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Conserved domains on  [gi|767915023|ref|XP_011531329|]
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ATP-binding cassette sub-family G member 5 isoform X6 [Homo sapiens]

Protein Classification

ABC transporter G family protein( domain architecture ID 1000947)

ABC transporter G (ABCG) family protein may be involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
3a01204 super family cl36780
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
3-474 2.94e-75

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


The actual alignment was detected with superfamily member TIGR00955:

Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 248.04  E-value: 2.94e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023    3 ELSLSHVADRLIGNYS-LGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQP 81
Cdd:TIGR00955 147 ALGLRKCANTRIGVPGrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQP 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   82 RSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYPCPEHSNPFDFYMDLTSVDtqsKEREIETSKRVQMIESAYKKS 161
Cdd:TIGR00955 227 SSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVI---PGSENESRERIEKICDSFAVS 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  162 AICHKTLKNIeRMKHLKTLPMV-----PFKTKDSPGVFSKLGVLLRRVTRNLVRNKLAVITRLLQNLIMGLF--LLFFVL 234
Cdd:TIGR00955 304 DIGRDMLVNT-NLWSGKAGGLVkdsenMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILigLIYLGQ 382
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  235 RVRSnvlKGaIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAVSDQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSV 314
Cdd:TIGR00955 383 GLTQ---KG-VQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSI 458
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  315 CYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIVNSVVALLSIAgVLVGSGFLRNIQEMPIPFKIISYF 394
Cdd:TIGR00955 459 TYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIP-FLLFGGFFINSDSIPVYFKWLSYL 537
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  395 TFQKYCSEILVVNEFYGL-NFTCGSSNvsvTTNPMCAFTQGIQfieKTCPGATSRFTMNFLILYSFIPALVILGIVVFKI 473
Cdd:TIGR00955 538 SWFRYGNEGLLINQWSDVdNIECTSAN---TTGPCPSSGEVIL---ETLSFRNADLYLDLIGLVILIFFFRLLAYFALRI 611

                  .
gi 767915023  474 R 474
Cdd:TIGR00955 612 R 612
 
Name Accession Description Interval E-value
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
3-474 2.94e-75

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 248.04  E-value: 2.94e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023    3 ELSLSHVADRLIGNYS-LGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQP 81
Cdd:TIGR00955 147 ALGLRKCANTRIGVPGrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQP 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   82 RSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYPCPEHSNPFDFYMDLTSVDtqsKEREIETSKRVQMIESAYKKS 161
Cdd:TIGR00955 227 SSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVI---PGSENESRERIEKICDSFAVS 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  162 AICHKTLKNIeRMKHLKTLPMV-----PFKTKDSPGVFSKLGVLLRRVTRNLVRNKLAVITRLLQNLIMGLF--LLFFVL 234
Cdd:TIGR00955 304 DIGRDMLVNT-NLWSGKAGGLVkdsenMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILigLIYLGQ 382
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  235 RVRSnvlKGaIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAVSDQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSV 314
Cdd:TIGR00955 383 GLTQ---KG-VQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSI 458
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  315 CYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIVNSVVALLSIAgVLVGSGFLRNIQEMPIPFKIISYF 394
Cdd:TIGR00955 459 TYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIP-FLLFGGFFINSDSIPVYFKWLSYL 537
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  395 TFQKYCSEILVVNEFYGL-NFTCGSSNvsvTTNPMCAFTQGIQfieKTCPGATSRFTMNFLILYSFIPALVILGIVVFKI 473
Cdd:TIGR00955 538 SWFRYGNEGLLINQWSDVdNIECTSAN---TTGPCPSSGEVIL---ETLSFRNADLYLDLIGLVILIFFFRLLAYFALRI 611

                  .
gi 767915023  474 R 474
Cdd:TIGR00955 612 R 612
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
2-104 3.15e-52

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: 175.92  E-value: 3.15e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   2 AELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQP 81
Cdd:cd03234  124 EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQP 203
                         90       100
                 ....*....|....*....|...
gi 767915023  82 RSELFQLFDKIAILSFGELIFCG 104
Cdd:cd03234  204 RSDLFRLFDRILLLSSGEIVYSG 226
PLN03211 PLN03211
ABC transporter G-25; Provisional
1-433 2.40e-42

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 159.27  E-value: 2.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:PLN03211 186 ISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  81 PRSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYPCPEHSNPFDFYMDLTSVDTQS---KEREIETSKrvQMIESA 157
Cdd:PLN03211 266 PSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANGVCQTdgvSEREKPNVK--QSLVAS 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023 158 YkkSAICHKTLKNIERMKHLKTLP---MVPFKTKDSPGV--------FSKLGVLLRRV---TRNLVRNKLAVITRLLQNL 223
Cdd:PLN03211 344 Y--NTLLAPKVKAAIEMSHFPQANarfVGSASTKEHRSSdrisistwFNQFSILLQRSlkeRKHESFNTLRVFQVIAAAL 421
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023 224 IMGLFLLFFVLRvrsnvlkgAIQDRVGLLY---QFVGATPYTgmlNAVNLFPVLRAVSDQESQDGLYQKWQMMLAYALHV 300
Cdd:PLN03211 422 LAGLMWWHSDFR--------DVQDRLGLLFfisIFWGVFPSF---NSVFVFPQERAIFVKERASGMYTLSSYFMARIVGD 490
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023 301 LPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIVNSVVALLSIAGVLVGsGFLrn 380
Cdd:PLN03211 491 LPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTG-GFY-- 567
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767915023 381 IQEMPIPFKIISYFTFQKYCSEILvVNEFYG----LNFTCGSSNVSVTTNPMCAFTQ 433
Cdd:PLN03211 568 VHKLPSCMAWIKYISTTFYSYRLL-INVQYGegkrISSLLGCSLPHGSDRASCKFVE 623
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
1-111 1.30e-25

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 104.76  E-value: 1.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:COG1131  116 LELFGLTDAADRKVGTLSGG-----MKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHY 190
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767915023  81 PrSELFQLFDKIAILSFGELIFCGTPAEMLD 111
Cdd:COG1131  191 L-EEAERLCDRVAIIDKGRIVADGTPDELKA 220
ABC2_membrane pfam01061
ABC-2 type transporter;
200-407 8.76e-19

ABC-2 type transporter;


Pssm-ID: 426023 [Multi-domain]  Cd Length: 204  Bit Score: 84.63  E-value: 8.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  200 LLRRVTRNLVRNKLAVITRLLQNLIMGLFLLFFVLRVRSnvlKGAIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAVSD 279
Cdd:pfam01061   1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGN---QQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  280 QESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIV 359
Cdd:pfam01061  78 RELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDA 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 767915023  360 NSVVALLSIAGVLVgSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVN 407
Cdd:pfam01061 158 SQLGPLVLLPLLLL-SGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
1-109 6.39e-08

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 54.36  E-value: 6.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNYSlGGIstgeRRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIhQ 80
Cdd:NF000106 129 LERFSLTEAAGRAAAKYS-GGM----RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTT-Q 202
                         90       100
                 ....*....|....*....|....*....
gi 767915023  81 PRSELFQLFDKIAILSFGELIFCGTPAEM 109
Cdd:NF000106 203 YMEEAEQLAHELTVIDRGRVIADGKVDEL 231
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
1-108 5.72e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 45.89  E-value: 5.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIvvlTI-- 78
Cdd:NF033858 382 LERFDLADVADALPDSLPLG-----IRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGV---TIfi 453
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767915023  79 --HqprselfqlF-------DKIAILSFGELIFCGTPAE 108
Cdd:NF033858 454 stH---------FmneaercDRISLMHAGRVLASDTPAA 483
 
Name Accession Description Interval E-value
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
3-474 2.94e-75

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 248.04  E-value: 2.94e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023    3 ELSLSHVADRLIGNYS-LGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQP 81
Cdd:TIGR00955 147 ALGLRKCANTRIGVPGrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQP 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   82 RSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYPCPEHSNPFDFYMDLTSVDtqsKEREIETSKRVQMIESAYKKS 161
Cdd:TIGR00955 227 SSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVI---PGSENESRERIEKICDSFAVS 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  162 AICHKTLKNIeRMKHLKTLPMV-----PFKTKDSPGVFSKLGVLLRRVTRNLVRNKLAVITRLLQNLIMGLF--LLFFVL 234
Cdd:TIGR00955 304 DIGRDMLVNT-NLWSGKAGGLVkdsenMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILigLIYLGQ 382
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  235 RVRSnvlKGaIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAVSDQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSV 314
Cdd:TIGR00955 383 GLTQ---KG-VQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSI 458
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  315 CYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIVNSVVALLSIAgVLVGSGFLRNIQEMPIPFKIISYF 394
Cdd:TIGR00955 459 TYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIP-FLLFGGFFINSDSIPVYFKWLSYL 537
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  395 TFQKYCSEILVVNEFYGL-NFTCGSSNvsvTTNPMCAFTQGIQfieKTCPGATSRFTMNFLILYSFIPALVILGIVVFKI 473
Cdd:TIGR00955 538 SWFRYGNEGLLINQWSDVdNIECTSAN---TTGPCPSSGEVIL---ETLSFRNADLYLDLIGLVILIFFFRLLAYFALRI 611

                  .
gi 767915023  474 R 474
Cdd:TIGR00955 612 R 612
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
2-104 3.15e-52

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: 175.92  E-value: 3.15e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   2 AELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQP 81
Cdd:cd03234  124 EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQP 203
                         90       100
                 ....*....|....*....|...
gi 767915023  82 RSELFQLFDKIAILSFGELIFCG 104
Cdd:cd03234  204 RSDLFRLFDRILLLSSGEIVYSG 226
PLN03211 PLN03211
ABC transporter G-25; Provisional
1-433 2.40e-42

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 159.27  E-value: 2.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:PLN03211 186 ISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  81 PRSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYPCPEHSNPFDFYMDLTSVDTQS---KEREIETSKrvQMIESA 157
Cdd:PLN03211 266 PSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANGVCQTdgvSEREKPNVK--QSLVAS 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023 158 YkkSAICHKTLKNIERMKHLKTLP---MVPFKTKDSPGV--------FSKLGVLLRRV---TRNLVRNKLAVITRLLQNL 223
Cdd:PLN03211 344 Y--NTLLAPKVKAAIEMSHFPQANarfVGSASTKEHRSSdrisistwFNQFSILLQRSlkeRKHESFNTLRVFQVIAAAL 421
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023 224 IMGLFLLFFVLRvrsnvlkgAIQDRVGLLY---QFVGATPYTgmlNAVNLFPVLRAVSDQESQDGLYQKWQMMLAYALHV 300
Cdd:PLN03211 422 LAGLMWWHSDFR--------DVQDRLGLLFfisIFWGVFPSF---NSVFVFPQERAIFVKERASGMYTLSSYFMARIVGD 490
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023 301 LPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIVNSVVALLSIAGVLVGsGFLrn 380
Cdd:PLN03211 491 LPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTG-GFY-- 567
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767915023 381 IQEMPIPFKIISYFTFQKYCSEILvVNEFYG----LNFTCGSSNVSVTTNPMCAFTQ 433
Cdd:PLN03211 568 VHKLPSCMAWIKYISTTFYSYRLL-INVQYGegkrISSLLGCSLPHGSDRASCKFVE 623
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
1-469 4.79e-42

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 160.27  E-value: 4.79e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023     1 MAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR-RNRIVVLTIH 79
Cdd:TIGR00956  189 MATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIY 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023    80 QPRSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYPCPEHSNPFDFymdLTSVdTQSKEREI--ETSKRV----QM 153
Cdd:TIGR00956  269 QCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADF---LTSL-TSPAERQIkpGYEKKVprtpQE 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   154 IESAYKKS-------AICHKTLKNIERMKHLKTLPMVPFKTKD------SPGVFSKLGVLLRRVTRNLVR---NKLAVIT 217
Cdd:TIGR00956  345 FETYWRNSpeyaqlmKEIDEYLDRCSESDTKEAYRESHVAKQSkrtrpsSPYTVSFSMQVKYCLARNFLRmkgNPSFTLF 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   218 RLLQNLIMGLFLLFFVLRVRSNVLKGAIqdRVGLLYQFVGATPYTGMLNAVNLFPVlRAVSDQESQDGLYQKWQMMLAYA 297
Cdd:TIGR00956  425 MVFGNIIMALILSSVFYNLPKNTSDFYS--RGGALFFAILFNAFSSLLEIASMYEA-RPIVEKHRKYALYHPSADAIASI 501
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   298 LHVLPFSVVATMIFSSVCYWTLGLHPEVARFGY-----FSAALLAPHL---IGEFLTLVLLGivqnpnivNSVVALLSIA 369
Cdd:TIGR00956  502 ISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFyllilFICTLAMSHLfrsIGAVTKTLSEA--------MTPAAILLLA 573
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   370 GVLVgSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVNEFYGLNFTC--------GSSNVSVtTNPMCA---------FT 432
Cdd:TIGR00956  574 LSIY-TGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGRRFECsqyvpsggGYDNLGV-TNKVCTvvgaepgqdYV 651
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 767915023   433 QGIQFIEKTCPGATSRFTMNFLILYSFIPALVILGIV 469
Cdd:TIGR00956  652 DGDDYLKLSFQYYNSHKWRNFGIIIGFTVFFFFVYIL 688
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
19-104 4.52e-33

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: 123.82  E-value: 4.52e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  19 LGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFG 98
Cdd:cd03213  109 LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQG 188

                 ....*.
gi 767915023  99 ELIFCG 104
Cdd:cd03213  189 RVIYFG 194
PLN03140 PLN03140
ABC transporter G family member; Provisional
4-410 2.54e-26

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 113.02  E-value: 2.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023    4 LSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVL-TIHQPR 82
Cdd:PLN03140  319 LGLDICKDTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLmSLLQPA 398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   83 SELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYPCPEHSNPFDFYMDLTS--------VDTQSKEREIETSKRVQMI 154
Cdd:PLN03140  399 PETFDLFDDIILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSkkdqeqywADRNKPYRYISVSEFAERF 478
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  155 ESAYKKSaichktlknieRMKHLKTLPMVPFKTKDSPGVFSKLGVLLRRVTRN--------LVRNKLAVITRLLQNLIMG 226
Cdd:PLN03140  479 KSFHVGM-----------QLENELSVPFDKSQSHKAALVFSKYSVPKMELLKAcwdkewllMKRNAFVYVFKTVQIIIVA 547
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  227 LFLLFFVLRVR---SNVLKGAIqdrvgllyqFVGATPYTGMLNAVNLFPVLRAVSDQ-----ESQDGLYQ-KWQMMLAYA 297
Cdd:PLN03140  548 AIASTVFLRTEmhtRNEEDGAL---------YIGALLFSMIINMFNGFAELALMIQRlpvfyKQRDLLFHpPWTFTLPTF 618
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  298 LHVLPFSVVATMIFSSVCYWTLGLHPEVARFgyFSAALLApHLIGEF---LTLVLLGIVQNPNIVNSVVALLSIAGVLVG 374
Cdd:PLN03140  619 LLGIPISIIESVVWVVITYYSIGFAPEASRF--FKQLLLV-FLIQQMaagIFRLIASVCRTMIIANTGGALVLLLVFLLG 695
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 767915023  375 sGFLRNIQEMPIPFKIISYFTFQKYCSEILVVNEFY 410
Cdd:PLN03140  696 -GFILPKGEIPNWWEWAYWVSPLSYGFNALAVNEMF 730
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
1-111 1.30e-25

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 104.76  E-value: 1.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:COG1131  116 LELFGLTDAADRKVGTLSGG-----MKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHY 190
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767915023  81 PrSELFQLFDKIAILSFGELIFCGTPAEMLD 111
Cdd:COG1131  191 L-EEAERLCDRVAIIDKGRIVADGTPDELKA 220
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
3-111 2.75e-23

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: 98.39  E-value: 2.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   3 ELSLSHVADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPr 82
Cdd:COG4555  119 LLGLEEFLDRRVGELS-----TGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIM- 192
                         90       100
                 ....*....|....*....|....*....
gi 767915023  83 SELFQLFDKIAILSFGELIFCGTPAEMLD 111
Cdd:COG4555  193 QEVEALCDRVVILHKGKVVAQGSLDELRE 221
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
1-111 2.74e-20

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: 90.10  E-value: 2.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDcmTANQIVVL--LVELAR-RNRIVVLT 77
Cdd:COG1120  122 LERTGLEHLADRPVDE-----LSGGERQRVLIARALAQEPPLLLLDEPTSHLD--LAHQLEVLelLRRLAReRGRTVVMV 194
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767915023  78 IHQPrsEL-FQLFDKIAILSFGELIFCGTPAEMLD 111
Cdd:COG1120  195 LHDL--NLaARYADRLVLLKDGRIVAQGPPEEVLT 227
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
4-428 1.19e-19

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 92.48  E-value: 1.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023     4 LSLSHVADRLIGnYSLGGISTGERRRVSIAAQLLQDPKVMLF-DEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPR 82
Cdd:TIGR00956  885 LEMESYADAVVG-VPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPS 963
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023    83 SELFQLFDKIAILSFG-ELIFCGTPAE----MLDFFNDCGYP-CPEHSNPFDFYMDLTSVDTqskereieTSKRVQMIES 156
Cdd:TIGR00956  964 AILFEEFDRLLLLQKGgQTVYFGDLGEnshtIINYFEKHGAPkCPEDANPAEWMLEVIGAAP--------GAHANQDYHE 1035
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   157 AYKKSAICHKTLKNIERM-KHLKTLPMVPFKTKDSPGVFSKLGVLLRRVTRNLV---RNKLAVITRLLQNLIMGLFLLFF 232
Cdd:TIGR00956 1036 VWRNSSEYQAVKNELDRLeAELSKAEDDNDPDALSKYAASLWYQFKLVLWRTFQqywRTPDYLYSKFFLTIFAALFIGFT 1115
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   233 VLRVRSNvLKGaIQDRVGLLYQFVgaTPYTGMLNA-VNLFPVLRAVSD-QESQDGLYQKWQMMLAYALHVLPFSVVATMI 310
Cdd:TIGR00956 1116 FFKVGTS-LQG-LQNQMFAVFMAT--VLFNPLIQQyLPPFVAQRDLYEvRERPSRTFSWLAFIAAQITVEIPYNLVAGTI 1191
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   311 FSSVCYWTLGLHPEVA-------RFGYFSAALLAPHLIgeFLTLVLLGIVQNPNIVN-SVVALLSIAGVLVGSGFLRNIQ 382
Cdd:TIGR00956 1192 FFFIWYYPVGFYWNASktgqvheRGVLFWLLSTMFFLY--FSTLGQMVISFNPNADNaAVLASLLFTMCLSFCGVLAPPS 1269
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 767915023   383 EMPiPFKIISY----FTfqkYCSEILVVNEFYGLNFTCGSSNVSVTTNPM 428
Cdd:TIGR00956 1270 RMP-GFWIFMYrcspFT---YLVQALLSTGLADVPVTCKVKELLTFNPPS 1315
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
1-110 2.89e-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: 86.62  E-value: 2.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIgnYSLggiSTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:COG1122  119 LELVGLEHLADRPP--HEL---SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHD 193
                         90       100       110
                 ....*....|....*....|....*....|
gi 767915023  81 PRsELFQLFDKIAILSFGELIFCGTPAEML 110
Cdd:COG1122  194 LD-LVAELADRVIVLDDGRIVADGTPREVF 222
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
3-108 5.45e-19

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: 85.63  E-value: 5.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   3 ELSLSHVADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELaRRNRIVVLTIHQPR 82
Cdd:cd03263  120 VLGLTDKANKRARTLS-----GGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMD 193
                         90       100
                 ....*....|....*....|....*.
gi 767915023  83 sELFQLFDKIAILSFGELIFCGTPAE 108
Cdd:cd03263  194 -EAEALCDRIAIMSDGKLRCIGSPQE 218
ABC2_membrane pfam01061
ABC-2 type transporter;
200-407 8.76e-19

ABC-2 type transporter;


Pssm-ID: 426023 [Multi-domain]  Cd Length: 204  Bit Score: 84.63  E-value: 8.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  200 LLRRVTRNLVRNKLAVITRLLQNLIMGLFLLFFVLRVRSnvlKGAIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAVSD 279
Cdd:pfam01061   1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGN---QQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  280 QESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIV 359
Cdd:pfam01061  78 RELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDA 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 767915023  360 NSVVALLSIAGVLVgSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVN 407
Cdd:pfam01061 158 SQLGPLVLLPLLLL-SGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
19-99 1.04e-18

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: 83.06  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  19 LGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPrSELFQLFDKIAILSFG 98
Cdd:cd00267   78 VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDP-ELAELAADRVIVLKDG 156

                 .
gi 767915023  99 E 99
Cdd:cd00267  157 K 157
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
19-104 1.25e-18

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 83.83  E-value: 1.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  19 LGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAIL-SF 97
Cdd:cd03232  106 LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLkRG 185

                 ....*..
gi 767915023  98 GELIFCG 104
Cdd:cd03232  186 GKTVYFG 192
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
1-104 2.42e-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: 2.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDcmTANQIVVL--LVELAR-RNRIVVLT 77
Cdd:cd03214   82 LELLGLAHLADRPFNE-----LSGGERQRVLLARALAQEPPILLLDEPTSHLD--IAHQIELLelLRRLAReRGKTVVMV 154
                         90       100
                 ....*....|....*....|....*...
gi 767915023  78 IHQPrsEL-FQLFDKIAILSFGELIFCG 104
Cdd:cd03214  155 LHDL--NLaARYADRVILLKDGRIVAQG 180
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
12-104 1.22e-17

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 81.15  E-value: 1.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  12 RLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVL-TIHQPRSELFQLFD 90
Cdd:cd03233  109 RCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFvSLYQASDEIYDLFD 188
                         90
                 ....*....|....
gi 767915023  91 KIAILSFGELIFCG 104
Cdd:cd03233  189 KVLVLYEGRQIYYG 202
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
6-111 5.03e-17

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 80.41  E-value: 5.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   6 LSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI-HQpRSE 84
Cdd:COG1127  131 LPGAADKMPSE-----LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVtHD-LDS 204
                         90       100
                 ....*....|....*....|....*..
gi 767915023  85 LFQLFDKIAILSFGELIFCGTPAEMLD 111
Cdd:COG1127  205 AFAIADRVAVLADGKIIAEGTPEELLA 231
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
5-109 1.31e-16

daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]


Pssm-ID: 130256 [Multi-domain]  Cd Length: 302  Bit Score: 80.13  E-value: 1.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023    5 SLSHVADRLIGNYSlGGIstgeRRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSE 84
Cdd:TIGR01188 113 ELGEAADRPVGTYS-GGM----RRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHY-MEE 186
                          90       100
                  ....*....|....*....|....*
gi 767915023   85 LFQLFDKIAILSFGELIFCGTPAEM 109
Cdd:TIGR01188 187 ADKLCDRIAIIDHGRIIAEGTPEEL 211
PLN03140 PLN03140
ABC transporter G family member; Provisional
1-331 1.44e-16

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 82.97  E-value: 1.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023    1 MAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTAnQIVVLLVelarRN-----RIVV 75
Cdd:PLN03140  999 MELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA-AIVMRTV----RNtvdtgRTVV 1073
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   76 LTIHQPRSELFQLFDKIAILSF-GELIFCGT----PAEMLDFFNDC-GYP-CPEHSNPFDFYMDLTSVDTQSKeREIETS 148
Cdd:PLN03140 1074 CTIHQPSIDIFEAFDELLLMKRgGQVIYSGPlgrnSHKIIEYFEAIpGVPkIKEKYNPATWMLEVSSLAAEVK-LGIDFA 1152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  149 KRvqmiesaYKKSAICHktlKNIERMKHLKTLPM----VPFKTKDSPGVFSKLGVLL--------RRVTRNLVRNKLAVI 216
Cdd:PLN03140 1153 EH-------YKSSSLYQ---RNKALVKELSTPPPgasdLYFATQYSQSTWGQFKSCLwkqwwtywRSPDYNLVRFFFTLA 1222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  217 TRLlqnLIMGLFLLFFVLRVRSNVLKGAIqdrvGLLYqfvGATPYTGMLNAVNLFPVL---RAVSDQESQDGLYQKWQMM 293
Cdd:PLN03140 1223 AAL---MVGTIFWKVGTKRSNANDLTMVI----GAMY---AAVLFVGINNCSTVQPMVaveRTVFYRERAAGMYSALPYA 1292
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 767915023  294 LAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYF 331
Cdd:PLN03140 1293 IAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWF 1330
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
4-109 1.77e-16

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: 78.18  E-value: 1.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   4 LSLSHVADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRS 83
Cdd:cd03265  119 VGLLEAADRLVKTYS-----GGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYME 193
                         90       100
                 ....*....|....*....|....*.
gi 767915023  84 ELFQLFDKIAILSFGELIFCGTPAEM 109
Cdd:cd03265  194 EAEQLCDRVAIIDHGRIIAEGTPEEL 219
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
1-111 2.24e-16

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 78.53  E-value: 2.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLigNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:COG1137  121 LEEFGITHLRKSK--AYSLSG---GERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHN 195
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767915023  81 PRsELFQLFDKIAILSFGELIFCGTPAEMLD 111
Cdd:COG1137  196 VR-ETLGICDRAYIISEGKVLAEGTPEEILN 225
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
23-100 3.09e-16

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: 76.28  E-value: 3.09e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPrSELFQLFDKIAILSFGEL 100
Cdd:cd03230   97 SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHIL-EEAERLCDRVAILNNGRI 173
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
6-104 5.53e-16

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 76.80  E-value: 5.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   6 LSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPrSEL 85
Cdd:cd03235  122 LSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDL-GLV 195
                         90
                 ....*....|....*....
gi 767915023  86 FQLFDKIAILSfGELIFCG 104
Cdd:cd03235  196 LEYFDRVLLLN-RTVVASG 213
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
23-108 7.61e-16

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: 76.84  E-value: 7.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR-RNRIVVLTIHQPrsELF-QLFDKIAILSFGEL 100
Cdd:cd03256  146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReEGITVIVSLHQV--DLArEYADRIVGLKDGRI 223

                 ....*...
gi 767915023 101 IFCGTPAE 108
Cdd:cd03256  224 VFDGPPAE 231
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
2-110 1.17e-15

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 76.04  E-value: 1.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   2 AELSLSHVADRLigNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQP 81
Cdd:cd03218  119 EEFHITHLRKSK--ASSLSG---GERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNV 193
                         90       100
                 ....*....|....*....|....*....
gi 767915023  82 RsELFQLFDKIAILSFGELIFCGTPAEML 110
Cdd:cd03218  194 R-ETLSITDRAYIIYEGKVLAEGTPEEIA 221
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
1-99 1.51e-15

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: 75.20  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIgnYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:cd03225  119 LELVGLEGLRDRSP--FTLSG---GQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHD 193
                         90
                 ....*....|....*....
gi 767915023  81 PrSELFQLFDKIAILSFGE 99
Cdd:cd03225  194 L-DLLLELADRVIVLEDGK 211
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
1-104 1.89e-15

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: 74.92  E-value: 1.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNYSlGGIstgeRRRVSIAAQLLQDPKVMLFDEPTTGLDcmTANQIVV--LLVELArRNRIVVLTI 78
Cdd:cd03264  115 LELVNLGDRAKKKIGSLS-GGM----RRRVGIAQALVGDPSILIVDEPTAGLD--PEERIRFrnLLSELG-EDRIVILST 186
                         90       100
                 ....*....|....*....|....*.
gi 767915023  79 HQpRSELFQLFDKIAILSFGELIFCG 104
Cdd:cd03264  187 HI-VEDVESLCNQVAVLNKGKLVFEG 211
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
6-108 4.15e-15

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: 74.78  E-value: 4.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   6 LSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSeL 85
Cdd:cd03219  133 LADLADRPAGE-----LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDV-V 206
                         90       100
                 ....*....|....*....|...
gi 767915023  86 FQLFDKIAILSFGELIFCGTPAE 108
Cdd:cd03219  207 MSLADRVTVLDQGRVIAEGTPDE 229
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
1-111 5.75e-15

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: 74.08  E-value: 5.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:cd03261  121 LEAVGLRGAEDLYPAE-----LSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTH 195
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767915023  81 PRSELFQLFDKIAILSFGELIFCGTPAEMLD 111
Cdd:cd03261  196 DLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
1-110 8.28e-15

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 275199 [Multi-domain]  Cd Length: 239  Bit Score: 73.85  E-value: 8.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023    1 MAELSLSHVADRLigNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:TIGR04406 120 LEEFQISHLRDNK--AMSLSG---GERRRVEIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHN 194
                          90       100       110
                  ....*....|....*....|....*....|
gi 767915023   81 PRsELFQLFDKIAILSFGELIFCGTPAEML 110
Cdd:TIGR04406 195 VR-ETLDICDRAYIISDGKVLAEGTPAEIV 223
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
20-104 9.04e-15

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: 73.17  E-value: 9.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  20 GGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGE 99
Cdd:cd03266  135 GGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHI-MQEVERLCDRVVVLHRGR 213

                 ....*
gi 767915023 100 LIFCG 104
Cdd:cd03266  214 VVYEG 218
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1-110 1.94e-14

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 72.81  E-value: 1.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI-H 79
Cdd:COG1119  127 LELLGLAHLADRPFGT-----LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVtH 201
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767915023  80 QPrSELFQLFDKIAILSFGELIFCGTPAEML 110
Cdd:COG1119  202 HV-EEIPPGITHVLLLKDGRVVAAGPKEEVL 231
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
21-110 5.76e-14

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 74.03  E-value: 5.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  21 GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELArRNRIVVLTIHQPRseLFQLFDKIAILSFGEL 100
Cdd:COG4987  471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLA--GLERMDRILVLEDGRI 547
                         90
                 ....*....|
gi 767915023 101 IFCGTPAEML 110
Cdd:COG4987  548 VEQGTHEELL 557
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
23-111 7.99e-14

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: 73.40  E-value: 7.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIF 102
Cdd:COG1123  144 SGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVE 223

                 ....*....
gi 767915023 103 CGTPAEMLD 111
Cdd:COG1123  224 DGPPEEILA 232
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
22-109 1.15e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 71.26  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQprSELFQLF-DKIAILSFGEL 100
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKI 215

                 ....*....
gi 767915023 101 IFCGTPAEM 109
Cdd:PRK13639 216 IKEGTPKEV 224
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
1-81 2.17e-13

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: 69.04  E-value: 2.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPTTGLDcmTANQIVV--LLVELARRNRIVVLTI 78
Cdd:COG4133  116 LEAVGLAGLADLPVRQLS-----AGQKRRVALARLLLSPAPLWLLDEPFTALD--AAGVALLaeLIAAHLARGGAVLLTT 188

                 ...
gi 767915023  79 HQP 81
Cdd:COG4133  189 HQP 191
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
21-114 1.55e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 68.34  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  21 GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGEL 100
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKI 254
                         90
                 ....*....|....
gi 767915023 101 IFCGTPAEMldFFN 114
Cdd:PRK13631 255 LKTGTPYEI--FTD 266
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
3-102 4.41e-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: 65.32  E-value: 4.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   3 ELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpR 82
Cdd:cd03268  113 VVGLKDSAKKKVKGFSLG-----MKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHL-L 186
                         90       100
                 ....*....|....*....|
gi 767915023  83 SELFQLFDKIAILSFGELIF 102
Cdd:cd03268  187 SEIQKVADRIGIINKGKLIE 206
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
23-108 7.45e-12

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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275314 [Multi-domain]  Cd Length: 277  Bit Score: 65.55  E-value: 7.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR-RNRIVVLTIHQpRSELFQLFDKIAILSFGELI 101
Cdd:TIGR04521 144 SGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHS-MEDVAEYADRVIVMHKGKIV 222

                  ....*..
gi 767915023  102 FCGTPAE 108
Cdd:TIGR04521 223 LDGTPRE 229
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
23-111 9.44e-12

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 66.85  E-value: 9.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRivvLTIhqprseLF---------QLFDKIA 93
Cdd:COG1123  406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELG---LTY------LFishdlavvrYIADRVA 476
                         90
                 ....*....|....*...
gi 767915023  94 ILSFGELIFCGTPAEMLD 111
Cdd:COG1123  477 VMYDGRIVEDGPTEEVFA 494
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
1-110 1.15e-11

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 64.53  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADrlignySLG-GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIH 79
Cdd:PRK10895 122 MEEFHIEHLRD------SMGqSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767915023  80 QPRsELFQLFDKIAILSFGELIFCGTPAEML 110
Cdd:PRK10895 196 NVR-ETLAVCERAYIVSQGHLIAHGTPTEIL 225
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
4-104 1.32e-11

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: 63.85  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   4 LSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRS 83
Cdd:cd03297  119 LGLDHLLNR-----YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLS 193
                         90       100
                 ....*....|....*....|.
gi 767915023  84 ELFQLFDKIAILSFGELIFCG 104
Cdd:cd03297  194 EAEYLADRIVVMEDGRLQYIG 214
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
21-99 2.19e-11

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: 62.59  E-value: 2.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  21 GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRI-VVLTIHQPRsELFQLFDKIAILSFGE 99
Cdd:cd03229  100 GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGItVVLVTHDLD-EAARLADRVVVLRDGK 178
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
20-110 2.60e-11

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 65.62  E-value: 2.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  20 GG--ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELArRNRIVVLTIHqpRSELFQLFDKIAILSF 97
Cdd:PRK11160 472 GGrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITH--RLTGLEQFDRICVMDN 548
                         90
                 ....*....|...
gi 767915023  98 GELIFCGTPAEML 110
Cdd:PRK11160 549 GQIIEQGTHQELL 561
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
23-100 3.09e-11

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 62.53  E-value: 3.09e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL-ARRNRIVVLTIHQPRsELFQLFDKIAILSFGEL 100
Cdd:COG4619  132 SGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPE-QIERVADRVLTLEAGRL 209
cbiO PRK13637
energy-coupling factor transporter ATPase;
22-108 3.10e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 63.91  E-value: 3.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELI 101
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224

                 ....*..
gi 767915023 102 FCGTPAE 108
Cdd:PRK13637 225 LQGTPRE 231
PQQ_ABC_ATP TIGR03864
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ...
22-110 5.44e-11

ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 274822 [Multi-domain]  Cd Length: 236  Bit Score: 62.69  E-value: 5.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVL-TIHqprselfqLFDKIA------I 94
Cdd:TIGR03864 133 LNGGHRRRVEIARALLHRPALLLLDEPTVGLDPASRAAITAHVRALARDQGLSVLwATH--------LVDEIEasdrlvV 204
                          90
                  ....*....|....*.
gi 767915023   95 LSFGELIFCGTPAEML 110
Cdd:TIGR03864 205 LHRGRVLADGAAAELR 220
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1-110 5.94e-11

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 62.72  E-value: 5.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHq 80
Cdd:PRK11231 123 MEQTRINHLADRRLTD-----LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH- 196
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767915023  81 prsELFQ---LFDKIAILSFGELIFCGTPAEML 110
Cdd:PRK11231 197 ---DLNQasrYCDHLVVLANGHVMAQGTPEEVM 226
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
1-113 8.00e-11

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: 64.05  E-value: 8.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023    1 MAELS--LSHVADRLIGnyslggistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRI-VVLT 77
Cdd:TIGR03269 155 MVQLShrITHIARDLSG---------GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIsMVLT 225
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767915023   78 IHQPRSeLFQLFDKIAILSFGELIFCGTPAEMLDFF 113
Cdd:TIGR03269 226 SHWPEV-IEDLSDKAIWLENGEIKEEGTPDEVVAVF 260
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
23-104 8.90e-11

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: 60.79  E-value: 8.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELArRNRIVVLTIHQPRSelFQLFDKIAILSFGELIF 102
Cdd:cd03247  100 SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLTG--IEHMDKILFLENGKIIM 176

                 ..
gi 767915023 103 CG 104
Cdd:cd03247  177 QG 178
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
6-110 9.34e-11

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 61.83  E-value: 9.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   6 LSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI-HQpRSE 84
Cdd:cd03258  130 LEDKADAYPAQ-----LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLItHE-MEV 203
                         90       100
                 ....*....|....*....|....*.
gi 767915023  85 LFQLFDKIAILSFGELIFCGTPAEML 110
Cdd:cd03258  204 VKRICDRVAVMEKGEVVEEGTVEEVF 229
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
22-104 2.07e-10

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: 60.81  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR-RNRIVVLTIHQPRsELFQLFDKIAILSFGEL 100
Cdd:cd03267  154 LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNReRGTTVLLTSHYMK-DIEALARRVLVIDKGRL 232

                 ....
gi 767915023 101 IFCG 104
Cdd:cd03267  233 LYDG 236
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
9-110 2.10e-10

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 61.22  E-value: 2.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   9 VADRLigNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTiHQPRsELFQL 88
Cdd:PRK14246 143 VYDRL--NSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNPQ-QVARV 218
                         90       100
                 ....*....|....*....|..
gi 767915023  89 FDKIAILSFGELIFCGTPAEML 110
Cdd:PRK14246 219 ADYVAFLYNGELVEWGSSNEIF 240
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
23-100 2.53e-10

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: 60.20  E-value: 2.53e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR-RNRIVVLTIHQPrsELFQLFDKIAILSFGEL 100
Cdd:cd03255  142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDP--ELAEYADRIIELRDGKI 218
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
21-95 4.10e-10

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: 61.92  E-value: 4.10e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915023   21 GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELArRNRIVVLTIHQPrsELFQLFDKIAIL 95
Cdd:TIGR02857 458 GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRL--ALAALADRIVVL 529
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
22-110 4.20e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 60.63  E-value: 4.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLtIHQPRSELFQLF-DKIAILSFGEL 100
Cdd:PRK13636 142 LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTII-IATHDIDIVPLYcDNVFVMKEGRV 220
                         90
                 ....*....|
gi 767915023 101 IFCGTPAEML 110
Cdd:PRK13636 221 ILQGNPKEVF 230
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
23-78 4.60e-10

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 59.44  E-value: 4.60e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI 78
Cdd:cd03257  147 SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFI 202
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
20-110 6.38e-10

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: 61.39  E-value: 6.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  20 GGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELArRNRIVVLTIHqpRSELFQLFDKIAILSFGE 99
Cdd:COG2274  610 SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAH--RLSTIRLADRIIVLDKGR 686
                         90
                 ....*....|.
gi 767915023 100 LIFCGTPAEML 110
Cdd:COG2274  687 IVEDGTHEELL 697
cbiO PRK13643
energy-coupling factor transporter ATPase;
22-123 6.65e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 60.13  E-value: 6.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELI 101
Cdd:PRK13643 145 LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHL-MDDVADYADYVYLLEKGHII 223
                         90       100
                 ....*....|....*....|....*..
gi 767915023 102 FCGTPAEM---LDFF--NDCGYPCPEH 123
Cdd:PRK13643 224 SCGTPSDVfqeVDFLkaHELGVPKATH 250
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1-50 7.48e-10

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: 57.27  E-value: 7.48e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 767915023    1 MAELSLSHVADRLIGNYSlGGISTGERRRVSIAAQLLQDPKVMLFDEPTT 50
Cdd:pfam00005 102 LEKLGLGDLADRPVGERP-GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
22-99 1.02e-09

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: 57.39  E-value: 1.02e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELaRRNRIVVLTIHqpRSELFQLFDKIAILSFGE 99
Cdd:cd03228   97 LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL-AKGKTVIVIAH--RLSTIRDADRIIVLDDGR 171
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
23-116 1.14e-09

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: 59.19  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL-ARRNRIVVLTIHQPrSELFQLFDKIAILSFGELI 101
Cdd:cd03294  162 SGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDL-DEALRLGDRIAIMKDGRLV 240
                         90       100
                 ....*....|....*....|....
gi 767915023 102 FCGTPAEML---------DFFNDC 116
Cdd:cd03294  241 QVGTPEEILtnpandyvrEFFRGV 264
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
22-111 1.37e-09

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: 58.40  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELArRNRIVVLTIHQPRSELFQlfDKIAILSFGELI 101
Cdd:cd03253  138 LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVNA--DKIIVLKDGRIV 214
                         90
                 ....*....|
gi 767915023 102 FCGTPAEMLD 111
Cdd:cd03253  215 ERGTHEELLA 224
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
4-118 1.44e-09

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 60.80  E-value: 1.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023     4 LSLSHVADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRS 83
Cdd:TIGR01257 2058 LGLSLYADRLAGTYS-----GGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHS-ME 2131
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 767915023    84 ELFQLFDKIAILSFGELIFCGTPAEMLDFFNDcGY 118
Cdd:TIGR01257 2132 ECEALCTRLAIMVKGAFQCLGTIQHLKSKFGD-GY 2165
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
9-123 1.78e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 58.31  E-value: 1.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   9 VADRLigNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTiHQPrSELFQL 88
Cdd:PRK14267 139 VKDRL--NDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSP-AQAARV 214
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767915023  89 FDKIAILSFGELIFCGtPAEMLdFFNdcgypcPEH 123
Cdd:PRK14267 215 SDYVAFLYLGKLIEVG-PTRKV-FEN------PEH 241
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
1-79 1.92e-09

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: 57.27  E-value: 1.92e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915023   1 MAELSLSHVADRLigNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIH 79
Cdd:cd03226  111 LKDLDLYALKERH--PLSLSG---GQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
1-79 1.93e-09

cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 57.05  E-value: 1.93e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915023    1 MAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIH 79
Cdd:TIGR01166 112 LTAVGASGLRERPTHC-----LSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
22-110 1.97e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 58.46  E-value: 1.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFqLFDKIAILSFGELI 101
Cdd:PRK13632 143 LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLI 221

                 ....*....
gi 767915023 102 FCGTPAEML 110
Cdd:PRK13632 222 AQGKPKEIL 230
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
1-110 2.18e-09

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 58.24  E-value: 2.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLignY-SLGGistGERRRVSIA---AQLLQD---PKVMLFDEPTTGLDcmTANQIVVL--LVELARRN 71
Cdd:PRK13548 119 LAQVDLAHLAGRD---YpQLSG---GEQQRVQLArvlAQLWEPdgpPRWLLLDEPTSALD--LAHQHHVLrlARQLAHER 190
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767915023  72 R---IVVLtiHqprsELFQ--LF-DKIAILSFGELIFCGTPAEML 110
Cdd:PRK13548 191 GlavIVVL--H----DLNLaaRYaDRIVLLHQGRLVADGTPAEVL 229
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
23-96 2.56e-09

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: 57.10  E-value: 2.56e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILS 96
Cdd:cd03293  133 SGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS 206
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
9-101 3.32e-09

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 57.19  E-value: 3.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   9 VADRLIGnyslGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLT--IHQPRSelf 86
Cdd:cd03260  133 VKDRLHA----LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQAAR--- 205
                         90
                 ....*....|....*
gi 767915023  87 qLFDKIAILSFGELI 101
Cdd:cd03260  206 -VADRTAFLLNGRLV 219
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
1-80 4.67e-09

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 56.95  E-value: 4.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRlignYSLGgISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:PRK11124 126 LERLRLKPYADR----FPLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
22-110 6.25e-09

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 56.94  E-value: 6.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPrSELFQLFDKIAILSFGELI 101
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDI-DLIYEISDAVYVLRQGQIL 215

                 ....*....
gi 767915023 102 FCGTPAEML 110
Cdd:PRK13638 216 THGAPGEVF 224
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
9-129 7.80e-09

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 56.32  E-value: 7.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   9 VADRLigNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELarRNRIVVLTIHQPRSELFQL 88
Cdd:PRK14239 138 VKDRL--HDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRI 213
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767915023  89 FDKIAILSFGELIFCGTPAEMldFFNdcgypcPEHSNPFDF 129
Cdd:PRK14239 214 SDRTGFFLDGDLIEYNDTKQM--FMN------PKHKETEDY 246
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1-108 8.21e-09

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 56.66  E-value: 8.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:COG4152  114 LERLGLGDRANKKVEELSKG-----NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ 188
                         90       100
                 ....*....|....*....|....*....
gi 767915023  81 PRS-ElfQLFDKIAILSFGELIFCGTPAE 108
Cdd:COG4152  189 MELvE--ELCDRIVIINKGRKVLSGSVDE 215
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
22-111 9.31e-09

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 56.76  E-value: 9.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELI 101
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHF-MEEAERLCDRLCVLEAGRKI 251
                         90
                 ....*....|
gi 767915023 102 FCGTPAEMLD 111
Cdd:PRK13536 252 AEGRPHALID 261
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
1-110 1.18e-08

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 56.77  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:PRK09536 124 MERTGVAQFADR-----PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHD 198
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767915023  81 prSELFQLF-DKIAILSFGELIFCGTPAEML 110
Cdd:PRK09536 199 --LDLAARYcDELVLLADGRVRAAGPPADVL 227
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
19-111 1.20e-08

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 56.35  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  19 LGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFG 98
Cdd:PRK13537 136 VGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHF-MEEAERLCDRLCVIEEG 214
                         90
                 ....*....|...
gi 767915023  99 ELIFCGTPAEMLD 111
Cdd:PRK13537 215 RKIAEGAPHALIE 227
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
22-81 1.23e-08

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: 57.37  E-value: 1.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVElARRNRIVVLTIHQP 81
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
22-116 1.54e-08

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 57.33  E-value: 1.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023    22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELfqLFDKIAILSFGELI 101
Cdd:TIGR01257 1062 LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADL--LGDRIAIISQGRLY 1139
                           90
                   ....*....|....*
gi 767915023   102 FCGTPAemldFFNDC 116
Cdd:TIGR01257 1140 CSGTPL----FLKNC 1150
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
4-110 1.54e-08

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 56.26  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   4 LSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI-HQPR 82
Cdd:COG4148  121 LGIGHLLDRRPAT-----LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVsHSLD 195
                         90       100
                 ....*....|....*....|....*...
gi 767915023  83 sELFQLFDKIAILSFGELIFCGTPAEML 110
Cdd:COG4148  196 -EVARLADHVVLLEQGRVVASGPLAEVL 222
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
20-104 1.58e-08

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: 54.81  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  20 GGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI-HQPrSELFQLFDKIAILSFG 98
Cdd:cd03298  127 GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVtHQP-EDAKRLAQRVVFLDNG 205

                 ....*.
gi 767915023  99 ELIFCG 104
Cdd:cd03298  206 RIAAQG 211
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
22-98 1.65e-08

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 56.64  E-value: 1.65e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFG 98
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
22-101 1.73e-08

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: 53.59  E-value: 1.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRsELFQLFDKIAILSFGELI 101
Cdd:cd03216   83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLD-EVFEIADRVTVLRDGRVV 161
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
1-68 1.79e-08

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 55.02  E-value: 1.79e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915023   1 MAELSLSHVADRlignYSLGgISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELA 68
Cdd:COG4161  126 LARLRLTDKADR----FPLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELS 188
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
22-80 1.95e-08

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: 54.46  E-value: 1.95e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:cd03262  136 LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
cbiO PRK13646
energy-coupling factor transporter ATPase;
22-118 2.44e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 55.17  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELA-RRNRIVVLTIHQpRSELFQLFDKIAILSFGEL 100
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHD-MNEVARYADEVIVMKEGSI 224
                         90
                 ....*....|....*...
gi 767915023 101 IFCGTPAEMldfFNDCGY 118
Cdd:PRK13646 225 VSQTSPKEL---FKDKKK 239
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
16-111 2.56e-08

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 55.81  E-value: 2.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  16 NYSLG---GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKI 92
Cdd:PRK10070 156 NYAHSypdELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRI 235
                         90
                 ....*....|....*....
gi 767915023  93 AILSFGELIFCGTPAEMLD 111
Cdd:PRK10070 236 AIMQNGEVVQVGTPDEILN 254
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
1-82 3.49e-08

lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 53.89  E-value: 3.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023    1 MAELSLSHVADRLigNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRI-VVLTIH 79
Cdd:TIGR02211 123 YEMLEKVGLEHRI--NHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTsFLVVTH 200

                  ...
gi 767915023   80 QPR 82
Cdd:TIGR02211 201 DLE 203
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
21-111 3.65e-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: 3.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  21 GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELArRNRIVVLTIHqpRSELFQLFDKIAILSFGEL 100
Cdd:cd03252  138 GLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAH--RLSTVKNADRIIVMEKGRI 214
                         90
                 ....*....|.
gi 767915023 101 IFCGTPAEMLD 111
Cdd:cd03252  215 VEQGSHDELLA 225
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
22-109 3.95e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 54.64  E-value: 3.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR-RNRIVVLTIHQpRSELFQLFDKIAILSFGEL 100
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHS-MEDAARYADQIVVMHKGTV 224

                 ....*....
gi 767915023 101 IFCGTPAEM 109
Cdd:PRK13634 225 FLQGTPREI 233
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
1-98 4.01e-08

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: 53.27  E-value: 4.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:cd03231  110 LARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQ 184
                         90
                 ....*....|....*...
gi 767915023  81 PrseLFQLFDKIAILSFG 98
Cdd:cd03231  185 D---LGLSEAGARELDLG 199
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
4-100 5.26e-08

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II 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. In members of 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: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 52.82  E-value: 5.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   4 LSLShVADRLIGNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNR-IVVLTIHQPr 82
Cdd:cd03215   91 LDLS-VAENIALSSLLSG---GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKaVLLISSELD- 165
                         90
                 ....*....|....*...
gi 767915023  83 sELFQLFDKIAILSFGEL 100
Cdd:cd03215  166 -ELLGLCDRILVMYEGRI 182
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
1-109 6.39e-08

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 54.36  E-value: 6.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNYSlGGIstgeRRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIhQ 80
Cdd:NF000106 129 LERFSLTEAAGRAAAKYS-GGM----RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTT-Q 202
                         90       100
                 ....*....|....*....|....*....
gi 767915023  81 PRSELFQLFDKIAILSFGELIFCGTPAEM 109
Cdd:NF000106 203 YMEEAEQLAHELTVIDRGRVIADGKVDEL 231
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
23-79 9.54e-08

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 53.55  E-value: 9.54e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL-ARRNRIVVLTIH 79
Cdd:COG4586  156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSH 213
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
23-79 9.64e-08

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 53.57  E-value: 9.64e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARR-NRIVVLTIH 79
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITH 220
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
22-70 1.07e-07

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 52.51  E-value: 1.07e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARR 70
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRL 194
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
22-80 1.11e-07

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 53.05  E-value: 1.11e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
9-110 1.70e-07

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 52.22  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   9 VADRLigNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTiHQPrSELFQL 88
Cdd:PRK14247 136 VKDRL--DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVT-HFP-QQAARI 211
                         90       100
                 ....*....|....*....|..
gi 767915023  89 FDKIAILSFGELIFCGTPAEML 110
Cdd:PRK14247 212 SDYVAFLYKGQIVEWGPTREVF 233
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
21-79 2.01e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 52.40  E-value: 2.01e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767915023  21 GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIH 79
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
cbiO PRK13640
energy-coupling factor transporter ATPase;
22-109 2.05e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 52.49  E-value: 2.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELfQLFDKIAILSFGELI 101
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLL 222

                 ....*...
gi 767915023 102 FCGTPAEM 109
Cdd:PRK13640 223 AQGSPVEI 230
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
21-79 2.09e-07

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 51.64  E-value: 2.09e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767915023  21 GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIH 79
Cdd:cd03292  136 ELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
22-110 2.15e-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: 53.27  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQivvllvelarrnriVVLTIHQPRSELFQLF------------ 89
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVD--------------VTHSILKAREEMEQTFiivshdmdfvld 493
                          90       100
                  ....*....|....*....|...
gi 767915023   90 --DKIAILSFGELIFCGTPAEML 110
Cdd:TIGR03269 494 vcDRAALMRDGKIVKIGDPEEIV 516
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
22-104 2.36e-07

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 51.13  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELI 101
Cdd:cd03269  129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAV 207

                 ...
gi 767915023 102 FCG 104
Cdd:cd03269  208 LYG 210
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
6-110 2.71e-07

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 51.71  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   6 LSHVADRLIGnySLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDcmTANQIVVL-LVE-LARRNRIVVLTIHQPRS 83
Cdd:PRK10575 137 LKPLAHRLVD--SLSG---GERQRAWIAMLVAQDSRCLLLDEPTSALD--IAHQVDVLaLVHrLSQERGLTVIAVLHDIN 209
                         90       100
                 ....*....|....*....|....*..
gi 767915023  84 ELFQLFDKIAILSFGELIFCGTPAEML 110
Cdd:PRK10575 210 MAARYCDYLVALRGGEMIAQGTPAELM 236
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
4-109 3.23e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 51.73  E-value: 3.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   4 LSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARR-NRIVVLTIHQpR 82
Cdd:PRK13652 125 LGLEELRDRVPHH-----LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQ-L 198
                         90       100
                 ....*....|....*....|....*..
gi 767915023  83 SELFQLFDKIAILSFGELIFCGTPAEM 109
Cdd:PRK13652 199 DLVPEMADYIYVMDKGRIVAYGTVEEI 225
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
1-82 3.53e-07

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: 50.43  E-value: 3.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023    1 MAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:TIGR01189 112 LAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQ 186

                  ..
gi 767915023   81 PR 82
Cdd:TIGR01189 187 DL 188
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
23-78 3.69e-07

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: 52.38  E-value: 3.69e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI 78
Cdd:COG4172  158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLI 213
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
23-81 3.90e-07

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 50.57  E-value: 3.90e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQP 81
Cdd:PRK13538 131 SAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
6-81 3.97e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 50.64  E-value: 3.97e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915023   6 LSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDcmTANQIVVLLVELARRNR--IVVLTIHQP 81
Cdd:PRK13539 117 LAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPTAALD--AAAVALFAELIRAHLAQggIVIAATHIP 187
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
4-100 4.29e-07

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: 50.72  E-value: 4.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   4 LSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRS 83
Cdd:cd03301  118 LQIEHLLDRKPKQ-----LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQV 192
                         90
                 ....*....|....*..
gi 767915023  84 ELFQLFDKIAILSFGEL 100
Cdd:cd03301  193 EAMTMADRIAVMNDGQI 209
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
22-111 5.72e-07

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: 50.42  E-value: 5.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELI 101
Cdd:cd03296  137 LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIE 216
                         90
                 ....*....|
gi 767915023 102 FCGTPAEMLD 111
Cdd:cd03296  217 QVGTPDEVYD 226
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
23-111 6.63e-07

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: 50.31  E-value: 6.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELArRNRIVVLTIHqpRSELFQLFDKIAILSFGELIF 102
Cdd:cd03251  140 SGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAH--RLSTIENADRIVVLEDGKIVE 216

                 ....*....
gi 767915023 103 CGTPAEMLD 111
Cdd:cd03251  217 RGTHEELLA 225
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
22-109 7.32e-07

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 51.26  E-value: 7.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELI 101
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216

                 ....*...
gi 767915023 102 FCGTPAEM 109
Cdd:PRK11432 217 QIGSPQEL 224
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
19-79 7.80e-07

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 50.65  E-value: 7.80e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915023  19 LGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIH 79
Cdd:PRK15056 140 IGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
cbiO PRK13649
energy-coupling factor transporter ATPase;
22-109 7.97e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 50.51  E-value: 7.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHqprselfqLFDKIA-------I 94
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH--------LMDDVAnyadfvyV 217
                         90
                 ....*....|....*
gi 767915023  95 LSFGELIFCGTPAEM 109
Cdd:PRK13649 218 LEKGKLVLSGKPKDI 232
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
18-98 8.30e-07

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 51.27  E-value: 8.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  18 SLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNR-IVVLTIHQPrsELFQLFDKIAILS 96
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKgIIIISSEMP--ELLGITDRILVMS 465

                 ..
gi 767915023  97 FG 98
Cdd:PRK10982 466 NG 467
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
22-109 8.66e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 50.47  E-value: 8.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLfDKIAILSFGELI 101
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEA-DRIIVMDSGKVV 223

                 ....*...
gi 767915023 102 FCGTPAEM 109
Cdd:PRK13633 224 MEGTPKEI 231
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
22-80 8.71e-07

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 50.13  E-value: 8.71e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
22-111 9.03e-07

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: 49.93  E-value: 9.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELI 101
Cdd:cd03300  131 LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
                         90
                 ....*....|
gi 767915023 102 FCGTPAEMLD 111
Cdd:cd03300  211 QIGTPEEIYE 220
hmuV PRK13547
heme ABC transporter ATP-binding protein;
22-110 9.90e-07

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 50.21  E-value: 9.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIA---AQL------LQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI-HQPRSELfQLFDK 91
Cdd:PRK13547 146 LSGGELARVQFArvlAQLwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPNLAA-RHADR 224
                         90
                 ....*....|....*....
gi 767915023  92 IAILSFGELIFCGTPAEML 110
Cdd:PRK13547 225 IAMLADGAIVAHGAPADVL 243
cbiO PRK13641
energy-coupling factor transporter ATPase;
22-109 9.91e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 50.21  E-value: 9.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELI 101
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHN-MDDVAEYADDVLVLEHGKLI 224

                 ....*...
gi 767915023 102 FCGTPAEM 109
Cdd:PRK13641 225 KHASPKEI 232
cbiO PRK13645
energy-coupling factor transporter ATPase;
22-110 1.02e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 50.39  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELI 101
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230

                 ....*....
gi 767915023 102 FCGTPAEML 110
Cdd:PRK13645 231 SIGSPFEIF 239
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
16-100 1.08e-06

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 50.94  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  16 NYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNrIVVLTIHQPRSELFQLFDKIAIL 95
Cdd:PRK09700 404 NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEIITVCDRIAVF 482

                 ....*
gi 767915023  96 SFGEL 100
Cdd:PRK09700 483 CEGRL 487
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
18-110 1.15e-06

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 49.93  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  18 SLGGISTGERRRVSIAAQLLQ-------DPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLfD 90
Cdd:PRK03695 123 SVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHA-D 201
                         90       100
                 ....*....|....*....|
gi 767915023  91 KIAILSFGELIFCGTPAEML 110
Cdd:PRK03695 202 RVWLLKQGKLLASGRRDEVL 221
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
21-118 1.18e-06

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: 49.06  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  21 GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGEL 100
Cdd:cd03217  104 GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDGRI 183
                         90
                 ....*....|....*...
gi 767915023 101 IFCGtPAEMLDFFNDCGY 118
Cdd:cd03217  184 VKSG-DKELALEIEKKGY 200
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
23-111 1.24e-06

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: 49.35  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRnRIVVLTIHQPRSELFQLFDKIAILSFGELIF 102
Cdd:cd03224  134 SGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVL 212

                 ....*....
gi 767915023 103 CGTPAEMLD 111
Cdd:cd03224  213 EGTAAELLA 221
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
4-109 1.35e-06

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 50.41  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   4 LSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARR-NRIVVLTIHQpR 82
Cdd:PRK11000 121 LQLAHLLDR-----KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHD-Q 194
                         90       100
                 ....*....|....*....|....*..
gi 767915023  83 SELFQLFDKIAILSFGELIFCGTPAEM 109
Cdd:PRK11000 195 VEAMTLADKIVVLDAGRVAQVGKPLEL 221
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
6-101 1.50e-06

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 50.18  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   6 LSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI-HQpRSE 84
Cdd:PRK11153 130 LSDKADRYPAQ-----LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLItHE-MDV 203
                         90
                 ....*....|....*..
gi 767915023  85 LFQLFDKIAILSFGELI 101
Cdd:PRK11153 204 VKRICDRVAVIDAGRLV 220
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
23-100 1.56e-06

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: 48.37  E-value: 1.56e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPrsELFQLFDKIAILSFGEL 100
Cdd:cd03246   98 SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP--ETLASADRILVLEDGRV 173
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
22-53 1.67e-06

ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 49.41  E-value: 1.67e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 53
Cdd:COG4598  155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
19-115 1.86e-06

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: 50.21  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   19 LGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNrIVVLTIHQPRSELFQLFDKIAILSFG 98
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEG-VAIIVVSSELAEVLGLSDRVLVIGEG 479
                          90
                  ....*....|....*..
gi 767915023   99 ELifCGtpaemlDFFND 115
Cdd:TIGR02633 480 KL--KG------DFVNH 488
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
23-123 1.87e-06

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 49.69  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRI-VVLTIHQP---RselfQLFDKIAILSFG 98
Cdd:COG1135  142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLtIVLITHEMdvvR----RICDRVAVLENG 217
                         90       100
                 ....*....|....*....|....*
gi 767915023  99 ELIFCGTpaeMLDFFNDcgypcPEH 123
Cdd:COG1135  218 RIVEQGP---VLDVFAN-----PQS 234
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
22-110 2.09e-06

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 49.42  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELI 101
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238

                 ....*....
gi 767915023 102 FCGTPAEML 110
Cdd:PRK15093 239 ETAPSKELV 247
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
3-79 2.91e-06

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: 49.78  E-value: 2.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   3 ELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC---MTANQIVvllVELARRNRIVVLTIH 79
Cdd:COG1245  199 KLGLENILDRDISE-----LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIyqrLNVARLI---RELAEEGKYVLVVEH 270
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
22-79 2.91e-06

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 48.97  E-value: 2.91e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARR-NRIVVLTIH 79
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITH 212
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
22-111 3.14e-06

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 48.17  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQprselFQLFDKIAilsfGELI 101
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE-----IGFAEKVA----SRLI 207
                         90
                 ....*....|....*...
gi 767915023 102 FC--------GTPAEMLD 111
Cdd:PRK09493 208 FIdkgriaedGDPQVLIK 225
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
20-100 3.31e-06

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 49.28  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  20 GGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNrIVVLTIHQPRSELFQLFDKIAILSFGE 99
Cdd:PRK15439 402 RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQGE 480

                 .
gi 767915023 100 L 100
Cdd:PRK15439 481 I 481
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
1-79 3.49e-06

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: 48.52  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC---MTANQIVvllVELARRNRIVVLT 77
Cdd:cd03236  124 VDQLELRHVLDRNIDQ-----LSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrLNAARLI---RELAEDDNYVLVV 195

                 ..
gi 767915023  78 IH 79
Cdd:cd03236  196 EH 197
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
23-111 4.16e-06

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 48.07  E-value: 4.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNR-IVVLTiHqprsEL-F--QLFDKIAILSFG 98
Cdd:COG1126  138 SGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMtMVVVT-H----EMgFarEVADRVVFMDGG 212
                         90
                 ....*....|...
gi 767915023  99 ELIFCGTPAEMLD 111
Cdd:COG1126  213 RIVEEGPPEEFFE 225
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
22-109 4.19e-06

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 48.68  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELI 101
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229

                 ....*...
gi 767915023 102 FCGTPAEM 109
Cdd:PRK11607 230 QIGEPEEI 237
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
22-78 4.85e-06

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 47.77  E-value: 4.85e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI 78
Cdd:PRK11248 129 LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLI 185
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
1-110 6.34e-06

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 47.67  E-value: 6.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:PRK10253 128 MQATGITHLADQ-----SVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLH 202
                         90       100       110
                 ....*....|....*....|....*....|
gi 767915023  81 PRSELFQLFDKIAILSFGELIFCGTPAEML 110
Cdd:PRK10253 203 DLNQACRYASHLIALREGKIVAQGAPKEIV 232
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
20-111 8.54e-06

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: 46.83  E-value: 8.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  20 GGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELaRRNRIVVLTIHQPRSELFQlfDKIAILSFGE 99
Cdd:cd03254  138 GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKNA--DKILVLDDGK 214
                         90
                 ....*....|..
gi 767915023 100 LIFCGTPAEMLD 111
Cdd:cd03254  215 IIEEGTHDELLA 226
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
6-108 1.04e-05

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 46.91  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   6 LSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSEL 85
Cdd:PRK11300 143 LLEHANRQAGN-----LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLV 217
                         90       100
                 ....*....|....*....|...
gi 767915023  86 FQLFDKIAILSFGELIFCGTPAE 108
Cdd:PRK11300 218 MGISDRIYVVNQGTPLANGTPEE 240
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
11-53 1.07e-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: 1.07e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 767915023  11 DRLIGNYSlgGistGERRRVSIAAQLLQDPKVMLFDEPTTGLD 53
Cdd:COG0488  147 DRPVSELS--G---GWRRRVALARALLSEPDLLLLDEPTNHLD 184
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
3-53 1.15e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 47.88  E-value: 1.15e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767915023   3 ELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 53
Cdd:PRK13409 199 RLGLENILDRDISE-----LSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
1-101 1.23e-05

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 47.69  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGL-DCMTANQIVVlLVELARRNRIVVLTIH 79
Cdd:PRK10762 126 LARLNLRFSSDKLVGELSIG-----EQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRV-IRELKSQGRGIVYISH 199
                         90       100
                 ....*....|....*....|..
gi 767915023  80 QPRsELFQLFDKIAILSFGELI 101
Cdd:PRK10762 200 RLK-EIFEICDDVTVFRDGQFI 220
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
10-81 1.31e-05

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 47.80  E-value: 1.31e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915023  10 ADRLigNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQP 81
Cdd:PRK10535 135 EDRV--EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
22-105 1.31e-05

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 46.54  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRI-VVLTIHQPRSELfQLFDKIAILSFGEL 100
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGItVVVTLHQVDYAL-RYCERIVALRQGHV 231

                 ....*
gi 767915023 101 IFCGT 105
Cdd:PRK09984 232 FYDGS 236
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
22-110 1.44e-05

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 46.71  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELI 101
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229

                 ....*....
gi 767915023 102 FCGTPAEML 110
Cdd:PRK15112 230 ERGSTADVL 238
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
20-151 1.93e-05

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: 46.39  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  20 GGI--STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV--ELARRNRIVVLTihqpRSELFQLFDKIAIL 95
Cdd:cd03291  156 GGItlSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVckLMANKTRILVTS----KMEHLKKADKILIL 231
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  96 SFGELIFCGTPAEMLDFFndcgypcPEHSNPFdfyMDLTSVDTQSKERE----IETSKRV 151
Cdd:cd03291  232 HEGSSYFYGTFSELQSLR-------PDFSSKL---MGYDTFDQFSAERRnsilTETLRRF 281
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
22-100 2.04e-05

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: 45.92  E-value: 2.04e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTiHqpRSELFQLFDKIAILSFGEL 100
Cdd:cd03248  151 LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIA-H--RLSTVERADQILVLDGGRI 226
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
5-96 2.17e-05

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 47.33  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023    5 SLSHVADRLIGNYSlGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSE 84
Cdd:PTZ00265 1343 SLPNKYDTNVGPYG-KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIA 1420
                          90
                  ....*....|..
gi 767915023   85 LFQLFDKIAILS 96
Cdd:PTZ00265 1421 SIKRSDKIVVFN 1432
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
22-106 2.67e-05

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: 45.18  E-value: 2.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVElARRNRIvVLTI-HqpRSELFQLFDKIAILSFGEL 100
Cdd:cd03244  140 LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCT-VLTIaH--RLDTIIDSDRILVLDKGRV 215

                 ....*.
gi 767915023 101 IFCGTP 106
Cdd:cd03244  216 VEFDSP 221
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
23-78 3.05e-05

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 46.24  E-value: 3.05e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI 78
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFI 482
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
11-108 3.10e-05

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 46.38  E-value: 3.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  11 DRLIGNYSlGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTiHQprseLFQL-- 88
Cdd:PRK11174 476 DTPIGDQA-AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQ----LEDLaq 549
                         90       100
                 ....*....|....*....|
gi 767915023  89 FDKIAILSFGELIFCGTPAE 108
Cdd:PRK11174 550 WDQIWVMQDGQIVQQGDYAE 569
cbiO PRK13642
energy-coupling factor transporter ATPase;
22-125 3.19e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 45.47  E-value: 3.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQlFDKIAILSFGELI 101
Cdd:PRK13642 141 LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEII 219
                         90       100
                 ....*....|....*....|....*..
gi 767915023 102 FCGTPAEMLDFFND---CGYPCPEHSN 125
Cdd:PRK13642 220 KEAAPSELFATSEDmveIGLDVPFSSN 246
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
23-104 3.98e-05

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 46.00  E-value: 3.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIF 102
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544

                 ..
gi 767915023 103 CG 104
Cdd:PRK10261 545 IG 546
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
6-110 4.11e-05

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 46.17  E-value: 4.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   6 LSHVADRLIG-NYSLggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELaRRNRIVVLTIHqpRSE 84
Cdd:PRK11176 466 MDNGLDTVIGeNGVL--LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAH--RLS 540
                         90       100
                 ....*....|....*....|....*.
gi 767915023  85 LFQLFDKIAILSFGELIFCGTPAEML 110
Cdd:PRK11176 541 TIEKADEILVVEDGEIVERGTHAELL 566
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
23-70 4.38e-05

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 45.83  E-value: 4.38e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARR 70
Cdd:COG4172  427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQRE 474
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
23-110 4.71e-05

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: 44.84  E-value: 4.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDcmTANQIVVL-LVELARRNRIVVLTIHqpRSELFQLFDKIAILSFGELI 101
Cdd:cd03249  141 SGGQKQRIAIARALLRNPKILLLDEATSALD--AESEKLVQeALDRAMKGRTTIVIAH--RLSTIRNADLIAVLQNGQVV 216

                 ....*....
gi 767915023 102 FCGTPAEML 110
Cdd:cd03249  217 EQGTHDELM 225
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
22-53 5.43e-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: 45.70  E-value: 5.43e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 767915023   22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 53
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
2-101 5.61e-05

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 45.67  E-value: 5.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   2 AELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQp 81
Cdd:PRK11288 121 AREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHR- 199
                         90       100
                 ....*....|....*....|
gi 767915023  82 RSELFQLFDKIAILSFGELI 101
Cdd:PRK11288 200 MEEIFALCDAITVFKDGRYV 219
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
1-108 5.72e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 45.89  E-value: 5.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIvvlTI-- 78
Cdd:NF033858 382 LERFDLADVADALPDSLPLG-----IRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGV---TIfi 453
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767915023  79 --HqprselfqlF-------DKIAILSFGELIFCGTPAE 108
Cdd:NF033858 454 stH---------FmneaercDRISLMHAGRVLASDTPAA 483
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
22-143 6.75e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 44.70  E-value: 6.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELArrNRIVVLTIHQPRSELFQLFDKIAILSFGELI 101
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLV 241
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767915023 102 FCGtPAEMLdffndcgYPCPEHSNPFDFYMDLTSvDTQSKER 143
Cdd:PRK14271 242 EEG-PTEQL-------FSSPKHAETARYVAGLSG-DVKDAKR 274
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
23-81 7.50e-05

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 43.79  E-value: 7.50e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRI-VVLTIHQP 81
Cdd:COG2401  138 STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGItLVVATHHY 197
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
20-109 8.49e-05

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 45.29  E-value: 8.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023    20 GGI--STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV--VLLVELARRNRIVVLTihqpRSELFQLFDKIAIL 95
Cdd:TIGR01271  545 GGItlSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFesCLCKLMSNKTRILVTS----KLEHLKKADKILLL 620
                           90
                   ....*....|....
gi 767915023    96 SFGELIFCGTPAEM 109
Cdd:TIGR01271  621 HEGVCYFYGTFSEL 634
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
22-110 8.63e-05

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 45.01  E-value: 8.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELI 101
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNR-FDEIPDFVQFAGVLADCTLA 214

                 ....*....
gi 767915023 102 FCGTPAEML 110
Cdd:PRK10938 215 ETGEREEIL 223
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
23-79 9.29e-05

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: 42.44  E-value: 9.29e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDcMTAnqIVVLLVELARRNRIVVLTIH 79
Cdd:cd03221   72 SGGEKMRLALAKLLLENPNLLLLDEPTNHLD-LES--IEALEEALKEYPGTVILVSH 125
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
22-82 1.04e-04

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 43.61  E-value: 1.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARR-NRIVVLTIHQPR 82
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQ 208
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
22-53 1.30e-04

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 44.34  E-value: 1.30e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 53
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
23-110 1.32e-04

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 44.39  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELaRRNRIVVL------TIhqprselfQLFDKIAILS 96
Cdd:COG1132  478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIViahrlsTI--------RNADRILVLD 548
                         90
                 ....*....|....
gi 767915023  97 FGELIFCGTPAEML 110
Cdd:COG1132  549 DGRIVEQGTHEELL 562
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
11-52 1.36e-04

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 44.25  E-value: 1.36e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767915023  11 DRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGL 52
Cdd:COG3845  136 DAKVED-----LSVGEQQRVEILKALYRGARILILDEPTAVL 172
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
22-72 1.47e-04

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 44.18  E-value: 1.47e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELaRRNR 72
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGR 521
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
22-79 2.04e-04

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 42.55  E-value: 2.04e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIH 79
Cdd:PRK10908 138 LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
22-99 2.06e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 43.10  E-value: 2.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGE 99
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
4-101 2.10e-04

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 43.32  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   4 LSLSHVADRLIGnySLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRS 83
Cdd:PRK11144 116 LGIEPLLDRYPG--SLSG---GEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLD 190
                         90
                 ....*....|....*...
gi 767915023  84 ELFQLFDKIAILSFGELI 101
Cdd:PRK11144 191 EILRLADRVVVLEQGKVK 208
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
22-111 2.24e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 42.80  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELfQLFDKIAILSFGELI 101
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVL 217
                         90
                 ....*....|
gi 767915023 102 FCGTPAEMLD 111
Cdd:PRK13647 218 AEGDKSLLTD 227
PLN03232 PLN03232
ABC transporter C family member; Provisional
22-109 2.70e-04

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 43.81  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQprSELFQLFDKIAILSFGELI 101
Cdd:PLN03232  741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQ--LHFLPLMDRIILVSEGMIK 818

                  ....*...
gi 767915023  102 FCGTPAEM 109
Cdd:PLN03232  819 EEGTFAEL 826
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
20-106 2.81e-04

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 42.01  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  20 GG--ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELArrNRIVVLTI-HQPRSELfqLFDKIAILS 96
Cdd:cd03369  122 GGlnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEF--TNSTILTIaHRLRTII--DYDKILVMD 197
                         90
                 ....*....|
gi 767915023  97 FGELIFCGTP 106
Cdd:cd03369  198 AGEVKEYDHP 207
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
20-95 3.67e-04

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: 41.69  E-value: 3.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  20 GGI--STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV--VLLVELaRRNRIVVLTIHQPrsELFQLFDKIAIL 95
Cdd:cd03250  124 KGInlSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFenCILGLL-LNNKTRILVTHQL--QLLPHADQIVVL 200
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-109 3.79e-04

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 42.70  E-value: 3.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   1 MAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLdcmTANQIVVLLV---ELARRNRIVVLT 77
Cdd:COG1129  125 LARLGLDIDPDTPVGDLSVA-----QQQLVEIARALSRDARVLILDEPTASL---TEREVERLFRiirRLKAQGVAIIYI 196
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767915023  78 IHqpR-SELFQLFDKIAILSFGELIFCGTPAEM 109
Cdd:COG1129  197 SH--RlDEVFEIADRVTVLRDGRLVGTGPVAEL 227
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
4-110 4.31e-04

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 43.01  E-value: 4.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023     4 LSLSHV-------ADRLIGNYSLGG--ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANqivvlLVELARRNRI- 73
Cdd:TIGR00957 1395 LELAHLktfvsalPDKLDHECAEGGenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN-----LIQSTIRTQFe 1469
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 767915023    74 --VVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEML 110
Cdd:TIGR00957 1470 dcTVLTIAH-RLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
29-109 4.43e-04

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 42.71  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  29 RVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLtIHQPRSELFQLFDKIAILSFGELIFCGTPAE 108
Cdd:COG3845  410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL-ISEDLDEILALSDRIAVMYEGRIVGEVPAAE 488

                 .
gi 767915023 109 M 109
Cdd:COG3845  489 A 489
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
16-111 4.48e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 42.05  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  16 NYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLfDKIAIL 95
Cdd:PRK13648 137 DYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEA-DHVIVM 215
                         90
                 ....*....|....*.
gi 767915023  96 SFGELIFCGTPAEMLD 111
Cdd:PRK13648 216 NKGTVYKEGTPTEIFD 231
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
23-67 4.77e-04

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 42.26  E-value: 4.77e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL 67
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDL 200
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
22-105 4.89e-04

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 42.54  E-value: 4.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELI 101
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248

                 ....
gi 767915023 102 FCGT 105
Cdd:PRK10261 249 ETGS 252
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
21-82 4.99e-04

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 41.59  E-value: 4.99e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767915023  21 GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDcMTANQIVVLLV-ELARRNRIVVLTIHQPR 82
Cdd:COG0396  140 GFSGGEKKRNEILQMLLLEPKLAILDETDSGLD-IDALRIVAEGVnKLRSPDRGILIITHYQR 201
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
20-110 5.28e-04

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 41.40  E-value: 5.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  20 GGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELaRRNRIVVLTIHQPRSELFQLFDKIAILSFGE 99
Cdd:PRK11614 136 GTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGH 214
                         90
                 ....*....|.
gi 767915023 100 LIFCGTPAEML 110
Cdd:PRK11614 215 VVLEDTGDALL 225
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
16-82 5.83e-04

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 40.77  E-value: 5.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915023  16 NYSLGGISTGERRRVSIAAQLLQDPK--VMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPR 82
Cdd:cd03238   82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
17-97 6.26e-04

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 40.42  E-value: 6.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  17 YSLGGISTGERRRVSIAAQL----LQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPrsELFQLFDKI 92
Cdd:cd03227   73 FTRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKL 150

                 ....*
gi 767915023  93 AILSF 97
Cdd:cd03227  151 IHIKK 155
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
4-53 9.16e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 41.72  E-value: 9.16e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767915023   4 LSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 53
Cdd:PRK13409 441 LQLERLLDK-----NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
18-100 9.46e-04

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 41.45  E-value: 9.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  18 SLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNrIVVLTIHQPRSELFQLFDKIAILSF 97
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLVMHE 480

                 ...
gi 767915023  98 GEL 100
Cdd:PRK13549 481 GKL 483
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
5-80 1.08e-03

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 41.94  E-value: 1.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915023    5 SLSHVADRLIGNySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL-ARRNRIVVLTIHQ 80
Cdd:PTZ00265  564 ALPDKYETLVGS-NASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHR 639
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
10-76 1.15e-03

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 41.44  E-value: 1.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915023  10 ADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVL 76
Cdd:PRK11288 390 REQLIMN-----LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLF 451
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
11-53 1.17e-03

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 41.14  E-value: 1.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 767915023  11 DRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 53
Cdd:PRK10762 390 EQAIGL-----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
22-100 1.34e-03

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 40.43  E-value: 1.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGEL 100
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
4-80 1.37e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 39.93  E-value: 1.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915023   4 LSLSHVADrlignYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 80
Cdd:PRK13540 115 FSLEHLID-----YPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
6-108 1.81e-03

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 40.45  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   6 LSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSEL 85
Cdd:PRK10851 126 LAHLADRYPAQ-----LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEA 200
                         90       100
                 ....*....|....*....|...
gi 767915023  86 FQLFDKIAILSFGELIFCGTPAE 108
Cdd:PRK10851 201 MEVADRVVVMSQGNIEQAGTPDQ 223
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
1-53 2.11e-03

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: 39.70  E-value: 2.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767915023   1 MAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 53
Cdd:cd03237  100 AKPLQIEQILDREVPE-----LSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
22-75 2.27e-03

ATP-binding cassette domain 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 more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 39.09  E-value: 2.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC---MTANQIVVLLVELARRNRIVV 75
Cdd:cd03222   72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrLNAARAIRRLSEEGKKTALVV 128
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
23-69 2.40e-03

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 40.07  E-value: 2.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR 69
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQR 209
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
4-53 3.24e-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: 40.15  E-value: 3.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767915023   4 LSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 53
Cdd:COG1245  443 LGLEKLLDK-----NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
30-101 3.62e-03

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 39.62  E-value: 3.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915023  30 VSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNR-IVVLTihqprSEL---FQLFDKIAILSFGELI 101
Cdd:COG1129  403 VVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKaVIVIS-----SELpelLGLSDRILVMREGRIV 473
PLN03130 PLN03130
ABC transporter C family member; Provisional
22-75 4.16e-03

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 39.72  E-value: 4.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767915023   22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV--VLLVELARRNRIVV 75
Cdd:PLN03130  741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdkCIKDELRGKTRVLV 796
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
22-109 5.28e-03

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 38.59  E-value: 5.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023  22 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELI 101
Cdd:PRK11831 144 LSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIV 223

                 ....*...
gi 767915023 102 FCGTPAEM 109
Cdd:PRK11831 224 AHGSAQAL 231
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
23-53 5.75e-03

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 39.28  E-value: 5.75e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLD 53
Cdd:COG0488  434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
6-108 7.23e-03

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 38.77  E-value: 7.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915023   6 LSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSEL 85
Cdd:PRK09452 134 LEEFAQRKPHQ-----LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEA 208
                         90       100
                 ....*....|....*....|...
gi 767915023  86 FQLFDKIAILSFGELIFCGTPAE 108
Cdd:PRK09452 209 LTMSDRIVVMRDGRIEQDGTPRE 231
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
23-53 7.39e-03

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 37.98  E-value: 7.39e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 767915023  23 STGERRRVSIAAQLLQDPKVMLFDEPTTGLD 53
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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