|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
109-611 |
2.95e-69 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 235.71 E-value: 2.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 109 LSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRdPSGL--SGDILVNGKPRPAN-FKCTSGYVPQNDVVMHTVTVRDN 184
Cdd:TIGR00955 41 LKNVSGVAKPGeLLAVMGSSGAGKTTLMNALAFRS-PKGVkgSGSVLLNGMPIDAKeMRAISAYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 185 LEFSAALRLPMTITRDEKRRRINEVLELLHLDKEQNTK----PRSKEL----RKRTSIAVELIAEHPILFLDDPTTDLDL 256
Cdd:TIGR00955 120 LMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRigvpGRVKGLsggeRKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 257 TTTTYVISVLRRMSMKGKTIIFSINQPQYSIFRFFDSLTLVASGKLMFHGPARDALEYFTSAGYQYESHNNPADFFLDVI 336
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 337 ngglcdTEEDGHEAGNYEELferkyqatKKLANMYAQSRLHSDT-RARLDQLLGQQQLDRNSAVETTC--VTPFWHQLMW 413
Cdd:TIGR00955 280 ------AVIPGSENESRERI--------EKICDSFAVSDIGRDMlVNTNLWSGKAGGLVKDSENMEGIgyNASWWTQFYA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 414 ITYQSFKN-IRGFLLVTAKQAVITATlAALVGIAFQILKNGCIEVYIRAGLLYLL---TIFQciTSVSAGELFVIDRDRF 489
Cdd:TIGR00955 346 LLKRSWLSvLRDPLLLKVRLIQTMMT-AILIGLIYLGQGLTQKGVQNINGALFLFltnMTFQ--NVFPVINVFTAELPVF 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 490 LHEHTSGYYRVSSYFFGKLLAELIPRRLLPSTIVLITYFIAGVKTSMSSFFAMLFTVMMLAYSASSLPLSIGAGENAVAV 569
Cdd:TIGR00955 423 LRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSM 502
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1958676843 570 PTLFVTIYFVFMLFFSGLSLYSGSLLPQLSWIQYFNIPHYGF 611
Cdd:TIGR00955 503 ALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGN 544
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
102-612 |
1.50e-52 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 191.25 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 102 QTRVIerLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPSGLSGDILVN-GKPRPANFKCTsGYVPQNDVVMHTV 179
Cdd:PLN03211 79 QERTI--LNGVTGMASPGeILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANnRKPTKQILKRT-GFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 180 TVRDNLEFSAALRLPMTITRDEKRRRINEVLELLHLDKEQNT-------KPRSKELRKRTSIAVELIAEHPILFLDDPTT 252
Cdd:PLN03211 156 TVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTiignsfiRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 253 DLDLTTTTYVISVLRRMSMKGKTIIFSINQPQYSIFRFFDSLTLVASGKLMFHGPARDALEYFTSAGYQYESHNNPADFF 332
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 333 LDVINgGLCDTeeDG---HEAGNYEELFERKYQATkkLANMYAQSRLHSDTRARLDQLLGQQQLDRNSAVETTCVTPFWH 409
Cdd:PLN03211 316 LDLAN-GVCQT--DGvseREKPNVKQSLVASYNTL--LAPKVKAAIEMSHFPQANARFVGSASTKEHRSSDRISISTWFN 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 410 QLMWITYQSFKNIR--GFLLVTAKQAVITATLAALVGIAFQILkngciEVYIRAGLLYLLTIFQCITSvSAGELFVIDRD 487
Cdd:PLN03211 391 QFSILLQRSLKERKheSFNTLRVFQVIAAALLAGLMWWHSDFR-----DVQDRLGLLFFISIFWGVFP-SFNSVFVFPQE 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 488 R--FLHEHTSGYYRVSSYFFGKLLAELIPRRLLPSTIVLITYFIAGVKTSMSSFFAMLFTVMMLAYSASSLPLSIGAGEN 565
Cdd:PLN03211 465 RaiFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIM 544
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1958676843 566 AVAVPTLFVTIYFVFMLFFSGlsLYSGSLLPQLSWIQYFNIPHYGFK 612
Cdd:PLN03211 545 DAKKASTIVTVTMLAFVLTGG--FYVHKLPSCMAWIKYISTTFYSYR 589
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
80-306 |
1.02e-45 |
|
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: 160.02 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 80 AVLSFHNISYreTVQSGfPLRQQTRVierLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPSGLSGDILVNGKPR 158
Cdd:cd03213 2 VTLSFRNLTV--TVKSS-PSKSGKQL---LKNVSGKAKPGeLTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 159 PA-NFKCTSGYVPQNDVVMHTVTVRDNLEFSAALrlpmtitrdekrRRInevlellhldkeqntkprSKELRKRTSIAVE 237
Cdd:cd03213 76 DKrSFRKIIGYVPQDDILHPTLTVRETLMFAAKL------------RGL------------------SGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958676843 238 LIAEHPILFLDDPTTDLDLTTTTYVISVLRRMSMKGKTIIFSINQPQYSIFRFFDSLTLVASGKLMFHG 306
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
69-606 |
5.60e-42 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 163.36 E-value: 5.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 69 NTSDPETLTKEAVLSFHNISYRETVQSGfplrqqTRVIerLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDpSGL 147
Cdd:TIGR00956 747 DEKDMEKESGEDIFHWRNLTYEVKIKKE------KRVI--LNNVDGWVKPGtLTALMGASGAGKTTLLNVLAERVT-TGV 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 148 --SGDILVNGKPRPANFKCTSGYVPQNDVVMHTVTVRDNLEFSAALRLPMTITRDEKRRRINEVLELLHLDKEQNT---- 221
Cdd:TIGR00956 818 itGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAvvgv 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 222 --KPRSKELRKRTSIAVELIAEhP--ILFLDDPTTDLDLTTTTYVISVLRRMSMKGKTIIFSINQPQYSIFRFFDSLTLV 297
Cdd:TIGR00956 898 pgEGLNVEQRKRLTIGVELVAK-PklLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLL 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 298 ASG-KLMFHGP----ARDALEYFTSAG-YQYESHNNPADFFLDVINGGL-CDTEEDGHEAGNYEELFERKYQATKKLANM 370
Cdd:TIGR00956 977 QKGgQTVYFGDlgenSHTIINYFEKHGaPKCPEDANPAEWMLEVIGAAPgAHANQDYHEVWRNSSEYQAVKNELDRLEAE 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 371 YAQSRLHSDTRARLdqllgqqqldrnsavetTCVTPFWHQ---LMWITYQSF-----KNIRGFLLVTAKQAVITATLAAl 442
Cdd:TIGR00956 1057 LSKAEDDNDPDALS-----------------KYAASLWYQfklVLWRTFQQYwrtpdYLYSKFFLTIFAALFIGFTFFK- 1118
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 443 VGIAFQILKNGCIEVYIraGLLYLLTIFQCITsvsagELFVIDRDRF-LHEHTSGYYRVSSYFFGKLLAElIPRRLLPST 521
Cdd:TIGR00956 1119 VGTSLQGLQNQMFAVFM--ATVLFNPLIQQYL-----PPFVAQRDLYeVRERPSRTFSWLAFIAAQITVE-IPYNLVAGT 1190
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 522 I-VLITYFIAGV--------KTSMSSFFAMLFTVMMLAYSASSLPLSIGAGENAvAVPTLFVTIYFVFMLFFSGLsLYSG 592
Cdd:TIGR00956 1191 IfFFIWYYPVGFywnasktgQVHERGVLFWLLSTMFFLYFSTLGQMVISFNPNA-DNAAVLASLLFTMCLSFCGV-LAPP 1268
|
570
....*....|....
gi 1958676843 593 SLLPQLsWIQYFNI 606
Cdd:TIGR00956 1269 SRMPGF-WIFMYRC 1281
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
81-300 |
2.80e-37 |
|
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: 136.99 E-value: 2.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 81 VLSFHNISYreTVqsgfPLRQQTRVIerLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPSGLSGDILVNGKPRP 159
Cdd:cd03232 3 VLTWKNLNY--TV----PVKGGKRQL--LNNISGYVKPGtLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 160 ANFKCTSGYVPQNDVVMHTVTVRDNLEFSAALRlpmtitrdekrrrinevlELlhldkeqntkprSKELRKRTSIAVELI 239
Cdd:cd03232 75 KNFQRSTGYVEQQDVHSPNLTVREALRFSALLR------------------GL------------SVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958676843 240 AEHPILFLDDPTTDLDLTTTTYVISVLRRMSMKGKTIIFSINQPQYSIFRFFDSLTLVASG 300
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRG 185
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
82-606 |
7.77e-34 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 138.44 E-value: 7.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 82 LSFHNISY-----RETVQSGFPlrqQTRvIERLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPSGLSGDILVNG 155
Cdd:PLN03140 868 MSFDDVNYfvdmpAEMKEQGVT---EDR-LQLLREVTGAFRPGvLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISG 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 156 KP-RPANFKCTSGYVPQNDVVMHTVTVRDNLEFSAALRLPMTITRDEKRRRINEVLELLHLDKEQNT-------KPRSKE 227
Cdd:PLN03140 944 FPkKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAivglpgvTGLSTE 1023
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 228 LRKRTSIAVELIAEHPILFLDDPTTDLDLTTTTYVISVLRRMSMKGKTIIFSINQPQYSIFRFFDSLTLVA-SGKLMFHG 306
Cdd:PLN03140 1024 QRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKrGGQVIYSG 1103
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 307 P----ARDALEYFTS--AGYQYESHNNPADFFLDVIN-GGLCDTEEDGHEAGNYEELFERKYQATKKLA-------NMYA 372
Cdd:PLN03140 1104 PlgrnSHKIIEYFEAipGVPKIKEKYNPATWMLEVSSlAAEVKLGIDFAEHYKSSSLYQRNKALVKELStpppgasDLYF 1183
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 373 QSRLHSDTRARLdqllgqqqldrnsaveTTCVtpfWHQlmWITY---QSFKNIRGFLLVTAkqAVITATLAALVGIAfqi 449
Cdd:PLN03140 1184 ATQYSQSTWGQF----------------KSCL---WKQ--WWTYwrsPDYNLVRFFFTLAA--ALMVGTIFWKVGTK--- 1237
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 450 lKNGCIEVYIRAGLLYLLTIFQCITSVSAGELFV-IDRDRFLHEHTSGYYRVSSYFFGKLLAElIPRRLLPST-IVLITY 527
Cdd:PLN03140 1238 -RSNANDLTMVIGAMYAAVLFVGINNCSTVQPMVaVERTVFYRERAAGMYSALPYAIAQVVCE-IPYVLIQTTyYTLIVY 1315
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 528 FIAGVKTSMSSFFAMLFTVMMlaysasSLPLSIGAGENAVAV-PTLFVTIYFVfMLFFSGLSLYSGSLLPQLS----WIQ 602
Cdd:PLN03140 1316 AMVAFEWTAAKFFWFYFISFF------SFLYFTYYGMMTVSLtPNQQVAAIFA-AAFYGLFNLFSGFFIPRPKipkwWVW 1388
|
....
gi 1958676843 603 YFNI 606
Cdd:PLN03140 1389 YYWI 1392
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
122-306 |
1.42e-28 |
|
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: 113.91 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 122 AIMGPQDGSRSLLLDVLAaRRDPSG--LSGDILVNGKPR-PANFKCTSGYVPQNDVVMHTVTVRDNLEFSAALRLPmTIT 198
Cdd:cd03234 37 AILGSSGSGKTTLLDAIS-GRVEGGgtTSGQILFNGQPRkPDQFQKCVAYVRQDDILLPGLTVRETLTYTAILRLP-RKS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 199 RDEKRRRINEVLELLHLDKEQNTKPRSKEL----RKRTSIAVELIAEHPILFLDDPTTDLDLTTTTYVISVLRRMSMKGK 274
Cdd:cd03234 115 SDAIRKKRVEDVLLRDLALTRIGGNLVKGIsggeRRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNR 194
|
170 180 190
....*....|....*....|....*....|..
gi 1958676843 275 TIIFSINQPQYSIFRFFDSLTLVASGKLMFHG 306
Cdd:cd03234 195 IVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
96-611 |
2.13e-28 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 121.37 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 96 GFPLRQQTRVIERLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPS--GLSGDILVNG------KPRpanFKCTS 166
Cdd:TIGR00956 64 KLKKFRDTKTFDILKPMDGLIKPGeLTVVLGRPGSGCSTLLKTIASNTDGFhiGVEGVITYDGitpeeiKKH---YRGDV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 167 GYVPQNDVVMHTVTVRDNLEFSAALRLPMT----ITRDEKRRRINEV-LELLHLDKEQNTKPR-------SKELRKRTSI 234
Cdd:TIGR00956 141 VYNAETDVHFPHLTVGETLDFAARCKTPQNrpdgVSREEYAKHIADVyMATYGLSHTRNTKVGndfvrgvSGGERKRVSI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 235 AVELIAEHPILFLDDPTTDLDLTTTTYVISVLRRMSMKGKTIIF-SINQPQYSIFRFFDSLTLVASGKLMFHGPARDALE 313
Cdd:TIGR00956 221 AEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLvAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 314 YFTSAGYQYESHNNPADFFLDVINgglcdTEEDGHEAGnYEEL-------FERKYQATKKLANMYAQ-----SRLHSDTR 381
Cdd:TIGR00956 301 YFEKMGFKCPDRQTTADFLTSLTS-----PAERQIKPG-YEKKvprtpqeFETYWRNSPEYAQLMKEideylDRCSESDT 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 382 ARLDQLLGQQQLDRNSAVETTCVTPFWHQLMWITYQSFKNIRGFLLVTAKQAVITATLAALVGIAFQILKNGCIEVYIRA 461
Cdd:TIGR00956 375 KEAYRESHVAKQSKRTRPSSPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRG 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 462 GLLYLLTIFQCITSVSagELF-VIDRDRFLHEH-TSGYYRVSSYFFGKLLAELIPRRLLPSTIVLITYFIAGVKTSMSSF 539
Cdd:TIGR00956 455 GALFFAILFNAFSSLL--EIAsMYEARPIVEKHrKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRF 532
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958676843 540 FAMLFTVMMLAYSASSLPLSIGAGENAVAVPTLFVTIYFVFMLFFSGLSLYSGSLLPQLSWIQYFNIPHYGF 611
Cdd:TIGR00956 533 FFYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAF 604
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
414-611 |
2.42e-25 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 103.89 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 414 ITYQSFKNIRGFLLVTAKQAVITATLAALVGIAFQILKNGcIEVYIRAGLLYLLTIFQCITSVSA-GELFVIDRDRFLHE 492
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQ-QGGLNRPGLLFFSILFNAFSALSGiSPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 493 HTSGYYRVSSYFFGKLLAElIPRRLLPSTIV-LITYFIAGVKTSMSSFFAMLFTVMMLAYSASSLPLSIGAGENAVAVPT 571
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSE-LPLSLLQSLIFlLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDAS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958676843 572 LFVTIYFVFMLFFSGLSLYSGSLLPQLSWIQYFNIPHYGF 611
Cdd:pfam01061 159 QLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAI 198
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
96-335 |
2.31e-14 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 76.81 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 96 GFPLRQQTRVIeRLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPS-GLSGDILVNGK------PRPanfkcTSG 167
Cdd:PLN03140 169 GINLAKKTKLT-ILKDASGIIKPSrMTLLLGPPSSGKTTLLLALAGKLDPSlKVSGEITYNGYrlnefvPRK-----TSA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 168 YVPQNDVVMHTVTVRDNLEFSAALR-------LPMTITRDEKRRRI---NEV---------------------LELLHLD 216
Cdd:PLN03140 243 YISQNDVHVGVMTVKETLDFSARCQgvgtrydLLSELARREKDAGIfpeAEVdlfmkatamegvksslitdytLKILGLD 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 217 KEQNTKPRSKELR-------KRTSIAVELIAEHPILFLDDPTTDLDLTTTTYVISVLRRM-SMKGKTIIFSINQPQYSIF 288
Cdd:PLN03140 323 ICKDTIVGDEMIRgisggqkKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIvHLTEATVLMSLLQPAPETF 402
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958676843 289 RFFDSLTLVASGKLMFHGPARDALEYFTSAGYQYESHNNPADFFLDV 335
Cdd:PLN03140 403 DLFDDIILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEV 449
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
148-315 |
1.42e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 70.48 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 148 SGDILVNGKP---RPANFKCTSGYVPQNDVVMHTVTVRDNLEFSAALRlpmTITRDEKRRRINEVLELLHLDKEQNTKPR 224
Cdd:COG1131 54 SGEVRVLGEDvarDPAEVRRRIGYVPQEPALYPDLTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 225 --SKELRKRTSIAVELIAEHPILFLDDPTTDLDLTTTTYVISVLRRMSMKGKTIIFSinqpqyS-----IFRFFDSLTLV 297
Cdd:COG1131 131 tlSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLS------ThyleeAERLCDRVAII 204
|
170
....*....|....*...
gi 1958676843 298 ASGKLMFHGPARDALEYF 315
Cdd:COG1131 205 DKGRIVADGTPDELKARL 222
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
79-306 |
1.98e-13 |
|
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: 69.21 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 79 EAVLSFHNISYREtvqsgfplRQQTRVIERLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPSG-LSGDILVNG- 155
Cdd:cd03233 1 ASTLSWRNISFTT--------GKGRSKIPILKDFSGVVKPGeMVLVLGRPGSGCSTLLKALANRTEGNVsVEGDIHYNGi 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 156 --KPRPANFKCTSGYVPQNDVVMHTVTVRDNLEFSAALRlpmtitRDEKRRRINevlellhldkeqntkprSKElRKRTS 233
Cdd:cd03233 73 pyKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALRCK------GNEFVRGIS-----------------GGE-RKRVS 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958676843 234 IAVELIAEHPILFLDDPTTDLDLTTTTYVISVLRRMSMK-GKTIIFSINQPQYSIFRFFDSLTLVASGKLMFHG 306
Cdd:cd03233 129 IAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
82-245 |
1.31e-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: 58.64 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 82 LSFHNISYRetvqsgFPLRQ-QTRVIERLS-SIsgimGPG-LNAIMGPQDGSRSLLLDVLAARRDPSglSGDILVNGKP- 157
Cdd:cd03293 1 LEVRNVSKT------YGGGGgAVTALEDISlSV----EEGeFVALVGPSGCGKSTLLRIIAGLERPT--SGEVLVDGEPv 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 158 RPANFKCtsGYVPQNDVVMHTVTVRDNLEFSAALRLpmtITRDEKRRRINEVLELLHLDKEQNTKPrsKEL----RKRTS 233
Cdd:cd03293 69 TGPGPDR--GYVFQQDALLPWLTVLDNVALGLELQG---VPKAEARERAEELLELVGLSGFENAYP--HQLsggmRQRVA 141
|
170
....*....|..
gi 1958676843 234 IAVELIAEHPIL 245
Cdd:cd03293 142 LARALAVDPDVL 153
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
109-246 |
7.46e-09 |
|
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: 54.96 E-value: 7.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 109 LSSISGIMGPG-LNAIMGPqDGS-RSLLLDVLAARRDPSglSGDILVNGKPRPAN----FKCTSGYVPQNDVVMHTVTVR 182
Cdd:pfam00005 1 LKNVSLTLNPGeILALVGP-NGAgKSTLLKLIAGLLSPT--EGTILLDGQDLTDDerksLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 183 DNLEFSAALRLPMtitRDEKRRRINEVLELLHLDKEQNTKPRS--KEL----RKRTSIAVELIAEHPILF 246
Cdd:pfam00005 78 ENLRLGLLLKGLS---KREKDARAEEALEKLGLGDLADRPVGErpGTLsggqRQRVAIARALLTKPKLLL 144
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
100-306 |
9.49e-09 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 55.84 E-value: 9.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 100 RQQTRVIERLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPSglSGDILVNG---KPRPANFKCTSGYVPQNDVV 175
Cdd:cd03266 12 RDVKKTVQAVDGVSFTVKPGeVTGLLGPNGAGKTTTLRMLAGLLEPD--AGFATVDGfdvVKEPAEARRRLGFVSDSTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 176 MHTVTVRDNLEFSAALRlpmTITRDEKRRRINEVLELLHLDK--EQNTKPRSKELRKRTSIAVELIAEHPILFLDDPTTD 253
Cdd:cd03266 90 YDRLTARENLEYFAGLY---GLKGDELTARLEELADRLGMEEllDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958676843 254 LDLTTTTYVISVLRRMSMKGKTIIFSINQPQySIFRFFDSLTLVASGKLMFHG 306
Cdd:cd03266 167 LDVMATRALREFIRQLRALGKCILFSTHIMQ-EVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
122-250 |
3.29e-08 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 54.43 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 122 AIMGPQDGSRSLLLDVLAARRDPSglSGDILVNGK---PRPANFKCTSGYVPQNDVVMHTVTVRDNLEFSAALRlpmTIT 198
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGELRPT--SGTAYINGYsirTDRKAARQSLGYCPQFDALFDELTVREHLRFYARLK---GLP 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958676843 199 RDEKRRRINEVLELLHLDKEQNTkpRSKEL----RKRTSIAVELIAEHPILFLDDP 250
Cdd:cd03263 107 KSEIKEEVELLLRVLGLTDKANK--RARTLsggmKRKLSLAIALIGGPSVLLLDEP 160
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
282-338 |
9.50e-08 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 54.53 E-value: 9.50e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958676843 282 QPQYSIFRFFDSLTLVASGKLM-FHGPARDALEYFTSAGYQYESHNNPADFFLDVING 338
Cdd:pfam19055 2 QPSYTLFKMFDDLILLAKGGLTvYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEG 59
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
122-279 |
2.30e-07 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 51.70 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 122 AIMGPqDGS-RSLLLDVLAARRDPSglSGDILVNGKP----RPANFKCTSGYVPQN-DVVMHTVTVRDNLEFSaaLRLpM 195
Cdd:cd03225 31 LIVGP-NGSgKSTLLRLLNGLLGPT--SGEVLVDGKDltklSLKELRRKVGLVFQNpDDQFFGPTVEEEVAFG--LEN-L 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 196 TITRDEKRRRINEVLELLHLDKEQNTKPRskEL----RKRTSIAVELIAEHPILFLDDPTTDLDLTTTTYVISVLRRMSM 271
Cdd:cd03225 105 GLPEEEIEERVEEALELVGLEGLRDRSPF--TLsggqKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA 182
|
....*...
gi 1958676843 272 KGKTIIFS 279
Cdd:cd03225 183 EGKTIIIV 190
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
122-278 |
3.40e-07 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 51.34 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 122 AIMGPQdGS-RSLLLDVLAARRDPSglSGDILVNGKP-------RPANFKCTS-GYVPQNDVVMHTVTVRDNLEfsaalr 192
Cdd:cd03255 34 AIVGPS-GSgKSTLLNILGGLDRPT--SGEVRVDGTDisklsekELAAFRRRHiGFVFQSFNLLPDLTALENVE------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 193 LPMTIT---RDEKRRRINEVLELLHLDKEQNTKPRskEL----RKRTSIAVELIAEHPILFLDDPTTDLDLTTTTYVISV 265
Cdd:cd03255 105 LPLLLAgvpKKERRERAEELLERVGLGDRLNHYPS--ELsggqQQRVAIARALANDPKIILADEPTGNLDSETGKEVMEL 182
|
170
....*....|....
gi 1958676843 266 LRRMS-MKGKTIIF 278
Cdd:cd03255 183 LRELNkEAGTTIVV 196
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
120-250 |
3.13e-05 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 45.79 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 120 LNAIMGPQDGSRSLLLDVLAARRDPSglSGDILVNGK------PRPANFkctsGYVPQNDVVMHTVTVRDNLEFsaALRL 193
Cdd:cd03296 30 LVALLGPSGSGKTTLLRLIAGLERPD--SGTILFGGEdatdvpVQERNV----GFVFQHYALFRHMTVFDNVAF--GLRV 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958676843 194 PMTITR---DEKRRRINEVLELLHLDKEQNTKPR--SKELRKRTSIAVELIAEHPILFLDDP 250
Cdd:cd03296 102 KPRSERppeAEIRAKVHELLKLVQLDWLADRYPAqlSGGQRQRVALARALAVEPKVLLLDEP 163
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
112-231 |
4.39e-05 |
|
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: 45.12 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 112 ISGIMGP---G----LNAIMGpqdgsrsllldvLAARRdpsglSGDILVNGKP---RPANFKCTSG--YVPQNDVVMHTV 179
Cdd:cd03224 28 IVALLGRngaGkttlLKTIMG------------LLPPR-----SGSIRFDGRDitgLPPHERARAGigYVPEGRRIFPEL 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1958676843 180 TVRDNLEFSAALRlpmtiTRDEKRRRINEVLELLhldkeqntkPRSKELRKR 231
Cdd:cd03224 91 TVEENLLLGAYAR-----RRAKRKARLERVYELF---------PRLKERRKQ 128
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
122-250 |
6.93e-05 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 44.67 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 122 AIMGPQDGSRSLLLDVLAARRDPSglSGDILVNG---KPRPANFKCTSGYVPQNDVVMHTVTVRDNLEFSAALrlpMTIT 198
Cdd:cd03265 30 GLLGPNGAGKTTTIKMLTTLLKPT--SGRATVAGhdvVREPREVRRRIGIVFQDLSVDDELTGWENLYIHARL---YGVP 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1958676843 199 RDEKRRRINEVLELLHL--DKEQNTKPRSKELRKRTSIAVELIAEHPILFLDDP 250
Cdd:cd03265 105 GAERRERIDELLDFVGLleAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
148-306 |
1.17e-04 |
|
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: 43.81 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 148 SGDILVNGKPRPANFKCTSGYVPQNDVVMHTVTVRDNLEFSAALRlpmTITRDEKRRRINEVLELLHLDKEQNTKPR--S 225
Cdd:cd03269 54 SGEVLFDGKPLDIAARNRIGYLPEERGLYPKMKVIDQLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRVEelS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 226 KELRKRTSIAVELIAEHPILFLDDPTTDLDLTTTTYVISVLRRMSMKGKTIIFSINQPQySIFRFFDSLTLVASGKLMFH 305
Cdd:cd03269 131 KGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQME-LVEELCDRVLLLNKGRAVLY 209
|
.
gi 1958676843 306 G 306
Cdd:cd03269 210 G 210
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
458-604 |
7.08e-04 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 41.34 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 458 YIRAGLLYLLTIFQCITSVSAGelFVIDRDRflheHTSGYYRVS-----SYFFGKLLAELIprRLLPST--IVLITYFIA 530
Cdd:COG0842 4 FLVPGLLAMSLLFTALMLTALS--IAREREQ----GTLERLLVTpvsrlEILLGKVLAYLL--RGLLQAllVLLVALLFF 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958676843 531 GVKTSMSSFFAMLFTVMMLAYSASSLPLSIGA----GENAVAVPTLFVTIyfvfMLFFSGLsLYSGSLLPQlsWIQYF 604
Cdd:COG0842 76 GVPLRGLSLLLLLLVLLLFALAFSGLGLLISTlarsQEQASAISNLVILP----LTFLSGA-FFPIESLPG--WLQAI 146
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
122-245 |
1.12e-03 |
|
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: 40.55 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 122 AIMGPQDGSRSLLLDVLAARRDPSglSGDILVNG--------KPRPanfkcTSGYVPQNDVVMHtVTVRDN--LEFSAAL 191
Cdd:cd03298 28 AIVGPSGSGKSTLLNLIAGFETPQ--SGRVLINGvdvtaappADRP-----VSMLFQENNLFAH-LTVEQNvgLGLSPGL 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958676843 192 RLpmtitRDEKRRRINEVLELLHLDKEQNTKPR--SKELRKRTSIAVELIAEHPIL 245
Cdd:cd03298 100 KL-----TAEDRQAIEVALARVGLAGLEKRLPGelSGGERQRVALARVLVRDKPVL 150
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
120-306 |
1.68e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 41.54 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 120 LNAIMGPQDGSRSLLLDVLAARRDPSglSGDILVNGKPRPANF---KCTSGYVPQNDVVMHTVTVRDNLEFSAALRlpmT 196
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPT--SGTVLVGGKDIETNLdavRQSLGMCPQHNILFHHLTVAEHILFYAQLK---G 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 197 ITRDEKRRRINEVLEL--LHLDKEQNTKPRSKELRKRTSIAVELIAEHPILFLDDPTTDLDLTTTTYVISVLRRMSmKGK 274
Cdd:TIGR01257 1033 RSWEEAQLEMEAMLEDtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGR 1111
|
170 180 190
....*....|....*....|....*....|..
gi 1958676843 275 TIIFSINQPQYSIFrFFDSLTLVASGKLMFHG 306
Cdd:TIGR01257 1112 TIIMSTHHMDEADL-LGDRIAIISQGRLYCSG 1142
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
122-313 |
1.94e-03 |
|
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: 41.04 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 122 AIMGPqDGS--RSLLLDVLAARRDPSGLSGDILVNGKP----RPANFKCTSGYVPQN-DVVMHTVTVRDNLEFsaALRLp 194
Cdd:COG1123 36 ALVGE-SGSgkSTLALALMGLLPHGGRISGEVLLDGRDllelSEALRGRRIGMVFQDpMTQLNPVTVGDQIAE--ALEN- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 195 MTITRDEKRRRINEVLELLHLDKEQNTKPR--SKELRKRTSIAVELIAEHPILFLDDPTTDLDLTTTTYVISVLRRMSMK 272
Cdd:COG1123 112 LGLSRAEARARVLELLEAVGLERRLDRYPHqlSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958676843 273 -GKTIIFsINQPQYSIFRFFDSLTLVASGKLMFHGPARDALE 313
Cdd:COG1123 192 rGTTVLL-ITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
123-279 |
1.99e-03 |
|
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: 40.08 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 123 IMGPQDGSRSLLLDVLAARRDPSglSGDILVNGKP-------RPANFKCTSGYVPQNDVVMHTVTVRDNLEFsaalrlPM 195
Cdd:cd03292 32 LVGPSGAGKSTLLKLIYKEELPT--SGTIRVNGQDvsdlrgrAIPYLRRKIGVVFQDFRLLPDRNVYENVAF------AL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 196 TIT---RDEKRRRINEVLELLHLDKEQNTKPR--SKELRKRTSIAVELIAEHPILFLDDPTTDLDLTTTTYVISVLRRMS 270
Cdd:cd03292 104 EVTgvpPREIRKRVPAALELVGLSHKHRALPAelSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKIN 183
|
....*....
gi 1958676843 271 MKGKTIIFS 279
Cdd:cd03292 184 KAGTTVVVA 192
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
122-245 |
3.86e-03 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 39.82 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 122 AIMGPQDGSRSLLLDVLAARRDPSglSGDILVNGKP--------RPANFkctsgyVPQNDVVMHTVTVRDNLEFSAAL-R 192
Cdd:PRK11607 49 ALLGASGCGKSTLLRMLAGFEQPT--AGQIMLDGVDlshvppyqRPINM------MFQSYALFPHMTVEQNIAFGLKQdK 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958676843 193 LPmtitRDEKRRRINEVLELLHLDKEQNTKPR--SKELRKRTSIAVELiAEHPIL 245
Cdd:PRK11607 121 LP----KAEIASRVNEMLGLVHMQEFAKRKPHqlSGGQRQRVALARSL-AKRPKL 170
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
109-306 |
4.65e-03 |
|
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: 38.67 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 109 LSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAarrdpsGL----SGDILVNGKPrPANFKCTSGYVPQNDVVMHT--VTV 181
Cdd:cd03235 15 LEDVSFEVKPGeFLAIVGPNGAGKSTLLKAIL------GLlkptSGSIRVFGKP-LEKERKRIGYVPQRRSIDRDfpISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 182 RDnlefSAALRL-----PMTITRDEKRRRINEVLE---LLHLDKEQNTkprskEL----RKRTSIAVELIAEHPILFLDD 249
Cdd:cd03235 88 RD----VVLMGLyghkgLFRRLSKADKAKVDEALErvgLSELADRQIG-----ELsggqQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 250 PTTDLDLTTTTYVISVLRRMSMKGKTIIFS---INQpqysIFRFFDSLTLVAsGKLMFHG 306
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRREGMTILVVthdLGL----VLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
91-250 |
7.47e-03 |
|
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: 38.47 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 91 ETVQSGFplRQQTRVIERLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPSglSGDILVNGKpRPanFKCTSGYV 169
Cdd:cd03267 21 GSLKSLF--KRKYREVEALKGISFTIEKGeIVGFIGPNGAGKTTTLKILSGLLQPT--SGEVRVAGL-VP--WKRRKKFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676843 170 PQNDVVMHTVT-------VRDNLEFSAAL-RLPmtitRDEKRRRINEVLELLHLDKEQNTKPRSKEL--RKRTSIAVELI 239
Cdd:cd03267 94 RRIGVVFGQKTqlwwdlpVIDSFYLLAAIyDLP----PARFKKRLDELSELLDLEELLDTPVRQLSLgqRMRAEIAAALL 169
|
170
....*....|.
gi 1958676843 240 AEHPILFLDDP 250
Cdd:cd03267 170 HEPEILFLDEP 180
|
|
| |
