|
Name |
Accession |
Description |
Interval |
E-value |
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
50-275 |
7.63e-113 |
|
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: 336.17 E-value: 7.63e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 50 RVRPWWDITSCRQQW--TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQD 127
Cdd:cd03234 2 RVLPWWDVGLKAKNWnkYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 128 CFSYVLQSDTLLSSLTVRETLHYTALLAIRRGNPGSFQKKVEAVMaelSLSHVADRLIGNYSLGGISTGERRRVSIAAQL 207
Cdd:cd03234 82 CVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDV---LLRDLALTRIGGNLVKGISGGERRRVSIAVQL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803088 208 LQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCG 275
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
60-580 |
1.55e-104 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 328.16 E-value: 1.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 60 CRQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQDCFSYVLQSDTLL 139
Cdd:TIGR00955 32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 140 SSLTVRETLHYTALLAIRRGNPGSfQKK--VEAVMAELSLSHVADRLIGNYS-LGGISTGERRRVSIAAQLLQDPKVMLF 216
Cdd:TIGR00955 112 PTLTVREHLMFQAHLRMPRRVTKK-EKRerVDEVLQALGLRKCANTRIGVPGrVKGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 217 DEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYPCPEHSN 296
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 297 PFDFYMDLTSVDtqsKEREIETSKRVQMIESAYKKSAICHKTLKNIeRMKHLKTLPMV-----PFKTKDSPGVFSKLGVL 371
Cdd:TIGR00955 271 PADFYVQVLAVI---PGSENESRERIEKICDSFAVSDIGRDMLVNT-NLWSGKAGGLVkdsenMEGIGYNASWWTQFYAL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 372 LRRVTRNLVRNKLAVITRLLQNLIMGLF--LLFFVLRVRSnvlKGaIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAVS 449
Cdd:TIGR00955 347 LKRSWLSVLRDPLLLKVRLIQTMMTAILigLIYLGQGLTQ---KG-VQNINGALFLFLTNMTFQNVFPVINVFTAELPVF 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 450 DQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNI 529
Cdd:TIGR00955 423 LRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSM 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 578803088 530 VNSVVALLSIAgVLVGSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVNEF 580
Cdd:TIGR00955 503 ALTVGPPFVIP-FLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQW 552
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
61-582 |
1.74e-64 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 223.60 E-value: 1.74e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 61 RQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTFLGEVYVNGRALRREQFQDCfSYVLQSDTLLS 140
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRI-QGNNFTGTILANNRKPTKQILKRT-GFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLHYTALLAIrrgnPGSFQKKV-----EAVMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVML 215
Cdd:PLN03211 154 HLTVRETLVFCSLLRL----PKSLTKQEkilvaESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 216 FDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYPCPEHS 295
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 296 NPFDFYMDLTSVDTQS---KEREIETSKrvQMIESAYkkSAICHKTLKNIERMKHLKTLP---MVPFKTKDSPGV----- 364
Cdd:PLN03211 310 NPADFLLDLANGVCQTdgvSEREKPNVK--QSLVASY--NTLLAPKVKAAIEMSHFPQANarfVGSASTKEHRSSdrisi 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 365 ---FSKLGVLLRRV---TRNLVRNKLAVITRLLQNLIMGLFLLFFVLRvrsnvlkgAIQDRVGLLY---QFVGATPYTgm 435
Cdd:PLN03211 386 stwFNQFSILLQRSlkeRKHESFNTLRVFQVIAAALLAGLMWWHSDFR--------DVQDRLGLLFfisIFWGVFPSF-- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 436 lNAVNLFPVLRAVSDQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEF 515
Cdd:PLN03211 456 -NSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQG 534
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 516 LTLVLLGIVQNPNIVNSVVALLSIAGVLVGsGFLrnIQEMPIPFKIISYFTFQKYCSEILvVNEFYG 582
Cdd:PLN03211 535 LGLALGAAIMDAKKASTIVTVTMLAFVLTG-GFY--VHKLPSCMAWIKYISTTFYSYRLL-INVQYG 597
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
50-275 |
2.79e-64 |
|
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: 209.33 E-value: 2.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 50 RVRPWWD-----ITSCRQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTfLGEVYVNGRALRREQ 124
Cdd:cd03213 1 GVTLSFRnltvtVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGV-SGEVLINGRPLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 125 FQDCFSYVLQSDTLLSSLTVRETLHYTALLAirrgnpgsfqkkveavmaelslshvadrlignyslgGISTGERRRVSIA 204
Cdd:cd03213 80 FRKIIGYVPQDDILHPTLTVRETLMFAAKLR------------------------------------GLSGGERKRVSIA 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 205 AQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCG 275
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
61-588 |
5.40e-54 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 198.79 E-value: 5.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 61 RQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRL-GRAGTFLGEVYVNGRALR--REQFQDCFSYVLQSDT 137
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdGFHIGVEGVITYDGITPEeiKKHYRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 138 LLSSLTVRETLHYTALLAIRRGNPGSFQKKVEA------VMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDP 211
Cdd:TIGR00956 149 HFPHLTVGETLDFAARCKTPQNRPDGVSREEYAkhiadvYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 212 KVMLFDEPTTGLDCMTANQIVVLLVELAR-RNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYP 290
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 291 CPEHSNPFDFymdLTSVdTQSKEREI--ETSKRV----QMIESAYKKS-------AICHKTLKNIERMKHLKTLPMVPFK 357
Cdd:TIGR00956 309 CPDRQTTADF---LTSL-TSPAERQIkpGYEKKVprtpQEFETYWRNSpeyaqlmKEIDEYLDRCSESDTKEAYRESHVA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 358 TKD------SPGVFSKLGVLLRRVTRNLVR---NKLAVITRLLQNLIMGLFLLFFVLRVRSNVLKGAIqdRVGLLYQFVG 428
Cdd:TIGR00956 385 KQSkrtrpsSPYTVSFSMQVKYCLARNFLRmkgNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYS--RGGALFFAIL 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 429 ATPYTGMLNAVNLFPVlRAVSDQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGY-----FS 503
Cdd:TIGR00956 463 FNAFSSLLEIASMYEA-RPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFyllilFI 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 504 AALLAPHL---IGEFLTLVLLGivqnpnivNSVVALLSIAGVLVgSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVNEF 580
Cdd:TIGR00956 542 CTLAMSHLfrsIGAVTKTLSEA--------MTPAAILLLALSIY-TGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEF 612
|
....*...
gi 578803088 581 YGLNFTCA 588
Cdd:TIGR00956 613 HGRRFECS 620
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
66-282 |
8.87e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 174.87 E-value: 8.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRRE--QFQDCFSYVLQSDTLLSSLT 143
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLL-RPTS--GEVRVLGEDVARDpaEVRRRIGYVPQEPALYPDLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLHYTALLairRGNPGS-FQKKVEAVMAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:COG1131 90 VRENLRFFARL---YGLPRKeARERIDELLELFGLTDAADRKVGTLSGG-----MKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 223 LDCMTANQIVVLLVELARRNRIVVLTIHQPrSELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:COG1131 162 LDPEARRELWELLRELAAEGKTVLLSTHYL-EEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
66-282 |
4.76e-46 |
|
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: 162.33 E-value: 4.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRRE--QFQDCFSYVLQSDTLLSSLT 143
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLL-KPDS--GSILIDGEDVRKEprEARRQIGVLPDERGLYDRLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLHYTALLairRGNPGS-FQKKVEAVMAELSLSHVADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:COG4555 91 VRENIRYFAEL---YGLFDEeLKKRIEELIELLGLEEFLDRRVGELS-----TGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 223 LDCMTANQIVVLLVELARRNRIVVLTIHQPrSELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:COG4555 163 LDVMARRLLREILRALKKEGKTVLFSSHIM-QEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
65-589 |
4.18e-45 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 172.22 E-value: 4.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRAlRREQFQDCFSYVLQSDTLLSSLTV 144
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRP-LDSSFQRSIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLHYTALLaiRRGNPGSFQKK---VEAVMAELSLSHVADRLIGnYSLGGISTGERRRVSIAAQLLQDPKVMLF-DEPT 220
Cdd:TIGR00956 854 RESLRFSAYL--RQPKSVSKSEKmeyVEEVIKLLEMESYADAVVG-VPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPT 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILS-------FGEL-IFCGTpaeMLDFFNDCGYP-C 291
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQkggqtvyFGDLgENSHT---IINYFEKHGAPkC 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 292 PEHSNPFDFYMDLTSVDTqskereieTSKRVQMIESAYKKSAICHKTLKNIERM-KHLKTLPMVPFKTKDSPGVFSKLGV 370
Cdd:TIGR00956 1008 PEDANPAEWMLEVIGAAP--------GAHANQDYHEVWRNSSEYQAVKNELDRLeAELSKAEDDNDPDALSKYAASLWYQ 1079
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 371 LLRRVTRNLV---RNKLAVITRLLQNLIMGLFLLFFVLRVRSNvLKGaIQDRVGLLYQFVgaTPYTGMLNA-VNLFPVLR 446
Cdd:TIGR00956 1080 FKLVLWRTFQqywRTPDYLYSKFFLTIFAALFIGFTFFKVGTS-LQG-LQNQMFAVFMAT--VLFNPLIQQyLPPFVAQR 1155
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 447 AVSD-QESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVA-------RFGYFSAALLAPHLIgeFLTL 518
Cdd:TIGR00956 1156 DLYEvRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFYWNASktgqvheRGVLFWLLSTMFFLY--FSTL 1233
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 519 VLLGIVQNPNIVN-SVVALLSIAGVLVGSGFLRNIQEMPiPFKIISY----FTfqkYCSEILVVNEFYGLNFTCAP 589
Cdd:TIGR00956 1234 GQMVISFNPNADNaAVLASLLFTMCLSFCGVLAPPSRMP-GFWIFMYrcspFT---YLVQALLSTGLADVPVTCKV 1305
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
65-275 |
6.28e-42 |
|
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: 149.70 E-value: 6.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRlGRAGTFLGEVYVNGRALrREQFQDCFSYVLQSDTLLSSLTV 144
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGR-KTAGVITGEILINGRPL-DKNFQRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLHYTALLAirrgnpgsfqkkveavmaelslshvadrlignyslgGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 224
Cdd:cd03232 97 REALRFSALLR------------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578803088 225 CMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAIL-SFGELIFCG 275
Cdd:cd03232 141 SQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLkRGGKTVYFG 192
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
66-282 |
6.79e-42 |
|
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: 151.35 E-value: 6.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL----RREQFQdCFSYVLQSDTLLSS 141
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSS---GEVLLDGRDLaslsRRELAR-RIAYVPQEPPAPFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 LTVRETLhytaLLAiRRGNPGSFQK-------KVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVM 214
Cdd:COG1120 90 LTVRELV----ALG-RYPHLGLFGRpsaedreAVEEALERTGLEHLADRPVDE-----LSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803088 215 LFDEPTTGLDcmTANQIVVL--LVELAR-RNRIVVLTIHQPrsEL-FQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:COG1120 160 LLDEPTSHLD--LAHQLEVLelLRRLAReRGRTVVMVLHDL--NLaARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
65-279 |
4.64e-41 |
|
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: 148.04 E-value: 4.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALR--REQFQDCFSYVLQSDTLLSSL 142
Cdd:cd03263 14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL-RPTS--GTAYINGYSIRtdRKAARQSLGYCPQFDALFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVRETLHYTALLairRGNPGSFQKK-VEAVMAELSLSHVADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPTT 221
Cdd:cd03263 91 TVREHLRFYARL---KGLPKSEIKEeVELLLRVLGLTDKANKRARTLS-----GGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578803088 222 GLDCMTANQIVVLLVELaRRNRIVVLTIHQPRsELFQLFDKIAILSFGELIFCGTPAE 279
Cdd:cd03263 163 GLDPASRRAIWDLILEV-RKGRSIILTTHSMD-EAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
68-581 |
3.95e-40 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 157.32 E-value: 3.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVRET 147
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVKET 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 148 LHYTAL-------------LAIRRGNPGSF-QKKVEAVMAELSLSHVADRLIGNYSLG------------------GIST 195
Cdd:PLN03140 260 LDFSARcqgvgtrydllseLARREKDAGIFpEAEVDLFMKATAMEGVKSSLITDYTLKilgldickdtivgdemirGISG 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 196 GERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVL-TIHQPRSELFQLFDKIAILSFGELIFC 274
Cdd:PLN03140 340 GQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLmSLLQPAPETFDLFDDIILLSEGQIVYQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 275 GTPAEMLDFFNDCGYPCPEHSNPFDFYMDLTS--------VDTQSKEREIETSKRVQMIESAYKKSaichktlknieRMK 346
Cdd:PLN03140 420 GPRDHILEFFESCGFKCPERKGTADFLQEVTSkkdqeqywADRNKPYRYISVSEFAERFKSFHVGM-----------QLE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 347 HLKTLPMVPFKTKDSPGVFSKLGVLLRRVTRN--------LVRNKLAVITRLLQNLIMGLFLLFFVLRVR---SNVLKGA 415
Cdd:PLN03140 489 NELSVPFDKSQSHKAALVFSKYSVPKMELLKAcwdkewllMKRNAFVYVFKTVQIIIVAAIASTVFLRTEmhtRNEEDGA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 416 IqdrvgllyqFVGATPYTGMLNAVNLFPVLRAVSDQ-----ESQDGLYQ-KWQMMLAYALHVLPFSVVATMIFSSVCYWT 489
Cdd:PLN03140 569 L---------YIGALLFSMIINMFNGFAELALMIQRlpvfyKQRDLLFHpPWTFTLPTFLLGIPISIIESVVWVVITYYS 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 490 LGLHPEVARFgyFSAALLApHLIGEF---LTLVLLGIVQNPNIVNSVVALLSIAGVLVGsGFLRNIQEMPIPFKIISYFT 566
Cdd:PLN03140 640 IGFAPEASRF--FKQLLLV-FLIQQMaagIFRLIASVCRTMIIANTGGALVLLLVFLLG-GFILPKGEIPNWWEWAYWVS 715
|
570
....*....|....*
gi 578803088 567 FQKYCSEILVVNEFY 581
Cdd:PLN03140 716 PLSYGFNALAVNEMF 730
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
66-282 |
1.20e-38 |
|
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: 142.04 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG-----------RALRREqfqdcFSYVLQ 134
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDS---GEILVDGqditglsekelYELRRR-----IGMLFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 135 SDTLLSSLTVRETLHYtALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVM 214
Cdd:COG1127 90 GGALFDSLTVFENVAF-PLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSE-----LSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 215 LFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI-HQpRSELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVtHD-LDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
65-282 |
1.35e-37 |
|
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: 139.17 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGR---ALRREQFQDC---FSYVLQSDTL 138
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS---GEVLIDGEdisGLSEAELYRLrrrMGMLFQSGAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 139 LSSLTVRETLHYtALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDE 218
Cdd:cd03261 89 FDSLTVFENVAF-PLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----LSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803088 219 PTTGLDCMTANQIVVLLVELARRNRIVVLTI-HQpRSELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKELGLTSIMVtHD-LDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
66-252 |
1.35e-35 |
|
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: 132.60 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR--REQFQDCFSYVLQSDTLLSSLT 143
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSA---GEVLWNGEPIRdaREDYRRRLAYLGHADGLKPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLHYTALLAIRRGNPGSfqkkVEAVMAELSLSHVADRLIGNYslggiSTGERRRVSIAAQLLQDPKVMLFDEPTTGL 223
Cdd:COG4133 92 VRENLRFWAALYGLRADREA----IDEALEAVGLAGLADLPVRQL-----SAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180
....*....|....*....|....*....
gi 578803088 224 DCMTANQIVVLLVELARRNRIVVLTIHQP 252
Cdd:COG4133 163 DAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
66-281 |
1.37e-35 |
|
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: 133.23 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQDCFS---YVLQ-SDTLLSS 141
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG-LLKPTS--GEVLVDGKDITKKNLRELRRkvgLVFQnPDDQLFA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 LTVRETLHYtALLaiRRGNPGSF-QKKVEAVMAELSLSHVADRLIgnYSLggiSTGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:COG1122 91 PTVEEDVAF-GPE--NLGLPREEiRERVEEALELVGLEHLADRPP--HEL---SGGQKQRVAIAGVLAMEPEVLVLDEPT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRIVVLTIHQPRsELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:COG1122 163 AGLDPRGRRELLELLKRLNKEGKTVIIVTHDLD-LVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
56-270 |
3.57e-35 |
|
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: 131.82 E-value: 3.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 56 DITSCRQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCF---SYV 132
Cdd:cd03225 4 NLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTS---GEVLVDGKDLTKLSLKELRrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 133 LQ-SDTLLSSLTVRETLhytALLAIRRGNPGS-FQKKVEAVMAELSLSHVADRLIgnYSLGGistGERRRVSIAAQLLQD 210
Cdd:cd03225 81 FQnPDDQFFGPTVEEEV---AFGLENLGLPEEeIEERVEEALELVGLEGLRDRSP--FTLSG---GQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 211 PKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPrSELFQLFDKIAILSFGE 270
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDL-DLLLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
66-282 |
1.66e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.98 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQdcFSYVLQSDTLLSS--LT 143
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTS---GTVRLFGKPPRRARRR--IGYVPQRAEVDWDfpIT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETL---HYTALLAIRRGNPGSFQkKVEAVMAELSLSHVADRLIGnySLGGistGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:COG1121 94 VRDVVlmgRYGRRGLFRRPSRADRE-AVDEALERVGLEDLADRPIG--ELSG---GQQQRVLLARALAQDPDLLLLDEPF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRIVVLTIHQPrSELFQLFDKIAILSfGELIFCGTPAEMLD 282
Cdd:COG1121 168 AGVDAATEEALYELLRELRREGKTILVVTHDL-GAVREYFDRVLLLN-RGLVAHGPPEEVLT 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
65-271 |
6.79e-34 |
|
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: 126.74 E-value: 6.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRRE--QFQDCFSYVLQSDTLLSSL 142
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLL-KPDS--GEIKVLGKDIKKEpeEVKRRIGYLPEEPSLYENL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVRETLHYtallairrgnpgsfqkkveavmaelslshvadrlignyslggiSTGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:cd03230 89 TVRENLKL-------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578803088 223 LDCMTANQIVVLLVELARRNRIVVLTIHQPrSELFQLFDKIAILSFGEL 271
Cdd:cd03230 126 LDPESRREFWELLRELKKEGKTILLSSHIL-EEAERLCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
66-275 |
4.54e-33 |
|
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: 124.86 E-value: 4.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR---REQFQDCFSYVLQsdtllssl 142
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSS---GEILLDGKDLAslsPKELARKIAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 tvretlhytallairrgnpgsfqkkveaVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:cd03214 81 ----------------------------ALELLGLAHLADRPFNE-----LSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 223 LDcmTANQIVVL--LVELAR-RNRIVVLTIHQPrsEL-FQLFDKIAILSFGELIFCG 275
Cdd:cd03214 128 LD--IAHQIELLelLRRLAReRGKTVVMVLHDL--NLaARYADRVILLKDGRIVAQG 180
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
67-502 |
1.20e-32 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 134.59 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRlgRAGTFL-GEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVR 145
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR--KTGGYIeGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 146 ETLHYTALLaiRRGNPGSFQKK---VEAVMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:PLN03140 972 ESLIYSAFL--RLPKEVSKEEKmmfVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 223 LDCMTAnQIVVLLVelarRN-----RIVVLTIHQPRSELFQLFDKIAILSF-GELIFCGT----PAEMLDFFNDC-GYP- 290
Cdd:PLN03140 1050 LDARAA-AIVMRTV----RNtvdtgRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPlgrnSHKIIEYFEAIpGVPk 1124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 291 CPEHSNPFDFYMDLTSVDTQSKeREIETSKRvqmiesaYKKSAICHktlKNIERMKHLKTLPM----VPFKTKDSPGVFS 366
Cdd:PLN03140 1125 IKEKYNPATWMLEVSSLAAEVK-LGIDFAEH-------YKSSSLYQ---RNKALVKELSTPPPgasdLYFATQYSQSTWG 1193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 367 KLGVLL--------RRVTRNLVRNKLAVITRLlqnLIMGLFLLFFVLRVRSNVLKGAIqdrvGLLYqfvGATPYTGMLNA 438
Cdd:PLN03140 1194 QFKSCLwkqwwtywRSPDYNLVRFFFTLAAAL---MVGTIFWKVGTKRSNANDLTMVI----GAMY---AAVLFVGINNC 1263
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 439 VNLFPVL---RAVSDQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYF 502
Cdd:PLN03140 1264 STVQPMVaveRTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWF 1330
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
67-275 |
1.85e-32 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 124.17 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRAL------RREqfqdcFSYVLQSDTLLS 140
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG-LERPDS--GEILIDGRDVtgvppeRRN-----IGMVFQDYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIgnyslGGISTGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:cd03259 86 HLTVAENIAFG--LKLRGVPKAEIRARVRELLELVGLEGLLNRYP-----HELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRI-VVLTIHQPrSELFQLFDKIAILSFGELIFCG 275
Cdd:cd03259 159 SALDAKLREELREELKELQRELGItTIYVTHDQ-EEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
69-221 |
2.84e-32 |
|
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: 121.60 E-value: 2.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR---REQFQDCFSYVLQSDTLLSSLTVR 145
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTE---GTILLDGQDLTddeRKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 146 ETLHYTALLAIRRGNPgsFQKKVEAVMAELSLSHVADRLIGNYSlGGISTGERRRVSIAAQLLQDPKVMLFDEPTT 221
Cdd:pfam00005 78 ENLRLGLLLKGLSKRE--KDARAEEALEKLGLGDLADRPVGERP-GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
65-282 |
2.99e-32 |
|
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: 130.41 E-value: 2.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQDC---FSYVLQS-DTLLS 140
Cdd:COG1123 18 DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEALRgrrIGMVFQDpMTQLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:COG1123 98 PVTVGDQIAEA--LENLGLSRAEARARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALALDPDLLIADEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:COG1123 171 TALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
65-271 |
3.72e-32 |
|
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: 123.37 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR-----------ALRREQfqdcFSYVL 133
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG-LDRPTS--GEVRVDGTdisklsekelaAFRRRH----IGFVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 134 QSDTLLSSLTVRETLhytALLAIRRGNPGSFQK-KVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPK 212
Cdd:cd03255 89 QSFNLLPDLTALENV---ELPLLLAGVPKKERReRAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 213 VMLFDEPTTGLDCMTANQIVVLLVELAR-RNRIVVLTIHQPrsELFQLFDKIAILSFGEL 271
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDP--ELAEYADRIIELRDGKI 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
66-275 |
3.94e-32 |
|
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: 123.41 E-value: 3.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQdcFSYVLQSDTLLSS--LT 143
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTS---GSIRVFGKPLEKERKR--IGYVPQRRSIDRDfpIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLhytaLLAiRRGNPGSFQ-------KKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLF 216
Cdd:cd03235 87 VRDVV----LMG-LYGHKGLFRrlskadkAKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 217 DEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPrSELFQLFDKIAILSfGELIFCG 275
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDL-GLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
53-275 |
3.98e-32 |
|
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: 122.76 E-value: 3.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 53 PWWDITSCRQQ--WTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALR--REQFQDC 128
Cdd:cd03233 5 SWRNISFTTGKgrSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKefAEKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 129 FSYVLQSDTLLSSLTVRETLHYTAllairrgnpgsfqkkveavmaelslshvadRLIGNYSLGGISTGERRRVSIAAQLL 208
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETLDFAL------------------------------RCKGNEFVRGISGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803088 209 QDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVL-TIHQPRSELFQLFDKIAILSFGELIFCG 275
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFvSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
69-279 |
2.78e-31 |
|
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: 121.78 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRREQ------------FQdcfsyVLQsd 136
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFL-RPTS--GSVLFDGEDITGLPpheiarlgigrtFQ-----IPR-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 137 tLLSSLTVRETL--------HYTALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLL 208
Cdd:cd03219 86 -LFPELTVLENVmvaaqartGSGLLLARARREEREARERAEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 209 QDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSeLFQLFDKIAILSFGELIFCGTPAE 279
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
65-272 |
3.19e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 121.30 E-value: 3.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR-----------ALRREQfqdcFSYVL 133
Cdd:COG1136 20 EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG-LDRPTS--GEVLIDGQdisslserelaRLRRRH----IGFVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 134 QSDTLLSSLTVRETLhytAL-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPK 212
Cdd:COG1136 93 QFFNLLPELTALENV---ALpLLLAGVSRKERRERARELLERVGLGDRLDHRPSQ-----LSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 213 VMLFDEPTTGLDCMTANQIVVLLVELARR-NRIVVLTIHQPRseLFQLFDKIAILSFGELI 272
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPE--LAARADRVIRLRDGRIV 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
65-281 |
7.19e-31 |
|
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: 120.34 E-value: 7.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRR----EQFQDCFSYVLQSDTLLS 140
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVG-LVKPDS--GKILLDGQDITKlpmhKRARLGIGYLPQEASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLhyTALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLigNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:cd03218 89 KLTVEENI--LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSK--ASSLSG---GERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRIVVLTIHQPRsELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILKDRGIGVLITDHNVR-ETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
65-270 |
1.82e-30 |
|
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: 116.58 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR---EQFQDCFSYVLQsdtllss 141
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTS---GEILIDGKDIAKlplEELRRRIGYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 ltvretlhytallairrgnpgsfqkkveavmaelslshvadrlignyslggISTGERRRVSIAAQLLQDPKVMLFDEPTT 221
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578803088 222 GLDCMTANQIVVLLVELARRNRIVVLTIHQPrSELFQLFDKIAILSFGE 270
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDP-ELAELAADRVIVLKDGK 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
65-267 |
4.22e-30 |
|
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: 117.96 E-value: 4.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQdcFSYVLQSDTLLSSLTV 144
Cdd:cd03293 16 AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG-LERPTS--GEVLVDGEPVTGPGPD--RGYVFQQDALLPWLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETlhyTAL-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGL 223
Cdd:cd03293 91 LDN---VALgLELQGVPKAEARERAEELLELVGLSGFENAYPHQ-----LSGGMRQRVALARALAVDPDVLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578803088 224 DCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILS 267
Cdd:cd03293 163 DALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
69-280 |
4.43e-30 |
|
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: 117.86 E-value: 4.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRRE--QFQDCFSYVLQSDTLLSSLTVRE 146
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTS---GRATVAGHDVVREprEVRRRIGIVFQDLSVDDELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 147 TLHYTALLAirrGNPGS-FQKKVEAVMAELSLSHVADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 225
Cdd:cd03265 93 NLYIHARLY---GVPGAeRRERIDELLDFVGLLEAADRLVKTYS-----GGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578803088 226 MTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:cd03265 165 QTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
27-281 |
3.30e-29 |
|
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: 122.18 E-value: 3.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 27 GAPATAPEPHSLGILHASYSvshrvrpwWDitscrqQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgra 106
Cdd:COG4987 323 AEPAPAPGGPSLELEDVSFR--------YP------GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR----- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 107 gtFL----GEVYVNG---RALRREQFQDCFSYVLQSDTLLSSlTVRETLhytaLLAirrgNPGSFQKKVEAVMAELSLSH 179
Cdd:COG4987 384 --FLdpqsGSITLGGvdlRDLDEDDLRRRIAVVPQRPHLFDT-TLRENL----RLA----RPDATDEELWAALERVGLGD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 180 VADRLIG--NYSLG----GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELArRNRIVVLTIHQPR 253
Cdd:COG4987 453 WLAALPDglDTWLGeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLA 531
|
250 260
....*....|....*....|....*...
gi 578803088 254 seLFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:COG4987 532 --GLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
66-275 |
3.55e-29 |
|
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: 114.98 E-value: 3.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGqIMCILGSSGSGKTTLLDAMSGRL-GRAGTflgeVYVNGRALR--REQFQDCFSYVLQSDTLLSSL 142
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTpPSSGT----IRIDGQDVLkqPQKLRRRIGYLPQEFGVYPNF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVRETLHYTALLaiRRGNPGSFQKKVEAVMAELSLSHVADRLIGNYSlGGIstgeRRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:cd03264 88 TVREFLDYIAWL--KGIPSKEVKARVDEVLELVNLGDRAKKKIGSLS-GGM----RRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578803088 223 LDcmTANQIVV--LLVELArRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCG 275
Cdd:cd03264 161 LD--PEERIRFrnLLSELG-EDRIVILSTHI-VEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
65-273 |
4.88e-29 |
|
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: 114.24 E-value: 4.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGralrrEQFQDCFSYVLQSDTLLSS--- 141
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILG-LIKPDS--GEITFDG-----KSYQKNIEALRRIGALIEApgf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 ---LTVRETLHYTALLAIRRgnpgsfQKKVEAVMAELSLSHVADRLIGNYSLggistGERRRVSIAAQLLQDPKVMLFDE 218
Cdd:cd03268 84 ypnLTARENLRLLARLLGIR------KKRIDEVLDVVGLKDSAKKKVKGFSL-----GMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578803088 219 PTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIF 273
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLISSHL-LSEIQKVADRIGIINKGKLIE 206
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
66-282 |
9.10e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 114.74 E-value: 9.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL------RREQFQdcFSYVLQSDTLL 139
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS---GRIFLDGEDIthlpmhKRARLG--IGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 140 SSLTVRETLhyTALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLigNYSLGGistGERRRVSIAAQLLQDPKVMLFDEP 219
Cdd:COG1137 91 RKLTVEDNI--LAVLELRKLSKKEREERLEELLEEFGITHLRKSK--AYSLSG---GERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803088 220 TTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRsELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:COG1137 164 FAGVDPIAVADIQKIIRHLKERGIGVLITDHNVR-ETLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
66-281 |
1.61e-28 |
|
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: 113.91 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRR----EQFQDCFSYVLQSDTLLSS 141
Cdd:TIGR04406 14 RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVG-LVRPDA--GKILIDGQDITHlpmhERARLGIGYLPQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 LTVRETLhyTALLAIR-RGNPGSFQKKVEAVMAELSLSHVADRLigNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:TIGR04406 91 LTVEENI--MAVLEIRkDLDRAEREERLEALLEEFQISHLRDNK--AMSLSG---GERRRVEIARALATNPKFILLDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRIVVLTIHQPRsELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:TIGR04406 164 AGVDPIAVGDIKKIIKHLKERGIGVLITDHNVR-ETLDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
41-275 |
6.59e-28 |
|
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: 112.04 E-value: 6.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 41 LHASYSVsHRVRPWWdITSCRQQWTRQ-----ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYV 115
Cdd:cd03267 6 LSKSYRV-YSKEPGL-IGSLKSLFKRKyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTS---GEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 116 NGRA--LRREQFQDCFSYVL-QSDTLLSSLTVRETlhYTALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNYSLGg 192
Cdd:cd03267 81 AGLVpwKRRKKFLRRIGVVFgQKTQLWWDLPVIDS--FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLG- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 193 istgERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR-RNRIVVLTIHQPRsELFQLFDKIAILSFGEL 271
Cdd:cd03267 158 ----QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNReRGTTVLLTSHYMK-DIEALARRVLVIDKGRL 232
|
....
gi 578803088 272 IFCG 275
Cdd:cd03267 233 LYDG 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
65-282 |
8.28e-28 |
|
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: 117.31 E-value: 8.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG-----------RALRRE-Q--FQDCFS 130
Cdd:COG1123 277 GVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTS---GSILFDGkdltklsrrslRELRRRvQmvFQDPYS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 131 yvlqsdTLLSSLTVRETLHYtALLAIRRGNPGSFQKKVEAVMAELSLS-HVADRLIgnYSLGGistGERRRVSIAAQLLQ 209
Cdd:COG1123 354 ------SLNPRMTVGDIIAE-PLRLHGLLSRAERRERVAELLERVGLPpDLADRYP--HELSG---GQRQRVAIARALAL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 210 DPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRivvLTIhqprseLF---------QLFDKIAILSFGELIFCGTPAEM 280
Cdd:COG1123 422 EPKLLILDEPTSALDVSVQAQILNLLRDLQRELG---LTY------LFishdlavvrYIADRVAVMYDGRIVEDGPTEEV 492
|
..
gi 578803088 281 LD 282
Cdd:COG1123 493 FA 494
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
60-271 |
1.84e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.91 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 60 CRQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGR--------ALRREqfqdcFSY 131
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTS---GEIYLDGKplsampppEWRRQ-----VAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 132 VLQSDTLLSSlTVRETLHYTALLAIRRGNPgsfqKKVEAVMAELSLSH-VADRLIGNyslggISTGERRRVSIAAQLLQD 210
Cdd:COG4619 79 VPQEPALWGG-TVRDNLPFPFQLRERKFDR----ERALELLERLGLPPdILDKPVER-----LSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803088 211 PKVMLFDEPTTGLDCMTANQIVVLLVEL-ARRNRIVVLTIHQPRsELFQLFDKIAILSFGEL 271
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPE-QIERVADRVLTLEAGRL 209
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
69-280 |
3.01e-27 |
|
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: 112.10 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRL----GRAGTFLGEVYVNGRALRREqfqdcFSYVLQSDTLLSSLTV 144
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLrptsGTARVAGYDVVREPRKVRRS-----IGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLHYTALLairRGNPGSF-QKKVEAVMAELSLSHVADRLIGNYSlGGIstgeRRRVSIAAQLLQDPKVMLFDEPTTGL 223
Cdd:TIGR01188 84 RENLEMMGRL---YGLPKDEaEERAEELLELFELGEAADRPVGTYS-GGM----RRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 224 DCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHY-MEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
65-267 |
5.37e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 110.18 E-value: 5.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQfQDCfSYVLQSDTLLSSLTV 144
Cdd:COG1116 23 GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG-LEKPTS--GEVLVDGKPVTGPG-PDR-GVVFQEPALLPWLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RE--TLHytalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:COG1116 98 LDnvALG----LELRGVPKAERRERARELLELVGLAGFEDAYPHQ-----LSGGMRQRVAIARALANDPEVLLMDEPFGA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 578803088 223 LDCMTANQIVVLLVELARRNRIVVLTI-HQPRsELFQLFDKIAILS 267
Cdd:COG1116 169 LDALTRERLQDELLRLWQETGKTVLFVtHDVD-EAVFLADRVVVLS 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
69-281 |
6.14e-27 |
|
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: 109.21 E-value: 6.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRAL-------RREQFQDcFSYVLQSDTLLSS 141
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LERPTS--GSVLVDGTDLtllsgkeLRKARRR-IGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 LTVRETLHYTALLAirrGNPGSFQ-KKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:cd03258 97 RTVFENVALPLEIA---GVPKAEIeERVLELLELVGLEDKADAYPAQ-----LSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRIVVLTI-HQpRSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:cd03258 169 SALDPETTQSILALLRDINRELGLTIVLItHE-MEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
56-281 |
7.30e-27 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 108.96 E-value: 7.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 56 DITSCRQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL------RREqfqdcF 129
Cdd:cd03299 2 KVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS---GKILLNGKDItnlppeKRD-----I 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 130 SYVLQSDTLLSSLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQ 209
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYG--LKKRKVDKKEIERKVLEIAEMLGIDHLLNR-----KPETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803088 210 DPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
66-279 |
1.03e-26 |
|
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: 108.81 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG-----------RALRREqfqdcFSYVLQ 134
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTS---GSVLIDGtdinklkgkalRQLRRQ-----IGMIFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 135 SDTLLSSLTVRET-----LHYTALL-AIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLL 208
Cdd:cd03256 86 QFNLIERLSVLENvlsgrLGRRSTWrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQ-----LSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803088 209 QDPKVMLFDEPTTGLDCMTANQIVVLLVELAR-RNRIVVLTIHQPrsELF-QLFDKIAILSFGELIFCGTPAE 279
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINReEGITVIVSLHQV--DLArEYADRIVGLKDGRIVFDGPPAE 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
68-250 |
1.20e-26 |
|
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: 107.73 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFSYVLQ-SDTLLSSLTVRE 146
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESS---GSILLNGKPIKAKERRKSIGYVMQdVDYQLFTDSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 147 TLHYTAllairrGNPGSFQKKVEAVMAELSLSHVADRLigNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCM 226
Cdd:cd03226 92 ELLLGL------KELDAGNEQAETVLKDLDLYALKERH--PLSLSG---GQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180
....*....|....*....|....
gi 578803088 227 TANQIVVLLVELARRNRIVVLTIH 250
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITH 184
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
61-249 |
2.05e-26 |
|
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: 107.59 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 61 RQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR---ALRREQFQDC---FSYVLQ 134
Cdd:cd03257 13 TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILG-LLKPTS--GSIIFDGKdllKLSRRLRKIRrkeIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 135 sDTLLS---SLTVRETLhyTALLAIRRGNPGSFQKKvEAVMAELSLSHVADRLIGNY--SLGGistGERRRVSIAAQLLQ 209
Cdd:cd03257 90 -DPMSSlnpRMTIGEQI--AEPLRIHGKLSKKEARK-EAVLLLLVGVGLPEEVLNRYphELSG---GQRQRVAIARALAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578803088 210 DPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI 249
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFI 202
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
67-282 |
4.29e-26 |
|
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: 106.36 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR----EQFQDCFSYVLQSDTLLSSL 142
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRS---GSIRFDGRDITGlpphERARAGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVRETLhytaLLAIRRGNPGSFQKKVEAVMAELS-LSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTT 221
Cdd:cd03224 91 TVEENL----LLGAYARRRAKRKARLERVYELFPrLKERRKQLAGT-----LSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 222 GLDCMTANQIVVLLVELARRnRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
69-275 |
8.02e-26 |
|
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: 105.45 E-value: 8.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSL---YVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFS-------YVLQSDTL 138
Cdd:cd03297 10 LPDFTLkidFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDG---GTIVLNGTVLFDSRKKINLPpqqrkigLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 139 LSSLTVRETLHYtallAIRRGNPGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDE 218
Cdd:cd03297 87 FPHLNVRENLAF----GLKRKRNREDRISVDELLDLLGLDHLLNR-----YPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 219 PTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCG 275
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
68-253 |
1.29e-25 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 105.59 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR-----------ALRREQfqdcFSYVLQSD 136
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG-LDRPTS--GTVRLAGQdlfaldedaraRLRARH----VGFVFQSF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 137 TLLSSLTVREtlhYTALLAIRRGNPGSFQkKVEAVMAELSLSHvadRLiGNYSlGGISTGERRRVSIAAQLLQDPKVMLF 216
Cdd:COG4181 100 QLLPTLTALE---NVMLPLELAGRRDARA-RARALLERVGLGH---RL-DHYP-AQLSGGEQQRVALARAFATEPAILFA 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 578803088 217 DEPTTGLDCMTANQIVVLLVELARRNRI-VVLTIHQPR 253
Cdd:COG4181 171 DEPTGNLDAATGEQIIDLLFELNRERGTtLVLVTHDPA 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
66-281 |
2.64e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.24 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRAL----------RREqfqdcfsyVL-Q 134
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGEL-SPDS--GEVRLNGRPLadwspaelarRRA--------VLpQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 135 SDTLLSSLTVRETLhytAL-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLignY-SLGGistGERRRVSIA---AQLLQ 209
Cdd:PRK13548 84 HSSLSFPFTVEEVV---AMgRAPHGLSRAEDDALVAAALAQVDLAHLAGRD---YpQLSG---GEQQRVQLArvlAQLWE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 210 D---PKVMLFDEPTTGLDcmTANQIVVL--LVELARRNR---IVVLtiHqprsELFQ--LF-DKIAILSFGELIFCGTPA 278
Cdd:PRK13548 155 PdgpPRWLLLDEPTSALD--LAHQHHVLrlARQLAHERGlavIVVL--H----DLNLaaRYaDRIVLLHQGRLVADGTPA 226
|
...
gi 578803088 279 EML 281
Cdd:PRK13548 227 EVL 229
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
66-281 |
4.00e-25 |
|
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: 104.30 E-value: 4.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLdAMSGRLGRAGTflGEVYVNGRALRREQFQDCFSY--VLQSDTLLSSLT 143
Cdd:TIGR03864 14 RRALDDVSFTVRPGRFVALLGPNGAGKSTLF-SLLTRLYVAQS--GQISVAGHDLRRAPRAALARLgvVFQQPTLDLDLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLHYTALL-AIRRGNPgsfQKKVEAVMAELSLSHVADRLIGnySLGGistGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:TIGR03864 91 VRQNLRYHAALhGLSRAEA---RARIAELLARLGLAERADDKVR--ELNG---GHRRRVEIARALLHRPALLLLDEPTVG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 223 LDCMTANQIVVLLVELARRNRIVVL-TIHqprselfqLFDKIA------ILSFGELIFCGTPAEML 281
Cdd:TIGR03864 163 LDPASRAAITAHVRALARDQGLSVLwATH--------LVDEIEasdrlvVLHRGRVLADGAAAELR 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
67-275 |
4.08e-25 |
|
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: 103.60 E-value: 4.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRREQFQDC--FSYVLQSDTLLSSLTV 144
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLL-EPDA--GFATVDGFDVVKEPAEARrrLGFVSDSTGLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLHYTALLairRG-NPGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGL 223
Cdd:cd03266 96 RENLEYFAGL---YGlKGDELTARLEELADRLGMEELLDR-----RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578803088 224 DCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCG 275
Cdd:cd03266 168 DVMATRALREFIRQLRALGKCILFSTHI-MQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
66-270 |
4.25e-25 |
|
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: 102.27 E-value: 4.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL-----RREQFQDCFSYVLQSDTLLS 140
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDS---GSILIDGEDLtdledELPPLRRRIGMVFQDFALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLHYtallairrgnpgsfqkkveavmaelslshvadrlignyslgGISTGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:cd03229 90 HLTVLENIAL-----------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRI-VVLTIHQPRsELFQLFDKIAILSFGE 270
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQLGItVVLVTHDLD-EAARLADRVVVLRDGK 178
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
66-281 |
9.81e-25 |
|
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: 103.24 E-value: 9.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgrAGTFLGEVYVNGRALRREQFQD------CFSYVLQsDTLL 139
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDL--PPTYGNDVRLFGERRGGEDVWElrkrigLVSPALQ-LRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 140 SSLTVRETL------------HYTALLairrgnpgsfQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQL 207
Cdd:COG1119 93 RDETVLDVVlsgffdsiglyrEPTDEQ----------RERARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803088 208 LQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI-HQPrSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVtHHV-EEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
66-270 |
2.79e-24 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 99.76 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNGRALR---REQFQDCFSYVLQsDTL 138
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR-------LYdptsGEILIDGVDLRdldLESLRKNIAYVPQ-DPF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 139 LSSLTVRETLhytallairrgnpgsfqkkveavmaelslshvadrlignyslggISTGERRRVSIAAQLLQDPKVMLFDE 218
Cdd:cd03228 87 LFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578803088 219 PTTGLDCMTANQIVVLLVELaRRNRIVVLTIHqpRSELFQLFDKIAILSFGE 270
Cdd:cd03228 123 ATSALDPETEALILEALRAL-AKGKTVIVIAH--RLSTIRDADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
68-281 |
6.14e-24 |
|
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: 106.46 E-value: 6.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNGRALR---REQFQDCFSYVLQSDTLLS 140
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG-------LYeptsGRILIDGIDLRqidPASLRRQIGVVLQDVFLFS 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SlTVRETlhytallaIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNYSL------GGISTGERRRVSIAAQLLQDPKVM 214
Cdd:COG2274 563 G-TIREN--------ITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTvvgeggSNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 215 LFDEPTTGLDCMTANQIVVLLVELArRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLL-KGRTVIIIAH--RLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
67-279 |
6.47e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 103.25 E-value: 6.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNGRAL------RREqfqdcFSYVLQSD 136
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-------FEtpdsGRILLDGRDVtglppeKRN-----VGMVFQDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 137 TLLSSLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLF 216
Cdd:COG3842 87 ALFPHLTVAENVAFG--LRMRGVPKAEIRARVAELLELVGLEGLADRYPHQ-----LSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803088 217 DEPTTGLDCMTANQIVVLLVELARRNRIVVLTI-HQpRSELFQLFDKIAILSFGELIFCGTPAE 279
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQRELGITFIYVtHD-QEEALALADRIAVMNDGRIEQVGTPEE 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
71-281 |
9.65e-24 |
|
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: 102.87 E-value: 9.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 71 DVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRAL---RREQF----QDCFSYVLQSDTLLSSLT 143
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAG-LERPDS--GRIRLGGEVLqdsARGIFlpphRRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLHYtallAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGL 223
Cdd:COG4148 94 VRGNLLY----GRKRAPRAERRISFDEVVELLGIGHLLDRRPAT-----LSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 224 DCMTANQIVVLLVELARRNRIVVLTI-HQPRsELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:COG4148 165 DLARKAEILPYLERLRDELDIPILYVsHSLD-EVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
67-253 |
1.34e-23 |
|
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: 99.35 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR-----------ALRREQFqdcfSYVLQS 135
Cdd:TIGR02211 19 RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGG-LDNPTS--GEVLFNGQslsklssneraKLRNKKL----GFIYQF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 136 DTLLSSLTVRETLHYTALlaIRRGNPGSFQKKVEAVMAELSLSHvadRLigNYSLGGISTGERRRVSIAAQLLQDPKVML 215
Cdd:TIGR02211 92 HHLLPDFTALENVAMPLL--IGKKSVKEAKERAYEMLEKVGLEH---RI--NHRPSELSGGERQRVAIARALVNQPSLVL 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 578803088 216 FDEPTTGLDCMTANQIVVLLVELARRNRI-VVLTIHQPR 253
Cdd:TIGR02211 165 ADEPTGNLDNNNAKIIFDLMLELNRELNTsFLVVTHDLE 203
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
69-287 |
1.47e-23 |
|
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: 100.41 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG-----------RALRREQFqdcfSYVLQSDT 137
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTS---GKVLIDGqdiaamsrkelRELRRKKI----SMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 138 LLSSLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFD 217
Cdd:cd03294 113 LLPHRTVLENVAFG--LEVQGVPRAEREERAAEALELVGLEGWEHKYPDE-----LSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 218 EPTTGLDCMTANQIVVLLVEL-ARRNRIVVLTIHQPrSELFQLFDKIAILSFGELIFCGTPAEML---------DFFNDC 287
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLqAELQKTIVFITHDL-DEALRLGDRIAIMKDGRLVQVGTPEEILtnpandyvrEFFRGV 264
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
69-281 |
3.39e-23 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 98.91 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLdAMSGRLGRAGTflGEVYVNGR--------ALRREqfqdcFSYVLQSDTLLS 140
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTM-KMINRLIEPTS--GEIFIDGEdireqdpvELRRK-----IGYVIQQIGLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLhyTALLAIRRGNPGSFQKKVEAVMAELSL--SHVADRlignYSlGGISTGERRRVSIAAQLLQDPKVMLFDE 218
Cdd:cd03295 89 HMTVEENI--ALVPKLLKWPKEKIRERADELLALVGLdpAEFADR----YP-HELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803088 219 PTTGLDCMTANQIVVLLVELARR-NRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQElGKTIVFVTHD-IDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
66-250 |
5.25e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 97.43 E-value: 5.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSG--RLGRagtflGEVYVNGR---ALRREQ-----------FQDCf 129
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeeRPTS-----GQVLVNGQdlsRLKRREipylrrrigvvFQDF- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 130 syvlqsdTLLSSLTVRETLHYtALLAIRRgNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQ 209
Cdd:COG2884 89 -------RLLPDRTVYENVAL-PLRVTGK-SRKEIRRRVREVLDLVGLSDKAKALPHE-----LSGGEQQRVAIARALVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578803088 210 DPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIH 250
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATH 195
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
67-280 |
9.31e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 99.76 E-value: 9.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtfL-----GEVYVNGR------ALRREqfqdcFSYVLQS 135
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG--------LedptsGEILIGGRdvtdlpPKDRN-----IAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 136 DTLLSSLTVRETLhytAL-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNysLGGistGERRRVSIAAQLLQDPKVM 214
Cdd:COG3839 84 YALYPHMTVYENI---AFpLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQ--LSG---GQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803088 215 LFDEPTTGLDCMTANQIVVLLVELARRNRIVVL--TiHQPrSELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIyvT-HDQ-VEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
65-279 |
1.81e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 97.87 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRREQfQDCFSYVLQSDTLLSSLTV 144
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIL-APDS--GEVLWDGEPLDPED-RRRIGYLPEERGLYPKMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLHYtalLAIRRG-NPGSFQKKVEAVMAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGL 223
Cdd:COG4152 89 GEQLVY---LARLKGlSKAEAKRRADEWLERLGLGDRANKKVEELSKG-----NQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 224 DCMTANQIVVLLVELARRNRIVVLTIHQPRS-ElfQLFDKIAILSFGELIFCGTPAE 279
Cdd:COG4152 161 DPVNVELLKDVIRELAAKGTTVIFSSHQMELvE--ELCDRIVIINKGRKVLSGSVDE 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
66-281 |
2.38e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.12 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGR-AGTFLGE------VYVNGRALRReqfqdcFSYVLQSDTL 138
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRdAGNIIIDdedislLPLHARARRG------IGYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 139 LSSLTVRETLhyTALLAIRRG-NPGSFQKKVEAVMAELSLSHVADrlignySLG-GISTGERRRVSIAAQLLQDPKVMLF 216
Cdd:PRK10895 90 FRRLSVYDNL--MAVLQIRDDlSAEQREDRANELMEEFHIEHLRD------SMGqSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803088 217 DEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRsELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVR-ETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
66-282 |
3.39e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 95.37 E-value: 3.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG---RALRREQFQDCFSYVLQsDTLLSSL 142
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQK---GQILIDGidiRDISRKSLRSMIGVVLQ-DTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVRETlhytallaIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNY------SLGGISTGERRRVSIAAQLLQDPKVMLF 216
Cdd:cd03254 92 TIMEN--------IRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYdtvlgeNGGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 217 DEPTTGLDCMTANQIVVLLVELaRRNRIVVLTIHQPRSELFQlfDKIAILSFGELIFCGTPAEMLD 282
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKNA--DKILVLDDGKIIEEGTHDELLA 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
59-253 |
1.89e-21 |
|
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: 92.42 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 59 SCRQQWtRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL--RREQFQDCFSYVLQSD 136
Cdd:TIGR01189 7 ACSRGE-RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDS---GEVRWNGTPLaeQRDEPHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 137 TLLSSLTVRETLHYTALLAirrgnpGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLF 216
Cdd:TIGR01189 83 GLKPELSALENLHFWAAIH------GGAQRTIEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 578803088 217 DEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPR 253
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
371-578 |
4.39e-21 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 91.57 E-value: 4.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 371 LLRRVTRNLVRNKLAVITRLLQNLIMGLFL--LFFVLRvrsnvLKGAIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAV 448
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFgtLFGNLG-----NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 449 SDQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPN 528
Cdd:pfam01061 76 LYRELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578803088 529 IVNSVVALLSIAGVLVgSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVN 578
Cdd:pfam01061 156 DASQLGPLVLLPLLLL-SGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
68-271 |
5.20e-21 |
|
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: 91.55 E-value: 5.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQD-CFSYVLQSDTLLSSLTVRE 146
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTS---GRIYIGGRDVTDLPPKDrDIAMVFQNYALYPHMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 147 TLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCM 226
Cdd:cd03301 92 NIAFG--LKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQ-----LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578803088 227 TANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGEL 271
Cdd:cd03301 165 LRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
67-282 |
1.19e-20 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 91.21 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLdamsgrlgRAGTFL-----GEVYVNG----------RALRREqfqdcFSY 131
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLL--------RCINLLeepdsGTITVDGedltdskkdiNKLRRK-----VGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 132 VLQSDTLLSSLTVRE--TLhytALLAIRRgnpgsfQKKVEAV---MAELS---LSHVADRlignY--SLGGistGERRRV 201
Cdd:COG1126 82 VFQQFNLFPHLTVLEnvTL---APIKVKK------MSKAEAEeraMELLErvgLADKADA----YpaQLSG---GQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 202 SIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNR-IVVLTiHqprsEL-F--QLFDKIAILSFGELIFCGTP 277
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMtMVVVT-H----EMgFarEVADRVVFMDGGRIVEEGPP 220
|
....*
gi 578803088 278 AEMLD 282
Cdd:COG1126 221 EEFFE 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
66-252 |
1.21e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.32 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVR 145
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAA---GTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 146 ETLHYTAllAIRRGNPGSfqkkVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDc 225
Cdd:PRK13539 92 ENLEFWA--AFLGGEELD----IAAALEAVGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPTAALD- 159
|
170 180
....*....|....*....|....*....
gi 578803088 226 mTANQIVVLLVELARRNR--IVVLTIHQP 252
Cdd:PRK13539 160 -AAAVALFAELIRAHLAQggIVIAATHIP 187
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
60-269 |
1.67e-20 |
|
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: 89.86 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 60 CRQQWtRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL--RREQFQDCFSYVLQSDT 137
Cdd:cd03231 8 CERDG-RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLA---GRVLLNGGPLdfQRDSIARGLLYLGHAPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 138 LLSSLTVRETLHYTALLAIRRGnpgsfqkkVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFD 217
Cdd:cd03231 84 IKTTLSVLENLRFWHADHSDEQ--------VEEALARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578803088 218 EPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPrseLFQLFDKIAILSFG 269
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD---LGLSEAGARELDLG 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
66-282 |
1.77e-20 |
|
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: 90.75 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLL-------DAMSGRlgragtflgeVYVNGRALRR---EQFQDCFSYVLQs 135
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILrllfrfyDVSSGS----------ILIDGQDIREvtlDSLRRAIGVVPQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 136 DTLLSSLTVRETlhytallaIRRGNPGSFQKKVEAVmAELSlsHVADRLIG---NYS--LG--G--ISTGERRRVSIAAQ 206
Cdd:cd03253 83 DTVLFNDTIGYN--------IRYGRPDATDEEVIEA-AKAA--QIHDKIMRfpdGYDtiVGerGlkLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 207 LLQDPKVMLFDEPTTGLDCMTANQIVVLLVELArRNRIVVLTIHQPRSELFQlfDKIAILSFGELIFCGTPAEMLD 282
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVNA--DKIIVLKDGRIVERGTHEELLA 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
66-281 |
2.87e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.46 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNG---RALRREQFQDCFSYVLQsDTL 138
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR-------FYdptsGRILIDGvdiRDLTLESLRRQIGVVPQ-DTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 139 LSSLTVREtlhytallAIRRGNPGSFQKKVEAVMAELSLSHVADRL-------IGNyslGGI--STGERRRVSIAAQLLQ 209
Cdd:COG1132 425 LFSGTIRE--------NIRYGRPDATDEEVEEAAKAAQAHEFIEALpdgydtvVGE---RGVnlSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803088 210 DPKVMLFDEPTTGLDCMTANQIVVLLVELaRRNRIVVL------TIhqprselfQLFDKIAILSFGELIFCGTPAEML 281
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERL-MKGRTTIViahrlsTI--------RNADRILVLDDGRIVEQGTHEELL 562
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
65-281 |
3.94e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.07 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSgRLGRagTFLGEVYVNGRALRR---EQFQDCFSYVLQSDTLLSS 141
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLT--PQSGTVFLGDKPISMlssRQLARRLALLPQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 LTVREtlhytaLLAIRRGNPGSF--------QKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKV 213
Cdd:PRK11231 91 ITVRE------LVAYGRSPWLSLwgrlsaedNARVNQAMEQTRINHLADRRLTD-----LSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 214 MLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHqprsELFQ---LFDKIAILSFGELIFCGTPAEML 281
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH----DLNQasrYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
65-251 |
3.94e-20 |
|
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: 89.13 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtfL-----GEVYVNG----------RALRREqfqdcF 129
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINL--------LeepdsGTIIIDGlkltddkkniNELRQK-----V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 130 SYVLQSDTLLSSLTVRETLHYtALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQ 209
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITL-APIKVKGMSKAEAEERALELLEKVGLADKADAYPAQ-----LSGGQQQRVAIARALAM 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578803088 210 DPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 251
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
67-250 |
4.55e-20 |
|
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: 88.25 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL---------RREQFQdcfsYVLQS-D 136
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQS---GAVLIDGEPLdysrkglleRRQRVG----LVFQDpD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 137 TLLSSLTVRETLHYTAL-LAirrGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVML 215
Cdd:TIGR01166 79 DQLFAADVDQDVAFGPLnLG---LSEAEVERRVREALTAVGASGLRERPTHC-----LSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180 190
....*....|....*....|....*....|....*
gi 578803088 216 FDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIH 250
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
65-266 |
5.26e-20 |
|
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: 93.51 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALR---REQFQDCFSYVLQSDTLLSS 141
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG-FVDPTE--GSIAVNGVPLAdadADSWRDQIAWVPQHPFLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 lTVRETLhytaLLAIRRGNPGSFQKKVEAV-----MAELSLSHvaDRLIGNYSlGGISTGERRRVSIAAQLLQDPKVMLF 216
Cdd:TIGR02857 411 -TIAENI----RLARPDASDAEIREALERAgldefVAALPQGL--DTPIGEGG-AGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578803088 217 DEPTTGLDCMTANQIVVLLVELArRNRIVVLTIHQPrsELFQLFDKIAIL 266
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRL--ALAALADRIVVL 529
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
65-275 |
5.57e-20 |
|
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: 88.49 E-value: 5.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMsgrlgrAGTFL---GEVYVNGRALRREQFQDcFSYVLQSDTLLSS 141
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMI------LGIILpdsGEVLFDGKPLDIAARNR-IGYLPEERGLYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 LTVRETLHYTALLairRG-NPGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:cd03269 85 MKVIDQLVYLAQL---KGlKKEEARRRIDEWLERLELSEYANK-----RVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCG 275
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
69-250 |
6.19e-20 |
|
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: 88.62 E-value: 6.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMsgrLGRAGTFLGEVYVNGRA---LRREQ---FQDCFSYVLQSDTLLSSL 142
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLI---YKEELPTSGTIRVNGQDvsdLRGRAipyLRRKIGVVFQDFRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGnyslgGISTGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:cd03292 94 NVYENVAFA--LEVTGVPPREIRKRVPAALELVGLSHKHRALPA-----ELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180
....*....|....*....|....*...
gi 578803088 223 LDCMTANQIVVLLVELARRNRIVVLTIH 250
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
66-282 |
6.75e-20 |
|
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: 89.08 E-value: 6.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLD-------AMSGRLGRAGTFLGevYVNGRALRREqfqdcFSYVLQSDTL 138
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKliqrfyvPENGRVLVDGHDLA--LADPAWLRRQ-----VGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 139 LSSlTVRETlhytallaIRRGNPGSFQKKVEAVmAELSLSHV--------ADRLIGNYSLGgISTGERRRVSIAAQLLQD 210
Cdd:cd03252 88 FNR-SIRDN--------IALADPGMSMERVIEA-AKLAGAHDfiselpegYDTIVGEQGAG-LSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803088 211 PKVMLFDEPTTGLDCMTANQIVVLLVELArRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAH--RLSTVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
69-282 |
7.08e-20 |
|
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: 88.94 E-value: 7.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQD-CFSYVLQSDTLLSSLTVRET 147
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG-LERPDS--GTILFGGEDATDVPVQErNVGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 148 LHYTalLAIR----RGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGL 223
Cdd:cd03296 95 VAFG--LRVKprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQ-----LSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 224 DCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:cd03296 168 DAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
68-241 |
9.06e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 88.72 E-value: 9.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRAL-------RREQFQDCFSYVLQSDTLLS 140
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGG-LDTPTS--GDVIFNGQPMsklssaaKAELRNQKLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLHYTALlaIRRGNPGSFQKKVEAVMAELSLSHVAdrligNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:PRK11629 101 DFTALENVAMPLL--IGKKKPAEINSRALEMLAAVGLEHRA-----NHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180
....*....|....*....|.
gi 578803088 221 TGLDCMTANQIVVLLVELARR 241
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRL 194
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
67-239 |
1.11e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 88.53 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAM-------SGRLGRAG-TFLGEVYVN---GRALRREqfqdcFSYVLQS 135
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIAGhQFDFSQKPSekaIRLLRQK-----VGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 136 DTLLSSLTVRETLhYTALLAIRRGNPGSFQKKVEAVMAELSLSHVADRlignYSLGgISTGERRRVSIAAQLLQDPKVML 215
Cdd:COG4161 91 YNLWPHLTVMENL-IEAPCKVLGLSKEQAREKAMKLLARLRLTDKADR----FPLH-LSGGQQQRVAIARALMMEPQVLL 164
|
170 180
....*....|....*....|....
gi 578803088 216 FDEPTTGLDCMTANQIVVLLVELA 239
Cdd:COG4161 165 FDEPTAALDPEITAQVVEIIRELS 188
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
69-281 |
1.54e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.14 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRRE-----QFQDCFSYVLQS-DTLLSSL 142
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSS---GRILFDGKPIDYSrkglmKLRESVGMVFQDpDNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVRETLHYTALlaiRRGNP-GSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTT 221
Cdd:PRK13636 99 SVYQDVSFGAV---NLKLPeDEVRKRVDNALKRTGIEHLKDK-----PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 222 GLDCMTANQIVVLLVELARRNRIVVLtIHQPRSELFQLF-DKIAILSFGELIFCGTPAEML 281
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKELGLTII-IATHDIDIVPLYcDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
68-282 |
1.88e-19 |
|
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: 87.67 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLL-------DAMSGRLGRAGTFLGEVYVNgrALRREqfqdcFSYVLQsDTLLS 140
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVnliprfyDVDSGRILIDGHDVRDYTLA--SLRRQ-----IGLVSQ-DVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETlhytallaIRRGNPGSFQKKVEAVmAELSLSH-VADRLIGNY--SLG--GI--STGERRRVSIAAQLLQDPKV 213
Cdd:cd03251 89 NDTVAEN--------IAYGRPGATREEVEEA-ARAANAHeFIMELPEGYdtVIGerGVklSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 214 MLFDEPTTGLDCMTANQIVVLLVELArRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLM-KNRTTFVIAH--RLSTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
67-280 |
2.22e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 88.60 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRRE-----QFQDCFSYVLQ-SDTLLS 140
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTS---GEVLIKGEPIKYDkksllEVRKTVGIVFQnPDDQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLHYTALlairrgNPG----SFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLF 216
Cdd:PRK13639 93 APTVEEDVAFGPL------NLGlskeEVEKRVKEALKAVGMEGFENKPPHH-----LSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803088 217 DEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQprSELFQLF-DKIAILSFGELIFCGTPAEM 280
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
67-282 |
2.53e-19 |
|
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: 87.29 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL------RREqfqdcFSYVLQSDTLLS 140
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTS---GEILLDGKDItnlpphKRP-----VNTVFQNYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:cd03300 86 HLTVFENIAFG--LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQ-----LSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
65-282 |
2.54e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 89.44 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRalrreqfqDCFS----------YVLQ 134
Cdd:COG1118 14 SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG-LETPDS--GRIVLNGR--------DLFTnlpprerrvgFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 135 SDTLLSSLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVM 214
Cdd:COG1118 83 HYALFPHMTVAENIAFG--LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQ-----LSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 215 LFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI-HQpRSELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:COG1118 156 LLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVtHD-QEEALELADRVVVMNQGRIEQVGTPDEVYD 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
66-272 |
2.82e-19 |
|
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: 86.85 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFL--GEVYVNGR----------ALRREqfqdcFSYVL 133
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPdeGEVLLDGKdiydldvdvlELRRR-----VGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 134 QSDTLLSsLTVRETLHYTalLAIRrgnpGSFQKKVEAVMAELSLS------HVADRLIGnyslGGISTGERRRVSIAAQL 207
Cdd:cd03260 88 QKPNPFP-GSIYDNVAYG--LRLH----GIKLKEELDERVEEALRkaalwdEVKDRLHA----LGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 208 LQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLT--IHQPRSelfqLFDKIAILSFGELI 272
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQAAR----VADRTAFLLNGRLV 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
67-281 |
5.45e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.65 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLL-------DAMSGrlgragtflgEVYVNGRALRR---EQFQDCFSYVLQSD 136
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLqlltrawDPQQG----------EILLNGQPIADyseAALRQAISVVSQRV 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 137 TLLSSlTVRETLhytaLLAirrgNPGSFQKKVEAVMAELSLSHVADrliGNYSL------GG--ISTGERRRVSIAAQLL 208
Cdd:PRK11160 424 HLFSA-TLRDNL----LLA----APNASDEALIEVLQQVGLEKLLE---DDKGLnawlgeGGrqLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803088 209 QDPKVMLFDEPTTGLDCMTANQIVVLLVELArRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITH--RLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
66-279 |
6.12e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.60 E-value: 6.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAM-------SGRLGRAGTFLGEVYVNGRALrreqfqdcfSYVLQSDTL 138
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIaglehqtSGHIRFHGTDVSRLHARDRKV---------GFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 139 LSSLTVRETLHY--TALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLF 216
Cdd:PRK10851 86 FRHMTVFDNIAFglTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQ-----LSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803088 217 DEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAE 279
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
67-251 |
6.41e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.22 E-value: 6.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAM-------SGRLGRAGT---FLGEVYVN-GRALRREqfqdcFSYVLQS 135
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNhfdFSKTPSDKaIRELRRN-----VGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 136 DTLLSSLTVRETLhYTALLAIRRGNPGSFQKKVEAVMAELSLSHVADRlignYSLGgISTGERRRVSIAAQLLQDPKVML 215
Cdd:PRK11124 91 YNLWPHLTVQQNL-IEAPCRVLGLSKDQALARAEKLLERLRLKPYADR----FPLH-LSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 578803088 216 FDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 251
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
68-281 |
1.29e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.36 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR----REQFQDCFSyVLQSDTLLSSLT 143
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA---GTVLVAGDDVEalsaRAASRRVAS-VPQDTSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETL------HYTallaiRRGNPGSFQKK-VEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLF 216
Cdd:PRK09536 94 VRQVVemgrtpHRS-----RFDTWTETDRAaVERAMERTGVAQFADR-----PVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 217 DEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQprSELFQLF-DKIAILSFGELIFCGTPAEML 281
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHD--LDLAARYcDELVLLADGRVRAAGPPADVL 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
68-252 |
1.34e-18 |
|
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: 89.34 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG---RALRREQFQDCFSYVLQSDTLLSSlTV 144
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ---GEVTLDGvpvSSLDQDEVRRRVSVCAQDAHLFDT-TV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLhytallaiRRGNPGSFQKKVEAVMAELSLSHVADRLIGNYS--LGG----ISTGERRRVSIAAQLLQDPKVMLFDE 218
Cdd:TIGR02868 426 RENL--------RLARPDATDEELWAALERVGLADWLRALPDGLDtvLGEggarLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|....
gi 578803088 219 PTTGLDCMTANQIVVLLVElARRNRIVVLTIHQP 252
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
62-272 |
1.37e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.16 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 62 QQWTRQI--LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSgRLGRAGTflGEVYVNGR--------ALRREQ------F 125
Cdd:PRK11153 12 PQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCIN-LLERPTS--GRVLVDGQdltalsekELRKARrqigmiF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 126 QDcFSyvlqsdtLLSSLTVRETLhytAL-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIA 204
Cdd:PRK11153 89 QH-FN-------LLSSRTVFDNV---ALpLELAGTPKAEIKARVTELLELVGLSDKADRYPAQ-----LSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 205 AQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI-HQpRSELFQLFDKIAILSFGELI 272
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLItHE-MDVVKRICDRVAVIDAGRLV 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
73-282 |
1.46e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 85.19 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 73 SLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNGRAL-RREQFQDCFSYVLQSDTLLSSLTVRET 147
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAG-------FLppdsGRILWNGQDLtALPPAERPVSMLFQENNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 148 LhytaLLAIR-RGNPGSFQK-KVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 225
Cdd:COG3840 92 I----GLGLRpGLKLTAEQRaQVEQALERVGLAGLLDRLPGQ-----LSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578803088 226 MTANQIVVLLVELARRNRIVVLTI-HQPRsELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:COG3840 163 ALRQEMLDLVDELCRERGLTVLMVtHDPE-DAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
66-279 |
1.46e-18 |
|
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: 85.97 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNG-----------RALRRE-----QF---Q 126
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLL-KPTS--GTVTIDGrditakkkkklKDLRKKvglvfQFpehQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 127 dcfsyvlqsdtlLSSLTVRETLHYtallairrGnPGSF-------QKKVEAVMAELSLSH-VADRlignySLGGISTGER 198
Cdd:TIGR04521 95 ------------LFEETVYKDIAF--------G-PKNLglseeeaEERVKEALELVGLDEeYLER-----SPFELSGGQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 199 RRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR-RNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTP 277
Cdd:TIGR04521 149 RRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHS-MEDVAEYADRVIVMHKGKIVLDGTP 227
|
..
gi 578803088 278 AE 279
Cdd:TIGR04521 228 RE 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
68-271 |
1.81e-18 |
|
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: 83.03 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR---REQFQDCFSYVLQSDTLLSsltv 144
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTS---GRVRLDGADISqwdPNELGDHVGYLPQDDELFS---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 retlhytallairrgnpGSfqkkveavmaelslshVADRLignyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 224
Cdd:cd03246 90 -----------------GS----------------IAENI--------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 578803088 225 CMTANQIVVLLVELARRNRIVVLTIHQPrsELFQLFDKIAILSFGEL 271
Cdd:cd03246 129 VEGERALNQAIAALKAAGATRIVIAHRP--ETLASADRILVLEDGRV 173
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
69-271 |
2.10e-18 |
|
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: 83.25 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRReqfqdcfsyvlqsdtllssLTVREtl 148
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPAS---GEITLDGKPVTR-------------------RSPRD-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 149 hytallAIRRGN---PGSfqKKVEAVMAELSlshVADRLIGNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 225
Cdd:cd03215 72 ------AIRAGIayvPED--RKREGLVLDLS---VAENIALSSLLSG---GNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 578803088 226 MTANQIVVLLVELARRNR-IVVLTIHQPrsELFQLFDKIAILSFGEL 271
Cdd:cd03215 138 GAKAEIYRLIRELADAGKaVLLISSELD--ELLGLCDRILVMYEGRI 182
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
67-275 |
3.44e-18 |
|
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: 82.36 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAgtfLGEVYVNGR--ALRREQFQDCFSYVLQSDTLLSSlTV 144
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ---QGEITLDGVpvSDLEKALSSLISVLNQRPYLFDT-TL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLHytallaiRRgnpgsfqkkveavmaelslshvadrlignyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 224
Cdd:cd03247 92 RNNLG-------RR----------------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578803088 225 CMTANQIVVLLVELArRNRIVVLTIHQPRSelFQLFDKIAILSFGELIFCG 275
Cdd:cd03247 131 PITERQLLSLIFEVL-KDKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
65-281 |
4.95e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 84.27 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRRE---QFQDCFSYVLQS-DTLLS 140
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQS---GEIKIDGITISKEnlkEIRKKIGIIFQNpDNQFI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:PRK13632 98 GATVEDDIAFG--LENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----LSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFqLFDKIAILSFGELIFCGTPAEML 281
Cdd:PRK13632 171 SMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEIL 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
71-241 |
5.14e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 85.10 E-value: 5.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 71 DVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGR---ALRREQFQD----CFSYVLQSDtlLSSL- 142
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEdllKLSEKELRKirgrEIQMIFQDP--MTSLn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 ---TVRETLHYtALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLiGNY--SLGGistGERRRVSIAAQLLQDPKVMLFD 217
Cdd:COG0444 101 pvmTVGDQIAE-PLRIHGGLSKAEARERAIELLERVGLPDPERRL-DRYphELSG---GMRQRVMIARALALEPKLLIAD 175
|
170 180
....*....|....*....|....
gi 578803088 218 EPTTGLDCMTANQIVVLLVELARR 241
Cdd:COG0444 176 EPTTALDVTIQAQILNLLKDLQRE 199
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
66-281 |
9.51e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 83.72 E-value: 9.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRL-----GRAGTFLGEVYVNGRALRREQFQD--CFSYVL-QSDT 137
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaPRGARVTGDVTLNGEPLAAIDAPRlaRLRAVLpQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 138 LLSSLTVRETLHYTALLAIRRGNPGSFQKKvEAVMAELSLSHvADRLIGNySLGGISTGERRRVSIA---AQL------L 208
Cdd:PRK13547 94 PAFAFSAREIVLLGRYPHARRAGALTHRDG-EIAWQALALAG-ATALVGR-DVTTLSGGELARVQFArvlAQLwpphdaA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803088 209 QDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI-HQPRSELfQLFDKIAILSFGELIFCGTPAEML 281
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPNLAA-RHADRIAMLADGAIVAHGAPADVL 243
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
71-275 |
2.35e-17 |
|
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: 81.00 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 71 DVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQD-CFSYVLQSDTLLSSLTVRETLH 149
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQS---GRVLINGVDVTAAPPADrPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 150 ytalLAIrrgNPG-----SFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 224
Cdd:cd03298 93 ----LGL---SPGlkltaEDRQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578803088 225 CMTANQIVVLLVELARRNRIVVLTI-HQPrSELFQLFDKIAILSFGELIFCG 275
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVtHQP-EDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
66-281 |
2.64e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.14 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDaMSGRLGRAGTflGEVYVNGRAL---RREQFQDCFSYVLQSDTLLSSL 142
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSE--GEILLDAQPLeswSSKAFARKVAYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVREtlhytaLLAIRR----GNPGSF----QKKVEAVMAELSLSHVADRLIGnySLGGistGERRRVSIAAQLLQDPKVM 214
Cdd:PRK10575 101 TVRE------LVAIGRypwhGALGRFgaadREKVEEAISLVGLKPLAHRLVD--SLSG---GERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 215 LFDEPTTGLDcmTANQIVVL-LVE-LARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:PRK10575 170 LLDEPTSALD--IAHQVDVLaLVHrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
66-252 |
2.91e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 80.62 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALR--REQFQDCFSYVLQSDTLLSSLT 143
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG-LARPDA--GEVLWQGEPIRrqRDEYHQDLLYLGHQPGIKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLHYTALLAirrGNPGSFQkkVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGL 223
Cdd:PRK13538 91 ALENLRFYQRLH---GPGDDEA--LWEALAQVGLAGFEDVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....*....
gi 578803088 224 DCMTANQIVVLLVELARRNRIVVLTIHQP 252
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
69-294 |
3.17e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.20 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNG-----------RALRREqfqdcFSYVLQSDT 137
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LERPTS--GSVLVDGvdltalserelRAARRK-----IGMIFQHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 138 LLSSLTVRETLhytAL-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLF 216
Cdd:COG1135 93 LLSSRTVAENV---ALpLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQ-----LSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 217 DEPTTGLDCMTANQIVVLLVELARRNRI-VVLTIHQP---RselfQLFDKIAILSFGELIFCGTpaeMLDFFNDcgypcP 292
Cdd:COG1135 165 DEATSALDPETTRSILDLLKDINRELGLtIVLITHEMdvvR----RICDRVAVLENGRIVEQGP---VLDVFAN-----P 232
|
..
gi 578803088 293 EH 294
Cdd:COG1135 233 QS 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
67-252 |
3.46e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.16 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMsGRLGRAGTflGEVYVNGR-----------ALRREQFqdcfSYVLQS 135
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLDKPTS--GTYRVAGQdvatldadalaQLRREHF----GFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 136 DTLLSSLTVRETLHYTALLAirrGNP-GSFQKKVEAVMAELSLshvADRLigNYSLGGISTGERRRVSIAAQLLQDPKVM 214
Cdd:PRK10535 95 YHLLSHLTAAQNVEVPAVYA---GLErKQRLLRAQELLQRLGL---EDRV--EYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 578803088 215 LFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQP 252
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
68-253 |
3.98e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.59 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLL-------DAMSGRLGRAGTFLGEVYVNGRALRREQFqdcFSYVLQSDTLLS 140
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLailagldDGSSGEVSLVGQPLHQMDEEARAKLRAKH---VGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLHYTALLaiRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:PRK10584 102 TLNALENVELPALL--RGESSRQSRNGAKALLEQLGLGKRLDHLPAQ-----LSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190
....*....|....*....|....*....|....
gi 578803088 221 TGLDCMTANQIVVLLVELARR-NRIVVLTIHQPR 253
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQ 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
66-281 |
4.55e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.25 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSgRL-----------GRAGTFLGEVY-VNGRALRREqfqdcFSYVL 133
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLN-RLieiydskikvdGKVLYFGKDIFqIDAIKLRKE-----VGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 134 QSDTLLSSLTVRETLHYtALLAIRRGNPGSFQKKVEAVMAELSL-SHVADRLigNYSLGGISTGERRRVSIAAQLLQDPK 212
Cdd:PRK14246 97 QQPNPFPHLSIYDNIAY-PLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRL--NSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 213 VMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTiHQPRsELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNPQ-QVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
69-272 |
1.51e-16 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 78.79 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNG--------RALRREqfqdcFSYVLQSDTLLS 140
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAG-LYKPTS--GSVLLDGtdirqldpADLRRN-----IGYVPQDVTLFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SlTVRETLHYTALLAirrgnpgsfqkKVEAVMAELSLSHVADrLIGNYSLG----------GISTGERRRVSIAAQLLQD 210
Cdd:cd03245 92 G-TLRDNITLGAPLA-----------DDERILRAAELAGVTD-FVNKHPNGldlqigergrGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803088 211 PKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTiHqpRSELFQLFDKIAILSFGELI 272
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIIT-H--RPSLLDLVDRIIVMDSGRIV 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
69-250 |
1.56e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.93 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSG--RLGRagtflGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVre 146
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGfvRLAS-----GKISILGQPTRQALQKNLVAYVPQSEEVDWSFPV-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 147 tLHYTALLAIRRGNPGSF-------QKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEP 219
Cdd:PRK15056 96 -LVEDVVMMGRYGHMGWLrrakkrdRQIVTAALARVDMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190
....*....|....*....|....*....|.
gi 578803088 220 TTGLDCMTANQIVVLLVELARRNRIVVLTIH 250
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
67-276 |
1.69e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.67 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRRE--------QFQDCFSYVLQSDTL 138
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREgrlardirKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 139 LSSLTVRETLHYTAL-------LAIRRGNPGSFQKKVEAvMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:PRK09984 98 VNRLSVLENVLIGALgstpfwrTCFSWFTREQKQRALQA-LTRVGMVHFAHQRVST-----LSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 212 KVMLFDEPTTGLDCMTANQIVVLLVELARRNRI-VVLTIHQPRSELfQLFDKIAILSFGELIFCGT 276
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDINQNDGItVVVTLHQVDYAL-RYCERIVALRQGHVFYDGS 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
67-251 |
1.99e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 79.24 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLdamsgrlgRAGTFL-----GEVYVNGRALR-------------REQFQDC 128
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFL--------RCINFLekpseGSIVVNGQTINlvrdkdgqlkvadKNQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 129 ---FSYVLQSDTLLSSLTVRETLHYTALLAIrrgnpgSFQKKVEAVMAELSLSHVA--DRLIGNYSLGgISTGERRRVSI 203
Cdd:PRK10619 91 rtrLTMVFQHFNLWSHMTVLENVMEAPIQVL------GLSKQEARERAVKYLAKVGidERAQGKYPVH-LSGGQQQRVSI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578803088 204 AAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 251
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
67-272 |
2.19e-16 |
|
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: 76.70 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALrreqfqdcfsyvlqsdtllSSLTVRE 146
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS---GEILVDGKEV-------------------SFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 147 tlhytallAIRRGnpgsfqkkVEAVmaelslshvadrlignYSLggiSTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCM 226
Cdd:cd03216 72 --------ARRAG--------IAMV----------------YQL---SVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 578803088 227 TANQIVVLLVELARRNRIVVLTIHQPRsELFQLFDKIAILSFGELI 272
Cdd:cd03216 117 EVERLFKVIRRLRAQGVAVIFISHRLD-EVFEIADRVTVLRDGRVV 161
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
72-281 |
3.01e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.82 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 72 VSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgragTFLGEVYVNGRAL----------RReqfqdcfSYVLQSDTLLSS 141
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL----PGSGSIQFAGQPLeawsaaelarHR-------AYLSQQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 LTVretLHYTALLAIRRGNPGSFQKKVEAVMAELSLshvADRLigNYSLGGISTGERRRVSIAAQLLQ-------DPKVM 214
Cdd:PRK03695 84 MPV---FQYLTLHQPDKTRTEAVASALNEVAEALGL---DDKL--GRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 215 LFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLfDKIAILSFGELIFCGTPAEML 281
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHA-DRVWLLKQGKLLASGRRDEVL 221
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
69-250 |
3.19e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 79.75 E-value: 3.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGR--ALRREQFQDCFSYVL-QSDTLLSSLTVR 145
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTS---GEVRVLGYvpFKRRKEFARRIGVVFgQRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 146 ETLHYTAllAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLDC 225
Cdd:COG4586 115 DSFRLLK--AIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLG-----QRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180
....*....|....*....|....*.
gi 578803088 226 MTANQIVVLLVEL-ARRNRIVVLTIH 250
Cdd:COG4586 188 VSKEAIREFLKEYnRERGTTILLTSH 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
80-287 |
3.68e-16 |
|
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: 82.75 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 80 QIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR--EQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIR 157
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTS---GTVLVGGKDIETnlDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGR 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 158 RGNPGsfQKKVEAVMAELSLSHVAdrligNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 237
Cdd:TIGR01257 1034 SWEEA--QLEMEAMLEDTGLHHKR-----NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK 1106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578803088 238 LARRNRIVVLTIHQPRSELfqLFDKIAILSFGELIFCGTPAemldFFNDC 287
Cdd:TIGR01257 1107 YRSGRTIIMSTHHMDEADL--LGDRIAIISQGRLYCSGTPL----FLKNC 1150
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
69-282 |
5.11e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.46 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSgRLGRAGTflGEVYVNG-----------RALRREQFqdcfSYVLQSDT 137
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN-RLIEPTR--GQVLIDGvdiakisdaelREVRRKKI----AMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 138 LLSSLTVRETLHYTALLAirrGNPGSFQKkveavmaELSLSHVADRLIGNYSLG---GISTGERRRVSIAAQLLQDPKVM 214
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELA---GINAEERR-------EKALDALRQVGLENYAHSypdELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803088 215 LFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
67-284 |
5.25e-16 |
|
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: 81.00 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSG-------------------------RLGRAGT------------- 108
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgriiyhvalcekcgyveRPSKVGEpcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 109 --FLGEVYVNGRALRRE---QFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRGnpgsfQKKVEAVMAELSLSHVADR 183
Cdd:TIGR03269 94 vdFWNLSDKLRRRIRKRiaiMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRA-----VDLIEMVQLSHRITHIARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 184 LIGnyslggistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRI-VVLTIHQPRSeLFQLFDK 262
Cdd:TIGR03269 169 LSG---------GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIsMVLTSHWPEV-IEDLSDK 238
|
250 260
....*....|....*....|..
gi 578803088 263 IAILSFGELIFCGTPAEMLDFF 284
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVAVF 260
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
66-249 |
6.30e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.82 E-value: 6.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLG-RAGTF-LGEVYVNGRALRReqfqdcfSYVLQSDTLLSSLT 143
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyQHGSItLDGKPVEGPGAER-------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLHYTALLAirrGNPGSFQKKVEAVM-AELSLSHVADRLIgnYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:PRK11248 87 VQDNVAFGLQLA---GVEKMQRLEIAHQMlKKVGLEGAEKRYI--WQLSG---GQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180
....*....|....*....|....*..
gi 578803088 223 LDCMTANQIVVLLVELARRNRIVVLTI 249
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLI 185
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
68-285 |
6.44e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.12 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRL-GRAGTF-LGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLT-- 143
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkSKYGTIqVGDIYIGDKKNNHELITNPYSKKIKNFKELRRRVsm 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLHY-----TALLAIRRGNPGSFQKKVEAvmAELSLSHVADRLIGNYSLG----GISTGERRRVSIAAQLLQDPKVM 214
Cdd:PRK13631 121 VFQFPEYqlfkdTIEKDIMFGPVALGVKKSEA--KKLAKFYLNKMGLDDSYLErspfGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 215 LFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEMldFFN 285
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTGTPYEI--FTD 266
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
76-289 |
7.03e-16 |
|
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: 81.60 E-value: 7.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 76 VESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR--EQFQDCFSYVLQSDTLLSSLTVRETLHYTAL 153
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTS---GDATVAGKSILTniSDVHQNMGYCPQFDAIDDLLTGREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 154 LairRGNPGsfqKKVEAV----MAELSLSHVADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTAN 229
Cdd:TIGR01257 2039 L---RGVPA---EEIEKVanwsIQSLGLSLYADRLAGTYS-----GGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 230 QIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDcGY 289
Cdd:TIGR01257 2108 MLWNTIVSIIREGRAVVLTSHS-MEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGD-GY 2165
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
61-266 |
9.69e-16 |
|
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: 75.97 E-value: 9.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 61 RQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRalrreqfqdcFSYVLQSDTLLS 140
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLS---GSVSVPGS----------IAYVSQEPWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SlTVRETlhytallaIRRGNPgsFQKK-----VEA--------VMAELSLSHVADRlignyslgGI--STGERRRVSIAA 205
Cdd:cd03250 80 G-TIREN--------ILFGKP--FDEEryekvIKAcalepdleILPDGDLTEIGEK--------GInlSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803088 206 QLLQDPKVMLFDEPTTGLDCMTANQIV--VLLVELaRRNRIVVLTIHQPrsELFQLFDKIAIL 266
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIFenCILGLL-LNNKTRILVTHQL--QLLPHADQIVVL 200
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
68-280 |
1.01e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.92 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLL-------DAMSGRLgragtFLGEVYVN-----GRALrreqfqdcfSYVLQS 135
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLrmiagleDITSGDL-----FIGEKRMNdvppaERGV---------GMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 136 DTLLSSLTVRETLHYTALLAirRGNPGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVML 215
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLA--GAKKEEINQRVNQVAEVLQLAHLLDR-----KPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 216 FDEPTTGLDCMTANQIVVLLVELARR-NRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHD-QVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
66-253 |
1.11e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.03 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTfLGEVYVNG----------RAlRREQFqdcfsYVLQS 135
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVT-SGSILLDGedilelspdeRA-RAGIF-----LAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 136 DTLLSSLTVRETLHyTALLAIRRGNPGS--FQKKVEAVMAELSLSH-VADRlignySL-GGISTGERRRVSIAAQLLQDP 211
Cdd:COG0396 86 PVEIPGVSVSNFLR-TALNARRGEELSAreFLKLLKEKMKELGLDEdFLDR-----YVnEGFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578803088 212 KVMLFDEPTTGLDcMTANQIVVLLV-ELARRNRIVVLTIHQPR 253
Cdd:COG0396 160 KLAILDETDSGLD-IDALRIVAEGVnKLRSPDRGILIITHYQR 201
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
69-279 |
1.27e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 77.40 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG----------RALRRE-----QFQDcfsYVL 133
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTS---GKIIIDGvditdkkvklSDIRKKvglvfQYPE---YQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 134 QSDTLLSSLtvretlhytALLAIRRG-NPGSFQKKVEAVMAELSLSH--VADRlignySLGGISTGERRRVSIAAQLLQD 210
Cdd:PRK13637 97 FEETIEKDI---------AFGPINLGlSEEEIENRVKRAMNIVGLDYedYKDK-----SPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 211 PKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAE 279
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
66-251 |
3.11e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.56 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAM-------SGRLGragtfLGEVYVNG-RALRREQ-----FQDCFSYV 132
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIR-----VGDITIDTaRSLSQQKglirqLRQHVGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 133 LQSDTLLSSLTVRETLHYTALlaIRRGNP-GSFQKKVEAVMAELSLSHVAD----RLIGnyslggistGERRRVSIAAQL 207
Cdd:PRK11264 91 FQNFNLFPHRTVLENIIEGPV--IVKGEPkEEATARARELLAKVGLAGKETsyprRLSG---------GQQQRVAIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578803088 208 LQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQ 251
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
67-282 |
4.14e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.13 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAM-------SGRLGRAGTFLGEVYVNGRALRREQfqdcfSYVLQSDTLL 139
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKVNDPKVDERLIRQEA-----GMVFQQFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 140 SSLTVRETLHYTALlAIRRGNPGSFQKKVEAVMAELSLSHVAdrligNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEP 219
Cdd:PRK09493 90 PHLTALENVMFGPL-RVRGASKEEAEKQARELLAKVGLAERA-----HHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 220 TTGLDCMTANQIVVLLVELARRNRIVVLTIHQprselFQLFDKIAilsfGELIFC--------GTPAEMLD 282
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAEEGMTMVIVTHE-----IGFAEKVA----SRLIFIdkgriaedGDPQVLIK 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
67-281 |
6.67e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.95 E-value: 6.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSG--RLGRAGTFLGEVYVNGRAL---------RREQFqdcfsyVLQS 135
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEARVSGEVYLDGQDIfkmdvielrRRVQM------VFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 136 DTLLSSLTVRETLHYTALLAIRRGNPGSFQKKVEAVMAELSL-SHVADRLigNYSLGGISTGERRRVSIAAQLLQDPKVM 214
Cdd:PRK14247 91 PNPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLwDEVKDRL--DAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 215 LFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTiHQPrSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVT-HFP-QQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
67-281 |
7.06e-15 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 74.50 E-value: 7.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLdAMSGRLgrAGTFLGEVYVNGRALRR---EQFQDCFSYVLQSDTLLSSlT 143
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVV-SLLERF--YDPTSGEILLDGVDIRDlnlRWLRSQIGLVSQEPVLFDG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETlhytallaIRRGNPGSFQKKVEAV--MAEL-----SLSHVADRLIGNY--SLGGistGERRRVSIAAQLLQDPKVM 214
Cdd:cd03249 93 IAEN--------IRYGKPDATDEEVEEAakKANIhdfimSLPDGYDTLVGERgsQLSG---GQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803088 215 LFDEPTTGLDcmTANQIVVL-LVELARRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:cd03249 162 LLDEATSALD--AESEKLVQeALDRAMKGRTTIVIAH--RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
65-224 |
7.44e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.41 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRaLRreqfqdcFSYVLQSDTLLSSLTV 144
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDS---GEVSIPKG-LR-------IGYLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETL-----------------------------HYTALLA-IRRGNPGSFQKKVEAVMAELSLSHV-ADRLIGNYSlgGi 193
Cdd:COG0488 79 LDTVldgdaelraleaeleeleaklaepdedleRLAELQEeFEALGGWEAEARAEEILSGLGFPEEdLDRPVSELS--G- 155
|
170 180 190
....*....|....*....|....*....|.
gi 578803088 194 stGERRRVSIAAQLLQDPKVMLFDEPTTGLD 224
Cdd:COG0488 156 --GWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
69-294 |
7.72e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.16 E-value: 7.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLG-RAGTF-LGEVYVNGRALRREqfqdcFSYVLQSDTLLSSLTVRE 146
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVtVGDIVVSSTSKQKE-----IKPVRKKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 147 TLHYTALLAIRRG--NPGSFQKKVEAVMAElSLSHVA-DRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGL 223
Cdd:PRK13643 97 LFEETVLKDVAFGpqNFGIPKEKAEKIAAE-KLEMVGlADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 224 DCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEM---LDFF--NDCGYPCPEH 294
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHL-MDDVADYADYVYLLEKGHIISCGTPSDVfqeVDFLkaHELGVPKATH 250
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
67-224 |
1.02e-14 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 74.45 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLdamsgrlgRAGTFL-----GEVYVNGRALR-------------REQFQDC 128
Cdd:COG4598 22 EVLKGVSLTARKGDVISIIGSSGSGKSTFL--------RCINLLetpdsGEIRVGGEEIRlkpdrdgelvpadRRQLQRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 129 ---FSYVLQSDTLLSSLTVRET-----LHytaLLAIRRGNPgsfQKKVEAVMAELSLSHVADrlignYSLGGISTGERRR 200
Cdd:COG4598 94 rtrLGMVFQSFNLWSHMTVLENvieapVH---VLGRPKAEA---IERAEALLAKVGLADKRD-----AYPAHLSGGQQQR 162
|
170 180
....*....|....*....|....
gi 578803088 201 VSIAAQLLQDPKVMLFDEPTTGLD 224
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALD 186
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
68-282 |
1.47e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.25 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTT----LLDAMSGRLGRAgTFLGE-VYVNGRALRREqfqdcFSYVLQSDTLLSSL 142
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTiarmILGMTSPDAGKI-TVLGVpVPARARLARAR-----IGVVPQFDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVRETL----HYTALLAirrgnpgsfqKKVEAVMAEL----SLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVM 214
Cdd:PRK13536 130 TVRENLlvfgRYFGMST----------REIEAVIPSLlefaRLESKADARVSD-----LSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803088 215 LFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHF-MEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
69-241 |
2.07e-14 |
|
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: 75.88 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSgRLGRAGtflGEVYVNG-----------RALRRE-Q--FQDCFSyvlq 134
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALL-RLIPSE---GEIRFDGqdldglsrralRPLRRRmQvvFQDPFG---- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 135 sdtllsSL----TVRET------LHYTALLAIRRgnpgsfQKKVEAVMAELSLSH-VADRLIGNYSlgGistGERRRVSI 203
Cdd:COG4172 374 ------SLsprmTVGQIiaeglrVHGPGLSAAER------RARVAEALEEVGLDPaARHRYPHEFS--G---GQRQRIAI 436
|
170 180 190
....*....|....*....|....*....|....*...
gi 578803088 204 AAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARR 241
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQRE 474
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
67-279 |
2.14e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.04 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtFL---GEVYVNG---RALRREQFQDCFSYVLQSDTLLS 140
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-------FLpyqGSLKINGielRELDPESWRKHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SlTVRETLhytaLLairrGNPGSFQKKVEAVMAELSLSHVADRL-------IGNYSlGGISTGERRRVSIAAQLLQDPKV 213
Cdd:PRK11174 437 G-TLRDNV----LL----GNPDASDEQLQQALENAWVSEFLPLLpqgldtpIGDQA-AGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803088 214 MLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTiHQprseLFQL--FDKIAILSFGELIFCGTPAE 279
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQ----LEDLaqWDQIWVMQDGQIVQQGDYAE 569
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
67-294 |
2.20e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 73.34 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSG--RLGRAGTFLGEVYVNGRALRRE-----QFQDCFSYVLQSDTLL 139
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEARVEGEVRLFGRNIYSPdvdpiEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 140 SSLTVRET----LHYTALLAIRrgnpGSFQKKVEAVMAELSL-SHVADRLigNYSLGGISTGERRRVSIAAQLLQDPKVM 214
Cdd:PRK14267 98 PHLTIYDNvaigVKLNGLVKSK----KELDERVEWALKKAALwDEVKDRL--NDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 215 LFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTiHQPrSELFQLFDKIAILSFGELIFCGtPAEMLdFFNdcgypcPEH 294
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSP-AQAARVSDYVAFLYLGKLIEVG-PTRKV-FEN------PEH 241
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
68-282 |
3.59e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSG-RLGRAGT--FLGEVyVNGRALRREQFqdcFSYVLQSDTLLSSLTV 144
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGlTHPDAGSisLCGEP-VPSRARHARQR---VGVVPQFDNLDPDFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETL----HYTALLAirrgnpGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:PRK13537 98 RENLlvfgRYFGLSA------AAARALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGKTILLTTHF-MEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
69-223 |
6.36e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 74.29 E-value: 6.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNGRALRREQFQDCFSY----VLQSDTLLS 140
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYG-------LYqpdsGEILIDGKPVRIRSPRDAIALgigmVHQHFMLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLhytaLLAIRRGNPGSF-----QKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVML 215
Cdd:COG3845 94 NLTVAENI----VLGLEPTKGGRLdrkaaRARIRELSERYGLDVDPDAKVED-----LSVGEQQRVEILKALYRGARILI 164
|
....*...
gi 578803088 216 FDEPTTGL 223
Cdd:COG3845 165 LDEPTAVL 172
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
65-280 |
6.93e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.14 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFSYV----LQSDTLLS 140
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTS---GSVLIRGEPITKENIREVRKFVglvfQNPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLhytALLAIRRG-NPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEP 219
Cdd:PRK13652 93 SPTVEQDI---AFGPINLGlDEETVAHRVSSALHMLGLEELRDRVPHH-----LSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803088 220 TTGLDCMTANQIVVLLVELARR-NRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQ-LDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
69-280 |
7.16e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRREQFQDCF----SYVLQSDTLLSSLTV 144
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVY-QPDS--GEILLDGEPVRFRSPRDAQaagiAIIHQELNLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLhYTALLAIRRG--NPGSFQKKVEAVMAELSLSHVADRLIGNYSLggistGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:COG1129 97 AENI-FLGREPRRGGliDWRAMRRRARELLARLGLDIDPDTPVGDLSV-----AQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803088 223 LdcmTANQIVVLLV---ELARRNRIVVLTIHqpR-SELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:COG1129 171 L---TEREVERLFRiirRLKAQGVAIIYISH--RlDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
66-300 |
7.20e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.73 E-value: 7.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMS--GRLGRAGTFLGEVYVNGR----------ALRREqfqdcFSYVL 133
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVTITGSIVYNGHniysprtdtvDLRKE-----IGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 134 QSDTLLSsLTVRETLHYTALLAirrgnpGSFQKKV--EAVmaELSL------SHVADRLigNYSLGGISTGERRRVSIAA 205
Cdd:PRK14239 93 QQPNPFP-MSIYENVVYGLRLK------GIKDKQVldEAV--EKSLkgasiwDEVKDRL--HDSALGLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 206 QLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELarRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMldFFN 285
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM--FMN 237
|
250
....*....|....*
gi 578803088 286 dcgypcPEHSNPFDF 300
Cdd:PRK14239 238 ------PKHKETEDY 246
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
34-286 |
1.04e-13 |
|
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: 73.71 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 34 EPHSLG--ILHASYSVShrvrpwWDITSCRqqwtRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlGRAGTFLG 111
Cdd:TIGR02633 249 EPHEIGdvILEARNLTC------WDVINPH----RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG--AYPGKFEG 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 112 EVYVNGRALRREQFQDCFSYVL-------QSDTLLSSLTVRETLHYTAL---LAIRRGNPGSFQKKVEAVMAELSLSHVA 181
Cdd:TIGR02633 317 NVFINGKPVDIRNPAQAIRAGIamvpedrKRHGIVPILGVGKNITLSVLksfCFKMRIDAAAELQIIGSAIQRLKVKTAS 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 182 DRLignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNrIVVLTIHQPRSELFQLFD 261
Cdd:TIGR02633 397 PFL----PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEG-VAIIVVSSELAEVLGLSD 471
|
250 260
....*....|....*....|....*
gi 578803088 262 KIAILSFGELifCGtpaemlDFFND 286
Cdd:TIGR02633 472 RVLVIGEGKL--KG------DFVNH 488
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
67-281 |
1.62e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.29 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRlGRAGTflGEVYVNGRALRREQ----FQDCFSYVLQSDTLLSSL 142
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRATS--GRIVFDGKDITDWQtakiMREAVAIVPEGRRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVRETLHYTALLAIRRgnpgSFQKKVEAVMAelSLSHVADRLIgnYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:PRK11614 96 TVEENLAMGGFFAERD----QFQERIKWVYE--LFPRLHERRI--QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 223 LDCMTANQIVVLLVELaRRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:PRK11614 168 LAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
66-280 |
1.76e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.95 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGR---ALRREQFQDC---FSYVLQSDTLL 139
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDH---GEILFDGEnipAMSRSRLYTVrkrMSMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 140 SSLTVRETLHY-----TALlairrgnPGSFQKKVeaVMaeLSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVM 214
Cdd:PRK11831 97 TDMNVFDNVAYplrehTQL-------PAPLLHST--VM--MKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 215 LFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
71-280 |
2.06e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.18 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 71 DVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtF----LGEVYVNGRALRR-EQFQDCFSYVLQSDTLLSSLTVR 145
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAG-------FeqptAGQIMLDGVDLSHvPPYQRPINMMFQSYALFPHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 146 ETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRliGNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 225
Cdd:PRK11607 110 QNIAFG--LKQDKLPKAEIASRVNEMLGLVHMQEFAKR--KPHQLSG---GQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578803088 226 MTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:PRK11607 183 KLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
71-279 |
2.19e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.24 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 71 DVSLYVESGQIMCILGSSGSGKTT-------LLDAMSGR---LGRagtflgEVYVNGRALRREqfqdcFSYVLQSDTLLS 140
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPASEGEawlFGQ------PVDAGDIATRRR-----VGYMSQAFSLYG 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRE--TLHytALLairrgnpgsFQ-------KKVEAVMAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDP 211
Cdd:NF033858 353 ELTVRQnlELH--ARL---------FHlpaaeiaARVAEMLERFDLADVADALPDSLPLG-----IRQRLSLAVAVIHKP 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 212 KVMLFDEPTTGLDCMTANQIVVLLVELARRNRIvvlTI----HqprselfqlF-------DKIAILSFGELIFCGTPAE 279
Cdd:NF033858 417 ELLILDEPTSGVDPVARDMFWRLLIELSREDGV---TIfistH---------FmneaercDRISLMHAGRVLASDTPAA 483
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
68-322 |
5.95e-13 |
|
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: 69.50 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAlrreQFQDCFSYVLQSdtllsslTVRET 147
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSE---GKIKHSGRI----SFSSQFSWIMPG-------TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 148 LHYTALLAIRRgnpgsFQKKVEAVMAELSLSHVADRLIGNYSLGGI--STGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 225
Cdd:cd03291 118 IIFGVSYDEYR-----YKSVVKACQLEEDITKFPEKDNTVLGEGGItlSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 226 MTANQIVVLLV--ELARRNRIVVLTihqpRSELFQLFDKIAILSFGELIFCGTPAEMLDFFndcgypcPEHSNPFdfyMD 303
Cdd:cd03291 193 FTEKEIFESCVckLMANKTRILVTS----KMEHLKKADKILILHEGSSYFYGTFSELQSLR-------PDFSSKL---MG 258
|
250 260
....*....|....*....|...
gi 578803088 304 LTSVDTQSKERE----IETSKRV 322
Cdd:cd03291 259 YDTFDQFSAERRnsilTETLRRF 281
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
68-280 |
6.60e-13 |
|
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: 72.25 E-value: 6.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAlrreQFQDCFSYVLQS---DTLLSSLTV 144
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSE---GKIKHSGRI----SFSPQTSWIMPGtikDNIIFGLSY 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 REtLHYTALlairrgnpgsfqkkVEAVMAELSLSHVADRLIGNYSLGGI--STGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:TIGR01271 514 DE-YRYTSV--------------IKACQLEEDIALFPEKDKTVLGEGGItlSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 223 LDCMTANQIV--VLLVELARRNRIVVLTihqpRSELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:TIGR01271 579 LDVVTEKEIFesCLCKLMSNKTRILVTS----KLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
68-280 |
7.83e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.13 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQD---CFsyVLQSDTLLSSLTV 144
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAG-LEKPTE--GQIFIDGEDVTHRSIQQrdiCM--VFQSYALFPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 224
Cdd:PRK11432 96 GENVGYG--LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQ-----ISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 225 CMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:PRK11432 169 ANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
66-289 |
9.29e-13 |
|
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: 67.17 E-value: 9.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTfLGEVYVNGralrreqfQDcfsyvlqsdtlLSSLTVR 145
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVT-EGEILFKG--------ED-----------ITDLPPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 146 ETlhytallaIRRGNPGSFQKKVEavMAELSLSHVADRLigNYslgGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 225
Cdd:cd03217 73 ER--------ARLGIFLAFQYPPE--IPGVKNADFLRYV--NE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803088 226 MTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGtPAEMLDFFNDCGY 289
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDGRIVKSG-DKELALEIEKKGY 200
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
68-251 |
1.08e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.28 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQ--FQDCFSYVLQSDTLLSSLTVR 145
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEK---GEILFERQSIKKDLctYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 146 ETLHYTalLAIRRGNPGsfqkkVEAVMAELSLSHVADrlignYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 225
Cdd:PRK13540 93 ENCLYD--IHFSPGAVG-----ITELCRLFSLEHLID-----YPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*.
gi 578803088 226 MTANQIVVLLVELARRNRIVVLTIHQ 251
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
65-224 |
1.33e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.03 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRL----------GRAGTFLgEVYVNGRALRREQFQDCFSYVLQ 134
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLapdagevhyrMRDGQLR-DLYALSEAERRRLLRTEWGFVHQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 135 S--DTLLSSLT----VRETL------HYTALlairRGNPGSFQKKVEAVMAELslshvaDRLIGNYSlGGIstgeRRRVS 202
Cdd:PRK11701 97 HprDGLRMQVSaggnIGERLmavgarHYGDI----RATAGDWLERVEIDAARI------DDLPTTFS-GGM----QQRLQ 161
|
170 180
....*....|....*....|..
gi 578803088 203 IAAQLLQDPKVMLFDEPTTGLD 224
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLD 183
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
68-277 |
1.42e-12 |
|
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: 67.13 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGR---ALRREQFQDCFSYVLQsDTLLSSLTV 144
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSS---GSILIDGVdisKIGLHDLRSRISIIPQ-DPVLFSGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETL----HYTallairrgnpgsfQKKVEAVMAELSL-SHVADRLIGNYSL---GG--ISTGERRRVSIAAQLLQDPKVM 214
Cdd:cd03244 95 RSNLdpfgEYS-------------DEELWQALERVGLkEFVESLPGGLDTVveeGGenLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803088 215 LFDEPTTGLDCMTANQIVVLLVElARRNRIvVLTI-HqpRSELFQLFDKIAILSFGELIFCGTP 277
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIRE-AFKDCT-VLTIaH--RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
65-279 |
1.81e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 69.21 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtF----LGEVYVNGRALRR---EQFQdcFSYVLQSDT 137
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-------FetpdSGRIMLDGQDITHvpaENRH--VNTVFQSYA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 138 LLSSLTVRETLHYtALLAIRRGNPgSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFD 217
Cdd:PRK09452 97 LFPHMTVFENVAF-GLRMQKTPAA-EITPRVMEALRMVQLEEFAQRKPHQ-----LSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803088 218 EPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAE 279
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
40-249 |
1.84e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.79 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 40 ILHASySVSHRVRPWWdiTSCRQQWtRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR- 118
Cdd:PRK10419 3 LLNVS-GLSHHYAHGG--LSGKHQH-QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG-LESPSQ--GNVSWRGEp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 119 --ALRREQ-----------FQDCFSYVLQSDTLLSSLtvRETL-HYTALLAIRRgnpgsfQKKVEAV--MAELSLSHvAD 182
Cdd:PRK10419 76 laKLNRAQrkafrrdiqmvFQDSISAVNPRKTVREII--REPLrHLLSLDKAER------LARASEMlrAVDLDDSV-LD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 183 RLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI 249
Cdd:PRK10419 147 KRPPQ-----LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFI 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
70-271 |
1.99e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.81 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 70 KDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR----REQFQDCFSYVLQS---DTLLSSL 142
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG---GEIRLNGKDISprspLDAVKKGMAYITESrrdNGFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVRETLHYTALLAIRR--GNPGSFQKKVEAVMAELSLSHVADRLIG-NYSLGGISTGERRRVSIAAQLLQDPKVMLFDEP 219
Cdd:PRK09700 357 SIAQNMAISRSLKDGGykGAMGLFHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578803088 220 TTGLDCMTANQIVVLLVELARRNrIVVLTIHQPRSELFQLFDKIAILSFGEL 271
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
71-250 |
2.44e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.21 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 71 DVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRA-----------LRREQ----FQDCFSyvlqs 135
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREilnlpekelnkLRAEQismiFQDPMT----- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 136 dTLLSSLTVRETLHYTALLAIRRGNPGSFQKKV---EAV-MAElslshvADRLIGNYSlGGISTGERRRVSIAAQLLQDP 211
Cdd:PRK09473 109 -SLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVrmlDAVkMPE------ARKRMKMYP-HEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578803088 212 KVMLFDEPTTGLDCMTANQIVVLLVELARR-NRIVVLTIH 250
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITH 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
73-249 |
2.64e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.53 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 73 SLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGralrreqfQDC---------FSYVLQSDTLLSSLT 143
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPAS---GSLTLNG--------QDHtttppsrrpVSMLFQENNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLHytalLAIrrgNPG-----SFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDE 218
Cdd:PRK10771 88 VAQNIG----LGL---NPGlklnaAQREKLHAIARQMGIEDLLARLPGQ-----LSGGQRQRVALARCLVREQPILLLDE 155
|
170 180 190
....*....|....*....|....*....|.
gi 578803088 219 PTTGLDCMTANQIVVLLVELARRNRIVVLTI 249
Cdd:PRK10771 156 PFSALDPALRQEMLTLVSQVCQERQLTLLMV 186
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
65-272 |
3.10e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.89 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDC----FSYV---LQSDT 137
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADS---GEIRLDGKPVRIRSPRDAiragIAYVpedRKGEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 138 LLSSLTVRETLHYTALLAIRRG---NPGSFQKKVEAVMAELSL-SHVADRLIGNYSlgGistGERRRVSIAAQLLQDPKV 213
Cdd:COG1129 341 LVLDLSIRENITLASLDRLSRGgllDRRRERALAEEYIKRLRIkTPSPEQPVGNLS--G---GNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803088 214 MLFDEPTTGLDCMTANQIVVLLVELARRNR-IVVLTihqprSEL---FQLFDKIAILSFGELI 272
Cdd:COG1129 416 LILDEPTRGIDVGAKAEIYRLIRELAAEGKaVIVIS-----SELpelLGLSDRILVMREGRIV 473
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
65-279 |
3.46e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 67.35 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDC---FSYVLQS-DTLLS 140
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEA---GTITVGGMVLSEETVWDVrrqVGMVFQNpDNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLhytALLAIRRGNPGS-FQKKVEAVMAELSLSHVADRliGNYSLGGistGERRRVSIAAQLLQDPKVMLFDEP 219
Cdd:PRK13635 96 GATVQDDV---AFGLENIGVPREeMVERVDQALRQVGMEDFLNR--EPHRLSG---GQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 220 TTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLfDKIAILSFGELIFCGTPAE 279
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQA-DRVIVMNKGEILEEGTPEE 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
69-272 |
3.70e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALR----REQFQDCFSYVLQSDTLLSSLTV 144
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSG-NYQPDA--GSILIDGQEMRfastTAALAAGVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLhYTALLAIRRGnpgSFQKKVEAVMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 224
Cdd:PRK11288 97 AENL-YLGQLPHKGG---IVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578803088 225 CMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELI 272
Cdd:PRK11288 173 AREIEQLFRVIRELRAEGRVILYVSHR-MEEIFALCDAITVFKDGRYV 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
56-289 |
4.66e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 66.73 E-value: 4.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 56 DITSCRQQWT---RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNG------------RAL 120
Cdd:PRK13646 7 NVSYTYQKGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALL-KPTT--GTVTVDDitithktkdkyiRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 121 RREqfqdcFSYVLQ-SDTLLSSLTV-RETLHytallairrgNPGSFQKKVEAVMA---ELSLSHVADRLIGNYSLGGIST 195
Cdd:PRK13646 84 RKR-----IGMVFQfPESQLFEDTVeREIIF----------GPKNFKMNLDEVKNyahRLLMDLGFSRDVMSQSPFQMSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 196 GERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELA-RRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFC 274
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHD-MNEVARYADEVIVMKEGSIVSQ 227
|
250
....*....|....*
gi 578803088 275 GTPAEMldfFNDCGY 289
Cdd:PRK13646 228 TSPKEL---FKDKKK 239
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
66-271 |
6.74e-12 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 65.57 E-value: 6.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALrrEQFQDCF-----SYVLQSDTLLS 140
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQG---GQVLLDGKPI--SQYEHKYlhskvSLVGQEPVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SlTVRETLHYtallairrgnpGSFQKKVEAVMAELSLSHvADRLIGNYSLG----------GISTGERRRVSIAAQLLQD 210
Cdd:cd03248 102 R-SLQDNIAY-----------GLQSCSFECVKEAAQKAH-AHSFISELASGydtevgekgsQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 211 PKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTiHqpRSELFQLFDKIAILSFGEL 271
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIA-H--RLSTVERADQILVLDGGRI 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
69-280 |
7.50e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 66.26 E-value: 7.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQ----FQDCFSYVLQS-DTLLSSLT 143
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSE---GKVYVDGLDTSDEEnlwdIRNKAGMVFQNpDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLHYTAL-LAIRrgnPGSFQKKVEAVMAELSLSHVADrlignYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:PRK13633 103 VEEDVAFGPEnLGIP---PEEIRERVDESLKKVGMYEYRR-----HAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578803088 223 LDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLfDKIAILSFGELIFCGTPAEM 280
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEA-DRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
69-281 |
1.12e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.58 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALrreQFQDcFSYVLQSDTLL-----SSLT 143
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS---GELLIDDHPL---HFGD-YSYRSQRIRMIfqdpsTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLHYTALLAIRRGNPGSFQKKVEAVMAELslshvadRLIG------NYSLGGISTGERRRVSIAAQLLQDPKVMLFD 217
Cdd:PRK15112 102 PRQRISQILDFPLRLNTDLEPEQREKQIIETL-------RQVGllpdhaSYYPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803088 218 EPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
71-272 |
1.17e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.44 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 71 DVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQDCFS-------YVLQSDTLLSSLT 143
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISG-LTRPQK--GRIVLNGRVLFDAEKGICLPpekrrigYVFQDARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLHYtallAIRRGNPGSFQKKVEAvmaeLSLSHVADRLIGnySLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGL 223
Cdd:PRK11144 93 VRGNLRY----GMAKSMVAQFDKIVAL----LGIEPLLDRYPG--SLSG---GEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578803088 224 DCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELI 272
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
68-281 |
1.27e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.39 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDC---FSYVLQSDTLLSSLTV 144
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAH---GHVWLDGEHIQHYASKEVarrIGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETL------HYTALLAIRRGNpgsfQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDE 218
Cdd:PRK10253 99 QELVargrypHQPLFTRWRKED----EEAVTKAMQATGITHLADQ-----SVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803088 219 PTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
72-281 |
1.36e-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: 67.13 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 72 VSLYVESGQIMCILGSSGSGKTTLLDAMSGRL----GRAGTFLGEVYVN---------GRALRR----EQFQDCFSYvlq 134
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLeptsGEVNVRVGDEWVDmtkpgpdgrGRAKRYigilHQEYDLYPH--- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 135 sDTLLSSLTVRETLHYTALLAIRRG-----NPGSFQKKVEAVmaelsLSHVADRLignyslggiSTGERRRVSIAAQLLQ 209
Cdd:TIGR03269 380 -RTVLDNLTEAIGLELPDELARMKAvitlkMVGFDEEKAEEI-----LDKYPDEL---------SEGERHRVALAQVLIK 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 210 DPKVMLFDEPTTGLDCMTANQivvllvelarrnriVVLTIHQPRSELFQLF--------------DKIAILSFGELIFCG 275
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVD--------------VTHSILKAREEMEQTFiivshdmdfvldvcDRAALMRDGKIVKIG 510
|
....*.
gi 578803088 276 TPAEML 281
Cdd:TIGR03269 511 DPEEIV 516
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
69-282 |
1.72e-11 |
|
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: 66.77 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTFLGEVYVNGRALRREQFQDC----FSYVLQSDTLLSSLTV 144
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGTWDGEIYWSGSPLKASNIRDTeragIVIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RET--LHYTALLAIRRGNPGSFQKKVEAVMAELSLSHVAD-RLIGNYSLggistGERRRVSIAAQLLQDPKVMLFDEPTT 221
Cdd:TIGR02633 96 AENifLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGG-----GQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803088 222 GLdcmTANQIVVLL---VELARRNrIVVLTIHQPRSELFQLFDKIAILSFGELIfCGTPAEMLD 282
Cdd:TIGR02633 171 SL---TEKETEILLdiiRDLKAHG-VACVYISHKLNEVKAVCDTICVIRDGQHV-ATKDMSTMS 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
65-275 |
2.07e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 63.71 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgraGTFLGEVYVNGRAlrreqfqdcfSYVLQSDT-LLSSLT 143
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIY---PPDSGTVTVRGRV----------SSLLGLGGgFNPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLHYTALLairRGNPGSFQKKVEAVMAELS-LSHVADRLIGNYslggiSTGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:cd03220 101 GRENIYLNGRL---LGLSRKEIDEKIDEIIEFSeLGDFIDLPVKTY-----SSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578803088 223 LDCMTANQIVVLLVELARRNRIVVLTIHQPRSeLFQLFDKIAILSFGELIFCG 275
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
64-281 |
2.15e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.64 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 64 WTR----QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR---------REQ----FQ 126
Cdd:PRK13638 8 WFRyqdePVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQK---GAVLWQGKPLDyskrgllalRQQvatvFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 127 D----CFSYVLQSDTLLS--SLTVRETlhytallairrgnpgSFQKKVEAVMAELSLSHVADRLIGnyslgGISTGERRR 200
Cdd:PRK13638 85 DpeqqIFYTDIDSDIAFSlrNLGVPEA---------------EITRRVDEALTLVDAQHFRHQPIQ-----CLSHGQKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 201 VSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPrSELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDI-DLIYEISDAVYVLRQGQILTHGAPGEV 223
|
.
gi 578803088 281 L 281
Cdd:PRK13638 224 F 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
66-224 |
2.39e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.24 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLG-RAGTFlgevyVNGRALRreqfqdcFSYVLQS-DTLLSSLT 143
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEpDSGTV-----KLGETVK-------IGYFDQHqEELDPDKT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETlhytallaIRRGNPGSFQKKVEAVMAELSLS-HVADRLIGnySLGGistGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:COG0488 396 VLDE--------LRDGAPGGTEQEVRGYLGRFLFSgDDAFKPVG--VLSG---GEKARLALAKLLLSPPNVLLLDEPTNH 462
|
..
gi 578803088 223 LD 224
Cdd:COG0488 463 LD 464
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
65-252 |
2.67e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtflgevyvngrALRREQFQDCFsyVLQSDTLLSSLTV 144
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-----------------ALKGTPVAGCV--DVPDNQFGREASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLhytallairrGNPGSFQKKVEaVMAELSLSHVA------DRLignyslggiSTGERRRVSIAAQLLQDPKVMLFDE 218
Cdd:COG2401 103 IDAI----------GRKGDFKDAVE-LLNAVGLSDAVlwlrrfKEL---------STGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 578803088 219 PTTGLDCMTANQIVVLLVELARRNRI-VVLTIHQP 252
Cdd:COG2401 163 FCSHLDRQTAKRVARNLQKLARRAGItLVVATHHY 197
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
65-249 |
2.73e-11 |
|
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: 66.25 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKT-TLLDAMsgRL--GRAGTFLGEVYVNG--------RALRREQ-------FQ 126
Cdd:COG4172 22 TVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL--RLlpDPAAHPSGSILFDGqdllglseRELRRIRgnriamiFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 127 DCfsyvlqsdtlLSSLT--------VRETLhytallAIRRGNPGsfqKKVEAVMAELsLSHV----ADRLIGNY--SLGG 192
Cdd:COG4172 100 EP----------MTSLNplhtigkqIAEVL------RLHRGLSG---AAARARALEL-LERVgipdPERRLDAYphQLSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 193 istGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI 249
Cdd:COG4172 160 ---GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLI 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
61-269 |
2.96e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.88 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 61 RQQWTRQILKDVSLYVESGQIMCILGSSGSGKT-TLLDAMsgRLGRAGTFL---GEVYVNG-----------RALRREQF 125
Cdd:PRK15134 17 QQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSPPVVypsGDIRFHGesllhaseqtlRGVRGNKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 126 QDCFSYVLQSdtlLSSLTVRETLHYTaLLAIRRGnpgsfqKKVEAVMAEL-------SLSHVADRLiGNYSlGGISTGER 198
Cdd:PRK15134 95 AMIFQEPMVS---LNPLHTLEKQLYE-VLSLHRG------MRREAARGEIlncldrvGIRQAAKRL-TDYP-HQLSGGER 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 199 RRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFG 269
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
64-251 |
3.39e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 63.12 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 64 WTRQI--LKDVSLYVESGQIMCILGSSGSGKTTLLDAMsgrLGRAGTFLGEVYVNGRALRREQFQDCFS-------YVLQ 134
Cdd:cd03290 10 WGSGLatLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI---LGEMQTLEGKVHWSNKNESEPSFEATRSrnrysvaYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 135 SDTLLSSlTVRETLHYtallairrGNPGSFQKkVEAVMAELSLSHVADRL-------IGNYSLGgISTGERRRVSIAAQL 207
Cdd:cd03290 87 KPWLLNA-TVEENITF--------GSPFNKQR-YKAVTDACSLQPDIDLLpfgdqteIGERGIN-LSGGQRQRICVARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 578803088 208 LQDPKVMLFDEPTTGLDCMTANQIVV--LLVELARRNRIVVLTIHQ 251
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHK 201
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
69-281 |
3.76e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.26 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRL--GRAGTFLGEVYVNG--------RALRRE-----QFQDcfsYVL 133
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisETGQTIVGDYAIPAnlkkikevKRLRKEiglvfQFPE---YQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 134 QSDTLLSSLtvretlhytALLAIRRG-NPGSFQKKVEAVMAELSLShvadRLIGNYSLGGISTGERRRVSIAAQLLQDPK 212
Cdd:PRK13645 104 FQETIEKDI---------AFGPVNLGeNKQEAYKKVPELLKLVQLP----EDYVKRSPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 213 VMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
69-272 |
4.10e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGR-AGT--FLG-EVYVNGralRREQFQDCFSYVLQSDTLLSSLTV 144
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRdAGSilYLGkEVTFNG---PKSSQEAGIGIIHQELNLIPQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLhytaLLAIRRGNP-GSFQ-KKV----EAVMAELSLSHVADRLIGNYSLggistGERRRVSIAAQLLQDPKVMLFDE 218
Cdd:PRK10762 97 AENI----FLGREFVNRfGRIDwKKMyaeaDKLLARLNLRFSSDKLVGELSI-----GEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578803088 219 PTTGL-DCMTANQIVVlLVELARRNRIVVLTIHQPRsELFQLFDKIAILSFGELI 272
Cdd:PRK10762 168 PTDALtDTETESLFRV-IRELKSQGRGIVYISHRLK-EIFEICDDVTVFRDGQFI 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
65-286 |
5.05e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.18 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMsgrlgrAGTFL---GEVYVNGRAlrreqfqdcfsyvlqsDTLLS- 140
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLI------AGILEptsGRVEVNGRV----------------SALLEl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 ------SLTVRETLHYTALLAirrgnpGSFQKKVEAVM---AELS-LSHVADRLIGNYslggiSTGERRRV--SIAAQLl 208
Cdd:COG1134 96 gagfhpELTGRENIYLNGRLL------GLSRKEIDEKFdeiVEFAeLGDFIDQPVKTY-----SSGMRARLafAVATAV- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 209 qDPKVMLFDEpttgldcmtanqivVLLV--------------ELARRNRIVVLTIHQPRSeLFQLFDKIAILSFGELIFC 274
Cdd:COG1134 164 -DPDILLVDE--------------VLAVgdaafqkkclarirELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVMD 227
|
250
....*....|..
gi 578803088 275 GTPAEMLDFFND 286
Cdd:COG1134 228 GDPEEVIAAYEA 239
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
67-277 |
5.72e-11 |
|
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: 62.43 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTL-------LDAMSGRLGRAGTFLGEVYVngRALRREqfqdcFSYVLQSDTLL 139
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLilalfrfLEAEEGKIEIDGIDISTIPL--EDLRSS-----LTIIPQDPTLF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 140 SSlTVRETL----HYTAllairrgnpgsfqkkvEAVMAELSLSHVADRLignyslggiSTGERRRVSIAAQLLQDPKVML 215
Cdd:cd03369 95 SG-TIRSNLdpfdEYSD----------------EEIYGALRVSEGGLNL---------SQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803088 216 FDEPTTGLDCMTANQIVVLLVELArrNRIVVLTI-HQPRSELfqLFDKIAILSFGELIFCGTP 277
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEF--TNSTILTIaHRLRTII--DYDKILVMDAGEVKEYDHP 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
55-280 |
5.86e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.77 E-value: 5.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 55 WDITScrqqwTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTflGEVYVNGRAlrreqfqdcfSYVLQ 134
Cdd:PLN03232 624 WDSKT-----SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAET--SSVVIRGSV----------AYVPQ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 135 SDTLLSSlTVRETLHYTAllairRGNPGSFQKKVEAVmaelSLSHVADRLIGN--YSLG----GISTGERRRVSIAAQLL 208
Cdd:PLN03232 687 VSWIFNA-TVRENILFGS-----DFESERYWRAIDVT----ALQHDLDLLPGRdlTEIGergvNISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803088 209 QDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQprSELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:PLN03232 757 SNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQ--LHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
66-280 |
5.91e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 63.50 E-value: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLG-RAGTF-LGE-VYVNG------RALRRE-----QFQD--CF 129
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQpTSGTVtIGErVITAGkknkklKPLRKKvgivfQFPEhqLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 130 SYVLQSDtllssltvretlhytallaIRRGnPGSF-------QKKVEAVMAELSLSH-VADRlignySLGGISTGERRRV 201
Cdd:PRK13634 100 EETVEKD-------------------ICFG-PMNFgvseedaKQKAREMIELVGLPEeLLAR-----SPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 202 SIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR-RNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHS-MEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
66-280 |
6.12e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.67 E-value: 6.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRRE---QFQDCFSYVLQS-DTLLSS 141
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKtvwDIREKVGIVFQNpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 LTVRETLhytALLAIRRGNPGS-FQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:PRK13640 100 ATVGDDV---AFGLENRAVPRPeMIKIVRDVLADVGMLDYIDSEPAN-----LSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELfQLFDKIAILSFGELIFCGTPAEM 280
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
69-280 |
7.58e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 63.31 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG------------RALRREqfqdcFSYVLQ-S 135
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSS---GTITIAGyhitpetgnknlKKLRKK-----VSLVFQfP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 136 DTLLSSLTVRETLHYTALlairrgNPG-SFQKKVEAVMAELSLSHVADRLIgNYSLGGISTGERRRVSIAAQLLQDPKVM 214
Cdd:PRK13641 95 EAQLFENTVLKDVEFGPK------NFGfSEDEAKEKALKWLKKVGLSEDLI-SKSPFELSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 215 LFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHN-MDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
69-280 |
1.07e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.28 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR---EQFQDC-FSYVL---QSDTLLSS 141
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAS---GSIRLDGEDITGlspRERRRLgVAYIPedrLGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 LTVRE----TLHYTALLAiRRG--NPGSFQKKVEAVMAELSL-SHVADRLIGNYSLGGIstgerRRVSIAAQLLQDPKVM 214
Cdd:COG3845 351 MSVAEnlilGRYRRPPFS-RGGflDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQ-----QKVILARELSRDPKLL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 215 LFDEPTTGLDCMTANQIVVLLVELARRNRIVVLtIHQPRSELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:COG3845 425 IAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL-ISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
76-250 |
1.20e-10 |
|
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: 62.38 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 76 VESGQIMCILGSSGSGKTTLLDAMSGRL-GRAGTFLGEVYVNG--RALRREQFQDCFSYVLQSDtllssLTVRETLHYTA 152
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLkPNLGKFDDPPDWDEilDEFRGSELQNYFTKLLEGD-----VKVIVKPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 153 LL-AIRRGNPGSFQKKV------EAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 225
Cdd:cd03236 98 LIpKAVKGKVGELLKKKdergklDELVDQLELRHVLDRNIDQ-----LSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*...
gi 578803088 226 ---MTANQIVvllVELARRNRIVVLTIH 250
Cdd:cd03236 173 kqrLNAARLI---RELAEDDNYVLVVEH 197
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
69-280 |
1.41e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.45 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVRETL 148
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQ---GSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 149 HYTALLAIRRG--NPGSFQKKVEAVMAE-LSLSHVADRLIGN--YSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGL 223
Cdd:PRK13649 100 EETVLKDVAFGpqNFGVSQEEAEALAREkLALVGISESLFEKnpFELSG---GQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803088 224 DCMTANQIVVLLVELARRNRIVVLTIHqprselfqLFDKIA-------ILSFGELIFCGTPAEM 280
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTH--------LMDDVAnyadfvyVLEKGKLVLSGKPKDI 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
65-267 |
1.44e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.27 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAgtfLGEVYVNGR---ALRREQFQDCFSYVLQSDTLLSS 141
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPT---SGTLLFEGEdisTLKPEIYRQQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 lTVRETLHYTALlaIRRGNPGsfQKKVEAVMAELSLshvaDRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTT 221
Cdd:PRK10247 96 -TVYDNLIFPWQ--IRNQQPD--PAIFLDDLERFAL----PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578803088 222 GLDcmTANQIVV--LLVELARRNRIVVLTIHQPRSELFQLfDKIAILS 267
Cdd:PRK10247 167 ALD--ESNKHNVneIIHRYVREQNIAVLWVTHDKDEINHA-DKVITLQ 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
69-281 |
1.52e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 62.31 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLG-RAGTFLGEVYVNGRALRREQFQDCFSYVLQS-DTLLSSLTVRE 146
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRpQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNpETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 147 TLHYTAL-LAIrrgNPGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 225
Cdd:PRK13644 98 DLAFGPEnLCL---PPIEIRKRVDRALAEIGLEKYRHR-----SPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 226 MTANQIVVLLVELARRNRIVVLTIHQprSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:PRK13644 170 DSGIAVLERIKKLHEKGKTIVYITHN--LEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
67-282 |
1.78e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.06 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLdamsgrLGRAGTFL---GEVYVNGRALRREQ-----------FQDcfsyv 132
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLL------LHLNGIYLpqrGRVKVMGREVNAENekwvrskvglvFQD----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 133 lqSDTLLSSLTVRETLhytALLAIRRG-NPGSFQKKVEAVMAELSLSHVADRliGNYSLggiSTGERRRVSIAAQLLQDP 211
Cdd:PRK13647 88 --PDDQVFSSTVWDDV---AFGPVNMGlDKDEVERRVEEALKAVRMWDFRDK--PPYHL---SYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 212 KVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELfQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
72-279 |
1.96e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.54 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 72 VSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR--------REQFQDCFSYV--LQSDTLLSS 141
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTG---GTILLRGQHIEglpghqiaRMGVVRTFQHVrlFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 LTVRETLHY-TALLAIRRGNPGSFQKKVEAV-MAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEP 219
Cdd:PRK11300 101 LLVAQHQQLkTGLFSGLLKTPAFRRAESEALdRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 220 TTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAE 279
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
69-224 |
2.25e-10 |
|
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: 61.27 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESG-----QIMCILGSSGSGKTTLLDAMSGRL----GRAGTFLGEVyvngralrreqfqdcfSYVLQSDTLL 139
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLkpdeGDIEIELDTV----------------SYKPQYIKAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 140 SSLTVRETLHytallAIRRGNPGSFQKKVEaVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEP 219
Cdd:cd03237 74 YEGTVRDLLS-----SITKDFYTHPYFKTE-IAKPLQIEQILDREVPE-----LSGGELQRVAIAACLSKDADIYLLDEP 142
|
....*
gi 578803088 220 TTGLD 224
Cdd:cd03237 143 SAYLD 147
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
65-243 |
2.26e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.44 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLL-------DAMSGRLGRAGTFLGEVyvNGRALRREqfqdcFSYVLQsDT 137
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLInllqrvfDPQSGRILIDGTDIRTV--TRASLRRN-----IAVVFQ-DA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 138 LLSSLTVRETlhytallaIRRGNPGSFQKKV-EAVMAELSLSHVADRLIGNYSLGG-----ISTGERRRVSIAAQLLQDP 211
Cdd:PRK13657 419 GLFNRSIEDN--------IRVGRPDATDEEMrAAAERAQAHDFIERKPDGYDTVVGergrqLSGGERQRLAIARALLKDP 490
|
170 180 190
....*....|....*....|....*....|..
gi 578803088 212 KVMLFDEPTTGLDCMTANQIVVLLVELaRRNR 243
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDEL-MKGR 521
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
69-282 |
2.64e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTFLGEVYVNGRALR----REQFQDCFSYVLQSDTLLSSLTV 144
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGTYEGEIIFEGEELQasniRDTERAGIAIIHQELALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RET------------LHYTALLAirrgnpgsfqkKVEAVMAELSLSHVADRLIGNYSLggistGERRRVSIAAQLLQDPK 212
Cdd:PRK13549 100 LENiflgneitpggiMDYDAMYL-----------RAQKLLAQLKLDINPATPVGNLGL-----GQQQLVEIAKALNKQAR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803088 213 VMLFDEPTTGLdcmTANQIVVLL--VELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIfcGT-PAEMLD 282
Cdd:PRK13549 164 LLILDEPTASL---TESETAVLLdiIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI--GTrPAAGMT 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
34-271 |
2.68e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 34 EPHSLG--ILHA-SYSVSHRVRPwwditscrqqwTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlGRAGTFL 110
Cdd:PRK13549 251 EPHTIGevILEVrNLTAWDPVNP-----------HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG--AYPGRWE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 111 GEVYVNGRALRREQFQDCFSYVL-------QSDTLLSSLTVRETLHYTALLAIRRG---NPGSFQKKVEAVMAELSLSHV 180
Cdd:PRK13549 318 GEIFIDGKPVKIRNPQQAIAQGIamvpedrKRDGIVPVMGVGKNITLAALDRFTGGsriDDAAELKTILESIQRLKVKTA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 181 ADRLignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNrIVVLTIHQPRSELFQLF 260
Cdd:PRK13549 398 SPEL----AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQG-VAIIVISSELPEVLGLS 472
|
250
....*....|.
gi 578803088 261 DKIAILSFGEL 271
Cdd:PRK13549 473 DRVLVMHEGKL 483
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
66-224 |
4.12e-10 |
|
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: 62.26 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtfLGEVYvNGRALRREQFQdcFSYVLQSDTLLSSLTVR 145
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--------VDKDF-NGEARPQPGIK--VGYLPQEPQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 146 ETL--------------------------HYTALLAirrgNPGSFQKKVEAVMA---ELSLSHVADRL---IGNYSLGGI 193
Cdd:TIGR03719 87 ENVeegvaeikdaldrfneisakyaepdaDFDKLAA----EQAELQEIIDAADAwdlDSQLEIAMDALrcpPWDADVTKL 162
|
170 180 190
....*....|....*....|....*....|.
gi 578803088 194 STGERRRVSIAAQLLQDPKVMLFDEPTTGLD 224
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
65-280 |
5.39e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 60.44 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSgRL------GRAGtflGEVYVNGR----------ALRREqfqdc 128
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLN-RMndlipgARVE---GEILLDGEdiydpdvdvvELRRR----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 129 FSYVLQSDTLLsSLTVRETLHYTA-LLAIRRgnpgsfqKKVEAVMAELSLSHVA------DRLigNYSLGGISTGERRRV 201
Cdd:COG1117 94 VGMVFQKPNPF-PKSIYDNVAYGLrLHGIKS-------KSELDEIVEESLRKAAlwdevkDRL--KKSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 202 SIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLT--IHQPRselfQLFDKIAILSFGELIFCGTPAE 279
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVThnMQQAA----RVSDYTAFFYLGELVEFGPTEQ 239
|
.
gi 578803088 280 M 280
Cdd:COG1117 240 I 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
66-271 |
5.54e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.08 E-value: 5.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLL-------DAMSGRLGRAGTFLGEVyvngRALRREQFQDCfsyvlqsdTL 138
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLrllagleTPSAGELLAGTAPLAEA----REDTRLMFQDA--------RL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 139 LSSLTVRETLHytalLAIRrgnpGSFQKKVEAVMAELSLshvADRliGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDE 218
Cdd:PRK11247 93 LPWKKVIDNVG----LGLK----GQWRDAALQALAAVGL---ADR--ANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578803088 219 PTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGEL 271
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
66-250 |
6.55e-10 |
|
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: 57.46 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgraGTFLGEVYVNGRALrreqfqdcFSYVLQsdtlLSSltvr 145
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGEL---EPDEGIVTWGSTVK--------IGYFEQ----LSG---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 146 etlhytallairrgnpgsfqkkveavmaelslshvadrlignyslggistGERRRVSIAAQLLQDPKVMLFDEPTTGLDc 225
Cdd:cd03221 74 --------------------------------------------------GEKMRLALAKLLLENPNLLLLDEPTNHLD- 102
|
170 180
....*....|....*....|....*
gi 578803088 226 MTAnqIVVLLVELARRNRIVVLTIH 250
Cdd:cd03221 103 LES--IEALEEALKEYPGTVILVSH 125
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
66-250 |
6.56e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.50 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQDC------FSYVLQSDTLL 139
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-IERPSA--GKIWFSGHDITRLKNREVpflrrqIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 140 SSLTVRETLHYTALLAIRRGNpgSFQKKVEAVMAELSLSHVADrligNYSLGgISTGERRRVSIAAQLLQDPKVMLFDEP 219
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAGASGD--DIRRRVSAALDKVGLLDKAK----NFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190
....*....|....*....|....*....|.
gi 578803088 220 TTGLDCMTANQIVVLLVELARRNRIVVLTIH 250
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
67-275 |
6.75e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 6.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR----EQFQDCFSYVLQSDTLLSSL 142
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTK---GTITINNINYNKldhkLAAQLGIGIIYQELSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVRETLhYTALLAIRR--GNPGSFQKKVEAVMAELsLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:PRK09700 96 TVLENL-YIGRHLTKKvcGVNIIDWREMRVRAAMM-LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCG 275
Cdd:PRK09700 174 SSLTNKEVDYLFLIMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
65-270 |
6.77e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 6.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAmsgrLGRAGTFLGEVYVNGRA----------------LRREqfqdc 128
Cdd:PRK14258 19 TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC----LNRMNELESEVRVEGRVeffnqniyerrvnlnrLRRQ----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 129 FSYVLQSDTLLSsLTVRETLHYTALLAIRRGNPgSFQKKVEAVMAELSL-SHVADRLigNYSLGGISTGERRRVSIAAQL 207
Cdd:PRK14258 90 VSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKL-EIDDIVESALKDADLwDEIKHKI--HKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803088 208 LQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGE 270
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
31-281 |
7.03e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.27 E-value: 7.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 31 TAPE---PHSLGILHASYSVshRVRPWWDItscrqqwtrqILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSgRLGRAG 107
Cdd:TIGR00957 1273 TAPPsgwPPRGRVEFRNYCL--RYREDLDL----------VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLF-RINESA 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 108 TflGEVYVNGRALRREQFQDCFS--YVLQSDTLLSSLTVRETLhytallairrgNPGSfQKKVEAVMAELSLSHV----- 180
Cdd:TIGR00957 1340 E--GEIIIDGLNIAKIGLHDLRFkiTIIPQDPVLFSGSLRMNL-----------DPFS-QYSDEEVWWALELAHLktfvs 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 181 --ADRLIGNYSLGG--ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANqivvlLVELARRNRI---VVLTIHQpR 253
Cdd:TIGR00957 1406 alPDKLDHECAEGGenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN-----LIQSTIRTQFedcTVLTIAH-R 1479
|
250 260
....*....|....*....|....*...
gi 578803088 254 SELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:TIGR00957 1480 LNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
61-238 |
8.19e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.36 E-value: 8.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 61 RQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLldamsgrlGRAGTFL-----GEVYVNG----------RALRREQF 125
Cdd:PRK11308 23 KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTL--------ARLLTMIetptgGELYYQGqdllkadpeaQKLLRQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 126 QdcfsYVLQSDtlLSSLTVRETLHY---------TALLAIRRgnpgsfQKKVEAVMAELSL--SHvADRLIGNYSlggis 194
Cdd:PRK11308 95 Q----IVFQNP--YGSLNPRKKVGQileepllinTSLSAAER------REKALAMMAKVGLrpEH-YDRYPHMFS----- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578803088 195 TGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL 238
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDL 200
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
67-249 |
9.90e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSgRLGRAGtflGEVYVNGRAL------------RREQ--FQDCFSyv 132
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQ---GEIWFDGQPLhnlnrrqllpvrHRIQvvFQDPNS-- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 133 lqsdTLLSSLTVRE------TLHYTALLAIRRgnpgsfQKKVEAVMAELSLSHVA-DRLIGNYSlggisTGERRRVSIAA 205
Cdd:PRK15134 374 ----SLNPRLNVLQiieeglRVHQPTLSAAQR------EQQVIAVMEEVGLDPETrHRYPAEFS-----GGQRQRIAIAR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578803088 206 QLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI 249
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFI 482
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
66-267 |
1.04e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 61.36 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflgevyvnGRALRREQFQDCF----SYvLQSDTLlss 141
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYGS--------GRIARPAGARVLFlpqrPY-LPLGTL--- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 ltvRETLHYTALlairrgnPGSF-QKKVEAVMAELSLSHVADRLIGNYSLGGI-STGERRRVSIAAQLLQDPKVMLFDEP 219
Cdd:COG4178 443 ---REALLYPAT-------AEAFsDAELREALEAVGLGHLAERLDEEADWDQVlSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578803088 220 TTGLDCMTANQIVVLLVElaRRNRIVVLTI-HqpRSELFQLFDKIAILS 267
Cdd:COG4178 513 TSALDEENEAALYQLLRE--ELPGTTVISVgH--RSTLAAFHDRVLELT 557
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
69-224 |
1.07e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.17 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFSYVL-------QSDTLLSS 141
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTS---GYVTLDGHEVVTRSPQDGLANGIvyisedrKRDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 LTVRETLHYTALLAIRRGNpGSFQKKVE--AVMAELSLSHV----ADRLIGNyslggISTGERRRVSIAAQLLQDPKVML 215
Cdd:PRK10762 345 MSVKENMSLTALRYFSRAG-GSLKHADEqqAVSDFIRLFNIktpsMEQAIGL-----LSGGNQQKVAIARGLMTRPKVLI 418
|
....*....
gi 578803088 216 FDEPTTGLD 224
Cdd:PRK10762 419 LDEPTRGVD 427
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
72-250 |
1.84e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.37 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 72 VSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGE-VYVNGRAL-------RREQFQDCFSYVLQSDtlLSSLT 143
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEkLEFNGQDLqrisekeRRNLVGAEVAMIFQDP--MTSLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLHYTALLAIRRGNPGSFQKKVEAVMAELSLSHVAD---RL-IGNYSLGGistGERRRVSIAAQLLQDPKVMLFDEP 219
Cdd:PRK11022 104 PCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasRLdVYPHQLSG---GMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190
....*....|....*....|....*....|..
gi 578803088 220 TTGLDCMTANQIVVLLVELARR-NRIVVLTIH 250
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKeNMALVLITH 212
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
69-281 |
2.16e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.03 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTT---LL----DAMSGrlgragtflgEVYVNGRALR-------REQFqdcfSYVLQ 134
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTianLLtrfyDIDEG----------EILLDGHDLRdytlaslRNQV----ALVSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 135 S-----DTLLSSLTVRETLHYT---ALLAIRRGNPGSFQKKVEavmaelslsHVADRLIG-NYSLggISTGERRRVSIAA 205
Cdd:PRK11176 425 NvhlfnDTIANNIAYARTEQYSreqIEEAARMAYAMDFINKMD---------NGLDTVIGeNGVL--LSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 206 QLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELaRRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAH--RLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
68-282 |
2.18e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR---EQFQDCFSY-VLQSDTLLSSLT 143
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS---GTLEIGGNPCARltpAKAHQLGIYlVPQEPLLFPNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETlhytalLAIRRGNPGSFQKKVEAVMAELSLShvadrLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGL 223
Cdd:PRK15439 103 VKEN------ILFGLPKRQASMQKMKQLLAALGCQ-----LDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 224 DCMTANQIVVLLVELARRNRIVVLTIHQPRsELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:PRK15439 172 TPAETERLFSRIRELLAQGVGIVFISHKLP-EIRQLADRISVMRDGTIALSGKTADLST 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
67-250 |
2.59e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.94 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRL----GRAGTFLGEVYVNGRALRREQFQDcfSYVLQSDTLLSSL 142
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLlpdtGTIEWIFKDEKNKKKTKEKEKVLE--KLVIQKTRFKKIK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVREtlhytallaIRRGNPGSFQkkveavMAELSLSHVA---DRLIGNYSLG---------------------------- 191
Cdd:PRK13651 99 KIKE---------IRRRVGVVFQ------FAEYQLFEQTiekDIIFGPVSMGvskeeakkraakyielvgldesylqrsp 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 192 -GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIH 250
Cdd:PRK13651 164 fELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
77-250 |
2.66e-09 |
|
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: 59.80 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 77 ESGQIMCILGSSGSGKTTLLDAMSGR----LGR--------------AGTFLGEvY----VNG--RALRREQFQDCFSYV 132
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGElkpnLGDydeepswdevlkrfRGTELQD-YfkklANGeiKVAHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 133 LqsdtllsSLTVRETLHYTAllaiRRGnpgsfqkKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPK 212
Cdd:COG1245 176 F-------KGTVRELLEKVD----ERG-------KLDELAEKLGLENILDRDISE-----LSGGELQRVAIAAALLRDAD 232
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578803088 213 VMLFDEPTTGLDC---MTANQIVvllVELARRNRIVVLTIH 250
Cdd:COG1245 233 FYFFDEPSSYLDIyqrLNVARLI---RELAEEGKYVLVVEH 270
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
55-246 |
2.72e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.52 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 55 WDITScrqqwTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgrAGTFLGEVYVNGRAlrreqfqdcfSYVLQ 134
Cdd:PLN03130 624 WDSKA-----ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGEL--PPRSDASVVIRGTV----------AYVPQ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 135 SDTLLSSlTVRETLHYTALLairrgNPGSFQKKVEAVmaelSLSHVADRL-------IGNYSLGgISTGERRRVSIAAQL 207
Cdd:PLN03130 687 VSWIFNA-TVRDNILFGSPF-----DPERYERAIDVT----ALQHDLDLLpggdlteIGERGVN-ISGGQKQRVSMARAV 755
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578803088 208 LQDPKVMLFDEPTTGLDCMTANQIV--VLLVELARRNRIVV 246
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVGRQVFdkCIKDELRGKTRVLV 796
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
66-282 |
3.31e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 59.74 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLdAMSGRLGRAGTflGEVYVNGRALrrEQFQDCFSY----VLQSDTLLSS 141
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVA-ALLQNLYQPTG--GQVLLDGVPL--VQYDHHYLHrqvaLVGQEPVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 142 LTVRETLHYtallairrgnpGSFQKKVEAVMAELSLSHvADRLIGNYSLGG----------ISTGERRRVSIAAQLLQDP 211
Cdd:TIGR00958 569 GSVRENIAY-----------GLTDTPDEEIMAAAKAAN-AHDFIMEFPNGYdtevgekgsqLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803088 212 KVMLFDEPTTGLDCmtanQIVVLLVEL-ARRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTPAEMLD 282
Cdd:TIGR00958 637 RVLILDEATSALDA----ECEQLLQESrSRASRTVLLIAH--RLSTVERADQILVLKKGSVVEMGTHKQLME 702
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
67-224 |
6.05e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.93 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtfL-----GEVYVNGR-------ALRreqfqDCfSYVLQ 134
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG--------LeritsGEIWIGGRvvnelepADR-----DI-AMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 135 SDTLLSSLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADR----LignyslggiSTGERRRVSIAAQLLQD 210
Cdd:PRK11650 84 NYALYPHMSVRENMAYG--LKIRGMPKAEIEERVAEAARILELEPLLDRkpreL---------SGGQRQRVAMGRAIVRE 152
|
170
....*....|....
gi 578803088 211 PKVMLFDEPTTGLD 224
Cdd:PRK11650 153 PAVFLFDEPLSNLD 166
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
70-271 |
7.05e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 70 KDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFS----YvLQSDTLLSSLTVR 145
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG---GRIMLNGKEINALSTAQRLArglvY-LPEDRQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 146 ETLHYTAlLAIRRGNPGSFQK-KVEAVMAE-------LSLSHVadrligNYSLGGISTGERRRVSIAAQLLQDPKVMLFD 217
Cdd:PRK15439 356 APLAWNV-CALTHNRRGFWIKpARENAVLEryrralnIKFNHA------EQAARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578803088 218 EPTTGLDCMTANQIVVLLVELARRNrIVVLTIHQPRSELFQLFDKIAILSFGEL 271
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
68-224 |
1.09e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.63 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVRET 147
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAG-LLHVES--GQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 148 LHYTALLAIRRGN--PGSfqkkveaVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 224
Cdd:PRK13543 103 LHFLCGLHGRRAKqmPGS-------ALAIVGLAGYEDTLVRQ-----LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
66-314 |
1.19e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.64 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAG--TFLGEVYVNGRALRreQFQDCFSYVLQSDTLLSSLT 143
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSgyRYSGDVLLGGRSIF--NYRDVLEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 144 VRETLHYTALLAIRRGNP----GSFQKKVEAVMAELSL-SHVADRLigNYSLGGISTGERRRVSIAAQLLQDPKVMLFDE 218
Cdd:PRK14271 112 PFPMSIMDNVLAGVRAHKlvprKEFRGVAQARLTEVGLwDAVKDRL--SDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 219 PTTGLDCMTANQIVVLLVELArrNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGtPAEMLdffndcgYPCPEHSNPF 298
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEG-PTEQL-------FSSPKHAETA 259
|
250
....*....|....*.
gi 578803088 299 DFYMDLTSvDTQSKER 314
Cdd:PRK14271 260 RYVAGLSG-DVKDAKR 274
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
73-224 |
1.32e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 73 SLY----VESGQIMCILGSSGSGKTTLLDAMSGR----LGR--------------AGTFLG----EVYVNG-RALRREQF 125
Cdd:PRK13409 89 KLYglpiPKEGKVTGILGPNGIGKTTAVKILSGElipnLGDyeeepswdevlkrfRGTELQnyfkKLYNGEiKVVHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 126 QDCFSYVLQSdtllsslTVRETLHYTAllaiRRGnpgsfqkKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAA 205
Cdd:PRK13409 169 VDLIPKVFKG-------KVRELLKKVD----ERG-------KLDEVVERLGLENILDRDISE-----LSGGELQRVAIAA 225
|
170
....*....|....*....
gi 578803088 206 QLLQDPKVMLFDEPTTGLD 224
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLD 244
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
66-267 |
1.36e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 54.47 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVyvnGRALRREQFqdcfsYVLQSdTLLSSLTVR 145
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWGS--GRI---GMPEGEDLL-----FLPQR-PYLPLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 146 ETLHYtallairrgnpgsfqkkveAVMAELSLshvadrlignyslggistGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 225
Cdd:cd03223 82 EQLIY-------------------PWDDVLSG------------------GEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578803088 226 MTANQIVVLLVELarrnRIVVLTI-HqpRSELFQLFDKIAILS 267
Cdd:cd03223 125 ESEDRLYQLLKEL----GITVISVgH--RPSLWKFHDRVLDLD 161
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
66-251 |
1.43e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.00 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAmsgrLGRAGTFLGEVYVNG---RALRREQFQDCFSYVLQSDTLLSSl 142
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSA----LLRLLSTEGEIQIDGvswNSVTLQTWRKAFGVIPQKVFIFSG- 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVRETLHYTALLAirrgnpgsfQKKVEAVMAELSLSHVADRLIG--NYSL--GG--ISTGERRRVSIAAQLLQDPKVMLF 216
Cdd:TIGR01271 1307 TFRKNLDPYEQWS---------DEEIWKVAEEVGLKSVIEQFPDklDFVLvdGGyvLSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190
....*....|....*....|....*....|....*
gi 578803088 217 DEPTTGLDCMTAnQIVVLLVELARRNRIVVLTIHQ 251
Cdd:TIGR01271 1378 DEPSAHLDPVTL-QIIRKTLKQSFSNCTVILSEHR 1411
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
66-279 |
2.27e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.48 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLdamsgrlgraGTFLGEVYVN-GRALRREQfqdcFSYVLQSDTLLSSlTV 144
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLL----------QSLLSQFEISeGRVWAERS----IAYVPQQAWIMNA-TV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETlhytaLLAIRRGNPGSFQKKVEAVMAELSLSHVADRL---IGNYSLgGISTGERRRVSIAAQLLQDPKVMLFDEPTT 221
Cdd:PTZ00243 738 RGN-----ILFFDEEDAARLADAVRVSQLEADLAQLGGGLeteIGEKGV-NLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 222 GLDCMTANQIV--VLLVELARRNRivVLTIHQprSELFQLFDKIAILSFGELIFCGTPAE 279
Cdd:PTZ00243 812 ALDAHVGERVVeeCFLGALAGKTR--VLATHQ--VHVVPRADYVVALGDGRVEFSGSSAD 867
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
69-282 |
2.67e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 55.53 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQDCFSY---VLQSDtllSSLTVR 145
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG-IEKVKS--GEIFYNNQAITDDNFEKLRKHigiVFQNP---DNQFVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 146 ETLHYTALLAIRrGNPGSFQKKVEAVMAELSLSHVADRliGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 225
Cdd:PRK13648 99 SIVKYDVAFGLE-NHAVPYDEMHRRVSEALKQVDMLER--ADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 226 MTANQIVVLLVELARRNRIVVLTIHQPRSELFQLfDKIAILSFGELIFCGTPAEMLD 282
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISITHDLSEAMEA-DHVIVMNKGTVYKEGTPTEIFD 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
165-280 |
2.89e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 165 QKKVEAVMAELSLSHVADRLIGNYSlGGIstgeRRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRI 244
Cdd:NF000106 122 RARADELLERFSLTEAAGRAAAKYS-GGM----RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGAT 196
|
90 100 110
....*....|....*....|....*....|....*.
gi 578803088 245 VVLTIhQPRSELFQLFDKIAILSFGELIFCGTPAEM 280
Cdd:NF000106 197 VLLTT-QYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
66-224 |
4.19e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.35 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMsgrlgragtfLGEVYVNGRALRREQfQDCFSYVLQS---DTLLsSL 142
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV----------LGLVAPDEGVIKRNG-KLRIGYVPQKlylDTTL-PL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVRETLhytallairRGNPGSFQKKVEAVMAELSLSHVADrlignYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:PRK09544 85 TVNRFL---------RLRPGTKKEDILPALKRVQAGHLID-----APMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
..
gi 578803088 223 LD 224
Cdd:PRK09544 151 VD 152
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
69-296 |
4.50e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 54.71 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRagtFLGEVYVNGRALRREQFQDC---FSYVLQS-DTLLSSLTV 144
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE---FEGKVKIDGELLTAENVWNLrrkIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLhytALLAIRRGNP-GSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGL 223
Cdd:PRK13642 100 EDDV---AFGMENQGIPrEEMIKRVDEALLAVNMLDFKTR-----EPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 224 DCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQlFDKIAILSFGELIFCGTPAEMLDFFND---CGYPCPEHSN 296
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDmveIGLDVPFSSN 246
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
66-224 |
4.62e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMsgrlgrAGT---FLGEVyvngralrreQFQDCFS--YVLQSDTLLS 140
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM------AGVdkeFEGEA----------RPAPGIKvgYLPQEPQLDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETL-----HYTALLA------IRRGNPGSFQKKVEAVMAELS--------------LSHVADRL---IGNYSLGG 192
Cdd:PRK11819 84 EKTVRENVeegvaEVKAALDrfneiyAAYAEPDADFDALAAEQGELQeiidaadawdldsqLEIAMDALrcpPWDAKVTK 163
|
170 180 190
....*....|....*....|....*....|..
gi 578803088 193 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 224
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
65-276 |
9.47e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.49 E-value: 9.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFlGEVYVNGRALRREQFQD--------CFSY----- 131
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILE-GDILFKGESILDLEPEErahlgiflAFQYpieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 132 -VLQSDTL-LSSLTVRETLHYTALlairrgNPGSFqkkVEAVMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQ 209
Cdd:CHL00131 98 gVSNADFLrLAYNSKRKFQGLPEL------DPLEF---LEIINEKLKLVGMDPSFLSRNVNEGFSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 210 DPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGT 276
Cdd:CHL00131 169 DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
69-269 |
1.33e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR----EQFQDCFSYVLQS--------- 135
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSA---GTITLHGKKINNhnanEAINHGFALVTEErrstgiyay 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 136 -DTLLSSL--TVRETLHYTALLAIRRGNpgSFQKKVEAVMAELSLSHVAdrlignySLGGISTGERRRVSIAAQLLQDPK 212
Cdd:PRK10982 341 lDIGFNSLisNIRNYKNKVGLLDNSRMK--SDTQWVIDSMRVKTPGHRT-------QIGSLSGGNQQKVIIGRWLLTQPE 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578803088 213 VMLFDEPTTGLDCMTANQIVVLLVELARRNR-IVVLTIHQPrsELFQLFDKIAILSFG 269
Cdd:PRK10982 412 ILMLDEPTRGIDVGAKFEIYQLIAELAKKDKgIIIISSEMP--ELLGITDRILVMSNG 467
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
64-282 |
1.36e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.95 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 64 WTRQI---LKDVSLYVESGQIMCILGSSGSGKTTLLDAMsgrLGRAGTFLGEVYVNGRAlrreqfqdcfSYVLQSdTLLS 140
Cdd:TIGR00957 646 WARDLpptLNGITFSIPEGALVAVVGQVGCGKSSLLSAL---LAEMDKVEGHVHMKGSV----------AYVPQQ-AWIQ 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLHYTALLairrgNPGSFQKKVEA--VMAELSLSHVADRL-IGNYSLGgISTGERRRVSIAAQLLQDPKVMLFD 217
Cdd:TIGR00957 712 NDSLRENILFGKAL-----NEKYYQQVLEAcaLLPDLEILPSGDRTeIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 218 EPTTGLDCMTANQIV--VLLVELARRNRIVVLTIHQpRSELFQLfDKIAILSFGELIFCGTPAEMLD 282
Cdd:TIGR00957 786 DPLSAVDAHVGKHIFehVIGPEGVLKNKTRILVTHG-ISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-251 |
4.18e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.79 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 17 VNRGS------QSSLEGAPA----TAPEPHSLGILHAsysvshrvrpwwDITS-CRQQWTRQILKDVSLYVESGQIMCIL 85
Cdd:PRK10789 280 VERGSaaysriRAMLAEAPVvkdgSEPVPEGRGELDV------------NIRQfTYPQTDHPALENVNFTLKPGQMLGIC 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 86 GSSGSGKTTLLdAMSGRLGRAGTflGEVYVNGRALRREQFQDC---FSYVLQSDTLLSSlTVRETlhytallaIRRGNPG 162
Cdd:PRK10789 348 GPTGSGKSTLL-SLIQRHFDVSE--GDIRFHDIPLTKLQLDSWrsrLAVVSQTPFLFSD-TVANN--------IALGRPD 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 163 SFQKKVEAVMaelSLSHVAD---RLIGNY--SLGG----ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVV 233
Cdd:PRK10789 416 ATQQEIEHVA---RLASVHDdilRLPQGYdtEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILH 492
|
250
....*....|....*...
gi 578803088 234 LLVELaRRNRIVVLTIHQ 251
Cdd:PRK10789 493 NLRQW-GEGRTVIISAHR 509
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
70-240 |
4.69e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.02 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 70 KDVSLYVESGQIMCILGSSGSGKTT-------LLDAMSGR---LGRAGTFLGEVyvNGRALRRE-Q--FQDCfsyvlqsd 136
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTfaraiigLVKATDGEvawLGKDLLGMKDD--EWRAVRSDiQmiFQDP-------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 137 tlLSSLTVRETLHYTALLAIRRGNP----GSFQKKVEAVMAELSLshvADRLIGNYSlGGISTGERRRVSIAAQLLQDPK 212
Cdd:PRK15079 108 --LASLNPRMTIGEIIAEPLRTYHPklsrQEVKDRVKAMMLKVGL---LPNLINRYP-HEFSGGQCQRIGIARALILEPK 181
|
170 180
....*....|....*....|....*...
gi 578803088 213 VMLFDEPTTGLDCMTANQIVVLLVELAR 240
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVNLLQQLQR 209
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
65-275 |
5.70e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 65 TRQI--LKDVSLYVESGQIMCILGSSGSGKTTlldamSGR--LGRAGTFLGEVYVNGR-----------ALRREQ---FQ 126
Cdd:PRK10261 334 TREVhaVEKVSFDLWPGETLSLVGESGSGKST-----TGRalLRLVESQGGEIIFNGQridtlspgklqALRRDIqfiFQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 127 DCFsyvlqsdtllSSLTVRETLHYTALLAIR---RGNPGSFQKKVEAVMAELSL--SHvADRLIGNYslggiSTGERRRV 201
Cdd:PRK10261 409 DPY----------ASLDPRQTVGDSIMEPLRvhgLLPGKAAAARVAWLLERVGLlpEH-AWRYPHEF-----SGGQRQRI 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803088 202 SIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCG 275
Cdd:PRK10261 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
69-224 |
6.87e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMC-----ILGSSGSGKTTLLDAMSGRLG-RAGTFLGEVYVngralrreqfqdcfSYVLQSDTLLSSL 142
Cdd:PRK13409 350 LGDFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKpDEGEVDPELKI--------------SYKPQYIKPDYDG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVREtlhytaLLAIRRGNPGSFQKKVEaVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTG 222
Cdd:PRK13409 416 TVED------LLRSITDDLGSSYYKSE-IIKPLQLERLLDK-----NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 483
|
..
gi 578803088 223 LD 224
Cdd:PRK13409 484 LD 485
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
50-224 |
9.31e-07 |
|
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: 51.71 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 50 RVRPW---WDITSCRQQWTRQIL----------KDVSLYVESGQIMC-----ILGSSGSGKTTLLDAMSGRLG-RAGTFL 110
Cdd:COG1245 319 RIRDEpieFEVHAPRREKEEETLveypdltksyGGFSLEVEGGEIREgevlgIVGPNGIGKTTFAKILAGVLKpDEGEVD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 111 GEVYVngralrreqfqdcfSY---VLQSDtllSSLTVRETLhytallaiRRGNPGSFQ-KKVEAVMAE-LSLSHVADRli 185
Cdd:COG1245 399 EDLKI--------------SYkpqYISPD---YDGTVEEFL--------RSANTDDFGsSYYKTEIIKpLGLEKLLDK-- 451
|
170 180 190
....*....|....*....|....*....|....*....
gi 578803088 186 gnySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 224
Cdd:COG1245 452 ---NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
193-281 |
3.03e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.42 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 193 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELI 272
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
....*....
gi 578803088 273 FCGTPAEML 281
Cdd:PRK15093 239 ETAPSKELV 247
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
68-251 |
5.75e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 48.31 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAmsgrLGRAGTFLGEVYVNG---RALRREQFQDCFSYVLQSDTLLSSlTV 144
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSA----FLRLLNTEGDIQIDGvswNSVPLQKWRKAFGVIPQKVFIFSG-TF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLhytallairrgNPGSFQKKVE--AVMAELSLSHVADRLIG--NYSL--GG--ISTGERRRVSIAAQLLQDPKVMLF 216
Cdd:cd03289 94 RKNL-----------DPYGKWSDEEiwKVAEEVGLKSVIEQFPGqlDFVLvdGGcvLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190
....*....|....*....|....*....|....*
gi 578803088 217 DEPTTGLDCMTAnQIVVLLVELARRNRIVVLTIHQ 251
Cdd:cd03289 163 DEPSAHLDPITY-QVIRKTLKQAFADCTVILSEHR 196
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
72-247 |
7.57e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 72 VSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFS--YVL-----QSDTLLSSLTV 144
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTA---GQVYLDGKPIDIRSPRDAIRagIMLcpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLhytALLAIRRGNPGSF--QKKVEAVMAELSLSHV------ADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLF 216
Cdd:PRK11288 349 ADNI---NISARRHHLRAGCliNNRWEAENADRFIRSLniktpsREQLIMN-----LSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190
....*....|....*....|....*....|.
gi 578803088 217 DEPTTGLDCMTANQIVVLLVELARRNRIVVL 247
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQGVAVLF 451
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
73-281 |
7.65e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 73 SLYVESGQIMCILGSSGSGKTTLLDAMSGRLgragTFL-GEVYVNGRALRR---EQFQDCFSYVLQSDT--LLS------ 140
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGEL----PLLsGERQSQFSHITRlsfEQLQKLVSDEWQRNNtdMLSpgeddt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 141 SLTVRETLhytaLLAIRRGNpgsfqkKVEAVMAELSLSHVADRLIgNYslggISTGERRRVSIAAQLLQDPKVMLFDEPT 220
Cdd:PRK10938 99 GRTTAEII----QDEVKDPA------RCEQLAQQFGITALLDRRF-KY----LSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803088 221 TGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQSGITLVLVLNR-FDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
62-272 |
7.74e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 62 QQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLldAMSgRLGRA-GTFL-GEVYVNGRALR----REQFQDCFSYV--- 132
Cdd:NF040905 269 LHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTEL--AMS-VFGRSyGRNIsGTVFKDGKEVDvstvSDAIDAGLAYVted 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 133 -----------LQSDTLLSSLT----------VRETL---HYTALLAIRrgNPGSFQKkveavmaelslshvadrlIGNy 188
Cdd:NF040905 346 rkgyglnliddIKRNITLANLGkvsrrgvideNEEIKvaeEYRKKMNIK--TPSVFQK------------------VGN- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 189 slggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLtIHQPRSELFQLFDKIAILSF 268
Cdd:NF040905 405 ----LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIV-ISSELPELLGMCDRIYVMNE 479
|
....
gi 578803088 269 GELI 272
Cdd:NF040905 480 GRIT 483
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
66-281 |
9.01e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 47.60 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMsgrLGRAGTFLGEVYVNG---RALRREQFQDCFSYVLQsDTLLSSL 142
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAF---FRMVDIFDGKIVIDGidiSKLPLHTLRSRLSIILQ-DPILFSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 143 TVR---------------ETLHYTALLAIRRGNPGSfqkkVEAVMAElslshvadrlignyslGG--ISTGERRRVSIAA 205
Cdd:cd03288 110 SIRfnldpeckctddrlwEALEIAQLKNMVKSLPGG----LDAVVTE----------------GGenFSVGQRQLFCLAR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803088 206 QLLQDPKVMLFDEPTTGLDCMTANqIVVLLVELARRNRIVVLTIHQPRSELFQlfDKIAILSFGELIFCGTPAEML 281
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVSTILDA--DLVLVLSRGILVECDTPENLL 242
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
68-224 |
1.27e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSG------------------RLG----RAGTflGEVY------VNGRA 119
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivaRLQqdppRNVE--GTVYdfvaegIEEQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 120 LRREQFQDCFSYVLQ--SDTLLSSL-TVRETLHYTallairrgNPGSFQKKVEAVMAELSLShvadrliGNYSLGGISTG 196
Cdd:PRK11147 96 EYLKRYHDISHLVETdpSEKNLNELaKLQEQLDHH--------NLWQLENRINEVLAQLGLD-------PDAALSSLSGG 160
|
170 180
....*....|....*....|....*...
gi 578803088 197 ERRRVSIAAQLLQDPKVMLFDEPTTGLD 224
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
72-218 |
2.57e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.10 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 72 VSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRAL---RREQFQDCFSYVLqSDTLLssltvretl 148
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTG-LYRPES--GEILLDGQPVtadNREAYRQLFSAVF-SDFHL--------- 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803088 149 hYTALLAIrrgNPGSFQKKVEAVMAELSLSH---VADRLIGNYSLggiSTGERRRVSIAAQLLQDPKVMLFDE 218
Cdd:COG4615 418 -FDRLLGL---DGEADPARARELLERLELDHkvsVEDGRFSTTDL---SQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
176-267 |
3.00e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 176 SLSHVADRLIGNYSlGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSE 255
Cdd:PTZ00265 1343 SLPNKYDTNVGPYG-KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIA 1420
|
90
....*....|..
gi 578803088 256 LFQLFDKIAILS 267
Cdd:PTZ00265 1421 SIKRSDKIVVFN 1432
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
66-253 |
3.64e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.55 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTfLGEVYVNGRALRREQFQD--------CFSYVLQ--- 134
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVT-GGTVEFKGKDLLELSPEDragegifmAFQYPVEipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 135 -SDTLLSSLTVRETLHYTALLAIRRGNpgsFQKKVEAVMAELSLShvADRLIGNYSLgGISTGERRRVSIAAQLLQDPKV 213
Cdd:PRK09580 93 vSNQFFLQTALNAVRSYRGQEPLDRFD---FQDLMEEKIALLKMP--EDLLTRSVNV-GFSGGEKKRNDILQMAVLEPEL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578803088 214 MLFDEPTTGLDcMTANQIVVLLVELARR-NRIVVLTIHQPR 253
Cdd:PRK09580 167 CILDESDSGLD-IDALKIVADGVNSLRDgKRSFIIVTHYQR 206
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
69-276 |
4.75e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.39 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR---------EQFQDCFSYVLQSDTLL 139
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAG---GLVQCDKMLLRRrsrqvielsEQSAAQMRHVRGADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 140 ------SSLTVRETLHYTALLAIRRGNPGSFQKKVEAVMAELSLSHV--ADRLIGNYSlGGISTGERRRVSIAAQLLQDP 211
Cdd:PRK10261 109 ifqepmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIpeAQTILSRYP-HQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803088 212 KVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGT 276
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
68-281 |
5.48e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.51 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSgRLGRAGTflGEVYVNGRALRREQFQD---CFSYVLQSDTLLSSlTV 144
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALF-RIVELEK--GRIMIDDCDVAKFGLTDlrrVLSIIPQSPVLFSG-TV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 145 RETLhytallairrgNPgsFQKKVEAVMAE-LSLSHVADrLIGNYSLG----------GISTGERRRVSIAAQLLQDPKV 213
Cdd:PLN03232 1327 RFNI-----------DP--FSEHNDADLWEaLERAHIKD-VIDRNPFGldaevseggeNFSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803088 214 MLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTiHqpRSELFQLFDKIAILSFGELIFCGTPAEML 281
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIA-H--RLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
66-281 |
6.74e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.86 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMsgrLGRAGTFLGEVYVNGR--------ALRRE----QfQDCfsyVL 133
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLL---MGYYPLTEGEIRLDGRplsslshsVLRQGvamvQ-QDP---VV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 134 QSDTLLSSLTVretlhytallairrGNPGSfQKKVEAVMAELSLSHVADRLI-GNYSLGG-----ISTGERRRVSIAAQL 207
Cdd:PRK10790 427 LADTFLANVTL--------------GRDIS-EEQVWQALETVQLAELARSLPdGLYTPLGeqgnnLSVGQKQLLALARVL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803088 208 LQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVL-----TIHQPrselfqlfDKIAILSFGELIFCGTPAEML 281
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIahrlsTIVEA--------DTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
69-253 |
1.59e-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: 42.70 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLdamsgrlgragtflgevyvngralrreqfQDCFSYVLQSdTLLSSLTVREtl 148
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV-----------------------------NEGLYASGKA-RLISFLPKFS-- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 149 hYTALLAIrrgnpGSFQKKVEAVMAELSLshvadrligNYSLGGISTGERRRVSIAAQLLQDPK--VMLFDEPTTGLDCM 226
Cdd:cd03238 59 -RNKLIFI-----DQLQFLIDVGLGYLTL---------GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180
....*....|....*....|....*..
gi 578803088 227 TANQIVVLLVELARRNRIVVLTIHQPR 253
Cdd:cd03238 124 DINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
78-268 |
3.75e-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: 41.58 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 78 SGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGevyvngralRREQFQdcfsyvlqsdtllssltvretlhytallair 157
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIGLALGGAQSATR---------RRSGVK------------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 158 rgnPGSFqkkVEAVMAELslshvadrligNYSLGGISTGERRRVSIAAQL----LQDPKVMLFDEPTTGLDCMTANQIVV 233
Cdd:cd03227 60 ---AGCI---VAAVSAEL-----------IFTRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAE 122
|
170 180 190
....*....|....*....|....*....|....*
gi 578803088 234 LLVELARRNRIVVLTIHQPrsELFQLFDKIAILSF 268
Cdd:cd03227 123 AILEHLVKGAQVIVITHLP--ELAELADKLIHIKK 155
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
68-280 |
5.41e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDamsgrlgragTFL-------GEVYVNGR--------ALRREqfqdcFSYV 132
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLL----------TFMrmvevcgGEIRVNGReigayglrELRRQ-----FSMI 1389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 133 LQsDTLLSSLTVRETLhytallairrgNPGSfQKKVEAVMAELSL----SHVADRLIG----------NYSLGgistgER 198
Cdd:PTZ00243 1390 PQ-DPVLFDGTVRQNV-----------DPFL-EASSAEVWAALELvglrERVASESEGidsrvleggsNYSVG-----QR 1451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803088 199 RRVSIAAQLLQ-DPKVMLFDEPTTGLDCMTANQIVVLlVELARRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTP 277
Cdd:PTZ00243 1452 QLMCMARALLKkGSGFILMDEATANIDPALDRQIQAT-VMSAFSAYTVITIAH--RLHTVAQYDKIIVMDHGAVAEMGSP 1528
|
...
gi 578803088 278 AEM 280
Cdd:PTZ00243 1529 REL 1531
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
69-121 |
6.79e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 6.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGrAGTFLGEVYVNGRALR 121
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGSYEGEILFDGEVCR 68
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
78-127 |
6.82e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 6.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 578803088 78 SGQIMCILGSSGSGKTTLLDAMSGRLGRAGTflGEVYVNGRALRREQFQD 127
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG--GVIYIDGEDILEEVLDQ 48
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
176-251 |
1.45e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 1.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 176 SLSHVADRLIGNySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL-ARRNRIVVLTIHQ 251
Cdd:PTZ00265 564 ALPDKYETLVGS-NASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHR 639
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
84-108 |
1.78e-03 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 40.65 E-value: 1.78e-03
10 20
....*....|....*....|....*...
gi 578803088 84 ILGSSGSGKTTLLDAM---SGRLGRAGT 108
Cdd:cd04170 4 LVGHSGSGKTTLAEALlyaTGAIDRLGR 31
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
193-246 |
3.08e-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: 3.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 578803088 193 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC---MTANQIVVLLVELARRNRIVV 246
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrLNAARAIRRLSEEGKKTALVV 128
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
66-103 |
6.11e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 6.11e-03
10 20 30
....*....|....*....|....*....|....*...
gi 578803088 66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRL 103
Cdd:PRK15064 332 GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGEL 369
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
69-108 |
6.91e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 6.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 578803088 69 LKDVSLYVESGQIMCILGSSGSGKTTLLD-----AMSGRLGRAGT 108
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypALANRLNGAKT 668
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
84-100 |
9.29e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 9.29e-03
|
| |
