEERFCKKVRAM---GTSCITISHRPALVAFHDIVLSL 232
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALkaaGATRIVIAHRPETLASADRILVL 168
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
30-234 |
6.54e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 95.37 E-value: 6.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV-GSDLNKE-----IFYV 103
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdIRDISRKslrsmIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 104 PQRPYTAVGTLREQLIYpltadqGIEPLTYDGMVDLLKNVDLEYLLERYP--LDKEVN-WGDELSLGEQQRLGMARLFYH 180
Cdd:cd03254 83 LQDTFLFSGTIMENIRL------GRPNATDEEVIEAAKEAGAHDFIMKLPngYDTVLGeNGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142837572 181 KPKFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRPALVAFHDIVLSLDG 234
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAHRLSTIKNADKILVLDD 212
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
30-225 |
1.09e-21 |
|
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: 94.49 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGN---VLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI-VKPGVGSDLN-------- 97
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIiFDGKDLLKLSrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 98 KEIFYVPQRPYTAVG---TLREQLIYPLTA--DQGIEPLTYDGMVDLLKNVDL-EYLLERYPldkevnwgDELSLGEQQR 171
Cdd:cd03257 82 KEIQMVFQDPMSSLNprmTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGVGLpEEVLNRYP--------HELSGGQRQR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 172 LGMARLFYHKPKFAILDECTSAVttDMEERFC-----KKVRA-MGTSCITISHRPALVAF 225
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSAL--DVSVQAQildllKKLQEeLGLTLLFITHDLGVVAK 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
42-234 |
2.60e-21 |
|
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: 92.93 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG-----VGSDLNKEIFYVPQRP--YTAVgTL 114
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdAREDYRRRLAYLGHADglKPEL-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 115 REQL-----IYPLTADQgiepltyDGMVDLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAILDE 189
Cdd:COG4133 93 RENLrfwaaLYGLRADR-------EAIDEALEAVGLAGLADLPV--------RQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1142837572 190 CTSAVTTDMEERFCKKVRAM---GTSCITISHRPALVAFHDiVLSLDG 234
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAAR-VLDLGD 204
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
26-224 |
3.00e-21 |
|
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: 92.71 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 26 EANHIEFSdvkvvTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV---KPGVGSDLNKEIFY 102
Cdd:cd03226 1 RIENISFS-----YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngKPIKAKERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 103 VPQRPYTAVG--TLREQLIYPLtadqgiePLTYDGMVD---LLKNVDLEYLLERYPLDkevnwgdeLSLGEQQRLGMARL 177
Cdd:cd03226 76 VMQDVDYQLFtdSVREELLLGL-------KELDAGNEQaetVLKDLDLYALKERHPLS--------LSGGQKQRLAIAAA 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1142837572 178 FYHKPKFAILDECTSAVTTDMEERFCKKVR---AMGTSCITISHRPALVA 224
Cdd:cd03226 141 LLSGKDLLIFDEPTSGLDYKNMERVGELIRelaAQGKAVIVITHDYEFLA 190
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
30-232 |
4.58e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 98.13 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFYV 103
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadaDSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 104 PQRPYTAVGTLREQLIYPL---TADQGIEPLTYDGMVDLLKnvDLEYLLERyPLDKEvnwGDELSLGEQQRLGMARLFYH 180
Cdd:TIGR02857 402 PQHPFLFAGTIAENIRLARpdaSDAEIREALERAGLDEFVA--ALPQGLDT-PIGEG---GAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1142837572 181 KPKFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRPALVAFHDIVLSL 232
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
31-235 |
1.52e-20 |
|
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: 91.06 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 31 EFSDVKVVTPAGNVLvDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLNKEIFYVPQRPYT 109
Cdd:cd03235 1 EVEDLTVSYGGHPVL-EDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPlEKERKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 110 AVGtlreqliYPLTADQ-----------GIEPLTYDGM--VD-LLKNVDLEYLLERyPLdkevnwgDELSLGEQQRLGMA 175
Cdd:cd03235 80 DRD-------FPISVRDvvlmglyghkgLFRRLSKADKakVDeALERVGLSELADR-QI-------GELSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142837572 176 RLFYHKPKFAILDECTSAVTTDMEERF---CKKVRAMGTSCITISHRPALV-AFHDIVLSLDGE 235
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIyelLRELRREGMTILVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
46-192 |
1.84e-20 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 88.86 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGSDLNKEIFYVPQ----RPYTavgTLR 115
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdLTDDERKSLRKEIGYVFQdpqlFPRL---TVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 116 EQLIYPLTaDQGIEPLTYDGMVD-LLKNVDLEYLLERYPLDKevnwGDELSLGEQQRLGMARLFYHKPKFAILDECTS 192
Cdd:pfam00005 78 ENLRLGLL-LKGLSKREKDARAEeALEKLGLGDLADRPVGER----PGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
30-224 |
2.98e-20 |
|
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: 95.36 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNV-LVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWP---LVSGHIVKPGV------GSDLNKE 99
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRdllelsEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 100 IFYVPQRPYTAvgtlreqlIYPLT-ADQGIEPLTYDGM---------VDLLKNVDLEYLLERYPldkevnwgDELSLGEQ 169
Cdd:COG1123 85 IGMVFQDPMTQ--------LNPVTvGDQIAEALENLGLsraeararvLELLEAVGLERRLDRYP--------HQLSGGQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142837572 170 QRLGMARLFYHKPKFAILDECTSA--VTTDME--ERFCKKVRAMGTSCITISHRPALVA 224
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTAldVTTQAEilDLLRELQRERGTTVLLITHDLGVVA 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
31-224 |
1.16e-19 |
|
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: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 31 EFSDVKVVTPAGNVLV-DDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGSDLNKEIFYV 103
Cdd:cd03225 1 ELKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 104 PQRPytavgtlREQLIYPLTAD---QGIEPLTYDG------MVDLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGM 174
Cdd:cd03225 81 FQNP-------DDQFFGPTVEEevaFGLENLGLPEeeieerVEEALELVGLEGLRDRSP--------FTLSGGQKQRVAI 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1142837572 175 ARLFYHKPKFAILDECTSAV----TTDMEERFcKKVRAMGTSCITISHRPALVA 224
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLdpagRRELLELL-KKLKAEGKTIIIVTHDLDLLL 198
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
30-224 |
1.24e-19 |
|
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: 88.93 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGSDLNKEIFYV 103
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdgkdITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 104 PQRPytavgtlREQLIYPLTAD--------QGIEPLTYDGMVD-LLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGM 174
Cdd:COG1122 81 FQNP-------DDQLFAPTVEEdvafgpenLGLPREEIRERVEeALELVGLEHLADRPP--------HELSGGQKQRVAI 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1142837572 175 ARLFYHKPKFAILDECTSAVttDMEER-----FCKKVRAMGTSCITISHRPALVA 224
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGL--DPRGRrelleLLKRLNKEGKTVIIVTHDLDLVA 198
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
31-226 |
1.63e-19 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 86.14 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 31 EFSDVKVVTPaGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGSDLNKEIFYVP 104
Cdd:cd00267 1 EIENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIlidgkdIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 105 QrpytavgtlreqliypltadqgiepltydgmvdllknvdleyllerypldkevnwgdeLSLGEQQRLGMARLFYHKPKF 184
Cdd:cd00267 80 Q----------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1142837572 185 AILDECTSAVTTDMEERFCKKVRAM---GTSCITISHRPALVAFH 226
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHDPELAELA 146
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
29-234 |
5.09e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 88.68 E-value: 5.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 29 HIEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI---------VKPgvgSDLNKE 99
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirdLTL---ESLRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 100 IFYVPQRPYTAVGTLREQLIYpltadqGIEPLTYDGMVDLLKNVDLEYLLERYP--LDKEVN-WGDELSLGEQQRLGMAR 176
Cdd:COG1132 416 IGVVPQDTFLFSGTIRENIRY------GRPDATDEEVEEAAKAAQAHEFIEALPdgYDTVVGeRGVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 177 LFYHKPKFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRPALVAFHDIVLSLDG 234
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLmkGRTTIVIAHRLSTIRNADRILVLDD 549
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
42-228 |
5.63e-18 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 82.48 E-value: 5.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGSDLNKEIFYVPQrpytavgtlr 115
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlldgkdLASLSPKELARKIAYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 116 eqliypltadqgiepltydgmvdLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAVT 195
Cdd:cd03214 81 -----------------------ALELLGLAHLADRPF--------NELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190
....*....|....*....|....*....|....
gi 1142837572 196 TDMEERFCKKVRAMGTSC-ITIshrpaLVAFHDI 228
Cdd:cd03214 130 IAHQIELLELLRRLARERgKTV-----VMVLHDL 158
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
30-226 |
1.44e-17 |
|
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: 86.88 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVV----TPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI---------VKPGVGSDL 96
Cdd:COG1123 261 LEVRNLSKRypvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltkLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 97 NKEIFYVPQRPYTAV---GTLREQLIYPLTADQGIEPLTYDGMV-DLLKNVDLEY-LLERYPldkevnwgDELSLGEQQR 171
Cdd:COG1123 341 RRRVQMVFQDPYSSLnprMTVGDIIAEPLRLHGLLSRAERRERVaELLERVGLPPdLADRYP--------HELSGGQRQR 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142837572 172 LGMARLFYHKPKFAILDECTSA----VTTDMEERFCKKVRAMGTSCITISHRPALVAFH 226
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSAldvsVQAQILNLLRDLQRELGLTYLFISHDLAVVRYI 471
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
30-234 |
2.32e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 82.02 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVkpgV-GSDLNK----EIFYVP 104
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVL---VnGQDLSRlkrrEIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 105 QRpytaVG------------TLREQLIYPLTAdQGIEPLTYDGMV-DLLKNVDLEYLLERYPldkevnwgDELSLGEQQR 171
Cdd:COG2884 79 RR----IGvvfqdfrllpdrTVYENVALPLRV-TGKSRKEIRRRVrEVLDLVGLSDKAKALP--------HELSGGEQQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 172 LGMARLFYHKPKFAILDECTSAVTTDMEER----FcKKVRAMGTSCITISHRPALV-AFHDIVLSLDG 234
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEimelL-EEINRRGTTVLIATHDLELVdRMPKRVLELED 212
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
29-219 |
5.61e-17 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 80.62 E-value: 5.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 29 HIEFSDVKV-VTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIF 101
Cdd:cd03244 2 DIEFKNVSLrYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskiglHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 102 YVPQRPYTAVGTLREQLiypltadqgiEPLTY--DGMV-DLLKNVDLEYLLERYP--LDKEVNWGDE-LSLGEQQRLGMA 175
Cdd:cd03244 82 IIPQDPVLFSGTIRSNL----------DPFGEysDEELwQALERVGLKEFVESLPggLDTVVEEGGEnLSVGQRQLLCLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1142837572 176 RLFYHKPKFAILDECTSAVTTDMEERFCKKVRAMGTSC--ITISHR 219
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCtvLTIAHR 197
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
688-873 |
1.56e-16 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 79.09 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 688 VTPSQKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT---KPSEGM---------FHVPQRPYTSL 755
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgKPLSAMpppewrrqvAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 756 GTLRDQIIYPLSREEAKIKvlslhrsgnnssasmllDDHLKTILENVRL-VYLLEREgwdstpnwEDVLSLGEQQRLGMA 834
Cdd:COG4619 88 GTVRDNLPFPFQLRERKFD-----------------RERALELLERLGLpPDILDKP--------VERLSGGERQRLALI 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1142837572 835 RLFFHHPKFGILDECTNA----TSVDVEEHLYRLATSMGITVI 873
Cdd:COG4619 143 RALLLQPDVLLLDEPTSAldpeNTRRVEELLREYLAEEGRAVL 185
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
42-224 |
1.65e-16 |
|
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: 79.90 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSD-----LNKEIFYVPQRPY-TAVGTLR 115
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkepreARRQIGVLPDERGlYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 116 EQL-----IYPLTADQgIEPLTYdgmvDLLKNVDLEYLLERypldkevNWGdELSLGEQQRLGMARLFYHKPKFAILDEC 190
Cdd:COG4555 93 ENIryfaeLYGLFDEE-LKKRIE----ELIELLGLEEFLDR-------RVG-ELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1142837572 191 TSAVTTDMEERFCKKVRAMGTSCITI---SHRPALVA 224
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVlfsSHIMQEVE 196
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
30-235 |
1.67e-16 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVkVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDL-NKEIFYVPQR-- 106
Cdd:COG1121 7 IELENL-TVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRaRRRIGYVPQRae 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 107 -----PYT-----AVGTLREQ-LIYPLTADQgiepltYDGMVDLLKNVDLEYLLERyPLdkevnwgDELSLGEQQRLGMA 175
Cdd:COG1121 86 vdwdfPITvrdvvLMGRYGRRgLFRRPSRAD------REAVDEALERVGLEDLADR-PI-------GELSGGQQQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142837572 176 RLFYHKPKFAILDECTSAVTTDMEERFC---KKVRAMGTSCITISHRPALVAFH-DIVLSLDGE 235
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYellRELRREGKTILVVTHDLGAVREYfDRVLLLNRG 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-220 |
2.59e-16 |
|
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: 83.18 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 16 DHSSPGNYVSEANHIEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV--- 92
Cdd:TIGR02868 321 SAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvs 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 93 ---GSDLNKEIFYVPQRPYTAVGTLREQLIYpltadqGIEPLTYDGMVDLLKNVDLEYLLERYP--LDKEVN-WGDELSL 166
Cdd:TIGR02868 401 sldQDEVRRRVSVCAQDAHLFDTTVRENLRL------ARPDATDEELWAALERVGLADWLRALPdgLDTVLGeGGARLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142837572 167 GEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRP 220
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAlsGRTVVLITHHL 530
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
30-201 |
9.50e-16 |
|
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: 76.85 E-value: 9.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLvDDLTLRVETG-SNLLitGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV-----GSDLNKEIFYV 103
Cdd:cd03264 1 LQLENLTKRYGKKRAL-DGVSLTLGPGmYGLL--GPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 104 PQ--RPYTAVgTLREQLIYpLTADQGIEPLTYDGMVD-LLKNVDLEyllERYplDKEVNwgdELSLGEQQRLGMARLFYH 180
Cdd:cd03264 78 PQefGVYPNF-TVREFLDY-IAWLKGIPSKEVKARVDeVLELVNLG---DRA--KKKIG---SLSGGMRRRVGIAQALVG 147
|
170 180
....*....|....*....|.
gi 1142837572 181 KPKFAILDECTsaVTTDMEER 201
Cdd:cd03264 148 DPSILIVDEPT--AGLDPEER 166
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-219 |
1.29e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.02 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 20 PGNYVSEANH--IEFSDVKVVTPAGNVLV-DDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG--- 93
Cdd:PRK11160 327 PTTSTAAADQvsLTLNNVSFTYPDQPQPVlKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiad 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 94 ---SDLNKEIFYVPQRPYTAVGTLREQLIypLTADQGIEpltyDGMVDLLKNVDLEYLLERY-PLDkevNW----GDELS 165
Cdd:PRK11160 407 yseAALRQAISVVSQRVHLFSATLRDNLL--LAAPNASD----EALIEVLQQVGLEKLLEDDkGLN---AWlgegGRQLS 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142837572 166 LGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEER-------FCKkvramGTSCITISHR 219
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQilellaeHAQ-----NKTVLMITHR 533
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
41-232 |
2.00e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 75.35 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 41 AGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlNKEIFYVPQR-------PYTAVGT 113
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----GARVAYVPQRsevpdslPLTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 114 L------REQLIYPLTADqgiepltyDGMV--DLLKNVDLEYLLERyPLdkevnwgDELSLGEQQRLGMARLFYHKPKFA 185
Cdd:NF040873 78 VamgrwaRRGLWRRLTRD--------DRAAvdDALERVGLADLAGR-QL-------GELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1142837572 186 ILDECTSAVTTDMEER---FCKKVRAMGTSCITISHRPALVAFHDIVLSL 232
Cdd:NF040873 142 LLDEPTTGLDAESRERiiaLLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
42-193 |
2.08e-15 |
|
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: 77.01 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV---KPgVGS----DLNKEIFYVPQRPYTAVG-T 113
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRD-LASlsrrELARRIAYVPQEPPAPFGlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 114 LREQLIYPLTADQGiePLTYDGMVDL------LKNVDLEYLLERyPLdkevnwgDELSLGEQQRLGMARLFYHKPKFAIL 187
Cdd:COG1120 92 VRELVALGRYPHLG--LFGRPSAEDReaveeaLERTGLEHLADR-PV-------DELSGGERQRVLIARALAQEPPLLLL 161
|
....*.
gi 1142837572 188 DECTSA 193
Cdd:COG1120 162 DEPTSH 167
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
30-219 |
3.24e-15 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 76.04 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPA--GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLN-----KEIF 101
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDiRDLNlrwlrSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 102 YVPQRPYTAVGTLREQLIYpltadqGIEPLTYDGMVDLLKNVDLEYLLERYP--LDKEV-NWGDELSLGEQQRLGMARLF 178
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRY------GKPDATDEEVEEAAKKANIHDFIMSLPdgYDTLVgERGSQLSGGQKQRIAIARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1142837572 179 YHKPKFAILDECTSAVTTDMEERFCKKV-RAM-GTSCITISHR 219
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALdRAMkGRTTIVIAHR 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
46-218 |
3.31e-15 |
|
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: 74.36 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV-----GSDLNKEIFYVPQRPYtavgtlreqlIY 120
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKdikkePEEVKRRIGYLPEEPS----------LY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 121 P-LTAdqgiepltydgmvdllknvdLEYLlerypldkevnwgdELSLGEQQRLGMARLFYHKPKFAILDECTSAVttDME 199
Cdd:cd03230 86 EnLTV--------------------RENL--------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL--DPE 129
|
170 180
....*....|....*....|....
gi 1142837572 200 ER-----FCKKVRAMGTSCITISH 218
Cdd:cd03230 130 SRrefweLLRELKKEGKTILLSSH 153
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
30-233 |
3.38e-15 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 76.11 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFYV 103
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDirevtlDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 104 PQRPYTAVGTLREQLIYpltadqGIEPLTYDGMVDLLKNVDLEYLLERYP--LDKEV-NWGDELSLGEQQRLGMARLFYH 180
Cdd:cd03253 81 PQDTVLFNDTIGYNIRY------GRPDATDEEVIEAAKAAQIHDKIMRFPdgYDTIVgERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1142837572 181 KPKFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRPALVAFHDIVLSLD 233
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLSTIVNADKIIVLK 209
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
40-234 |
6.74e-15 |
|
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: 75.22 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 40 PAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFYVPQRPYTAVGT 113
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlaladpAWLRRQVGVVLQENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 114 LREQLIyplTADQG------IEPLTYDGMVDLLKNVDLEY---LLERypldkevnwGDELSLGEQQRLGMARLFYHKPKF 184
Cdd:cd03252 92 IRDNIA---LADPGmsmervIEAAKLAGAHDFISELPEGYdtiVGEQ---------GAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1142837572 185 AILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRPALVAFHDIVLSLDG 234
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADRIIVMEK 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
42-234 |
8.00e-15 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 74.04 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVkpgvgsdLNKEIFYVPQRPYTAVGTLREQLI-- 119
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS-------VPGSIAYVSQEPWIQNGTIRENILfg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 120 YPLTADQgiepltYDgmvDLLKNVDLEYLLERYPLdkevnwGDE---------LSLGEQQRLGMARLFYHKPKFAILDEC 190
Cdd:cd03250 90 KPFDEER------YE---KVIKACALEPDLEILPD------GDLteigekginLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1142837572 191 TSAVTTDMEERFCKKV----RAMGTSCITISHRPALVAFHDIVLSLDG 234
Cdd:cd03250 155 LSAVDAHVGRHIFENCilglLLNNKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
42-220 |
1.18e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 73.68 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSD-----LNKEIFYVPQRP-YTAVGTLR 115
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDfqrdsIARGLLYLGHAPgIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 116 EQLIY--PLTADQGIEpltydgmvDLLKNVDLEYlLERYPLdkevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSA 193
Cdd:cd03231 92 ENLRFwhADHSDEQVE--------EALARVGLNG-FEDRPV-------AQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|
gi 1142837572 194 VTTDMEERFCKKVR---AMGTSCITISHRP 220
Cdd:cd03231 156 LDKAGVARFAEAMAghcARGGMVVLTTHQD 185
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
680-882 |
1.28e-14 |
|
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: 72.42 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 680 ISFHEVDIVTPSQKLLA-RKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTkpsegMFHVPQRPYtSLGTL 758
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL-----IDGVDLRDL-DLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 759 RDQIIYpLSREeakikvlslhrsgnnssaSMLLDDhlkTILENVrlvylleregwdstpnwedvLSLGEQQRLGMARLFF 838
Cdd:cd03228 75 RKNIAY-VPQD------------------PFLFSG---TIRENI--------------------LSGGQRQRIAIARALL 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1142837572 839 HHPKFGILDECT----NATSVDVEEHLYRLatSMGITVITSSQRPALI 882
Cdd:cd03228 113 RDPPILILDEATsaldPETEALILEALRAL--AKGKTVIVIAHRLSTI 158
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
41-221 |
1.42e-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: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 41 AGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlnKEIFYVP--QRPytaVG------ 112
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG------RDVTGVPpeRRN---IGmvfqdy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 113 ------TLREQLIYPLTADQGIEPLTYDGMVDLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAI 186
Cdd:cd03259 82 alfphlTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYP--------HELSGGQQQRVALARALAREPSLLL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1142837572 187 LDECTSAVTTDMEERFCKKVRAM----GTSCITISHRPA 221
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELqrelGITTIYVTHDQE 192
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
671-882 |
2.37e-14 |
|
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: 77.11 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 671 AISAASKETISFHEVDIVTPSQKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT---------KPS 741
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdlsdlDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 742 EGMFH---VPQRPYTSLGTLRDQIIypLSREEAKikvlslhrsgnnssasmllDDHLKTILENVRLVYLLER--EGWDsT 816
Cdd:COG4988 408 SWRRQiawVPQNPYLFAGTIRENLR--LGRPDAS-------------------DEELEAALEAAGLDEFVAAlpDGLD-T 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 817 PnwedV------LSLGEQQRLGMARLFFHHPKFGILDECTnaTSVDVE------EHLYRLATsmGITVITSSQRPALI 882
Cdd:COG4988 466 P----LgeggrgLSGGQAQRLALARALLRDAPLLLLDEPT--AHLDAEteaeilQALRRLAK--GRTVILITHRLALL 535
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
692-889 |
3.91e-14 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 72.13 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 692 QKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKPSEGMFHVPQRPYTSLGTLRDQI-IYP-LSRE 769
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADgLKPeLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 770 EAkikvLSLHRSGNNSSASmllDDHLKTILENVRLVYLLEREGwdstpnweDVLSLGEQQRLGMARLFFHHPKFGILDEC 849
Cdd:COG4133 94 EN----LRFWAALYGLRAD---REAIDEALEAVGLAGLADLPV--------RQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1142837572 850 TNA---TSVD-VEEHLYRLATSMGITVITSSQRPALIPFHALEL 889
Cdd:COG4133 159 FTAldaAGVAlLAELIAAHLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
30-218 |
3.93e-14 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 73.10 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV------GSDLNKEIFYV 103
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdireqdPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 104 PQR----PYTAVgtlrEQLIYPLTADQGIEPLTYDGMVD-LLKNVDLE--YLLERYPldkevnwgDELSLGEQQRLGMAR 176
Cdd:cd03295 81 IQQiglfPHMTV----EENIALVPKLLKWPKEKIRERADeLLALVGLDpaEFADRYP--------HELSGGQQQRVGVAR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1142837572 177 LFYHKPKFAILDECTSA---VTTD-MEERFCKKVRAMGTSCITISH 218
Cdd:cd03295 149 ALAADPPLLLMDEPFGAldpITRDqLQEEFKRLQQELGKTIVFVTH 194
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
25-189 |
4.51e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 73.20 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 25 SEANHIEFSDVKVV--TPAGNVLV-DDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLNKEI 100
Cdd:COG1116 3 AAAPALELRGVSKRfpTGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 101 FYVPQRPytavgTLreqliYP-LTADQGIE-PLTYDGMV---------DLLKNVDLEYLLERYPldkevnwgDELSLGEQ 169
Cdd:COG1116 83 GVVFQEP-----AL-----LPwLTVLDNVAlGLELRGVPkaerrerarELLELVGLAGFEDAYP--------HQLSGGMR 144
|
170 180
....*....|....*....|
gi 1142837572 170 QRLGMARLFYHKPKFAILDE 189
Cdd:COG1116 145 QRVAIARALANDPEVLLMDE 164
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
30-200 |
5.88e-14 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 72.21 E-value: 5.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLvDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSG------------HIVKPGVG-SDL 96
Cdd:cd03260 1 IELRDLNVYYGDKHAL-KDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdegevlldgkDIYDLDVDvLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 97 NKEIFYVPQRPYTAVGTLREQLIYPLTAdQGIepltydgmvdlLKNVDLEYL----LERYPLDKEVN---WGDELSLGEQ 169
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGLRL-HGI-----------KLKEELDERveeaLRKAALWDEVKdrlHALGLSGGQQ 147
|
170 180 190
....*....|....*....|....*....|....*
gi 1142837572 170 QRLGMARLFYHKPKFAILDECTSAV----TTDMEE 200
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALdpisTAKIEE 182
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
30-233 |
8.58e-14 |
|
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: 75.55 E-value: 8.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSD------LNKEIFYV 103
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdidrhtLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 104 PQRPYTAVGTLREQLIypLTADQGIEPLTYDGMVDLLK-NVDLEYLLERYPLDKEVNwGDELSLGEQQRLGMARLFYHKP 182
Cdd:TIGR01193 554 PQEPYIFSGSILENLL--LGAKENVSQDEIWAACEIAEiKDDIENMPLGYQTELSEE-GSSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1142837572 183 KFAILDECTSAVTTDMEERFCKKVRAMG-TSCITISHRPALVAFHDIVLSLD 233
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNLQdKTIIFVAHRLSVAKQSDKIIVLD 682
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
29-234 |
9.07e-14 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 71.73 E-value: 9.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 29 HIEFSDVKVV---TPAGNVLvDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV---KPGVGSD---LNKE 99
Cdd:cd03248 11 IVKFQNVTFAyptRPDTLVL-QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPISQYEhkyLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 100 IFYVPQRPYTAVGTLREQLIYPLTA---DQGIEPLTYDGMVDLLKNVDLEYlleryplDKEVNW-GDELSLGEQQRLGMA 175
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGLQScsfECVKEAAQKAHAHSFISELASGY-------DTEVGEkGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142837572 176 RLFYHKPKFAILDECTSAVTTDMEERFCKKVRA--MGTSCITISHRPALVAFHDIVLSLDG 234
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDwpERRTVLVIAHRLSTVERADQILVLDG 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
30-233 |
9.39e-14 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 71.88 E-value: 9.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKV-VTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFY 102
Cdd:cd03251 1 VEFKNVTFrYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDvrdytlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 103 VPQRPYTAVGTLREQLIYpltadqGIEPLTYDGMVDLLKNVDLEYLLERYPLDKEVNWGD---ELSLGEQQRLGMARLFY 179
Cdd:cd03251 81 VSQDVFLFNDTVAENIAY------GRPGATREEVEEAARAANAHEFIMELPEGYDTVIGErgvKLSGGQRQRIAIARALL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142837572 180 HKPKFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRPALVAFHDIVLSLD 233
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAHRLSTIENADRIVVLE 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
46-223 |
1.08e-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: 70.77 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLNKE--IFYVPQ-RPYTAVGTLREQLIYpL 122
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARnrIGYLPEeRGLYPKMKVIDQLVY-L 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 123 TADQGIEPltydgmVDLLKNVDleYLLERYPL-DKEVNWGDELSLGEQQRLGMARLFYHKPKFAILDECTSA---VTTDM 198
Cdd:cd03269 95 AQLKGLKK------EEARRRID--EWLERLELsEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGldpVNVEL 166
|
170 180
....*....|....*....|....*
gi 1142837572 199 EERFCKKVRAMGTSCITISHRPALV 223
Cdd:cd03269 167 LKDVIRELARAGKTVILSTHQMELV 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
30-194 |
1.67e-13 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 71.06 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNKEIFYVPQRPYT 109
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT--DINKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 110 AVGTLREQ--LIYPLTADQGI------EPLTYDGMVDLLKNVDLE---YLLERYPL-DKEVNWGDELSLGEQQRLGMARL 177
Cdd:cd03256 79 QIGMIFQQfnLIERLSVLENVlsgrlgRRSTWRSLFGLFPKEEKQralAALERVGLlDKAYQRADQLSGGQQQRVAIARA 158
|
170
....*....|....*..
gi 1142837572 178 FYHKPKFAILDECTSAV 194
Cdd:cd03256 159 LMQQPKLILADEPVASL 175
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
46-194 |
1.69e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 70.86 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSnllIT---GPNGSGKSSLFRVLGGLWPLVSGHIVkpgV-GSDLNKE-------IFYVPQRP--YTAVg 112
Cdd:COG1131 16 LDGVSLTVEPGE---IFgllGPNGAGKTTTIRMLLGLLRPTSGEVR---VlGEDVARDpaevrrrIGYVPQEPalYPDL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 113 TLREQLIYplTAD-QGIEPLTYDGMVD-LLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAILDEC 190
Cdd:COG1131 89 TVRENLRF--FARlYGLPRKEARERIDeLLELFGLTDAADRKV--------GTLSGGMKQRLGLALALLHDPELLILDEP 158
|
....
gi 1142837572 191 TSAV 194
Cdd:COG1131 159 TSGL 162
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
45-225 |
2.15e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.37 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 45 LVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLwplvsgHIVKPGVGSdlnkeiFYVPQRPYTAVGTLREQLIYPLTA 124
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA------LKGTPVAGC------VDVPDNQFGREASLIDAIGRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 125 DQGIEPLTYDGMVDllknvdlEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCK 204
Cdd:COG2401 113 KDAVELLNAVGLSD-------AVLWLRRF--------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180
....*....|....*....|....*
gi 1142837572 205 KV----RAMGTSCITISHRPALVAF 225
Cdd:COG2401 178 NLqklaRRAGITLVVATHHYDVIDD 202
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
30-226 |
2.50e-13 |
|
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: 70.13 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLNKEifyvpQRPY 108
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvSDLRGR-----AIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 109 --TAVGTLRE--QLIYPLTADQGIE---PLTYDGMVDLLKNVDLeyLLERYPL-DKEVNWGDELSLGEQQRLGMARLFYH 180
Cdd:cd03292 76 lrRKIGVVFQdfRLLPDRNVYENVAfalEVTGVPPREIRKRVPA--ALELVGLsHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1142837572 181 KPKFAILDECTSAVTTDMEERFC---KKVRAMGTSCITISHRPALVAFH 226
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMnllKKINKAGTTVVVATHAKELVDTT 202
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
30-192 |
2.64e-13 |
|
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: 70.50 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTpAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGG-LWPLVSGHIV----KPGVGS--DLNKEIFY 102
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRlfgeRRGGEDvwELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 103 V-P--QRPYTAVGTLREQLIYPLTADQGIePLTYDGM-----VDLLKNVDLEYLLERYpldkevnWGdELSLGEQQRLGM 174
Cdd:COG1119 83 VsPalQLRFPRDETVLDVVLSGFFDSIGL-YREPTDEqreraRELLELLGLAHLADRP-------FG-TLSQGEQRRVLI 153
|
170
....*....|....*...
gi 1142837572 175 ARLFYHKPKFAILDECTS 192
Cdd:COG1119 154 ARALVKDPELLILDEPTA 171
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
30-189 |
4.06e-13 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 69.42 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGN---VLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV---KPGVGSdlNKEIFYV 103
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgEPVTGP--GPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 104 PQRPYtavgtlreqlIYP-LTADQGIE-PLTYDGMVD---------LLKNVDLEYLLERYPldkevnwgDELSLGEQQRL 172
Cdd:cd03293 79 FQQDA----------LLPwLTVLDNVAlGLELQGVPKaeareraeeLLELVGLSGFENAYP--------HQLSGGMRQRV 140
|
170
....*....|....*..
gi 1142837572 173 GMARLFYHKPKFAILDE 189
Cdd:cd03293 141 ALARALAVDPDVLLLDE 157
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
42-208 |
5.46e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 68.54 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG-----VGSDLNKEIFYVPQRP-YTAVGTLR 115
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeQRDEPHENILYLGHLPgLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 116 EQLIYpLTADQGIEPLTYDGMVDLLKNVDLEYLLERYpldkevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSAVT 195
Cdd:TIGR01189 92 ENLHF-WAAIHGGAQRTIEDALAAVGLTGFEDLPAAQ-----------LSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170
....*....|...
gi 1142837572 196 TDMEERFCKKVRA 208
Cdd:TIGR01189 160 KAGVALLAGLLRA 172
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
313-882 |
5.61e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 72.50 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 313 IPHLRCHPRPLPLRVAAMLkilvprlfdkqGGQLLAVAVLVFSRTWISDRIASLNGTTVKFVLeqdkdafIRLIGVSILQ 392
Cdd:COG1132 13 LRYLRPYRGLLILALLLLL-----------LSALLELLLPLLLGRIIDALLAGGDLSALLLLL-------LLLLGLALLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 393 SGANSFVAPSLRTLTAKLALGWRIRMTNHMLR----YYLKRNafykvfnmSGKSIdadQRLTLDVDKLTTDLAGLVTGMV 468
Cdd:COG1132 75 ALLSYLQRYLLARLAQRVVADLRRDLFEHLLRlplsFFDRRR--------TGDLL---SRLTNDVDAVEQFLAHGLPQLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 469 KPLVDI-------LWFTWRMkllsgrrGVAILyAYMLLGLGFLRAISPDFGHLSGQEQELEGTF-RFMHSRLRTHAESIA 540
Cdd:COG1132 144 RSVVTLigalvvlFVIDWRL-------ALIVL-LVLPLLLLVLRLFGRRLRKLFRRVQEALAELnGRLQESLSGIRVVKA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 541 FfGGGSREKAMVEAKFVKLINHSKILLRKQWLYGIVDDFVTkqlphNVTWGLSLLYAlehkGDRALTS--TQGELAhALR 618
Cdd:COG1132 216 F-GREERELERFREANEELRRANLRAARLSALFFPLMELLG-----NLGLALVLLVG----GLLVLSGslTVGDLV-AFI 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 619 FLASVVSQSFIAFGDILELhkkFLELSGGINRIFELeeftrFAQRNTVVSP-NAISAA-SKETISFHEVDIVTPSQKLLA 696
Cdd:COG1132 285 LYLLRLFGPLRQLANVLNQ---LQRALASAERIFEL-----LDEPPEIPDPpGAVPLPpVRGEIEFENVSFSYPGDRPVL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 697 RKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT---------KPSE-----GMfhVPQRPYtsL--GTLRD 760
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidgvdirdlTLESlrrqiGV--VPQDTF--LfsGTIRE 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 761 QIIYplSREEAkikvlslhrsgnnssasmllDDhlKTILENVRLVYLLER-----EGWDsTPnwedV------LSLGEQQ 829
Cdd:COG1132 433 NIRY--GRPDA--------------------TD--EEVEEAAKAAQAHEFiealpDGYD-TV----VgergvnLSGGQRQ 483
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142837572 830 RLGMARLFFHHPKFGILDECTNAtsVDVE------EHLYRLATsmGITVITSSQRPALI 882
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSA--LDTEtealiqEALERLMK--GRTTIVIAHRLSTI 538
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
699-851 |
5.78e-13 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 67.29 E-value: 5.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 699 LSCDVVQGKSLLLTGPNGSGKSSIFRVL-RDLWPTfSGRVTkPSEGMFHVPQRPYTS--LGTLR--DQIIYPLSREEakI 773
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIaGLLSPT-EGTIL-LDGQDLTDDERKSLRkeIGYVFqdPQLFPRLTVRE--N 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 774 KVLSLHRSGNNSSASmllDDHLKTILENVRLVYLLEReGWDSTPNwedVLSLGEQQRLGMARLFFHHPKFGILDECTN 851
Cdd:pfam00005 80 LRLGLLLKGLSKREK---DARAEEALEKLGLGDLADR-PVGERPG---TLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
697-882 |
8.60e-13 |
|
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: 67.24 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 697 RKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTkpsegMFHVPQRPYtSLGTLRDQIIYPLSREEakikvl 776
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR-----LDGADISQW-DPNELGDHVGYLPQDDE------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 777 slhrsgnnssasmLLDDhlkTILENVrlvylleregwdstpnwedvLSLGEQQRLGMARLFFHHPKFGILDECTNATSVD 856
Cdd:cd03246 87 -------------LFSG---SIAENI--------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180
....*....|....*....|....*....
gi 1142837572 857 VEEHLYRLATSM---GITVITSSQRPALI 882
Cdd:cd03246 131 GERALNQAIAALkaaGATRIVIAHRPETL 159
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
42-202 |
9.59e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.98 E-value: 9.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLNK---EIFYV-PQRPYTAVGTLREQ 117
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaeACHYLgHRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 118 L-----IYPlTADQGIEpltydgmvDLLKNVDLEYLLERyPldkevnwGDELSLGEQQRLGMARLF-YHKPKFaILDECT 191
Cdd:PRK13539 94 LefwaaFLG-GEELDIA--------AALEAVGLAPLAHL-P-------FGYLSAGQKRRVALARLLvSNRPIW-ILDEPT 155
|
170
....*....|.
gi 1142837572 192 SAVTTDMEERF 202
Cdd:PRK13539 156 AALDAAAVALF 166
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
48-220 |
1.34e-12 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 67.71 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 48 DLTLRVETGSNLL-ITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG-VGSDLNKEIFYVPQRpyTAVG------------T 113
Cdd:cd03297 14 TLKIDFDLNEEVTgIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtVLFDSRKKINLPPQQ--RKIGlvfqqyalfphlN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 114 LREQLIYPL-TADQGIEPLTYDGMVDLLknvDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTS 192
Cdd:cd03297 92 VRENLAFGLkRKRNREDRISVDELLDLL---GLDHLLNRYP--------AQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190
....*....|....*....|....*....|..
gi 1142837572 193 AVTTDMEERFCKKVRAMGTS----CITISHRP 220
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNlnipVIFVTHDL 192
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
30-219 |
1.43e-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: 66.30 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLvDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIvkpgvgsdlnkeifYVPQRPYT 109
Cdd:cd03216 1 LELRGITKRFGGVKAL-DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI--------------LVDGKEVS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 110 AVGTLREQliypltaDQGIepltydGMVdllknvdleyllerYpldkevnwgdELSLGEQQRLGMARLFYHKPKFAILDE 189
Cdd:cd03216 66 FASPRDAR-------RAGI------AMV--------------Y----------QLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190
....*....|....*....|....*....|...
gi 1142837572 190 CTSAVTTDMEERF---CKKVRAMGTSCITISHR 219
Cdd:cd03216 109 PTAALTPAEVERLfkvIRRLRAQGVAVIFISHR 141
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
46-189 |
2.22e-12 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 67.24 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLNKEifyvpqrPYTAVGTLRE-QLIYP-LT 123
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-------ALRRIGALIEaPGFYPnLT 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142837572 124 ADqgiEPLTYDGMVDLLKNVDLEYLLErypldkEVNWGDE-------LSLGEQQRLGMARLFYHKPKFAILDE 189
Cdd:cd03268 89 AR---ENLRLLARLLGIRKKRIDEVLD------VVGLKDSakkkvkgFSLGMKQRLGIALALLGNPDLLILDE 152
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-219 |
2.56e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.64 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 26 EANHIEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLvSGHIVKPGVG-SDLN-----KE 99
Cdd:PRK11174 346 DPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIElRELDpeswrKH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 100 IFYVPQRPYTAVGTLREQLIY--PLTADQGIEpltydgmvDLLKNVDLEYLLERYP--LDKEVnwGDE---LSLGEQQRL 172
Cdd:PRK11174 425 LSWVGQNPQLPHGTLRDNVLLgnPDASDEQLQ--------QALENAWVSEFLPLLPqgLDTPI--GDQaagLSVGQAQRL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1142837572 173 GMARLFYHKPKFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHR 219
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQ 543
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
46-233 |
2.89e-12 |
|
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: 66.67 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFYVPQRPYTAVGTLREQL- 118
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDistiplEDLRSSLTIIPQDPTLFSGTIRSNLd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 119 IYPLTADQGIepltydgmvdllknvdleyllerYPLDKEVNWGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDM 198
Cdd:cd03369 104 PFDEYSDEEI-----------------------YGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1142837572 199 EERFCKKVRAM--GTSCITISHRPALVAFHDIVLSLD 233
Cdd:cd03369 161 DALIQKTIREEftNSTILTIAHRLRTIIDYDKILVMD 197
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
698-876 |
3.15e-12 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 66.47 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 698 KLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKPSEGMFHvPQRPYTSLGTLRD-QIIYP-LSREEAkIKV 775
Cdd:cd03268 18 DISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALIEaPGFYPnLTAREN-LRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 776 LSLHRSGNNSSASMLLDdhlktilenvrlVYLLEREGWDSTPNwedvLSLGEQQRLGMARLFFHHPKFGILDECTNATSV 855
Cdd:cd03268 96 LARLLGIRKKRIDEVLD------------VVGLKDSAKKKVKG----FSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180
....*....|....*....|....*
gi 1142837572 856 D----VEEHLYRLATSmGITVITSS 876
Cdd:cd03268 160 DgikeLRELILSLRDQ-GITVLISS 183
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
30-218 |
4.49e-12 |
|
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: 68.16 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVV--TPAGNV-LVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWP---LVSGHIV-KpgvGSDLN----- 97
Cdd:COG0444 2 LEVRNLKVYfpTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILfD---GEDLLklsek 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 98 -------KEIFYVPQRPYTA---VGTLREQLIYPLTADQGIEPLTYDGMV-DLLKNVDL---EYLLERYPLdkevnwgdE 163
Cdd:COG0444 79 elrkirgREIQMIFQDPMTSlnpVMTVGDQIAEPLRIHGGLSKAEARERAiELLERVGLpdpERRLDRYPH--------E 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142837572 164 LSLGEQQRLGMARLFYHKPKFAILDECTSA--VTT-----DMEERFCKKvraMGTSCITISH 218
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTAldVTIqaqilNLLKDLQRE---LGLAILFITH 209
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
30-230 |
6.30e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 69.37 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPA-GNVLV-DDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV---KPGVGSD---LNKEIF 101
Cdd:TIGR00958 479 IEFQDVSFSYPNrPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgVPLVQYDhhyLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 102 YVPQRPYTAVGTLREQLIYPLTA---DQGIEPLTYDGMVDLLKNVDLEYlleryplDKEVN-WGDELSLGEQQRLGMARL 177
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAYGLTDtpdEEIMAAAKAANAHDFIMEFPNGY-------DTEVGeKGSQLSGGQKQRIAIARA 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1142837572 178 FYHKPKFAILDECTSAVTTDMEERFCKKVRAMGTSCITISHRPALV--AFHDIVL 230
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVerADQILVL 686
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
654-883 |
6.46e-12 |
|
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: 69.24 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 654 LEEFTRFAQRNTVVSPNA--ISAASKETISFHEVDIVTPSQKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWP 731
Cdd:TIGR02857 294 AEALFAVLDAAPRPLAGKapVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 732 TFSGRVTKPSEGMFH------------VPQRPYTSLGTLRDQIIypLSREEAKIKVL--SLHRSGnnssasmlLDDHLKT 797
Cdd:TIGR02857 374 PTEGSIAVNGVPLADadadswrdqiawVPQHPFLFAGTIAENIR--LARPDASDAEIreALERAG--------LDEFVAA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 798 IlenvrlvylleREGWDsTPNWED--VLSLGEQQRLGMARLFFHHPKFGILDECT----NATSVDVEEHLYRLATsmGIT 871
Cdd:TIGR02857 444 L-----------PQGLD-TPIGEGgaGLSGGQAQRLALARAFLRDAPLLLLDEPTahldAETEAEVLEALRALAQ--GRT 509
|
250
....*....|..
gi 1142837572 872 VITSSQRPALIP 883
Cdd:TIGR02857 510 VLLVTHRLALAA 521
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
41-246 |
7.92e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 7.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 41 AGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLNKEIF-----YVPQRPYTAVGTL 114
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDiSTLKPEIYrqqvsYCAQTPTLFGDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 115 REQLIYP-LTADQGIEPltyDGMVDllknvDLEYL-LERYPLDKEVNwgdELSLGEQQRLGMARLFYHKPKFAILDECTS 192
Cdd:PRK10247 98 YDNLIFPwQIRNQQPDP---AIFLD-----DLERFaLPDTILTKNIA---ELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 193 AV----TTDMEERFCKKVRAMGTSCITISHRPALVAFHDIVLSLDGEGGwNVQHRRDD 246
Cdd:PRK10247 167 ALdesnKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAG-EMQEARYE 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
680-889 |
7.94e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.84 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 680 ISFHEVDIVTPSQKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVL-RDLWPTfSGRVTkpsegMFHVpqrpytSLGTL 758
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLyGEERPT-SGQVL-----VNGQ------DLSRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 759 RDQIIYPLSReeaKIK-VLSLHRsgnnssasmLLDDhlKTILENV----------------------RLVYLLEREgwDS 815
Cdd:COG2884 70 KRREIPYLRR---RIGvVFQDFR---------LLPD--RTVYENValplrvtgksrkeirrrvrevlDLVGLSDKA--KA 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 816 TPnweDVLSLGEQQRLGMARLFFHHPKFGILDECTN----ATSVDVEEHLYRLAtSMGITVITSSqrpalipfHALEL 889
Cdd:COG2884 134 LP---HELSGGEQQRVAIARALVNRPELLLADEPTGnldpETSWEIMELLEEIN-RRGTTVLIAT--------HDLEL 199
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
30-201 |
1.32e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.50 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLvDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLNKEIFYVPQRpy 108
Cdd:PRK09493 2 IEFKNVSKHFGPTQVL-HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvNDPKVDERLIRQE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 109 taVGTLREQL-IYP-LTADQGIE--PLTYDGM---------VDLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMA 175
Cdd:PRK09493 79 --AGMVFQQFyLFPhLTALENVMfgPLRVRGAskeeaekqaRELLAKVGLAERAHHYP--------SELSGGQQQRVAIA 148
|
170 180
....*....|....*....|....*.
gi 1142837572 176 RLFYHKPKFAILDECTSAVttDMEER 201
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSAL--DPELR 172
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
42-193 |
1.45e-11 |
|
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: 65.34 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlnKEIFYVP--QRPYTAVG------- 112
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG------KDITNLPphKRPVNTVFqnyalfp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 113 --TLREQLIYPLTADQGIEPLTYDGMVDLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAILDEC 190
Cdd:cd03300 86 hlTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKP--------SQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
...
gi 1142837572 191 TSA 193
Cdd:cd03300 158 LGA 160
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-257 |
2.98e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKV-VTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFY 102
Cdd:PLN03232 1235 IKFEDVHLrYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDvakfglTDLRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 103 VPQRPYTAVGTLREQliypltadqgIEPLTYDGMVDL---LKNVDLEYLLERYP--LDKEVNWGDE-LSLGEQQRLGMAR 176
Cdd:PLN03232 1315 IPQSPVLFSGTVRFN----------IDPFSEHNDADLweaLERAHIKDVIDRNPfgLDAEVSEGGEnFSVGQRQLLSLAR 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 177 LFYHKPKFAILDECTSAVTTDMEERFCKKVRAMGTSC--ITISHRPALVAFHDIVLSLdgEGGWNVQHRRDDSSFSTEES 254
Cdd:PLN03232 1385 ALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCtmLVIAHRLNTIIDCDKILVL--SSGQVLEYDSPQELLSRDTS 1462
|
...
gi 1142837572 255 DFS 257
Cdd:PLN03232 1463 AFF 1465
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
697-876 |
4.14e-11 |
|
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: 63.32 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 697 RKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT---KPSEGMFH----VPQRPYTSlgtlRDqiiYPLSRE 769
Cdd:cd03235 16 EDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgKPLEKERKrigyVPQRRSID----RD---FPISVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 770 EAkikVLS--LHRSGNNSSASMLLDDHLKTILENVRLVYLLERegwdstPNWEdvLSLGEQQRLGMARLFFHHPKFGILD 847
Cdd:cd03235 89 DV---VLMglYGHKGLFRRLSKADKAKVDEALERVGLSELADR------QIGE--LSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190
....*....|....*....|....*....|....
gi 1142837572 848 ECTnaTSVDV--EEHLYRLATSM---GITVITSS 876
Cdd:cd03235 158 EPF--AGVDPktQEDIYELLRELrreGMTILVVT 189
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
692-875 |
4.80e-11 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 62.45 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 692 QKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVtkpsegmfhvpqrpytslgTLRDQIIYPLSREEa 771
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-------------------LLDGKDLASLSPKE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 772 kikvLSLHRSgnnssasmllddHLKTILENVRLVYLLEREgWDStpnwedvLSLGEQQRLGMARLFFHHPKFGILDECTN 851
Cdd:cd03214 71 ----LARKIA------------YVPQALELLGLAHLADRP-FNE-------LSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180
....*....|....*....|....*...
gi 1142837572 852 A----TSVDVEEHLYRLATSMGITVITS 875
Cdd:cd03214 127 HldiaHQIELLELLRRLARERGKTVVMV 154
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
42-193 |
5.56e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 65.35 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNKeifyVP--QRPYTAV-------- 111
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ--DITH----VPaeNRHVNTVfqsyalfp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 112 -GTLREQLIYPL----TADQGIEPLTYDGmvdlLKNVDLEYLLERYPLDkevnwgdeLSLGEQQRLGMARLFYHKPKFAI 186
Cdd:PRK09452 100 hMTVFENVAFGLrmqkTPAAEITPRVMEA----LRMVQLEEFAQRKPHQ--------LSGGQQQRVAIARAVVNKPKVLL 167
|
....*..
gi 1142837572 187 LDECTSA 193
Cdd:PRK09452 168 LDESLSA 174
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-233 |
8.30e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.12 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 15 LDHSSPGNYVSEANHIEFSDVKV-VTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSS----LFRVLGGlwplVSGHIVK 89
Cdd:TIGR00957 1270 IQETAPPSGWPPRGRVEFRNYCLrYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINES----AEGEIII 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 90 PGVG------SDLNKEIFYVPQRPYTAVGTLREQLiypltadqgiEPLTYDGMVDLLKNVDLEYL---LERYP--LDKEV 158
Cdd:TIGR00957 1346 DGLNiakiglHDLRFKITIIPQDPVLFSGSLRMNL----------DPFSQYSDEEVWWALELAHLktfVSALPdkLDHEC 1415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 159 NWGDE-LSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCKKVRAMGTSC--ITISHRPALVAFHDIVLSLD 233
Cdd:TIGR00957 1416 AEGGEnLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCtvLTIAHRLNTIMDYTRVIVLD 1493
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
44-235 |
9.57e-11 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 63.43 E-value: 9.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 44 VLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLN------------KEIFYV-------P 104
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQ--DIAamsrkelrelrrKKISMVfqsfallP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 105 QRpytavgTLREQLIYPLTAdQGIEPLT-YDGMVDLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPK 183
Cdd:cd03294 116 HR------TVLENVAFGLEV-QGVPRAErEERAAEALELVGLEGWEHKYP--------DELSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 184 FAILDECTSA----VTTDMEERFCKKVRAMGTSCITISHRP--ALVAFHDIVLSLDGE 235
Cdd:cd03294 181 ILLMDEAFSAldplIRREMQDELLRLQAELQKTIVFITHDLdeALRLGDRIAIMKDGR 238
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
695-891 |
1.01e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 61.99 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 695 LARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKPSEGMFHVPQRPYTSLGTL--RDQIIYPLSREEak 772
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLghLPGLKPELSALE-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 773 ikvlslhrsgNNSSASMLLDDHLKTILENVRLVYLLEREgwdSTPnwEDVLSLGEQQRLGMARLFFHHPKFGILDECTNA 852
Cdd:TIGR01189 93 ----------NLHFWAAIHGGAQRTIEDALAAVGLTGFE---DLP--AAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1142837572 853 TSVD--------VEEHLYRlatsMGITVITSSQrpALIPFHALELKL 891
Cdd:TIGR01189 158 LDKAgvallaglLRAHLAR----GGIVLLTTHQ--DLGLVEARELRL 198
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
30-218 |
1.05e-10 |
|
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: 61.43 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVkVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNKEIFYVPQRPyT 109
Cdd:cd03229 1 LELKNV-SKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE--DLTDLEDELPPLR-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 110 AVGTLREQL-IYP-LTAdqgiepltydgmvdlLKNVdleylleRYPldkevnwgdeLSLGEQQRLGMARLFYHKPKFAIL 187
Cdd:cd03229 77 RIGMVFQDFaLFPhLTV---------------LENI-------ALG----------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190
....*....|....*....|....*....|....*
gi 1142837572 188 DECTSA---VTTDMEERFCKKVRAM-GTSCITISH 218
Cdd:cd03229 125 DEPTSAldpITRREVRALLKSLQAQlGITVVLVTH 159
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
42-218 |
1.29e-10 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 62.35 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLNKE---IFYVPQR----PYTAVgt 113
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDiTNLPPEkrdISYVPQNyalfPHMTV-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 114 lREQLIYPLTAdQGIEPLTYDGMV-DLLKNVDLEYLLERYPLdkevnwgdELSLGEQQRLGMARLFYHKPKFAILDECTS 192
Cdd:cd03299 89 -YKNIAYGLKK-RKVDKKEIERKVlEIAEMLGIDHLLNRKPE--------TLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190
....*....|....*....|....*....|
gi 1142837572 193 AVTTDMEERF---CKKVR-AMGTSCITISH 218
Cdd:cd03299 159 ALDVRTKEKLreeLKKIRkEFGVTVLHVTH 188
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
42-193 |
1.60e-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: 61.78 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLNKeifyvpqrpyTAVGTLREQLiyp 121
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK----------KNINELRQKV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 122 ltadqgiepltydGMV----------DLLKNVDL-----------------EYLLERYPL-DKEVNWGDELSLGEQQRLG 173
Cdd:cd03262 79 -------------GMVfqqfnlfphlTVLENITLapikvkgmskaeaeeraLELLEKVGLaDKADAYPAQLSGGQQQRVA 145
|
170 180
....*....|....*....|
gi 1142837572 174 MARLFYHKPKFAILDECTSA 193
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSA 165
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
46-223 |
2.03e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.19 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVkpGVGSDLNKE--------------IFYVPQ---RPY 108
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVA--WLGKDLLGMkddewravrsdiqmIFQDPLaslNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 109 TAVG-TLREQLI--YPLTADQGIEPLTYDGM--VDLLKNvdleyLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPK 183
Cdd:PRK15079 115 MTIGeIIAEPLRtyHPKLSRQEVKDRVKAMMlkVGLLPN-----LINRYP--------HEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1142837572 184 FAILDECTSAVTTDMEER---FCKKV-RAMGTSCITISHRPALV 223
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQvvnLLQQLqREMGLSLIFIAHDLAVV 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
648-850 |
2.05e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.46 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 648 INRIFELEEFTRFAQRNTVVSPNAisaaskeTISFHEVDIVTPSQKLLA-RKLSCDVVQGKSLLLTGPNGSGKSSIFRVL 726
Cdd:PRK11160 314 INEITEQKPEVTFPTTSTAAADQV-------SLTLNNVSFTYPDQPQPVlKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 727 RDLWPTFSGRVT---KP----SE-----GMFHVPQRPYTSLGTLRDQIIypLSREEAKikvlslhrsgnnssasmllDDH 794
Cdd:PRK11160 387 TRAWDPQQGEILlngQPiadySEaalrqAISVVSQRVHLFSATLRDNLL--LAAPNAS-------------------DEA 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142837572 795 LKTILENVRLVYLLE-REGWDStpnW----EDVLSLGEQQRLGMARLFFHHPKFGILDECT 850
Cdd:PRK11160 446 LIEVLQQVGLEKLLEdDKGLNA---WlgegGRQLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
705-877 |
2.06e-10 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 61.80 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 705 QGKSLLLTGPNGSGKSSIFRVL-RDLWPTfSGRVTKPSEGMFHVPQRPYTSLG------------TLRDQI-----IYPL 766
Cdd:COG4555 26 DGEITGLLGPNGAGKTTLLRMLaGLLKPD-SGSILIDGEDVRKEPREARRQIGvlpderglydrlTVRENIryfaeLYGL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 767 SREEAKIKVLSLhrsgnnsSASMLLDDHLKTILENvrlvylleregwdstpnwedvLSLGEQQRLGMARLFFHHPKFGIL 846
Cdd:COG4555 105 FDEELKKRIEEL-------IELLGLEEFLDRRVGE---------------------LSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1142837572 847 DECTNAtsVDVE------EHLYRLATSmGITVITSSQ 877
Cdd:COG4555 157 DEPTNG--LDVMarrllrEILRALKKE-GKTVLFSSH 190
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-189 |
2.79e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.93 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 21 GNYVSEANHIEFSDvkvvtpAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVkpgVGSDLnkEI 100
Cdd:COG0488 312 GKKVLELEGLSKSY------GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK---LGETV--KI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 101 FYVPQRpytavgtlREQLiypltadqgiepltydgmvDLLKNVdLEYLLERYPLDKEVNW----------GDE------- 163
Cdd:COG0488 381 GYFDQH--------QEEL-------------------DPDKTV-LDELRDGAPGGTEQEVrgylgrflfsGDDafkpvgv 432
|
170 180
....*....|....*....|....*.
gi 1142837572 164 LSLGEQQRLGMARLFYHKPKFAILDE 189
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDE 458
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
681-893 |
2.84e-10 |
|
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: 59.57 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 681 SFHEVDIVTPSQKLLaRKLSCDVVQGKSLLLTGPNGSGKSSIFRVLrdlwptfsGRVTKPSEGmfhvpqrpytslgtlrd 760
Cdd:cd00267 1 EIENLSFRYGGRTAL-DNVSLTLKAGEIVALVGPNGSGKSTLLRAI--------AGLLKPTSG----------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 761 qIIYPLSREEAKIKVLSLHRsgnnssasmllddhlktilenvRLVYLLEregwdstpnwedvLSLGEQQRLGMARLFFHH 840
Cdd:cd00267 55 -EILIDGKDIAKLPLEELRR----------------------RIGYVPQ-------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142837572 841 PKFGILDECTNATSVD----VEEHLYRLATSmGITVITSSQRPALIPFHALELKLID 893
Cdd:cd00267 99 PDLLLLDEPTSGLDPAsrerLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLK 154
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
30-235 |
3.76e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.59 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGN---VLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLNKEIFYVPQ 105
Cdd:PRK10535 5 LELKDIRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 106 RPYTAVGTLREQLIYPLTADQGIE-PLTYDGMVDLLKNVDLEYLLERYPLDKEVNWG-DELSLGEQQRLGMARLFYHKPK 183
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEvPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQpSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142837572 184 FAILDECTSAVTTDMEER---FCKKVRAMGTSCITISHRPALVAFHDIVLSL-DGE 235
Cdd:PRK10535 165 VILADEPTGALDSHSGEEvmaILHQLRDRGHTVIIVTHDPQVAAQAERVIEIrDGE 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
48-194 |
3.78e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.28 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 48 DLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlNKEIFYVPQR----PYTAVGTLREQLIYPLT 123
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----KLRIGYVPQKlyldTTLPLTVNRFLRLRPGT 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142837572 124 ADQGIEPltydgmvdLLKNVDLEYLLErYPLDKevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSAV 194
Cdd:PRK09544 97 KKEDILP--------ALKRVQAGHLID-APMQK-------LSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
42-218 |
3.84e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.93 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNkeifYVP--QRPYTAV-------- 111
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV--DLS----HVPpyQRPINMMfqsyalfp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 112 -GTLREQLIYPLTADQGIEPLTYDGMVDLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAILDEC 190
Cdd:PRK11607 105 hMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKP--------HQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190
....*....|....*....|....*....|..
gi 1142837572 191 TSAVTTDMEERFCKKV----RAMGTSCITISH 218
Cdd:PRK11607 177 MGALDKKLRDRMQLEVvdilERVGVTCVMVTH 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-189 |
4.10e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 62.05 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 26 EANHIE--FSDVKVVtpagnvlvDDLTLRVETGSnllIT---GPNGSGKSSLFRVLGGLWPLVSGHI-VKpgvGSDLNKE 99
Cdd:COG4152 3 ELKGLTkrFGDKTAV--------DDVSFTVPKGE---IFgllGPNGAGKTTTIRIILGILAPDSGEVlWD---GEPLDPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 100 ----IFYVPQ-RpytavG-----TLREQLIYpLTAdqgiepltydgmvdlLKNVD-------LEYLLERYPL----DKEV 158
Cdd:COG4152 69 drrrIGYLPEeR-----GlypkmKVGEQLVY-LAR---------------LKGLSkaeakrrADEWLERLGLgdraNKKV 127
|
170 180 190
....*....|....*....|....*....|.
gi 1142837572 159 nwgDELSLGEQQRLGMARLFYHKPKFAILDE 189
Cdd:COG4152 128 ---EELSKGNQQKVQLIAALLHDPELLILDE 155
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
46-212 |
4.69e-10 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 60.53 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSG---------------HIVKPGVGsdlnkeifYVPQrpyta 110
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsirfdgrditglpphERARAGIG--------YVPE----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 111 vgtlrEQLIYP-LTADQGIEPLTYDGMVDLLKNvDLEYLLERYPLDKEV--NWGDELSLGEQQRLGMARLFYHKPKFAIL 187
Cdd:cd03224 83 -----GRRIFPeLTVEENLLLGAYARRRAKRKA-RLERVYELFPRLKERrkQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180
....*....|....*....|....*....
gi 1142837572 188 DECTS----AVTTDMEERFcKKVRAMGTS 212
Cdd:cd03224 157 DEPSEglapKIVEEIFEAI-RELRDEGVT 184
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
46-234 |
4.71e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.57 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVkpgVGS---------DLNKEIFYVPQRPYTA-VG-TL 114
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT---VGGmvlseetvwDVRRQVGMVFQNPDNQfVGaTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 115 REQLIYPLtADQGIEpltYDGMV----DLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAILDEC 190
Cdd:PRK13635 100 QDDVAFGL-ENIGVP---REEMVervdQALRQVGMEDFLNREP--------HRLSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1142837572 191 TSAVTTDMEERFCKKVRAM----GTSCITISHRPALVAFHDIVLSLDG 234
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLkeqkGITVLSITHDLDEAAQADRVIVMNK 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
42-189 |
4.86e-10 |
|
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: 60.35 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNK------EIFYVPQR----PYTAV 111
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR--DVTDlppkdrDIAMVFQNyalyPHMTV 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 112 gtlREQLIYPLTADQGIEPLTYDGMVDLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAILDE 189
Cdd:cd03301 90 ---YDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKP--------KQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-219 |
5.02e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 23 YVSEANHI--EFSDVKVVtpagnvlvDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWP--------LVSGHIVKPGV 92
Cdd:PRK13549 4 YLLEMKNItkTFGGVKAL--------DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtyegeiIFEGEELQASN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 93 GSD--------LNKEIFYVPQrpytavgtlreqliypLTADQGI---EPLTYDGMVDLLK-NVDLEYLLERYPLDKEVNW 160
Cdd:PRK13549 76 IRDteragiaiIHQELALVKE----------------LSVLENIflgNEITPGGIMDYDAmYLRAQKLLAQLKLDINPAT 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142837572 161 G-DELSLGEQQRLGMARLFYHKPKFAILDECTSAVT---TDMEERFCKKVRAMGTSCITISHR 219
Cdd:PRK13549 140 PvGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTeseTAVLLDIIRDLKAHGIACIYISHK 202
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
26-219 |
5.24e-10 |
|
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: 60.46 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 26 EANHIEFSDVKVVTPAgnvlVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNKEIFYVPQ 105
Cdd:cd03266 5 DALTKRFRDVKKTVQA----VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF--DVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 106 RpytaVG------------TLREQLIYpLTADQGIEPLTYDGMVD-LLKNVDLEYLLERYpldkevnwGDELSLGEQQRL 172
Cdd:cd03266 79 R----LGfvsdstglydrlTARENLEY-FAGLYGLKGDELTARLEeLADRLGMEELLDRR--------VGGFSTGMRQKV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1142837572 173 GMARLFYHKPKFAILDECTSA---VTTDMEERFCKKVRAMGTSCITISHR 219
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGldvMATRALREFIRQLRALGKCILFSTHI 195
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
650-879 |
6.59e-10 |
|
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: 62.76 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 650 RIFELEEFTRFAQrnTVVSPNAISAASKE-TISFHEVDIVTPSQKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRD 728
Cdd:TIGR02868 306 RIVEVLDAAGPVA--EGSAPAAGAVGLGKpTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 729 LWPTFSGRVTKPSEGMFHV------------PQRPYTSLGTLRDQIIypLSREEAKikvlslhrsgnnssasmllDDHLK 796
Cdd:TIGR02868 384 LLDPLQGEVTLDGVPVSSLdqdevrrrvsvcAQDAHLFDTTVRENLR--LARPDAT-------------------DEELW 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 797 TILENVRLVYLLER--EGWDsTPNWED--VLSLGEQQRLGMARLFFHHPKFGILDECTNATSVDVEEHLYR--LATSMGI 870
Cdd:TIGR02868 443 AALERVGLADWLRAlpDGLD-TVLGEGgaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEdlLAALSGR 521
|
....*....
gi 1142837572 871 TVITSSQRP 879
Cdd:TIGR02868 522 TVVLITHHL 530
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
697-874 |
6.65e-10 |
|
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: 60.27 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 697 RKLSCDVVQGKSLLLTGPNGSGKSSIFRV---LRDLWPTF--SGRV-----------TKPSE-----GMfhVPQRPYTSL 755
Cdd:cd03260 17 KDISLDIPKGEITALIGPSGCGKSTLLRLlnrLNDLIPGApdEGEVlldgkdiydldVDVLElrrrvGM--VFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 756 GTLRDQIIYPlsreeakikvLSLHRsgnnssasMLLDDHLKTILENV-RLVYLleregwdstpnWEDV--------LSLG 826
Cdd:cd03260 95 GSIYDNVAYG----------LRLHG--------IKLKEELDERVEEAlRKAAL-----------WDEVkdrlhalgLSGG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1142837572 827 EQQRLGMARLFFHHPKFGILDECTNA----TSVDVEEHLYRLATSMGITVIT 874
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSAldpiSTAKIEELIAELKKEYTIVIVT 197
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
680-890 |
7.28e-10 |
|
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: 60.48 E-value: 7.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 680 ISFHEVDIVTPSQKLLaRKLSCDVVQGKSLLLTGPNGSGKSSIFRVL-RDLWPTFSGRVT-----KPSEGMFHVPQRpyt 753
Cdd:COG1119 4 LELRNVTVRRGGKTIL-DDISWTVKPGEHWAILGPNGAGKSTLLSLItGDLPPTYGNDVRlfgerRGGEDVWELRKR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 754 sLG----TLRDQIIYPLSREEAkikVLS-------LHRsgnNSSASMLldDHLKTILENVRLVYLLEREgWDStpnwedv 822
Cdd:COG1119 80 -IGlvspALQLRFPRDETVLDV---VLSgffdsigLYR---EPTDEQR--ERARELLELLGLAHLADRP-FGT------- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142837572 823 LSLGEQQRLGMARLFFHHPKFGILDECTN----ATSVDVEEHLYRLATSMGITVITSSQRPALIP---FHALELK 890
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAgldlGARELLLALLDKLAAEGAPTLVLVTHHVEEIPpgiTHVLLLK 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
42-189 |
7.69e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.43 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG-----VGSDLNKEIFYVPQRPytAVGTLre 116
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrQRDEYHQDLLYLGHQP--GIKTE-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 117 qliypLTAD------QGI-EPLTYDGMVDLLKNVDL---EYLLERYpldkevnwgdeLSLGEQQRLGMARLFYHKPKFAI 186
Cdd:PRK13538 89 -----LTALenlrfyQRLhGPGDDEALWEALAQVGLagfEDVPVRQ-----------LSAGQQRRVALARLWLTRAPLWI 152
|
...
gi 1142837572 187 LDE 189
Cdd:PRK13538 153 LDE 155
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
41-193 |
1.06e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 60.13 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 41 AGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIvkpgvgsDLNkeifyvpQRPYT----------- 109
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEV-------RLN-------GRPLAawspwelarrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 110 AVgtLREQ--LIYPLTADQ----GIEPLTYDGMVDL------LKNVDLEYLLER-YPldkevnwgdELSLGEQQRLGMAR 176
Cdd:COG4559 78 AV--LPQHssLAFPFTVEEvvalGRAPHGSSAAQDRqivreaLALVGLAHLAGRsYQ---------TLSGGEQQRVQLAR 146
|
170 180
....*....|....*....|....
gi 1142837572 177 LF-------YHKPKFAILDECTSA 193
Cdd:COG4559 147 VLaqlwepvDGGPRWLFLDEPTSA 170
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
46-189 |
1.19e-09 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 59.66 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV-GSDLN---KEIFYVPQRpYTAVG--TLREQLI 119
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdATDVPvqeRNVGFVFQH-YALFRhmTVFDNVA 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142837572 120 YPLTADQGIEPLTYDGM----VDLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAILDE 189
Cdd:cd03296 97 FGLRVKPRSERPPEAEIrakvHELLKLVQLDWLADRYP--------AQLSGGQRQRVALARALAVEPKVLLLDE 162
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
61-258 |
1.22e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 61 ITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFYVPQRPYTAVGTLREQLiypltadqgiEPLTYD 134
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDiskfglMDLRKVLGIIPQAPVLFSGTVRFNL----------DPFNEH 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 135 GMVDL---LKNVDLEYLLERYP--LDKEVNWGDE-LSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCKKVRA 208
Cdd:PLN03130 1340 NDADLwesLERAHLKDVIRRNSlgLDAEVSEAGEnFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE 1419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1142837572 209 MGTSC--ITISHRPALVAFHDIVLSLDgeGGWNVQHRRDDSSFSTEESDFSS 258
Cdd:PLN03130 1420 EFKSCtmLIIAHRLNTIIDCDRILVLD--AGRVVEFDTPENLLSNEGSAFSK 1469
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
38-218 |
1.32e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 59.70 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 38 VTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLgglwplvSGHivkPGV----------GSDL---------NK 98
Cdd:COG0396 8 VSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL-------MGH---PKYevtsgsilldGEDIlelspderaRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 99 EIFYVPQRP------------YTAVGTLREQLIYPLTADQGIEpltydgmvDLLKNVDL-EYLLERYpldkeVNWGdeLS 165
Cdd:COG0396 78 GIFLAFQYPveipgvsvsnflRTALNARRGEELSAREFLKLLK--------EKMKELGLdEDFLDRY-----VNEG--FS 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142837572 166 LGEQQR---LGMARLfyhKPKFAILDECTS--------AVTtdmeeRFCKKVRAMGTSCITISH 218
Cdd:COG0396 143 GGEKKRneiLQMLLL---EPKLAILDETDSgldidalrIVA-----EGVNKLRSPDRGILIITH 198
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
680-882 |
1.68e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 61.66 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 680 ISFHEVDIVTPSQ--KLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT---KPSEGMFH-------- 746
Cdd:TIGR00958 479 IEFQDVSFSYPNRpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgVPLVQYDHhylhrqva 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 747 -VPQRPYTSLGTLRDQIIYPLSR-EEAKIKvlslhrsgnnSSASMLLDDHLKTILENvrlvyllereGWDSTPNWEDV-L 823
Cdd:TIGR00958 559 lVGQEPVLFSGSVRENIAYGLTDtPDEEIM----------AAAKAANAHDFIMEFPN----------GYDTEVGEKGSqL 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142837572 824 SLGEQQRLGMARLFFHHPKFGILDECTNATSVDVEEHLYRLATSMGITVITSSQRPALI 882
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTV 677
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
700-873 |
2.04e-09 |
|
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: 61.07 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 700 SCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT---KPSEGMFH------------VPQRPYTSL---GTLRDQ 761
Cdd:COG1123 285 SLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgKDLTKLSRrslrelrrrvqmVFQDPYSSLnprMTVGDI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 762 IIYPL------SREEAKIKVLSLhrsgnnssasmllddhlktiLENVRLvyllEREGWDSTPnWEdvLSLGEQQRLGMAR 835
Cdd:COG1123 365 IAEPLrlhgllSRAERRERVAEL--------------------LERVGL----PPDLADRYP-HE--LSGGQRQRVAIAR 417
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1142837572 836 LFFHHPKFGILDECTNA--TSV--DVEEHLYRLATSMGITVI 873
Cdd:COG1123 418 ALALEPKLLILDEPTSAldVSVqaQILNLLRDLQRELGLTYL 459
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
680-882 |
2.40e-09 |
|
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: 60.69 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 680 ISFHEVDIVTPSQKLLA-RKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWP---TFSGRVT-------KPSE------ 742
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAvDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLldgrdllELSEalrgrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 743 -GMfhVPQRPYTSL--GTLRDQIIYPL-----SREEAKIKVLSLhrsgnnssasmllddhlktiLENVRLVYLLEREGWD 814
Cdd:COG1123 85 iGM--VFQDPMTQLnpVTVGDQIAEALenlglSRAEARARVLEL--------------------LEAVGLERRLDRYPHQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142837572 815 stpnwedvLSLGEQQRLGMARLFFHHPKFGILDECTNA----TSVDVEEHLYRLATSMGITVITSSQRPALI 882
Cdd:COG1123 143 --------LSGGQRQRVAIAMALALDPDLLIADEPTTAldvtTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
680-882 |
2.52e-09 |
|
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: 58.37 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 680 ISFHEVDIVTPSQKLLA-RKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRV---------TKPSE---GMFH 746
Cdd:cd03245 3 IEFRNVSFSYPNQEIPAlDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirqLDPADlrrNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 747 VPQRPYTSLGTLRDQII--YPLSREEAKIKVLSLhrsgnnSSASMLLDDHLKTiLEnvrlvyLLEREGWDStpnwedvLS 824
Cdd:cd03245 83 VPQDVTLFYGTLRDNITlgAPLADDERILRAAEL------AGVTDFVNKHPNG-LD------LQIGERGRG-------LS 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 825 LGEQQRLGMARLFFHHPKFGILDECTNATSVDVEEHLY-RLATSM-GITVITSSQRPALI 882
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKeRLRQLLgDKTLIIITHRPSLL 202
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
699-891 |
2.54e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 57.89 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 699 LSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKPSEGMFHvpQRPYTSLGTL----RDQIIYPLSREEakiK 774
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF--QRDSIARGLLylghAPGIKTTLSVLE---N 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 775 VLSLHRSGNNSSASMLLDDHLKTILENVRLVYlleregwdstpnwedvLSLGEQQRLGMARLFFHHPKFGILDECTNATS 854
Cdd:cd03231 94 LRFWHADHSDEQVEEALARVGLNGFEDRPVAQ----------------LSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1142837572 855 VDVEEhlyRLATSM-------GITVITSSQRPALIPFHALELKL 891
Cdd:cd03231 158 KAGVA---RFAEAMaghcargGMVVLTTHQDLGLSEAGARELDL 198
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
46-223 |
3.50e-09 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 58.22 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV---------KP------GVGsdlnkEIFYVPqRPYTA 110
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgeditglPPheiarlGIG-----RTFQIP-RLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 111 VgTLREQLIYPLTADQGiEPLTYDGMV-----------DLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFY 179
Cdd:cd03219 90 L-TVLENVMVAAQARTG-SGLLLARARreereareraeELLERVGLADLADRPA--------GELSYGQQRRLEIARALA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1142837572 180 HKPKFAILDECTSAVTTDMEERFC---KKVRAMGTSCITISHRPALV 223
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAeliRELRERGITVLLVEHDMDVV 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
26-233 |
3.66e-09 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 56.94 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 26 EANHIEFSdvkvVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV-----GSDLNKEI 100
Cdd:cd03247 2 SINNVSFS----YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 101 FYVPQRPYTAVGTLREqliypltadqgiepltydgmvdllknvdleyllerypldkevNWGDELSLGEQQRLGMARLFYH 180
Cdd:cd03247 78 SVLNQRPYLFDTTLRN------------------------------------------NLGRRFSGGERQRLALARILLQ 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1142837572 181 KPKFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRPALVAFHDIVLSLD 233
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVlkDKTLIWITHHLTGIEHMDKILFLE 170
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
30-233 |
3.80e-09 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 60.12 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTP-AGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFY 102
Cdd:TIGR02203 331 VEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDladytlASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 103 VPQRPYTAVGTLREQLIYPLTADQGIEPLTydgmvDLLKNVDLEYLLERYPLDKEVNWGDE---LSLGEQQRLGMARLFY 179
Cdd:TIGR02203 411 VSQDVVLFNDTIANNIAYGRTEQADRAEIE-----RALAAAYAQDFVDKLPLGLDTPIGENgvlLSGGQRQRLAIARALL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142837572 180 HKPKFAILDECTSAVTTDmEERFCKKV--RAM-GTSCITISHRPALVAFHDIVLSLD 233
Cdd:TIGR02203 486 KDAPILILDEATSALDNE-SERLVQAAleRLMqGRTTLVIAHRLSTIEKADRIVVMD 541
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
699-876 |
4.26e-09 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 56.64 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 699 LSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLwptfsgrvTKPSEGMFHVpqrpytsLGtlrdqiiYPLSREEAKIKvlsl 778
Cdd:cd03230 19 ISLTVEKGEIYGLLGPNGAGKTTLIKIILGL--------LKPDSGEIKV-------LG-------KDIKKEPEEVK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 779 HRSG----NNSsasmlLDDHLkTILENVRLvylleregwdstpnwedvlSLGEQQRLGMARLFFHHPKFGILDECTNA-- 852
Cdd:cd03230 73 RRIGylpeEPS-----LYENL-TVRENLKL-------------------SGGMKQRLALAQALLHDPELLILDEPTSGld 127
|
170 180
....*....|....*....|....*.
gi 1142837572 853 --TSVDVEEHLYRLAtSMGITVITSS 876
Cdd:cd03230 128 peSRREFWELLRELK-KEGKTILLSS 152
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
48-193 |
4.89e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 57.72 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 48 DLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLN-----KEIFYVPQRpytaVGTLREQL-IYP 121
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSktpsdKAIRELRRN----VGMVFQQYnLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 122 -LTADQG-IE-PLTYDGMVD---------LLKNVDLEYLLERYPLdkevnwgdELSLGEQQRLGMARLFYHKPKFAILDE 189
Cdd:PRK11124 96 hLTVQQNlIEaPCRVLGLSKdqalaraekLLERLRLKPYADRFPL--------HLSGGQQQRVAIARALMMEPQVLLFDE 167
|
....
gi 1142837572 190 CTSA 193
Cdd:PRK11124 168 PTAA 171
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
45-224 |
5.87e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.75 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 45 LVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLNKEIFYVPQ-RPYTAVGTLREQL-IYPL 122
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiKLRKEVGMVFQQPnPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 123 TA--DQGIEPLTYDGMVDL--LKNVdLEYLLERYPLDKEV-----NWGDELSLGEQQRLGMARLFYHKPKFAILDECTSA 193
Cdd:PRK14246 105 LSiyDNIAYPLKSHGIKEKreIKKI-VEECLRKVGLWKEVydrlnSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190
....*....|....*....|....*....|....*
gi 1142837572 194 V----TTDMEERFCKKVRAMgtSCITISHRPALVA 224
Cdd:PRK14246 184 IdivnSQAIEKLITELKNEI--AIVIVSHNPQQVA 216
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
706-858 |
9.92e-09 |
|
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: 56.85 E-value: 9.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 706 GKSLLLTGPNGSGKSSIFRVLRDLWPTFSGR----------VTKPS--EGMFHVPQRPYTSLGTLRDQIIYplSREEAKi 773
Cdd:cd03254 29 GETVAIVGPTGAGKTTLINLLMRFYDPQKGQilidgidirdISRKSlrSMIGVVLQDTFLFSGTIMENIRL--GRPNAT- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 774 kvlslhrsgnnssasmllDDHLKTILENVRLVYLLER--EGWDSTPNWE-DVLSLGEQQRLGMARLFFHHPKFGILDECT 850
Cdd:cd03254 106 ------------------DEEVIEAAKEAGAHDFIMKlpNGYDTVLGENgGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
....*...
gi 1142837572 851 naTSVDVE 858
Cdd:cd03254 168 --SNIDTE 173
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
12-232 |
1.21e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.58 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 12 DRSLDHSSPGNYVSEANHIEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG 91
Cdd:PRK10790 323 DGPRQQYGNDDRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 92 ------VGSDLNKEIFYVPQRPYTAVGTLREQLIypLTADqgiepLTYDGMVDLLKNVDLEYLLERYP------LDKEvn 159
Cdd:PRK10790 403 rplsslSHSVLRQGVAMVQQDPVVLADTFLANVT--LGRD-----ISEEQVWQALETVQLAELARSLPdglytpLGEQ-- 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142837572 160 wGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRPALVAFHDIVLSL 232
Cdd:PRK10790 474 -GNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLSTIVEADTILVL 547
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-219 |
1.33e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.30 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 26 EANHI--EFSDVKVVtpagnvlvDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWP--------------LVSGHIV- 88
Cdd:TIGR02633 3 EMKGIvkTFGGVKAL--------DGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtwdgeiywsgspLKASNIRd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 89 --KPGVgSDLNKEIFYVPQRpytavgTLREQLI--YPLTADQGIepLTYDGMVDLLKNVDLEYLLERYPLDKEVNwgdEL 164
Cdd:TIGR02633 75 teRAGI-VIIHQELTLVPEL------SVAENIFlgNEITLPGGR--MAYNAMYLRAKNLLRELQLDADNVTRPVG---DY 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 165 SLGEQQRLGMARLFYHKPKFAILDECTSAVT---TDMEERFCKKVRAMGTSCITISHR 219
Cdd:TIGR02633 143 GGGQQQLVEIAKALNKQARLLILDEPSSSLTekeTEILLDIIRDLKAHGVACVYISHK 200
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
30-191 |
1.52e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 54.38 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVvTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlNKEIFYVPQrpyt 109
Cdd:cd03221 1 IELENLSK-TYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----TVKIGYFEQ---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 110 avgtlreqliypltadqgiepltydgmvdllknvdleyllerypldkevnwgdeLSLGEQQRLGMARLFYHKPKFAILDE 189
Cdd:cd03221 71 ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
..
gi 1142837572 190 CT 191
Cdd:cd03221 97 PT 98
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
692-883 |
1.59e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 692 QKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLwptfsgRVTKPSEGMFHVPQRPYTSLGTLRDQIiypLSREEA 771
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA------LKGTPVAGCVDVPDNQFGREASLIDAI---GRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 772 KIKVLSLHRSGNNSSASMLlddhlktilenvRLVylleregwdstpnweDVLSLGEQQRLGMARLFFHHPKFGILDECTN 851
Cdd:COG2401 113 KDAVELLNAVGLSDAVLWL------------RRF---------------KELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1142837572 852 A----TSVDVEEHLYRLATSMGITVITSSQRP----ALIP 883
Cdd:COG2401 166 HldrqTAKRVARNLQKLARRAGITLVVATHHYdvidDLQP 205
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
706-874 |
2.04e-08 |
|
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: 55.94 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 706 GKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT---KPSEGMFH---------VPQRPYTSLGTLRDQIIYPL---SREE 770
Cdd:cd03248 40 GEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPISQYEHkylhskvslVGQEPVLFARSLQDNIAYGLqscSFEC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 771 AKIKVLSLHRSGNNSsasmllddhlktilenvrlvyLLEREGWDSTPNWEDVLSLGEQQRLGMARLFFHHPKFGILDECT 850
Cdd:cd03248 120 VKEAAQKAHAHSFIS---------------------ELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180
....*....|....*....|....*...
gi 1142837572 851 NATSVD----VEEHLYRLATSMGITVIT 874
Cdd:cd03248 179 SALDAEseqqVQQALYDWPERRTVLVIA 206
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
41-225 |
2.63e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 54.84 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 41 AGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGL--WPLVSGHIvkpgvgsdlnkeifyvpqrpytavgTLREQL 118
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEI-------------------------LFKGED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 119 IYPLTADQ----GI-----EPLTYDGmvdlLKNVDleYLleRYpldkeVNWGdeLSLGEQQRLGMARLFYHKPKFAILDE 189
Cdd:cd03217 66 ITDLPPEErarlGIflafqYPPEIPG----VKNAD--FL--RY-----VNEG--FSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190
....*....|....*....|....*....|....*....
gi 1142837572 190 CTSAVTTD---MEERFCKKVRAMGTSCITISHRPALVAF 225
Cdd:cd03217 131 PDSGLDIDalrLVAEVINKLREEGKSVLIITHYQRLLDY 169
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
46-230 |
2.65e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.28 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGS------DLNKEIFYVPQRPYTA-VG-TLREQ 117
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteenvwDIRHKIGMVFQNPDNQfVGaTVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 118 LIYPLtADQGIEpltYDGMVD----LLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSA 193
Cdd:PRK13650 103 VAFGL-ENKGIP---HEEMKErvneALELVGMQDFKEREP--------ARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1142837572 194 VttDMEERF-----CKKVR-AMGTSCITISHRPALVAFHDIVL 230
Cdd:PRK13650 171 L--DPEGRLeliktIKGIRdDYQMTVISITHDLDEVALSDRVL 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
690-882 |
2.98e-08 |
|
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: 57.54 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 690 PSQKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVtkpsegMF-HVPQRPYtSLGTLRDQIIYplsr 768
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI------LIdGIDLRQI-DPASLRRQIGV---- 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 769 eeakikVLSlhrsgnnssasmllDDHL--KTILENVRLvylleregWDSTPNWEDV------------------------ 822
Cdd:COG2274 554 ------VLQ--------------DVFLfsGTIRENITL--------GDPDATDEEIieaarlaglhdfiealpmgydtvv 605
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 823 ------LSLGEQQRLGMARLFFHHPKFGILDECTNATSVDVEEHLYR--LATSMGITVITSSQRPALI 882
Cdd:COG2274 606 geggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEnlRRLLKGRTVIIIAHRLSTI 673
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
46-189 |
3.25e-08 |
|
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: 55.37 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNKE---------IFYVPQrpytavG---- 112
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGE--DITGLpphriarlgIGYVPE------Grrif 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 113 ---TLREQLI---YPLTADQGIEPltydgmvdllknvDLEYLLERYPLDKEV--NWGDELSLGEQQRLGMARLFYHKPKF 184
Cdd:COG0410 91 pslTVEENLLlgaYARRDRAEVRA-------------DLERVYELFPRLKERrrQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
....*
gi 1142837572 185 AILDE 189
Cdd:COG0410 158 LLLDE 162
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
38-212 |
3.43e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.61 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 38 VTPagnvLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlnkEIFYVPQRPYTAVGTLREQ 117
Cdd:TIGR01271 438 VTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 118 LIYPLTADQgiepLTYDGMVdllKNVDLEYLLERYPLDKEVNWGD---ELSLGEQQRLGMARLFYHKPKFAILDECTSA- 193
Cdd:TIGR01271 507 IIFGLSYDE----YRYTSVI---KACQLEEDIALFPEKDKTVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFTHl 579
|
170 180
....*....|....*....|....*..
gi 1142837572 194 -VTTDME--ER-FCK----KVRAMGTS 212
Cdd:TIGR01271 580 dVVTEKEifEScLCKlmsnKTRILVTS 606
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-194 |
3.51e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 32 FS-DVKVVTPAgnvlVDDLTLRVETGSNLLITGPNGSGKSSLFR-VLGGLWPLVSGHIVKPGvgsdlnkEIFYVPQRPYT 109
Cdd:PLN03232 622 FSwDSKTSKPT----LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-------SVAYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 110 AVGTLREQLIY-----PLTADQGIEPLTYDGMVDLLKNVDLEYLLERypldkevnwGDELSLGEQQRLGMARLFYHKPKF 184
Cdd:PLN03232 691 FNATVRENILFgsdfeSERYWRAIDVTALQHDLDLLPGRDLTEIGER---------GVNISGGQKQRVSMARAVYSNSDI 761
|
170
....*....|
gi 1142837572 185 AILDECTSAV 194
Cdd:PLN03232 762 YIFDDPLSAL 771
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
680-886 |
3.69e-08 |
|
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: 55.03 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 680 ISFHEVDIVTPSQKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT---------KPSE-----GMf 745
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdgkditkkNLRElrrkvGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 746 hVPQRPytslgtlRDQIIYP--------------LSREEAKIKVlslhrsgnnssasmllddhlKTILENVRLVYLLERE 811
Cdd:COG1122 80 -VFQNP-------DDQLFAPtveedvafgpenlgLPREEIRERV--------------------EEALELVGLEHLADRP 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1142837572 812 gwdstPNwedVLSLGEQQRLGMARLFFHHPKFGILDECTN----ATSVDVEEHLYRLATSmGITVITSSQRPALIPFHA 886
Cdd:COG1122 132 -----PH---ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAgldpRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELA 201
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
30-231 |
3.80e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 56.77 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVkVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGG-LWP-----LVSGHIVKPGVGSDLNKEIFYV 103
Cdd:PRK09536 4 IDVSDL-SVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGtLTPtagtvLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 104 PQRPYTAVGTLREQLIypltaDQGIEPLT--YDGMVDLLKNVdLEYLLERYPLDKEVNWG-DELSLGEQQRLGMARLFYH 180
Cdd:PRK09536 83 PQDTSLSFEFDVRQVV-----EMGRTPHRsrFDTWTETDRAA-VERAMERTGVAQFADRPvTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1142837572 181 KPKFAILDECTSAVTTDMEERFCKKVRAMGTscitiSHRPALVAFHDIVLS 231
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVD-----DGKTAVAAIHDLDLA 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
42-189 |
5.16e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 56.61 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlNKEIFYVPQRPYTAVG-TLREQLiy 120
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----GLRIGYLPQEPPLDDDlTVLDTV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 121 pLTADQG----------IEPLTYDGMVDLLKNVDLEYLLERY---------------------PLDKEVNwgdELSLGEQ 169
Cdd:COG0488 83 -LDGDAElraleaeleeLEAKLAEPDEDLERLAELQEEFEALggweaearaeeilsglgfpeeDLDRPVS---ELSGGWR 158
|
170 180
....*....|....*....|
gi 1142837572 170 QRLGMARLFYHKPKFAILDE 189
Cdd:COG0488 159 RRVALARALLSEPDLLLLDE 178
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
47-222 |
5.61e-08 |
|
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: 54.57 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 47 DDLTLRVETGSNLLITGPNGSGKSSLFRVLGG--LWPLVSGHI-VKpgvGSDLN---------KEIFYVPQRPYTAVG-T 113
Cdd:TIGR01978 17 KGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTIlFK---GQDLLelepderarAGLFLAFQYPEEIPGvS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 114 LREQLIYPLTA---DQGIEPLTYDGMVDLLK-NVDL----EYLLERYpldkeVNWGdeLSLGEQQR---LGMARLfyhKP 182
Cdd:TIGR01978 94 NLEFLRSALNArrsARGEEPLDLLDFEKLLKeKLALldmdEEFLNRS-----VNEG--FSGGEKKRneiLQMALL---EP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1142837572 183 KFAILDECTSAVTTDMEERFCK---KVRAMGTSCITISHRPAL 222
Cdd:TIGR01978 164 KLAILDEIDSGLDIDALKIVAEginRLREPDRSFLIITHYQRL 206
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
47-219 |
5.75e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 47 DDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKpgvgsdLNKEI-FYVPQRPYTA-VGTLREQL--IYPL 122
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILY------LGKEVtFNGPKSSQEAgIGIIHQELnlIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 123 TADQGI----EPLTYDGMVD----------LLKNVDLeylleRYPLDKEVNwgdELSLGEQQRLGMARLFYHKPKFAILD 188
Cdd:PRK10762 95 TIAENIflgrEFVNRFGRIDwkkmyaeadkLLARLNL-----RFSSDKLVG---ELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190
....*....|....*....|....*....|....
gi 1142837572 189 ECTSAVT-TDMEERF--CKKVRAMGTSCITISHR 219
Cdd:PRK10762 167 EPTDALTdTETESLFrvIRELKSQGRGIVYISHR 200
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
26-193 |
6.16e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.78 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 26 EANHIEFSDvkvvtpAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIvkpgvgsDLNkeifyvpQ 105
Cdd:PRK13548 4 EARNLSVRL------GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV-------RLN-------G 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 106 RPYT-----------AVgtLREQ--LIYPLTADQ----GIEPLTY-----DGMVD-LLKNVDLEYLLER-YPldkevnwg 161
Cdd:PRK13548 64 RPLAdwspaelarrrAV--LPQHssLSFPFTVEEvvamGRAPHGLsraedDALVAaALAQVDLAHLAGRdYP-------- 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 1142837572 162 dELSLGEQQRLGMARLF------YHKPKFAILDECTSA 193
Cdd:PRK13548 134 -QLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSA 170
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
692-875 |
7.33e-08 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 54.66 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 692 QKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT---------KPSE-----GMfhVPQRPYTSLG- 756
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlaslSRRElarriAY--VPQEPPAPFGl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 757 TLRDQII---YPlsreeakikvlslHRSGNNSSASmllDDHLK--TILENVRLVYLLEREgWDStpnwedvLSLGEQQRL 831
Cdd:COG1120 91 TVRELVAlgrYP-------------HLGLFGRPSA---EDREAveEALERTGLEHLADRP-VDE-------LSGGERQRV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1142837572 832 GMARLFFHHPKFGILDECTNA----TSVDVEEHLYRLATSMGITVITS 875
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHldlaHQLEVLELLRRLARERGRTVVMV 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
47-219 |
7.55e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.80 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 47 DDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV---KP------------GVGsdlnkeifYVPQRPytav 111
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILidgKPvrirsprdaialGIG--------MVHQHF---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 112 gtlreQLIYPLTADQ----GIEPLTYdGMVDLLK-NVDLEYLLERYPL----DKEVnwgDELSLGEQQRLGMARLFYHKP 182
Cdd:COG3845 90 -----MLVPNLTVAEnivlGLEPTKG-GRLDRKAaRARIRELSERYGLdvdpDAKV---EDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1142837572 183 KFAILDECTsAVTTDME-ERF---CKKVRAMGTSCITISHR 219
Cdd:COG3845 161 RILILDEPT-AVLTPQEaDELfeiLRRLAAEGKSIIFITHK 200
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
680-878 |
8.31e-08 |
|
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: 54.03 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 680 ISFHEVDI-VTPSQKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKPSEGMFHVpqrpytSLGTL 758
Cdd:cd03252 1 ITFEHVRFrYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA------DPAWL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 759 RDQIIYPLSREeakikvLSLHRSGNNSSASMLLDDHLKTILENVRLV----YLLE-REGWDSTPNWEDV-LSLGEQQRLG 832
Cdd:cd03252 75 RRQVGVVLQEN------VLFNRSIRDNIALADPGMSMERVIEAAKLAgahdFISElPEGYDTIVGEQGAgLSGGQRQRIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1142837572 833 MARLFFHHPKFGILDECTNATSVDVEEHLYR--LATSMGITVITSSQR 878
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRnmHDICAGRTVIIIAHR 196
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
699-876 |
8.57e-08 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 53.91 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 699 LSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT--------KPSEGMFH---VPQRP--YTSLgTLRDQI--- 762
Cdd:COG1131 19 VSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvarDPAEVRRRigyVPQEPalYPDL-TVRENLrff 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 763 --IYPLSREEAKIKVLS-LHRSGnnssasmlLDDHLKTILENvrlvylleregwdstpnwedvLSLGEQQRLGMARLFFH 839
Cdd:COG1131 98 arLYGLPRKEARERIDElLELFG--------LTDAADRKVGT---------------------LSGGMKQRLGLALALLH 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1142837572 840 HPKFGILDECTNAtsVDVE------EHLYRLATSmGITVITSS 876
Cdd:COG1131 149 DPELLILDEPTSG--LDPEarrelwELLRELAAE-GKTVLLST 188
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
42-189 |
9.15e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.13 E-value: 9.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDL-------NKEIFYVPQRP------- 107
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlplharaRRGIGYLPQEAsifrrls 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 108 ----YTAVGTLREQLIYPLTADQGIEpltydgmvdLLKNVDLEYLLErypldkevNWGDELSLGEQQRLGMARLFYHKPK 183
Cdd:PRK10895 95 vydnLMAVLQIRDDLSAEQREDRANE---------LMEEFHIEHLRD--------SMGQSLSGGERRRVEIARALAANPK 157
|
....*.
gi 1142837572 184 FAILDE 189
Cdd:PRK10895 158 FILLDE 163
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
47-239 |
1.10e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 53.95 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 47 DDLTLRVETGS-----NLLITGPNGSGKSSLFRVLGGLwplvsghiVKPGVG---SDLNKeIFYVPQR---PYTavGTLR 115
Cdd:cd03237 11 GEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGV--------LKPDEGdieIELDT-VSYKPQYikaDYE--GTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 116 eQLIYPLTADQGIEPLTydgMVDLLKNVDLEYLLERypldkEVNwgdELSLGEQQRLGMARLFYHKPKFAILDEcTSAvT 195
Cdd:cd03237 80 -DLLSSITKDFYTHPYF---KTEIAKPLQIEQILDR-----EVP---ELSGGELQRVAIAACLSKDADIYLLDE-PSA-Y 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142837572 196 TDMEERFckkvraMGTSCIT--ISH--RPALVAFHDI---------VLSLDGEGGWN 239
Cdd:cd03237 146 LDVEQRL------MASKVIRrfAENneKTAFVVEHDIimidyladrLIVFEGEPSVN 196
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
39-192 |
1.38e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.90 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 39 TPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG--------SDLNKEIFYVPQRP-YT 109
Cdd:PRK13637 16 TPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitdkkvklSDIRKKVGLVFQYPeYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 110 avgtLREQLIYPLTA---------DQGIEPLTYDGMvdllKNVDLEY--LLERYPLdkevnwgdELSLGEQQRLGMARLF 178
Cdd:PRK13637 96 ----LFEETIEKDIAfgpinlglsEEEIENRVKRAM----NIVGLDYedYKDKSPF--------ELSGGQKRRVAIAGVV 159
|
170
....*....|....
gi 1142837572 179 YHKPKFAILDECTS 192
Cdd:PRK13637 160 AMEPKILILDEPTA 173
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-188 |
1.64e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 53.71 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 21 GNYVSEANHIEFSDVKVVtpaGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFR-VLGGLWPlVSGHIVKPGvgsdlnkE 99
Cdd:cd03291 31 RKHSSDDNNLFFSNLCLV---GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEP-SEGKIKHSG-------R 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 100 IFYVPQRPYTAVGTLREQLIYPLTADQgiepLTYDGMVdllKNVDLEYLLERYP-LDKEV--NWGDELSLGEQQRLGMAR 176
Cdd:cd03291 100 ISFSSQFSWIMPGTIKENIIFGVSYDE----YRYKSVV---KACQLEEDITKFPeKDNTVlgEGGITLSGGQRARISLAR 172
|
170
....*....|..
gi 1142837572 177 LFYHKPKFAILD 188
Cdd:cd03291 173 AVYKDADLYLLD 184
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
29-233 |
2.43e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.58 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 29 HIEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFY 102
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDirtvtrASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 103 VPQRPYTAVGTLREQLIYpltadqGIEPLTYDGMVDLLKNVDLEYLLERYPLDKEVNWGD---ELSLGEQQRLGMARLFY 179
Cdd:PRK13657 414 VFQDAGLFNRSIEDNIRV------GRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGErgrQLSGGERQRLAIARALL 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142837572 180 HKPKFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRPALVAFHDIVLSLD 233
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELmkGRTTFIIAHRLSTVRNADRILVFD 543
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
702-873 |
2.92e-07 |
|
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: 52.11 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 702 DVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRV-------TKPSE-----------GMfhVPQRpYTSLGTL--RDQ 761
Cdd:cd03255 26 SIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdiSKLSEkelaafrrrhiGF--VFQS-FNLLPDLtaLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 762 IIYPL-----SREEAKIKVLSLhrsgnnssasmllddhlktiLENVRLVYLLERegwdsTPNWedvLSLGEQQRLGMARL 836
Cdd:cd03255 103 VELPLllagvPKKERRERAEEL--------------------LERVGLGDRLNH-----YPSE---LSGGQQQRVAIARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1142837572 837 FFHHPKFGILDECTNA----TSVDVEEHLYRLATSMGITVI 873
Cdd:cd03255 155 LANDPKIILADEPTGNldseTGKEVMELLRELNKEAGTTIV 195
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
46-218 |
3.22e-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: 52.73 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI---------------VKPGVG---------SDL----N 97
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlfdgrditglpphriARLGIArtfqnprlfPELtvleN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 98 keiFYVPQRPYTAVGTLREQLIYPLTADQgiEPLTYDGMVDLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARL 177
Cdd:COG0411 100 ---VLVAAHARLGRGLLAALLRLPRARRE--EREARERAEELLERVGLADRADEPA--------GNLSYGQQRRLEIARA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1142837572 178 FYHKPKFAILDECTSAVTTDMEERFC---KKVRA-MGTSCITISH 218
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPEETEELAeliRRLRDeRGITILLIEH 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
46-218 |
3.50e-07 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 54.04 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHiVKPGVGS---DLNKEIFYVPQRPYTAVGTLREQL-IYP 121
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE-VNVRVGDewvDMTKPGPDGRGRAKRYIGILHQEYdLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 122 -------LTADQGIE-PLTYDGM--VDLLKNVDL-----EYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAI 186
Cdd:TIGR03269 379 hrtvldnLTEAIGLElPDELARMkaVITLKMVGFdeekaEEILDKYP--------DELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190
....*....|....*....|....*....|....*.
gi 1142837572 187 LDECTSAV----TTDMEERFCKKVRAMGTSCITISH 218
Cdd:TIGR03269 451 LDEPTGTMdpitKVDVTHSILKAREEMEQTFIIVSH 486
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
30-192 |
3.52e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 52.69 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKV-VTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNKE--------- 99
Cdd:PRK13632 8 IKVENVSFsYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI--TISKEnlkeirkki 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 100 --IFYVPQRPYT--------AVGtLREQLIYPLTADQGIEpltydgmvDLLKNVDLEYLLERYPLdkevnwgdELSLGEQ 169
Cdd:PRK13632 86 giIFQNPDNQFIgatveddiAFG-LENKKVPPKKMKDIID--------DLAKKVGMEDYLDKEPQ--------NLSGGQK 148
|
170 180
....*....|....*....|...
gi 1142837572 170 QRLGMARLFYHKPKFAILDECTS 192
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTS 171
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
49-194 |
4.10e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.18 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 49 LTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlnkEIFYVPQRPYTAVGTLREQLIYpltaDQGI 128
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------SVAYVPQQAWIQNDSLRENILF----GKAL 725
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142837572 129 EPLTYDGMVD---LLKnvDLEYLleryPLDKEVNWGDE---LSLGEQQRLGMARLFYHKPKFAILDECTSAV 194
Cdd:TIGR00957 726 NEKYYQQVLEacaLLP--DLEIL----PSGDRTEIGEKgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
45-219 |
4.37e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.49 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 45 LVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV--KPGVGSDL---NKEIFYVPQR----PYTavgTLR 115
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILfeRQSIKKDLctyQKQLCFVGHRsginPYL---TLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 116 EQLIYPLTADQGiePLTYDGMVDLLKnvdLEYLLErYPLDKevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSAVT 195
Cdd:PRK13540 93 ENCLYDIHFSPG--AVGITELCRLFS---LEHLID-YPCGL-------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180
....*....|....*....|....*..
gi 1142837572 196 TDMEERFCKKV---RAMGTSCITISHR 219
Cdd:PRK13540 160 ELSLLTIITKIqehRAKGGAVLLTSHQ 186
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
46-218 |
4.39e-07 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 51.95 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLNKEIFyvpQRPYTAVGTLREQLIYPLTAD 125
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF---LRRIGVVFGQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 126 QG---------IEPLTY----DGMVDLLknvDLEYLlerypLDKEVNwgdELSLGEQQRLGMARLFYHKPKFAILDECT- 191
Cdd:cd03267 114 DSfyllaaiydLPPARFkkrlDELSELL---DLEEL-----LDTPVR---QLSLGQRMRAEIAAALLHEPEILFLDEPTi 182
|
170 180 190
....*....|....*....|....*....|
gi 1142837572 192 --SAVTTDMEERFCKK-VRAMGTSCITISH 218
Cdd:cd03267 183 glDVVAQENIRNFLKEyNRERGTTVLLTSH 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
697-882 |
4.83e-07 |
|
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: 51.31 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 697 RKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKPSEGMFHVPQRPYTSL-GTL----RDQIIYP------ 765
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLVfqnpDDQFFGPtveeev 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 766 --------LSREEAKIKVlslhrsgnNSSASMLLDDHLKTilenvRLVYLleregwdstpnwedvLSLGEQQRLGMARLF 837
Cdd:cd03225 98 afglenlgLPEEEIEERV--------EEALELVGLEGLRD-----RSPFT---------------LSGGQKQRVAIAGVL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1142837572 838 FHHPKFGILDECTN----ATSVDVEEHLYRLAtSMGITVITSSQRPALI 882
Cdd:cd03225 150 AMDPDILLLDEPTAgldpAGRRELLELLKKLK-AEGKTIIIVTHDLDLL 197
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
46-218 |
5.23e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.11 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNK----EIFYVPQRPYTAVGTLREQLIYP 121
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV--DIAKisdaELREVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 122 LTADQGIEPLTYDGM---------VDLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTS 192
Cdd:PRK10070 122 TVLDNTAFGMELAGInaeerrekaLDALRQVGLENYAHSYP--------DELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190
....*....|....*....|....*....|
gi 1142837572 193 A----VTTDMEERFCKKVRAMGTSCITISH 218
Cdd:PRK10070 194 AldplIRTEMQDELVKLQAKHQRTIVFISH 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-219 |
5.47e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.10 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 26 EANHI--EFSDVKVVtpagnvlvDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGSD-L 96
Cdd:COG1129 6 EMRGIskSFGGVKAL--------DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIlldgepVRFRSPRDaQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 97 NKEIFYVPQrpytavgtlrEQLIYP-LTADQ----GIEPLTYdGMVD----------LLKNVDLEYlleryPLDKEVnwg 161
Cdd:COG1129 78 AAGIAIIHQ----------ELNLVPnLSVAEniflGREPRRG-GLIDwramrrrareLLARLGLDI-----DPDTPV--- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142837572 162 DELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERF---CKKVRAMGTSCITISHR 219
Cdd:COG1129 139 GDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLfriIRRLKAQGVAIIYISHR 199
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
697-873 |
6.64e-07 |
|
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: 51.28 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 697 RKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT--------KPSE-----GMFHVPQrpytslgtlRDQII 763
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfdgrditgLPPHeraraGIGYVPE---------GRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 764 YPLSREEakikvlslhrsgnN--SSASMLLDDHLKTILENV-----RLVYLLEREGwdstpnweDVLSLGEQQRLGMARL 836
Cdd:cd03224 88 PELTVEE-------------NllLGAYARRRAKRKARLERVyelfpRLKERRKQLA--------GTLSGGEQQMLAIARA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1142837572 837 FFHHPKFGILDECTNATS---VD-VEEHLYRLAtSMGITVI 873
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLApkiVEeIFEAIRELR-DEGVTIL 186
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
16-216 |
8.11e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.14 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 16 DHSSPGNYVSEAnhIEFSDVKVvTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV-----KP 90
Cdd:PRK13536 30 KASIPGSMSTVA--IDLAGVSK-SYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpVP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 91 GVGSDLNKEIFYVPQ-----RPYTAvgtlREQLI-YPltadqgieplTYDGMVDLLKNVDLEYLLERYPLDKEVNWG-DE 163
Cdd:PRK13536 107 ARARLARARIGVVPQfdnldLEFTV----RENLLvFG----------RYFGMSTREIEAVIPSLLEFARLESKADARvSD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1142837572 164 LSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCKKVRAMGTSCITI 216
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTI 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
30-218 |
8.14e-07 |
|
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: 50.96 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVkVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG--VGSDLNKEIFYVPQRp 107
Cdd:cd03261 1 IELRGL-TKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedISGLSEAELYRLRRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 108 ytaVG------------TLREQLIYPLTADQGIEPLTYDGMVDL-LKNVDLEYLLERYPldkevnwgDELSLGEQQRLGM 174
Cdd:cd03261 79 ---MGmlfqsgalfdslTVFENVAFPLREHTRLSEEEIREIVLEkLEAVGLRGAEDLYP--------AELSGGMKKRVAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1142837572 175 AR--------LFYHKPkFAILDECTSAVTTDMeERFCKKvrAMGTSCITISH 218
Cdd:cd03261 148 ARalaldpelLLYDEP-TAGLDPIASGVIDDL-IRSLKK--ELGLTSIMVTH 195
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
30-233 |
1.13e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 51.14 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGS-------DLNKEIFY 102
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfsklqGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 103 VPQRPYTA-VG-TLREQLIYPlTADQGIEPLTYDGMVDL-LKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFY 179
Cdd:PRK13644 82 VFQNPETQfVGrTVEEDLAFG-PENLCLPPIEIRKRVDRaLAEIGLEKYRHRSP--------KTLSGGQGQCVALAGILT 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142837572 180 HKPKFAILDECTSAVTTDMEE---RFCKKVRAMGTSCITISHRPALVAFHDIVLSLD 233
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIavlERIKKLHEKGKTIVYITHNLEELHDADRIIVMD 209
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
28-233 |
1.33e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 50.95 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 28 NHIEFSDVKVVTPAGNV-LVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGG-LWP--------LVSGHIVKPGVGSDLN 97
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPddnpnskiTVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 98 KEIFYVPQRPYTA-VG-TLREQLIYPLTADQGIEPLTYDGMVDLLKNVDLEYLLERYPLDkevnwgdeLSLGEQQRLGMA 175
Cdd:PRK13640 84 EKVGIVFQNPDNQfVGaTVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPAN--------LSGGQKQRVAIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142837572 176 RLFYHKPKFAILDECTSAVTTDMEERFCKKVRAM----GTSCITISHRPALVAFHDIVLSLD 233
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITHDIDEANMADQVLVLD 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
697-878 |
2.04e-06 |
|
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: 49.59 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 697 RKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDlwptfsgrVTKPSEGMFHVPQRPYTSLG-----------------TLR 759
Cdd:cd03269 17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILG--------IILPDSGEVLFDGKPLDIAArnrigylpeerglypkmKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 760 DQIIY-----PLSREEAKIKVLS-LHRSGnnssasmlLDDHlktilENVRLvylleregwdstpnweDVLSLGEQQRLGM 833
Cdd:cd03269 89 DQLVYlaqlkGLKKEEARRRIDEwLERLE--------LSEY-----ANKRV----------------EELSKGNQQKVQF 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1142837572 834 ARLFFHHPKFGILDECTNA---TSVDVEEHLYRLATSMGITVITSSQR 878
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGldpVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
693-891 |
2.14e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.42 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 693 KLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLwptfsgrvTKPSEGMFHVPQRPytslgtLRDQiiyplsREEAK 772
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGL--------ARPDAGEVLWQGEP------IRRQ------RDEYH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 773 IKVLSL-HRSGnnssasmlLDDHLkTILENVR-------------LVYLLEREGWDSTpnwEDV----LSLGEQQRLGMA 834
Cdd:PRK13538 74 QDLLYLgHQPG--------IKTEL-TALENLRfyqrlhgpgddeaLWEALAQVGLAGF---EDVpvrqLSAGQQRRVALA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142837572 835 RLFFHHPKFGILDECTNA---TSVDV-EEHLYRLATSMGITVITSSQRPALIPFHALELKL 891
Cdd:PRK13538 142 RLWLTRAPLWILDEPFTAidkQGVARlEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRL 202
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
29-197 |
2.19e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 50.85 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 29 HIEFSDVKVV--TPAGNVL-VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV------GSDLNKE 99
Cdd:COG1135 1 MIELENLSKTfpTKGGPVTaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltalsERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 100 ------IFyvpqrpytavgtlreQ---LIYPLTADQGIE-PLTYDGM--------VD-LLKNVDLEYLLERYPldkevnw 160
Cdd:COG1135 81 rrkigmIF---------------QhfnLLSSRTVAENVAlPLEIAGVpkaeirkrVAeLLELVGLSDKADAYP------- 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1142837572 161 gDELSLGEQQRLGMARLFYHKPKfaIL--DECTSAV---TTD 197
Cdd:COG1135 139 -SQLSGGQKQRVGIARALANNPK--VLlcDEATSALdpeTTR 177
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
42-191 |
2.39e-06 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 49.68 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWP------LVSGH-IVKPgvGSDLNKEIFYVPQRPYTAVG-T 113
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKptsgraTVAGHdVVRE--PREVRRRIGIVFQDLSVDDElT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 114 LREQL-----IYPL---TADQGIEpltydgmvDLLKNVDLeyllerypLDKEvnwgDEL----SLGEQQRLGMARLFYHK 181
Cdd:cd03265 90 GWENLyiharLYGVpgaERRERID--------ELLDFVGL--------LEAA----DRLvktySGGMRRRLEIARSLVHR 149
|
170
....*....|
gi 1142837572 182 PKFAILDECT 191
Cdd:cd03265 150 PEVLFLDEPT 159
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
46-223 |
2.72e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.01 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSD---------LNKEIFYVPQRPYTAVGTlRE 116
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspgklqaLRRDIQFIFQDPYASLDP-RQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 117 QLIYPLtadqgIEPLTYDGMVD---LLKNVdlEYLLERYPLDKEVNW--GDELSLGEQQRLGMARLFYHKPKFAILDECT 191
Cdd:PRK10261 419 TVGDSI-----MEPLRVHGLLPgkaAAARV--AWLLERVGLLPEHAWryPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190
....*....|....*....|....*....|....*.
gi 1142837572 192 SAVTTDMEERFCKKV----RAMGTSCITISHRPALV 223
Cdd:PRK10261 492 SALDVSIRGQIINLLldlqRDFGIAYLFISHDMAVV 527
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
48-193 |
2.85e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.28 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 48 DLTLRVETGSNLLITGPNGSGKSSLFR-VLGGLWPLVSGHIVKPGvgsdlnkEIFYVPQRPYTAVGTLREQLIYPLTAD- 125
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-------TVAYVPQVSWIFNATVRDNILFGSPFDp 707
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142837572 126 ----QGIEPLTYDGMVDLLKNVDLEYLLERypldkevnwGDELSLGEQQRLGMARLFYHKPKFAILDECTSA 193
Cdd:PLN03130 708 eryeRAIDVTALQHDLDLLPGGDLTEIGER---------GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
42-191 |
3.06e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.43 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVD---DLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG---------VGSDL-NKEIFYVPQ--- 105
Cdd:PRK11629 18 GSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaAKAELrNQKLGFIYQfhh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 106 --RPYTAVgtlrEQLIYPLTADQGIEPLTYDGMVDLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPK 183
Cdd:PRK11629 98 llPDFTAL----ENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRP--------SELSGGERQRVAIARALVNNPR 165
|
....*...
gi 1142837572 184 FAILDECT 191
Cdd:PRK11629 166 LVLADEPT 173
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
711-874 |
3.75e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.14 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 711 LTGPNGSGKSSIFRVLR---DLWPT--FSGRVTKPSEGMFHVPqrpyTSLGTLRDQIIYPLSREEAKIKV-------LSL 778
Cdd:PRK14247 34 LMGPSGSGKSTLLRVFNrliELYPEarVSGEVYLDGQDIFKMD----VIELRRRVQMVFQIPNPIPNLSIfenvalgLKL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 779 HRSGNNSSAsmlLDDHLKTILENVRLvylleregWDSTPNWEDV----LSLGEQQRLGMARLFFHHPKFGILDECTN--- 851
Cdd:PRK14247 110 NRLVKSKKE---LQERVRWALEKAQL--------WDEVKDRLDApagkLSGGQQQRLCIARALAFQPEVLLADEPTAnld 178
|
170 180
....*....|....*....|....
gi 1142837572 852 -ATSVDVEEHLYRLATSMGITVIT 874
Cdd:PRK14247 179 pENTAKIESLFLELKKDMTIVLVT 202
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
39-192 |
3.76e-06 |
|
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: 51.06 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 39 TPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLfrvLGGLWPLVS--GHIVKPGVGSD------LNKEIFYVPQRPYTA 110
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTL---LSALLRLLSteGEIQIDGVSWNsvtlqtWRKAFGVIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 111 VGTLREQL-IYPLTADQGIEPLTydgmvdllKNVDLEYLLERYP--LDKE-VNWGDELSLGEQQRLGMARLFYHKPKFAI 186
Cdd:TIGR01271 1305 SGTFRKNLdPYEQWSDEEIWKVA--------EEVGLKSVIEQFPdkLDFVlVDGGYVLSNGHKQLMCLARSILSKAKILL 1376
|
....*.
gi 1142837572 187 LDECTS 192
Cdd:TIGR01271 1377 LDEPSA 1382
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
672-881 |
4.61e-06 |
|
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: 48.77 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 672 ISAASKETISFHEVDivtpsqkllarKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKPSEGMFHVP--Q 749
Cdd:cd03300 3 LENVSKFYGGFVALD-----------GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPphK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 750 RPYTSLG---------TLRDQIIYPLSREEAKIKVLSlhrsgnnssasmllddhlKTILENVRLVYLLEREGWDStpnwe 820
Cdd:cd03300 72 RPVNTVFqnyalfphlTVFENIAFGLRLKKLPKAEIK------------------ERVAEALDLVQLEGYANRKP----- 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142837572 821 DVLSLGEQQRLGMARLFFHHPKFGILDECTNATSVDVEEH----LYRLATSMGITVI--TSSQRPAL 881
Cdd:cd03300 129 SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDmqleLKRLQKELGITFVfvTHDQEEAL 195
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
699-876 |
4.99e-06 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 48.93 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 699 LSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT---KPSEGMFH----VPQRPYTSLGtlrdqiiYPLSREEA 771
Cdd:COG1121 25 VSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgKPPRRARRrigyVPQRAEVDWD-------FPITVRDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 772 kikVLS--LHRSGNNSSASMLLDDHLKTILENVRLVYLLER---EgwdstpnwedvLSLGEQQRLGMARLFFHHPKFGIL 846
Cdd:COG1121 98 ---VLMgrYGRRGLFRRPSRADREAVDEALERVGLEDLADRpigE-----------LSGGQQQRVLLARALAQDPDLLLL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1142837572 847 DECTnaTSVDV--EEHLYRLATSM---GITVITSS 876
Cdd:COG1121 164 DEPF--AGVDAatEEALYELLRELrreGKTILVVT 196
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
692-873 |
5.42e-06 |
|
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: 47.57 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 692 QKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLrdlwptfsGRVTKPSEGmfhvpqrpytsLGTLRDQIIYPLSREEA 771
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCI--------AGLEEPDSG-----------SILIDGEDLTDLEDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 772 KIKvlslhrsgnnSSASMLLDD-----HLkTILENVRLVylleregwdstpnwedvLSLGEQQRLGMARLFFHHPKFGIL 846
Cdd:cd03229 73 PLR----------RRIGMVFQDfalfpHL-TVLENIALG-----------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190
....*....|....*....|....*....|.
gi 1142837572 847 DECTNA----TSVDVEEHLYRLATSMGITVI 873
Cdd:cd03229 125 DEPTSAldpiTRREVRALLKSLQAQLGITVV 155
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
46-234 |
5.53e-06 |
|
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: 48.48 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI-------VKPGVGSDLNKE---IFYVPQRPYTAVGTLR 115
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkneSEPSFEATRSRNrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 116 EQLIY--PLTADQG---IEPLTYDGMVDLLKNVDLEYLLERypldkevnwGDELSLGEQQRLGMARLFYHKPKFAILDEC 190
Cdd:cd03290 97 ENITFgsPFNKQRYkavTDACSLQPDIDLLPFGDQTEIGER---------GINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1142837572 191 TSAVTTD-----MEERFCKKVRAMGTSCITISHRPALVAFHDIVLSL-DG 234
Cdd:cd03290 168 FSALDIHlsdhlMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMkDG 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
26-228 |
5.88e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.08 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 26 EANHIEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLN-KEIFYVP 104
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSrKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 105 QrpytAVGTLREQLIYPLTADQGIEPLTYdGMVDLLKNVD-----LEYLLERY---PL-DKEVNWgdeLSLGEQQRLGMA 175
Cdd:PRK13636 82 E----SVGMVFQDPDNQLFSASVYQDVSF-GAVNLKLPEDevrkrVDNALKRTgieHLkDKPTHC---LSFGQKKRVAIA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142837572 176 RLFYHKPKFAILDECTSAV----TTDMEERFCKKVRAMGtscITIshrpaLVAFHDI 228
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLdpmgVSEIMKLLVEMQKELG---LTI-----IIATHDI 202
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
693-738 |
6.19e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 47.95 E-value: 6.19e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1142837572 693 KLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT 738
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK 60
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
49-189 |
6.61e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.92 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 49 LTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI---VKPGVGSDLNKEIFYVPQRP--YTAVGTLrEQLIYpLT 123
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidGKTATRGDRSRFMAYLGHLPglKADLSTL-ENLHF-LC 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142837572 124 ADQGIEPLTYDG-MVDLLKNVDLEYLLERypldkevnwgdELSLGEQQRLGMARLFYHKPKFAILDE 189
Cdd:PRK13543 108 GLHGRRAKQMPGsALAIVGLAGYEDTLVR-----------QLSAGQKKRLALARLWLSPAPLWLLDE 163
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
33-258 |
7.94e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 48.37 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 33 SDVKVVTPAGNVLVDDLTLRVET---------------GSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG---- 93
Cdd:cd03288 9 SNSGLVGLGGEIKIHDLCVRYENnlkpvlkhvkayikpGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDiskl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 94 --SDLNKEIFYVPQRPYTAVGTLREQLiypltadqgiEP---LTYDGMVDLLKNVDLEYLLERYP--LDKEVNWGDE-LS 165
Cdd:cd03288 89 plHTLRSRLSIILQDPILFSGSIRFNL----------DPeckCTDDRLWEALEIAQLKNMVKSLPggLDAVVTEGGEnFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 166 LGEQQRLGMARLFYHKPKFAILDECTSAVttDM-EERFCKKVRAMG---TSCITISHRPALVAFHDIVLSLdgEGGWNVQ 241
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASI--DMaTENILQKVVMTAfadRTVVTIAHRVSTILDADLVLVL--SRGILVE 234
|
250
....*....|....*..
gi 1142837572 242 HRRDDSSFSTEESDFSS 258
Cdd:cd03288 235 CDTPENLLAQEDGVFAS 251
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
46-87 |
8.06e-06 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 47.91 E-value: 8.06e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI 87
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV 79
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
693-880 |
8.11e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 48.50 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 693 KLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT--------------------KPSEGMFHVPQRPY 752
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKvdgkvlyfgkdifqidaiklRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 753 TSLgTLRDQIIYPLSREEAKIKvlslhrsgnnssasmlldDHLKTILENVRLVYLLEREGWDSTPNWEDVLSLGEQQRLG 832
Cdd:PRK14246 103 PHL-SIYDNIAYPLKSHGIKEK------------------REIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1142837572 833 MARLFFHHPKFGILDECTN----ATSVDVEEHLYRLATSMGITVITSSQRPA 880
Cdd:PRK14246 164 IARALALKPKVLLMDEPTSmidiVNSQAIEKLITELKNEIAIVIVSHNPQQV 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
690-863 |
8.98e-06 |
|
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: 48.00 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 690 PSQKLLaRKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT--------------KPSEGMfhVPQRpyTSL 755
Cdd:cd03253 12 PGRPVL-KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtldslRRAIGV--VPQD--TVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 756 --GTLRDQIIY--PLSREEAKI---KVLSLHRSGNNssasmlLDDHLKTIL-EnvRLVYLleregwdstpnwedvlSLGE 827
Cdd:cd03253 87 fnDTIGYNIRYgrPDATDEEVIeaaKAAQIHDKIMR------FPDGYDTIVgE--RGLKL----------------SGGE 142
|
170 180 190
....*....|....*....|....*....|....*.
gi 1142837572 828 QQRLGMARLFFHHPKFGILDECTNATSVDVEEHLYR 863
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQA 178
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
27-189 |
8.99e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 48.19 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 27 ANHIEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPL------VSGHIVKPGVGSDLNKEI 100
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPqrgrvkVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 101 FYVPQRPYTAV--GTLREQLIY-PLtaDQGIEPLTYDGMV-DLLKNVDLEYLLERYPLdkevnwgdELSLGEQQRLGMAR 176
Cdd:PRK13647 82 GLVFQDPDDQVfsSTVWDDVAFgPV--NMGLDKDEVERRVeEALKAVRMWDFRDKPPY--------HLSYGQKKRVAIAG 151
|
170
....*....|...
gi 1142837572 177 LFYHKPKFAILDE 189
Cdd:PRK13647 152 VLAMDPDVIVLDE 164
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
51-224 |
9.25e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.85 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 51 LRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLNKEifyvpQRpytavGTLREQ----------LI 119
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlHQMDEE-----AR-----AKLRAKhvgfvfqsfmLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 120 YPLTADQGIE-PLTYDGMVDLLKNVDLEYLLERYPLDKEVN-WGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTD 197
Cdd:PRK10584 101 PTLNALENVElPALLRGESSRQSRNGAKALLEQLGLGKRLDhLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190
....*....|....*....|....*....|.
gi 1142837572 198 MEERFCKKV----RAMGTSCITISHRPALVA 224
Cdd:PRK10584 181 TGDKIADLLfslnREHGTTLILVTHDLQLAA 211
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
34-224 |
9.66e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.57 E-value: 9.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 34 DVKVVTPAGNVL-VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLwpLVSGHIVKpgvGSDL--NKEIFYVPQR---- 106
Cdd:PRK09473 19 RVTFSTPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL--LAANGRIG---GSATfnGREILNLPEKelnk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 107 ------------------PYTAVGtlrEQLIYPLTADQGIEPLT-YDGMVDLLKNVDLEYLLER---YPldkevnwgDEL 164
Cdd:PRK09473 94 lraeqismifqdpmtslnPYMRVG---EQLMEVLMLHKGMSKAEaFEESVRMLDAVKMPEARKRmkmYP--------HEF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 165 SLGEQQRLGMARLFYHKPKFAILDECTSA--VT------TDMEErfCKkvRAMGTSCITISHRPALVA 224
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTAldVTvqaqimTLLNE--LK--REFNTAIIMITHDLGVVA 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
711-880 |
1.03e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 47.85 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 711 LTGPNGSGKSSIFRVLR---DLWP--TFSGRVTKPSEGMFhvpqRPYTSLGTLRDQI--------IYPLSREEAKIKVLS 777
Cdd:PRK14239 36 LIGPSGSGKSTLLRSINrmnDLNPevTITGSIVYNGHNIY----SPRTDTVDLRKEIgmvfqqpnPFPMSIYENVVYGLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 778 LhrsgNNSSASMLLDDHLKTILENVRLvylleregwdstpnWEDV----------LSLGEQQRLGMARLFFHHPKFGILD 847
Cdd:PRK14239 112 L----KGIKDKQVLDEAVEKSLKGASI--------------WDEVkdrlhdsalgLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1142837572 848 ECTNA----TSVDVEEHLYRLATSMGITVITSSQRPA 880
Cdd:PRK14239 174 EPTSAldpiSAGKIEETLLGLKDDYTMLLVTRSMQQA 210
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-224 |
1.04e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 47.56 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG--VGSDLNKEIFYVpQRP 107
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdITRLKNREVPFL-RRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 108 YTAVGTLREQLIYPLTADQGIEPLTYDGMV--DLLKNVDLEyLLERYPLDKEVNWGDELSLGEQQRLGMARLFYHKPKFA 185
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASgdDIRRRVSAA-LDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1142837572 186 ILDECTSAVTTDMEE---RFCKKVRAMGTSCITISHRPALVA 224
Cdd:PRK10908 160 LADEPTGNLDDALSEgilRLFEEFNRVGVTVLMATHDIGLIS 201
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
26-189 |
1.21e-05 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 48.54 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 26 EANHIE--FSDVKVVTpagnvlvdDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPgvGSDL------N 97
Cdd:PRK10851 4 EIANIKksFGRTQVLN--------DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH--GTDVsrlharD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 98 KEIFYVPQ-----RPYTAVGTLREQL-IYPLTADQGIEPLTYDGMVdLLKNVDLEYLLERYPldkevnwgDELSLGEQQR 171
Cdd:PRK10851 74 RKVGFVFQhyalfRHMTVFDNIAFGLtVLPRRERPNAAAIKAKVTQ-LLEMVQLAHLADRYP--------AQLSGGQKQR 144
|
170
....*....|....*...
gi 1142837572 172 LGMARLFYHKPKFAILDE 189
Cdd:PRK10851 145 VALARALAVEPQILLLDE 162
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
30-192 |
1.38e-05 |
|
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: 47.81 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLV-DDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLNKEIFYVPQRpy 108
Cdd:TIGR04520 1 IEVENVSFSYPESEKPAlKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 109 taVGTLRE----QLIYPLTAD--------QGIEPltyDGMV----DLLKNVDLEYLLERYPLdkevnwgdELSLGEQQRL 172
Cdd:TIGR04520 79 --VGMVFQnpdnQFVGATVEDdvafglenLGVPR---EEMRkrvdEALKLVGMEDFRDREPH--------LLSGGQKQRV 145
|
170 180
....*....|....*....|
gi 1142837572 173 GMARLFYHKPKFAILDECTS 192
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATS 165
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
46-87 |
1.83e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 47.00 E-value: 1.83e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI 87
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
48-219 |
2.01e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 48 DLTLRVETGSNLLitGPNGSGKSSLFRVLGGLWPLVSGHI---------VKPGVGSDLNkeIFYVPQRPYT-AVGTLREQ 117
Cdd:PRK15439 31 DFTLHAGEVHALL--GGNGAGKSTLMKIIAGIVPPDSGTLeiggnpcarLTPAKAHQLG--IYLVPQEPLLfPNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 118 LIYPLTADQGieplTYDGMVDLLKNVDLEyllerypLDKEVNWGdELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTD 197
Cdd:PRK15439 107 ILFGLPKRQA----SMQKMKQLLAALGCQ-------LDLDSSAG-SLEVADRQIVEILRGLMRDSRILILDEPTASLTPA 174
|
170 180
....*....|....*....|....*
gi 1142837572 198 MEERFCKKVRAM---GTSCITISHR 219
Cdd:PRK15439 175 ETERLFSRIRELlaqGVGIVFISHK 199
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
30-218 |
2.33e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.18 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG--VGSDLNKE-IFYVPQR 106
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqpTRQALQKNlVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 107 P------------------YTAVGTLREqliyPLTADQGIepltydgMVDLLKNVDLEYLLERYPldkevnwgDELSLGE 168
Cdd:PRK15056 87 EevdwsfpvlvedvvmmgrYGHMGWLRR----AKKRDRQI-------VTAALARVDMVEFRHRQI--------GELSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1142837572 169 QQRLGMARLFYHKPKFAILDECTSAVTTDMEER---FCKKVRAMGTSCITISH 218
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARiisLLRELRDEGKTMLVSTH 200
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
36-198 |
2.38e-05 |
|
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: 46.34 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 36 KVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSG--HIVKPGVGSDLNK---EIFYVPQRPyTA 110
Cdd:cd03263 8 KTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtaYINGYSIRTDRKAarqSLGYCPQFD-AL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 111 VGTL--REQLIYpLTADQGIepltYDGMVDLLKNVDLEYL-LERYpLDKEVNwgdELSLGEQQRLGMARLFYHKPKFAIL 187
Cdd:cd03263 87 FDELtvREHLRF-YARLKGL----PKSEIKEEVELLLRVLgLTDK-ANKRAR---TLSGGMKRKLSLAIALIGGPSVLLL 157
|
170
....*....|.
gi 1142837572 188 DEctsaVTTDM 198
Cdd:cd03263 158 DE----PTSGL 164
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
699-863 |
2.43e-05 |
|
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: 46.31 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 699 LSCDVVQGKSLLLTGPNGSGKSSIFR-VLRDLWPTfSGRVTKPSeGMFHVPQRPYTSLGTLRDQII--YPLSREEAKiKV 775
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKL-SGSVSVPG-SIAYVSQEPWIQNGTIRENILfgKPFDEERYE-KV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 776 LslhrsgnnsSASMLLDDhLKtILENVRLVYLLEReGwdSTpnwedvLSLGEQQRLGMARLFFHHPKFGILDECTNATSV 855
Cdd:cd03250 101 I---------KACALEPD-LE-ILPDGDLTEIGEK-G--IN------LSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
....*...
gi 1142837572 856 DVEEHLYR 863
Cdd:cd03250 161 HVGRHIFE 168
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
711-851 |
2.72e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 47.75 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 711 LTGPNGSGKSSIFRVLRDLWPTFSGRVTKPS-EGMFHVPQRPYTSLG-TLRDQIIYPLSREEAKIKVLS-LHRSGNNSSA 787
Cdd:COG0488 29 LVGRNGAGKSTLLKILAGELEPDSGEVSIPKgLRIGYLPQEPPLDDDlTVLDTVLDGDAELRALEAELEeLEAKLAEPDE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 788 SMLLDDHLKTILEnvrlvyllEREGWD--------------STPNWE---DVLSLGEQQRLGMARLFFHHPKFGILDECT 850
Cdd:COG0488 109 DLERLAELQEEFE--------ALGGWEaearaeeilsglgfPEEDLDrpvSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
.
gi 1142837572 851 N 851
Cdd:COG0488 181 N 181
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-78 |
2.82e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 47.62 E-value: 2.82e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 21 GNYVSEANHIE--FSDvkvvtpagNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGG 78
Cdd:TIGR03719 319 GDKVIEAENLTkaFGD--------KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG 370
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
688-864 |
3.43e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.26 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 688 VTPSQKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKPSE-GMFHVPQRPYTSlGTLrdqiiyPL 766
Cdd:PRK09544 12 VSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlRIGYVPQKLYLD-TTL------PL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 767 SREeakiKVLSLHrsGNNSSASMLlddhlkTILENVRLVYLLEREgwdstpnwEDVLSLGEQQRLGMARLFFHHPKFGIL 846
Cdd:PRK09544 85 TVN----RFLRLR--PGTKKEDIL------PALKRVQAGHLIDAP--------MQKLSGGETQRVLLARALLNRPQLLVL 144
|
170
....*....|....*...
gi 1142837572 847 DECTNATSVDVEEHLYRL 864
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDL 162
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
46-192 |
3.63e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 46.62 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLNKEIF-------YVPQRPYTA-VGTLREQ 117
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdirnkagMVFQNPDNQiVATIVEE 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142837572 118 LIYPLTADQGIEPLTYDGMVD-LLKNVDL-EYllERYPldkevnwGDELSLGEQQRLGMARLFYHKPKFAILDECTS 192
Cdd:PRK13633 106 DVAFGPENLGIPPEEIRERVDeSLKKVGMyEY--RRHA-------PHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
48-220 |
3.83e-05 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 45.95 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 48 DLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsdlnkEIFYVP--QRPYTAVgtLREQLIYP-LTA 124
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV------DVTAAPpaDRPVSML--FQENNLFAhLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 125 DQGI----------EPLTYDGMVDLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAV 194
Cdd:cd03298 88 EQNVglglspglklTAEDRQAIEVALARVGLAGLEKRLP--------GELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190
....*....|....*....|....*....|
gi 1142837572 195 ----TTDMEERFCKKVRAMGTSCITISHRP 220
Cdd:cd03298 160 dpalRAEMLDLVLDLHAETKMTVLMVTHQP 189
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
61-189 |
4.23e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.79 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 61 ITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG-VGSDLNKEIF---------YVPQ--R--P-YTAVGTLReqliYPLTAd 125
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGIClppekrrigYVFQdaRlfPhYKVRGNLR----YGMAK- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142837572 126 qgIEPLTYDGMVDLLknvDLEYLLERYPLDkevnwgdeLSLGEQQRLGMARLFYHKPKFAILDE 189
Cdd:PRK11144 104 --SMVAQFDKIVALL---GIEPLLDRYPGS--------LSGGEKQRVAIGRALLTAPELLLMDE 154
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
30-192 |
4.25e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.22 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDL-NKEIFYVPQRpy 108
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdKKSLLEVRKT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 109 taVGTL----REQLIYPlTADQGIE--PLTY--------DGMVDLLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGM 174
Cdd:PRK13639 80 --VGIVfqnpDDQLFAP-TVEEDVAfgPLNLglskeeveKRVKEALKAVGMEGFENKPP--------HHLSGGQKKRVAI 148
|
170
....*....|....*...
gi 1142837572 175 ARLFYHKPKFAILDECTS 192
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTS 166
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
36-202 |
5.05e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 46.85 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 36 KVVTPAGNVLvDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV-KPGVgsdlnkEIFYVPQRPY------ 108
Cdd:TIGR03719 12 KVVPPKKEIL-KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARpQPGI------KVGYLPQEPQldptkt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 109 ------TAVGTLREQL-----IYPLTADqgiEPLTYDGM----------VDLLKNVDLEYLLERY-------PLDKEVNw 160
Cdd:TIGR03719 85 vrenveEGVAEIKDALdrfneISAKYAE---PDADFDKLaaeqaelqeiIDAADAWDLDSQLEIAmdalrcpPWDADVT- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1142837572 161 gdELSLGEQQRLGMARLFYHKPKFAILDECTS---AVTTDMEERF 202
Cdd:TIGR03719 161 --KLSGGERRRVALCRLLLSKPDMLLLDEPTNhldAESVAWLERH 203
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
697-881 |
5.30e-05 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 45.79 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 697 RKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKPSEGMFHVPQRPyTSLG------------TLRDQIIY 764
Cdd:cd03296 19 DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RNVGfvfqhyalfrhmTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 765 PLsreeaKIKvlslHRSGNNSSASMllDDHLKTILENVRLVYLLERegwdsTPNWedvLSLGEQQRLGMARLFFHHPKFG 844
Cdd:cd03296 98 GL-----RVK----PRSERPPEAEI--RAKVHELLKLVQLDWLADR-----YPAQ---LSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1142837572 845 ILDECTNATSVDVEEHLY----RLATSMGITVI--TSSQRPAL 881
Cdd:cd03296 159 LLDEPFGALDAKVRKELRrwlrRLHDELHVTTVfvTHDQEEAL 201
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-88 |
5.53e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 45.85 E-value: 5.53e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142837572 30 IEFSDVKVV----TPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV 88
Cdd:COG1101 2 LELKNLSKTfnpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL 64
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
46-192 |
6.09e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.85 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGS------DLNKEIFYVPQRPYTA-VGTLREQL 118
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLtaenvwNLRRKIGMVFQNPDNQfVGATVEDD 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142837572 119 IYPLTADQGIEpltydgMVDLLKNVDlEYLLERYPLDKEVNWGDELSLGEQQRLGMARLFYHKPKFAILDECTS 192
Cdd:PRK13642 103 VAFGMENQGIP------REEMIKRVD-EALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
30-253 |
7.17e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 45.59 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVV----TPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGS----D 95
Cdd:PRK13641 3 IKFENVDYIyspgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyhITPETGNknlkK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 96 LNKEIFYVPQRPYTAV--GTLREQLIY-PLT---ADQGIEpltyDGMVDLLKNVDL-EYLLERYPLdkevnwgdELSLGE 168
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLfeNTVLKDVEFgPKNfgfSEDEAK----EKALKWLKKVGLsEDLISKSPF--------ELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 169 QQRLGMARLFYHKPKFAILDECTSAV----TTDMEERFcKKVRAMGTSCITISHRPALVA-FHDIVLSLdgEGGWNVQHR 243
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLdpegRKEMMQLF-KDYQKAGHTVILVTHNMDDVAeYADDVLVL--EHGKLIKHA 227
|
250
....*....|
gi 1142837572 244 RDDSSFSTEE 253
Cdd:PRK13641 228 SPKEIFSDKE 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
699-873 |
7.78e-05 |
|
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: 45.12 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 699 LSCDVVQGKSLLLTGPNGSGKSSIFRVLrdlwptfSGrVTKPSEG--MF------HVPQRPYTSLGTLRD-QIIYPLS-- 767
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLI-------SG-FLRPTSGsvLFdgeditGLPPHEIARLGIGRTfQIPRLFPel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 768 --REEAKIKVLSLHRSGNNSSASML-LDDHLKTILENVRLVYLLERegWDSTPnweDVLSLGEQQRLGMARLFFHHPKFG 844
Cdd:cd03219 91 tvLENVMVAAQARTGSGLLLARARReEREARERAEELLERVGLADL--ADRPA---GELSYGQQRRLEIARALATDPKLL 165
|
170 180 190
....*....|....*....|....*....|..
gi 1142837572 845 ILDECT---NATSVDVEEHLYRLATSMGITVI 873
Cdd:cd03219 166 LLDEPAaglNPEETEELAELIRELRERGITVL 197
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-88 |
8.01e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 8.01e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 21 GNYVSEANHIE--FSDvkvvtpagNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV 88
Cdd:PRK11819 321 GDKVIEAENLSksFGD--------RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK 382
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
699-874 |
8.22e-05 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 44.56 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 699 LSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRV------TKPSE---GMFHVPQRPYTSLG--TLRDQIIY--- 764
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpIKAKErrkSIGYVMQDVDYQLFtdSVREELLLglk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 765 PLSREEAKIkvlslhrsgnnssasmllddhlKTILENVRLVYLLEREGWDstpnwedvLSLGEQQRLGMARLFFHHPKFG 844
Cdd:cd03226 99 ELDAGNEQA----------------------ETVLKDLDLYALKERHPLS--------LSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 1142837572 845 ILDECTnaTSVDvEEHLYRLATSMG--------ITVIT 874
Cdd:cd03226 149 IFDEPT--SGLD-YKNMERVGELIRelaaqgkaVIVIT 183
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
57-194 |
1.06e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 45.18 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 57 SNLLITGPNGSGKSSLFRVLGGLWPLVSGH-------IVKPGVgSDLNKEIFYVPQRPYTAV-GTLREQLIYPLTADQGI 128
Cdd:PRK13652 31 SRIAVIGPNGAGKSTLFRHFNGILKPTSGSvlirgepITKENI-REVRKFVGLVFQNPDDQIfSPTVEQDIAFGPINLGL 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142837572 129 EPLTYDGMVD-LLKNVDLEYLLERYPldkevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAV 194
Cdd:PRK13652 110 DEETVAHRVSsALHMLGLEELRDRVP--------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
44-235 |
1.09e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 44 VLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKpgvgsdlNKEIFYVPQRPYTAVGTLREQLIYplt 123
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-------ERSIAYVPQQAWIMNATVRGNILF--- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 124 adqgIEPLTYDGMVDLLKNVDLEYLLERYPLDKEVNWGDE---LSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEE 200
Cdd:PTZ00243 744 ----FDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
170 180 190
....*....|....*....|....*....|....*...
gi 1142837572 201 RFCKKV---RAMGTSCITISHRPALVAFHDIVLSLDGE 235
Cdd:PTZ00243 820 RVVEECflgALAGKTRVLATHQVHVVPRADYVVALGDG 857
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
26-230 |
1.10e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 45.13 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 26 EANHIEFSDVKVVTPAGNVL-VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGSDLNK 98
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 99 EIFYVPQRPYTA-VGTlreqlIYPLTADQGIE--PLTYDGMV----DLLKNVDLeyllerypLDKEVNWGDELSLGEQQR 171
Cdd:PRK13648 84 HIGIVFQNPDNQfVGS-----IVKYDVAFGLEnhAVPYDEMHrrvsEALKQVDM--------LERADYEPNALSGGQKQR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142837572 172 LGMARLFYHKPKFAILDECTSAVTTDMEERFCKKVRAM----GTSCITISH--RPALVAFHDIVL 230
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITHdlSEAMEADHVIVM 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
680-878 |
1.10e-04 |
|
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: 44.41 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 680 ISFHEVDI-VTPSQKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLrdlwptFsgRVTKPSEGMFH------------ 746
Cdd:cd03244 3 IEFKNVSLrYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLAL------F--RLVELSSGSILidgvdiskiglh 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 747 --------VPQRPYTSLGTLRDQIIyPLSR--EEAKIKVLSlhrsgnnssasmllDDHLKTILENV--RLVYLLEREGwd 814
Cdd:cd03244 75 dlrsrisiIPQDPVLFSGTIRSNLD-PFGEysDEELWQALE--------------RVGLKEFVESLpgGLDTVVEEGG-- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 815 stpnweDVLSLGEQQRLGMARLFFHHPKFGILDECTnaTSVDVE--EHLYRLATSM--GITVITSSQR 878
Cdd:cd03244 138 ------ENLSVGQRQLLCLARALLRKSKILVLDEAT--ASVDPEtdALIQKTIREAfkDCTVLTIAHR 197
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
679-881 |
1.14e-04 |
|
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: 44.43 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 679 TISFHEVDIVTPsqkllarkLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKPSEGMFHVP--QRP----- 751
Cdd:cd03259 7 SKTYGSVRALDD--------LSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPpeRRNigmvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 752 -----YTSLgTLRDQIIYPL-----SREEAKIKVLSLhrsgnnssasmllddhlktiLENVRLVYLLERegwdstpnWED 821
Cdd:cd03259 79 qdyalFPHL-TVAENIAFGLklrgvPKAEIRARVREL--------------------LELVGLEGLLNR--------YPH 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 822 VLSLGEQQRLGMARLFFHHPKFGILDECTNAtsVDVE------EHLYRLATSMGITVI--TSSQRPAL 881
Cdd:cd03259 130 ELSGGQQQRVALARALAREPSLLLLDEPLSA--LDAKlreelrEELKELQRELGITTIyvTHDQEEAL 195
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
697-878 |
1.15e-04 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 44.28 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 697 RKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKPSEGMFHVPQRPYTSLGTLRDQI-IYP-LSREEAKIK 774
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTgLYDrLTARENLEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 775 VLSLHrsGNNSSAsmlLDDHLKTILENVRLVYLLEREGWDstpnwedvLSLGEQQRLGMARLFFHHPKFGILDECTNATS 854
Cdd:cd03266 102 FAGLY--GLKGDE---LTARLEELADRLGMEELLDRRVGG--------FSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190
....*....|....*....|....*....|.
gi 1142837572 855 V-------DVEEHLYRLatsmGITVITSSQR 878
Cdd:cd03266 169 VmatralrEFIRQLRAL----GKCILFSTHI 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
127-230 |
1.27e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 127 GIEPLTYDGMVDLLKNVDLEYLLERYPLDKEVN---WGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFC 203
Cdd:PTZ00265 1319 GKEDATREDVKRACKFAAIDEFIESLPNKYDTNvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1398
|
90 100 110
....*....|....*....|....*....|.
gi 1142837572 204 KKVRAM----GTSCITISHRPALVAFHDIVL 230
Cdd:PTZ00265 1399 KTIVDIkdkaDKTIITIAHRIASIKRSDKIV 1429
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
699-848 |
1.50e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.50 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 699 LSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKPSEGMFHVPQRPYTSLGtlrdqiIYPLSREEAKIKVLSL 778
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRG------IGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142837572 779 HrsgNNSSASMLLDDHLKTILENVRLVYLLEREGWDS-TPNWEDVLSLGEQQRLGMARLFFHHPKFGILDE 848
Cdd:PRK10895 96 Y---DNLMAVLQIRDDLSAEQREDRANELMEEFHIEHlRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
698-882 |
1.76e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.23 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 698 KLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKPSEGMFHVP---------------QRPYTSLG---TLR 759
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgklqalrrdiqfifQDPYASLDprqTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 760 DQIIYPlsreeakikvLSLHRSGNNSSASMllddhlktilenvRLVYLLEREGWDSTPNWE--DVLSLGEQQRLGMARLF 837
Cdd:PRK10261 422 DSIMEP----------LRVHGLLPGKAAAA-------------RVAWLLERVGLLPEHAWRypHEFSGGQRQRICIARAL 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1142837572 838 FHHPKFGILDECTNATSVDVEEH----LYRLATSMGITVITSSQRPALI 882
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSIRGQiinlLLDLQRDFGIAYLFISHDMAVV 527
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
680-767 |
2.58e-04 |
|
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: 42.69 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 680 ISFHEVDIVTPSQKLLARK-LSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT---KP--------SEGMFHV 747
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKnLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITldgVPvsdlekalSSLISVL 80
|
90 100
....*....|....*....|
gi 1142837572 748 PQRPYTSLGTLRDQIIYPLS 767
Cdd:cd03247 81 NQRPYLFDTTLRNNLGRRFS 100
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
702-873 |
3.22e-04 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 42.03 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 702 DVVQGKSLLLTGPNGSGKSSIFRVLrdlwptfSGrVTKPSEGMFHVPQRPYTslgtlrdqiiyPLSREEAkikvlslHRS 781
Cdd:cd03216 22 SVRRGEVHALLGENGAGKSTLMKIL-------SG-LYKPDSGEILVDGKEVS-----------FASPRDA-------RRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 782 GnnssasmllddhlktilenVRLVYLLeregwdstpnwedvlSLGEQQRLGMARLFFHHPKFGILDECTNATSVDVEEHL 861
Cdd:cd03216 76 G-------------------IAMVYQL---------------SVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170
....*....|....*
gi 1142837572 862 Y---RLATSMGITVI 873
Cdd:cd03216 122 FkviRRLRAQGVAVI 136
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
47-73 |
3.64e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.51 E-value: 3.64e-04
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
46-193 |
4.15e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 43.90 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPlVSGHIVKpgVGSDLN-----------KEIFYVPQRPYtavGTL 114
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRF--DGQDLDglsrralrplrRRMQVVFQDPF---GSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 115 --ReqliypLTADQGI-EPLTYDG-----------MVDLLKNVDL-EYLLERYPldkevnwgDELSLGEQQRLGMARLFY 179
Cdd:COG4172 376 spR------MTVGQIIaEGLRVHGpglsaaerrarVAEALEEVGLdPAARHRYP--------HEFSGGQRQRIAIARALI 441
|
170
....*....|....
gi 1142837572 180 HKPKFAILDECTSA 193
Cdd:COG4172 442 LEPKLLVLDEPTSA 455
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
47-230 |
6.00e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 47 DDLTLRVETGSN-----LLITGPNGSGKSSLFRVLGGlwplvsghIVKPGVGS-DLNKEIFYVPQRPYTAV-GTLrEQLI 119
Cdd:PRK13409 351 GDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAG--------VLKPDEGEvDPELKISYKPQYIKPDYdGTV-EDLL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 120 YPLTADQGIEPLTydgmVDLLKNVDLEYLlerypLDKEVNwgdELSLGEQQRLGMARLFYHKPKFAILDECTSAVttDME 199
Cdd:PRK13409 422 RSITDDLGSSYYK----SEIIKPLQLERL-----LDKNVK---DLSGGELQRVAIAACLSRDADLYLLDEPSAHL--DVE 487
|
170 180 190
....*....|....*....|....*....|...
gi 1142837572 200 ERF--CKKVRAMgtscITISHRPALVAFHDIVL 230
Cdd:PRK13409 488 QRLavAKAIRRI----AEEREATALVVDHDIYM 516
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
39-189 |
7.09e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 42.53 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 39 TPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPlVSGHIVKPGVGSD------LNKEIFYVPQRPYTAVG 112
Cdd:cd03289 13 TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNsvplqkWRKAFGVIPQKVFIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 113 TLREQL-IYPLTADQGIEPLTydgmvdllKNVDLEYLLERYP--LDKE-VNWGDELSLGEQQRLGMARLFYHKPKFAILD 188
Cdd:cd03289 92 TFRKNLdPYGKWSDEEIWKVA--------EEVGLKSVIEQFPgqLDFVlVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163
|
.
gi 1142837572 189 E 189
Cdd:cd03289 164 E 164
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
21-218 |
8.76e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.04 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 21 GNYVSEANHIEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLNKEI 100
Cdd:PRK10522 314 PQAFPDWQTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 101 FYvpQRPYTAVGT---LREQLIYPltadQGIEPltydgmvdllKNVDLEYLLERYPLDKEVNWGDE------LSLGEQQR 171
Cdd:PRK10522 394 DY--RKLFSAVFTdfhLFDQLLGP----EGKPA----------NPALVEKWLERLKMAHKLELEDGrisnlkLSKGQKKR 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1142837572 172 LGMARLFYHKPKFAILDECtsAVTTD-MEERFCKKV-----RAMGTSCITISH 218
Cdd:PRK10522 458 LALLLALAEERDILLLDEW--AADQDpHFRREFYQVllpllQEMGKTIFAISH 508
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
42-200 |
9.39e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.08 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVL-VDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV---GSDLN----------KEIFYVPQRP 107
Cdd:PRK14243 21 GSFLaVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVtfhGKNLYapdvdpvevrRRIGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 108 YTAVGTLREQLIYpltadqGIEPLTYDGmvdllknvDLEYLLERyPLDKEVNW----------GDELSLGEQQRLGMARL 177
Cdd:PRK14243 101 NPFPKSIYDNIAY------GARINGYKG--------DMDELVER-SLRQAALWdevkdklkqsGLSLSGGQQQRLCIARA 165
|
170 180
....*....|....*....|....*..
gi 1142837572 178 FYHKPKFAILDECTSAV----TTDMEE 200
Cdd:PRK14243 166 IAVQPEVILMDEPCSALdpisTLRIEE 192
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
53-202 |
9.55e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 41.97 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 53 VETGSNLLITGPNGSGKSSLFRVLGG-LWPLVSGH--------IVKPGVGSDLnkeifyvpQRPYTAvgtLREQLIYPLT 123
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGkLKPNLGKFddppdwdeILDEFRGSEL--------QNYFTK---LLEGDVKVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 124 ADQGIE--PLTYDGMV-DLLKNVD----LEYLLERYPLDKEVNWG-DELSLGEQQRLGMARLFYHKPKFAILDECTSAVt 195
Cdd:cd03236 92 KPQYVDliPKAVKGKVgELLKKKDergkLDELVDQLELRHVLDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYL- 170
|
....*..
gi 1142837572 196 tDMEERF 202
Cdd:cd03236 171 -DIKQRL 176
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
699-879 |
1.23e-03 |
|
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: 41.49 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 699 LSCDVVQGKSLLLTGPNGSGKSSIF-----RVLRDlwPTFSGRVT----KPSEGMF-----HVPQRPYTSLG-TLRDQII 763
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLdaisgRVEGG--GTTSGQILfngqPRKPDQFqkcvaYVRQDDILLPGlTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 764 YplsreeakIKVLSLHRSGNNSSASMLLDDHLK-----TILENVRLVYLleregwdstpnwedvlSLGEQQRLGMARLFF 838
Cdd:cd03234 104 Y--------TAILRLPRKSSDAIRKKRVEDVLLrdlalTRIGGNLVKGI----------------SGGERRRVSIAVQLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1142837572 839 HHPKFGILDECTNA----TSVDVEEHLYRLATSmGITVITSSQRP 879
Cdd:cd03234 160 WDPKVLILDEPTSGldsfTALNLVSTLSQLARR-NRIVILTIHQP 203
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
26-226 |
1.33e-03 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 41.00 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 26 EANHIEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGL--WPLVSGHIVKPGVGSDLN---KEI 100
Cdd:cd03213 5 SFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRsfrKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 101 FYVPQrpytavgtlrEQLIYP-LTADQGIEpltydgMVDLLKNvdleyllerypldkevnwgdeLSLGEQQRLGMARLFY 179
Cdd:cd03213 85 GYVPQ----------DDILHPtLTVRETLM------FAAKLRG---------------------LSGGERKRVSIALELV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1142837572 180 HKPKFAILDECTSAVTTDMEERFCKKVRAM---GTSCITISHRPALVAFH 226
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLadtGRTIICSIHQPSSEIFE 177
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
697-882 |
1.76e-03 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 40.29 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 697 RKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVT-KPSEGMFHVPQR-------PYT-----SLGTLRDQII 763
Cdd:NF040873 9 HGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRrAGGARVAYVPQRsevpdslPLTvrdlvAMGRWARRGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 764 Y-PLSREEAKIKVLSLHRSGnnssasmlLDDhlktiLENVRLvylleregwdstpnweDVLSLGEQQRLGMARLFFHHPK 842
Cdd:NF040873 89 WrRLTRDDRAAVDDALERVG--------LAD-----LAGRQL----------------GELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1142837572 843 FGILDECTNATSVDVEEHLYRL---ATSMGITVITSSQRPALI 882
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALlaeEHARGATVVVVTHDLELV 182
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
42-87 |
1.98e-03 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 40.84 E-value: 1.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1142837572 42 GNVLVDDLTLRVETGSnllIT---GPNGSGKSSLFRVLGGLWPLVSGHI 87
Cdd:COG4604 13 GKVVLDDVSLTIPKGG---ITaliGPNGAGKSTLLSMISRLLPPDSGEV 58
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
47-230 |
2.06e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 41.69 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 47 DDLTLRVETGS-----NLLITGPNGSGKSSLFRVLGGlwplvsghIVKPGVGS-DLNKEIFYVPQRPYTAV-GTLREQLI 119
Cdd:COG1245 352 GGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAG--------VLKPDEGEvDEDLKISYKPQYISPDYdGTVEEFLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 120 YPLTADQGIEPLTydgmVDLLKNVDLEYLlerypLDKEVnwgDELSLGEQQRLGMARLFYHKPKFAILDEcTSAvTTDME 199
Cdd:COG1245 424 SANTDDFGSSYYK----TEIIKPLGLEKL-----LDKNV---KDLSGGELQRVAIAACLSRDADLYLLDE-PSA-HLDVE 489
|
170 180 190
....*....|....*....|....*....|...
gi 1142837572 200 ERF--CKKVRAMgtscITISHRPALVAFHDIVL 230
Cdd:COG1245 490 QRLavAKAIRRF----AENRGKTAMVVDHDIYL 518
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
46-224 |
2.08e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.27 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 46 VDDLTLRVETGSNLLITGPNGSGKS--SLfrvlgglwpLVSGHIVKPGV---------GSDLNK------------EIFY 102
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSvsSL---------AIMGLIDYPGRvmaeklefnGQDLQRisekerrnlvgaEVAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 103 VPQRPYTAVG---TLREQLIYPLTADQGIEPLT-YDGMVDLLKNV---DLEYLLERYPldkevnwgDELSLGEQQRLGMA 175
Cdd:PRK11022 94 IFQDPMTSLNpcyTVGFQIMEAIKVHQGGNKKTrRQRAIDLLNQVgipDPASRLDVYP--------HQLSGGMSQRVMIA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1142837572 176 RLFYHKPKFAILDECTSA--VTTDME--ERFCKKVRAMGTSCITISHRPALVA 224
Cdd:PRK11022 166 MAIACRPKLLIADEPTTAldVTIQAQiiELLLELQQKENMALVLITHDLALVA 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
688-847 |
2.41e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 41.82 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 688 VTPSQKLLARKLScdvvQGKSLLLTGPNGSGKSSIFRV-LRDLWPT-----FSGRVTkpsegmfHVPQRPYTSLGTLRDQ 761
Cdd:TIGR01271 438 VTPVLKNISFKLE----KGQLLAVAGSTGSGKSSLLMMiMGELEPSegkikHSGRIS-------FSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 762 IIYPLSREEakikvlslHRSGNNSSASMLLDDhlktilenvrLVYLLERegwDSTPNWED--VLSLGEQQRLGMARLFFH 839
Cdd:TIGR01271 507 IIFGLSYDE--------YRYTSVIKACQLEED----------IALFPEK---DKTVLGEGgiTLSGGQRARISLARAVYK 565
|
....*...
gi 1142837572 840 HPKFGILD 847
Cdd:TIGR01271 566 DADLYLLD 573
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
42-199 |
2.43e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 42 GNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGhIVKpgvGSDlNKEIFYVPQRPYtavgtlreqliyp 121
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG-TVK---WSE-NANIGYYAQDHA------------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 122 ltADQGIEPLTYDGMVDLLKNVDLEYLLeRYPLDKEVNWGDE-------LSLGEQQRLGMARLFYHKPKFAILDECTSAV 194
Cdd:PRK15064 393 --YDFENDLTLFDWMSQWRQEGDDEQAV-RGTLGRLLFSQDDikksvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHM 469
|
....*
gi 1142837572 195 ttDME 199
Cdd:PRK15064 470 --DME 472
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
30-87 |
2.60e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 40.98 E-value: 2.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI 87
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI 61
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
692-873 |
3.18e-03 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 40.48 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 692 QKLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVL-RDLWPTfSGRVT---------KPSEGMFH---VPQrpYTSLGtl 758
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGELTPS-SGEVRlngrplaawSPWELARRravLPQ--HSSLA-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 759 rdqiiYPLSREEakikVLSLHRSGNNSSASmLLDDHLKTILENVRLVYLLERegwdstpnweDVLSL--GEQQRLGMARL 836
Cdd:COG4559 88 -----FPFTVEE----VVALGRAPHGSSAA-QDRQIVREALALVGLAHLAGR----------SYQTLsgGEQQRVQLARV 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1142837572 837 F-------FHHPKFGILDECTnaTSVDV--EEHLYRLA---TSMGITVI 873
Cdd:COG4559 148 LaqlwepvDGGPRWLFLDEPT--SALDLahQHAVLRLArqlARRGGGVV 194
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-224 |
3.76e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 30 IEFSDVKVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKpgvGSDLNKEIF---YVPQR 106
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFR---SAKVRMAVFsqhHVDGL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 107 PYTAVGTLREQLIYPLTADQGIEplTYDGMVDLLKNVDLEYLLerypldkevnwgdELSLGEQQRLGMARLFYHKPKFAI 186
Cdd:PLN03073 586 DLSSNPLLYMMRCFPGVPEQKLR--AHLGSFGVTGNLALQPMY-------------TLSGGQKSRVAFAKITFKKPHILL 650
|
170 180 190
....*....|....*....|....*....|....*...
gi 1142837572 187 LDECTSAVTTDMEERFCKKVRAMGTSCITISHRPALVA 224
Cdd:PLN03073 651 LDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLIS 688
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-78 |
4.03e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 4.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1142837572 25 SEANHIEFSDVkVVTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGG 78
Cdd:PRK10938 256 ANEPRIVLNNG-VVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
38-197 |
4.25e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.77 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 38 VTPAGNVLVDDLTLRVETGSNLLITGPNGSGKSSLFRVLGGL--WPLVSGHIVKPgvGSDL---------NKEIFYVPQR 106
Cdd:PRK09580 9 VSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFK--GKDLlelspedraGEGIFMAFQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 107 PY------------TAVGTLREQliypltadQGIEPLTYDGMVDLLKnvDLEYLLERYP--LDKEVNWGdeLSLGEQQR- 171
Cdd:PRK09580 87 PVeipgvsnqfflqTALNAVRSY--------RGQEPLDRFDFQDLME--EKIALLKMPEdlLTRSVNVG--FSGGEKKRn 154
|
170 180
....*....|....*....|....*...
gi 1142837572 172 --LGMARLfyhKPKFAILDECTSAVTTD 197
Cdd:PRK09580 155 diLQMAVL---EPELCILDESDSGLDID 179
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
48-87 |
5.63e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 40.17 E-value: 5.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1142837572 48 DLTLRveTGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI 87
Cdd:COG4615 352 DLTIR--RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
680-851 |
7.27e-03 |
|
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: 37.81 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 680 ISFHEVDIVTPSQKLLaRKLSCDVVQGKSLLLTGPNGSGKSSIFRVLrdlwptfSGRvTKPSEGMFHVPQrpytslgtlr 759
Cdd:cd03221 1 IELENLSKTYGGKLLL-KDISLTINPGDRIGLVGRNGAGKSTLLKLI-------AGE-LEPDEGIVTWGS---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 760 dqiiyplsreeakikvlslhrsgnnssasmllddhlktileNVRLVYLleregwdstpnweDVLSLGEQQRLGMARLFFH 839
Cdd:cd03221 62 -----------------------------------------TVKIGYF-------------EQLSGGEKMRLALAKLLLE 87
|
170
....*....|..
gi 1142837572 840 HPKFGILDECTN 851
Cdd:cd03221 88 NPNLLLLDEPTN 99
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
693-764 |
7.44e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.15 E-value: 7.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142837572 693 KLLARKLSCDVVQGKSLLLTGPNGSGKSSIFRVLRDLWPTFSGRVTKpSEGMFHVPQRPYTSLGTLRDQIIY 764
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-ERSIAYVPQQAWIMNATVRGNILF 743
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-233 |
7.96e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.15 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 26 EANHIEFSDVKVVTPAGNVLV-DDLTLRVETGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG--VGS----DLNK 98
Cdd:PTZ00243 1305 QAGSLVFEGVQMRYREGLPLVlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGreIGAyglrELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142837572 99 EIFYVPQRPYTAVGTLReqliypltadQGIEPLTYDGMVDLLKNVDLEYLLERYPLDKE------VNWGDELSLGEQQRL 172
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVR----------QNVDPFLEASSAEVWAALELVGLRERVASESEgidsrvLEGGSNYSVGQRQLM 1454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142837572 173 GMARLFYHK-PKFAILDECTSAVTTDMEERFCKKVRAM--GTSCITISHRPALVAFHDIVLSLD 233
Cdd:PTZ00243 1455 CMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAfsAYTVITIAHRLHTVAQYDKIIVMD 1518
|
|
| |
