|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
319-818 |
1.50e-49 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 185.64 E-value: 1.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTER---LGGEILINGQQVSRRGLRELCSYVpaLEVSSLDPRMSVQC 395
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAISAYV--QQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 396 TLNFHAALRGPIDRSDLE--ERMDVLIEDLGL----NTV--RASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMD 467
Cdd:TIGR00955 119 HLMFQAHLRMPRRVTKKEkrERVDEVLQALGLrkcaNTRigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 468 IFDTFFLVEYLRQWCSGGRIVIMTLQPPTFEILSMCSGVLLLSGGRTVFSGSRADLPRHMGELGYPCPPFKNPADYYLDL 547
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 548 VTLDDLSAAAMLESSARI------ESLANAWDQINS-----EPPLAAPPASLPNFTMKAGFFGQISALIKRF--AGYKQP 614
Cdd:TIGR00955 279 LAVIPGSENESRERIEKIcdsfavSDIGRDMLVNTNlwsgkAGGLVKDSENMEGIGYNASWWTQFYALLKRSwlSVLRDP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 615 gsLLTWIsKLIAAAVLSLFIGCIFWDVPASdpQLSYHDRLG----------YHHCVMVLVYWPLVMLTIRdtqedrrhae 684
Cdd:TIGR00955 359 --LLLKV-RLIQTMMTAILIGLIYLGQGLT--QKGVQNINGalflfltnmtFQNVFPVINVFTAELPVFL---------- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 685 RDIRLGLYTRSLYIIVQSLLGLFPSLCIWLAYLLPAHSMAGLYtysnssdTGIYLYmGYMLLYLTLIQTLALFCAHLLPC 764
Cdd:TIGR00955 424 RETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLR-------SGATHF-LTFLFLVTLVANVATSFGYLISC 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24649836 765 KVS----ASIVNGLISLAVAAVGGYLVHPQNLAQFWSWLQFVSPERWLLPVLVQDEYS 818
Cdd:TIGR00955 496 AFSstsmALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWS 553
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
319-518 |
9.70e-33 |
|
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: 126.62 E-value: 9.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTE---RLGGEILINGQQVSRRGLRELCSYVPALEVssLDPRMSVQC 395
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKCVAYVRQDDI--LLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 396 TLNFHAALRGPIDRSDLEERM---DVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTF 472
Cdd:cd03234 101 TLTYTAILRLPRKSSDAIRKKrveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24649836 473 FLVEYLRQWCSGGRIVIMTLQPPTFEILSMCSGVLLLSGGRTVFSG 518
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
319-518 |
1.15e-29 |
|
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: 116.50 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLG--GEILINGQQVSRRGLRELCSYVPALEVssLDPRMSVQCT 396
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRKIIGYVPQDDI--LHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 397 LNFHAALRGpidrsdleermdvliedlglntvrasnvstLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTFFLVE 476
Cdd:cd03213 103 LMFAAKLRG------------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24649836 477 YLRQWCSGGRIVIMTLQPPTFEILSMCSGVLLLSGGRTVFSG 518
Cdd:cd03213 153 LLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
319-523 |
1.77e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 114.39 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMatsqreG------SALAECLAGLTERLGGEILINGQQVSRRG--LRELCSYVPalEVSSLDPR 390
Cdd:COG1131 16 LDGVSLTVEPGEIFGLL------GpngagkTTTIRMLLGLLRPTSGEVRVLGEDVARDPaeVRRRIGYVP--QEPALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 391 MSVQCTLNFHAALRGpIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFD 470
Cdd:COG1131 88 LTVRENLRFFARLYG-LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24649836 471 TFFLVEYLRQWCSGGRIVIMT---LQpptfEILSMCSGVLLLSGGRTVFSGSRADL 523
Cdd:COG1131 167 RRELWELLRELAAEGKTVLLSthyLE----EAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
319-817 |
1.79e-24 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 110.58 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAgltERL------GGEILINGQQVSRRGLRELcSYVPALEVSSldPRMS 392
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLA---ERVttgvitGGDRLVNGRPLDSSFQRSI-GYVQQQDLHL--PTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 393 VQCTLNFHAALRGPIDRSDLE--ERMDVLIEDLGLNTVRASNVST----LTHSEKQRLSVACQLLAQSSLLI-LDQVTSN 465
Cdd:TIGR00956 853 VRESLRFSAYLRQPKSVSKSEkmEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 466 MDIFDTFFLVEYLRQWCSGGRIVIMTLQPPTFEILSMCSGVLLLS-GGRTVFSGsraDLPRHMGEL--------GYPCPP 536
Cdd:TIGR00956 933 LDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQkGGQTVYFG---DLGENSHTIinyfekhgAPKCPE 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 537 FKNPADYYLDLVtlddlSAAAmlESSARI------------ESLANAWDQINSEPPLAA---PPASLPNFTMKagFFGQ- 600
Cdd:TIGR00956 1010 DANPAEWMLEVI-----GAAP--GAHANQdyhevwrnsseyQAVKNELDRLEAELSKAEddnDPDALSKYAAS--LWYQf 1080
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 601 ISALIKRFAGY-KQPGSLLtwiSKLIAAAVLSLFIGCIFWDVpasdpQLSYHDRlgyhHCVMVLVYWPLVMLT------- 672
Cdd:TIGR00956 1081 KLVLWRTFQQYwRTPDYLY---SKFFLTIFAALFIGFTFFKV-----GTSLQGL----QNQMFAVFMATVLFNpliqqyl 1148
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 673 -----IRDTQEDRRHAERdirlgLYTRSLYIIVQSLLGL-FPSLCIWLAYLLpAHSMAGLY---TYSNS-SDTGIYLYMG 742
Cdd:TIGR00956 1149 ppfvaQRDLYEVRERPSR-----TFSWLAFIAAQITVEIpYNLVAGTIFFFI-WYYPVGFYwnaSKTGQvHERGVLFWLL 1222
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24649836 743 YMLLYLtLIQTLALFCAHLLPCKVSASIVNGLISLAVAAVGGYLVHPQNLAQFWSWLQFVSPERWLLPVLVQDEY 817
Cdd:TIGR00956 1223 STMFFL-YFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGL 1296
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
319-830 |
2.40e-24 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 109.20 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTE--RLGGEILINGQQVSRRGLRELcSYVPALEVssLDPRMSVQCT 396
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNRKPTKQILKRT-GFVTQDDI--LYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 397 LNFHAALRGP--IDRSDLEERMDVLIEDLGL----NTVRA-SNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIF 469
Cdd:PLN03211 161 LVFCSLLRLPksLTKQEKILVAESVISELGLtkceNTIIGnSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 470 DTFFLVEYLRQWCSGGRIVIMTLQPPTFEILSMCSGVLLLSGGRTVFSGSRADLPRHMGELGYPcPPFK-NPADYYLDLV 548
Cdd:PLN03211 241 AAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFS-PSFPmNPADFLLDLA 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 549 T-LDDLSAAAMLESSARIESLANAWDQINSePPLAAPPASLPNFTMKAGF--------------------FGQISALIKR 607
Cdd:PLN03211 320 NgVCQTDGVSEREKPNVKQSLVASYNTLLA-PKVKAAIEMSHFPQANARFvgsastkehrssdrisistwFNQFSILLQR 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 608 FAGYKQPGSLLTW-ISKLIAAAVLSlfiGCIFWDVPASDpqlsYHDRLGYhhCVMVLVYW---PLVMLTIRDTQEdRRHA 683
Cdd:PLN03211 399 SLKERKHESFNTLrVFQVIAAALLA---GLMWWHSDFRD----VQDRLGL--LFFISIFWgvfPSFNSVFVFPQE-RAIF 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 684 ERDIRLGLYTRSLYIIVQSLLGLFPSLCIWLAYLLPAHSMAGLytysnSSDTGIYLY-MGYMLLYLTLIQTLAL-FCAHL 761
Cdd:PLN03211 469 VKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGL-----KPELGAFLLtLLVLLGYVLVSQGLGLaLGAAI 543
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 762 LPCKVSASIVNgLISLAVAAVGGYLVHpqNLAQFWSWLQFVSPERWLLPVLVQDEY-SAETLSNSAGLQL 830
Cdd:PLN03211 544 MDAKKASTIVT-VTMLAFVLTGGFYVH--KLPSCMAWIKYISTTFYSYRLLINVQYgEGKRISSLLGCSL 610
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
317-513 |
2.67e-20 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 90.22 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 317 PCLRGVSMQAKAGDLFAIMATSqreG---SALAECLAGLTERLGGEILINGQQVSRRGLRELcsyvpALEVSSL--DPRM 391
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPN---GsgkSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL-----RRKVGLVfqNPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 392 SVQCT-----LNFHAALRGpIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNM 466
Cdd:cd03225 87 QFFGPtveeeVAFGLENLG-LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24649836 467 DIFDTFFLVEYLRQWCSGGRIVIMTlqppT---FEILSMCSGVLLLSGGR 513
Cdd:cd03225 166 DPAGRRELLELLKKLKAEGKTIIIV----ThdlDLLLELADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
307-513 |
2.09e-19 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 85.76 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 307 NIQVHCLDvNPCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSR---RGLRELCSYVPale 383
Cdd:cd00267 4 NLSFRYGG-RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlplEELRRRIGYVP--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 384 vssldprmsvQctlnfhaalrgpidrsdleermdvliedlglntvrasnvstLTHSEKQRLSVACQLLAQSSLLILDQVT 463
Cdd:cd00267 80 ----------Q-----------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24649836 464 SNMDIFDTFFLVEYLRQWCSGGRIVIMTLQPPTfEILSMCSGVLLLSGGR 513
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPE-LAELAADRVIVLKDGK 157
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
319-518 |
6.08e-17 |
|
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: 80.49 E-value: 6.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSR--RGLRELCSYVPALEvsSLDPRMSVQCT 396
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepAEARRRLGFVSDST--GLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 397 LNFHAALRGpIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTFFLVE 476
Cdd:cd03266 99 LEYFAGLYG-LKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24649836 477 YLRQWCSGGRIVIMT---LQpptfEILSMCSGVLLLSGGRTVFSG 518
Cdd:cd03266 178 FIRQLRALGKCILFSthiMQ----EVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
343-518 |
3.69e-16 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 78.00 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 343 SALAECLAGLTERLGGEILINGQQVSRRG--LRELCSYVPalEVSSLDPRMSVQCTLNFHAALRGpIDRSDLEERMDVLI 420
Cdd:cd03264 39 TTLMRILATLTPPSSGTIRIDGQDVLKQPqkLRRRIGYLP--QEFGVYPNFTVREFLDYIAWLKG-IPSKEVKARVDEVL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 421 EDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTFFLVEYLRQwCSGGRIVIMTlqppTF--- 497
Cdd:cd03264 116 ELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSE-LGEDRIVILS----THive 190
|
170 180
....*....|....*....|.
gi 24649836 498 EILSMCSGVLLLSGGRTVFSG 518
Cdd:cd03264 191 DVESLCNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
319-491 |
4.97e-16 |
|
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: 77.52 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAImatsqrEG------SALAECLAGLTERLGGEILINGQQVSRRG--LRELCSYVPALevSSLDPR 390
Cdd:COG4133 18 FSGLSFTLAAGEALAL------TGpngsgkTTLLRILAGLLPPSAGEVLWNGEPIRDARedYRRRLAYLGHA--DGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 391 MSVQCTLNFHAALRG-PIDRSDLEErmdvLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIF 469
Cdd:COG4133 90 LTVRENLRFWAALYGlRADREAIDE----ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180
....*....|....*....|..
gi 24649836 470 DTFFLVEYLRQWCSGGRIVIMT 491
Cdd:COG4133 166 GVALLAELIAAHLARGGAVLLT 187
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
316-523 |
1.59e-15 |
|
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: 76.39 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 316 NPCLRGVSMQAKAGDLFAIMATSqreGSA---LAECLAGLTERLGGEILINGQQV--SRRGLRELCSYVPALEVssLDPR 390
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHN---GAGkttTLKMLTGELRPTSGTAYINGYSIrtDRKAARQSLGYCPQFDA--LFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 391 MSVQCTLNFHAALRGpIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFD 470
Cdd:cd03263 90 LTVREHLRFYARLKG-LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24649836 471 TFFLVEYLrQWCSGGRIVIMTLQPPTfEILSMCSGVLLLSGGRTVFSGSRADL 523
Cdd:cd03263 169 RRAIWDLI-LEVRKGRSIILTTHSMD-EAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
319-464 |
6.01e-15 |
|
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: 73.07 E-value: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSqreG---SALAECLAGLTERLGGEILINGQQVSRRGLREL---CSYVPalEVSSLDPRMS 392
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPN---GagkSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrkeIGYVF--QDPQLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24649836 393 VQCTLNFHAALRGPIDRSDlEERMDVLIEDLGL----NTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTS 464
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREK-DARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
319-518 |
1.04e-14 |
|
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: 73.24 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMatsqreG------SALAECLAGLTERLGGEILINGQQVSRRGLREL---CSYVP-ALEVssld 388
Cdd:cd03214 15 LDDLSLSIEAGEIVGIL------GpngagkSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELarkIAYVPqALEL---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 389 prmsvqctlnfhaalrgpIDRSDLEERmdvliedlglntvrasNVSTLTHSEKQRLSVAcQLLAQ-SSLLILDQVTSNMD 467
Cdd:cd03214 85 ------------------LGLAHLADR----------------PFNELSGGERQRVLLA-RALAQePPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24649836 468 IFDTFFLVEYLRQWC-SGGRIVIMTLQPPTFeILSMCSGVLLLSGGRTVFSG 518
Cdd:cd03214 130 IAHQIELLELLRRLArERGKTVVMVLHDLNL-AARYADRVILLKDGRIVAQG 180
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
319-518 |
1.87e-14 |
|
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: 72.66 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTER--LGGEILINGQQVSRRGLRElCSYVPALEVssLDPRMSVQCT 396
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKNFQRS-TGYVEQQDV--HSPNLTVREA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 397 LNFHAALRGpidrsdleermdvliedlglntvrasnvstLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTFFLVE 476
Cdd:cd03232 100 LRFSALLRG------------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24649836 477 YLRQWCSGGRIVIMTLQPPTFEILSMCSGVLLL-SGGRTVFSG 518
Cdd:cd03232 150 FLKKLADSGQAILCTIHQPSASIFEKFDRLLLLkRGGKTVYFG 192
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
319-515 |
2.77e-14 |
|
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: 72.67 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSRRGLRELCSYVPAlevsslDPRM-----SV 393
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQ------DVDYqlftdSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 394 QCTLnfhaaLRGPIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTFF 473
Cdd:cd03226 90 REEL-----LLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24649836 474 LVEYLRQWCSGGRIVIMTLQPPTFeILSMCSGVLLLSGGRTV 515
Cdd:cd03226 165 VGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANGAIV 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
319-518 |
5.33e-14 |
|
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: 71.93 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSRRGlRELCSYVPalEVSSLDPRMSVQCTLN 398
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-RNRIGYLP--EERGLYPKMKVIDQLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 399 FHAALRGpIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTFFLVEYL 478
Cdd:cd03269 93 YLAQLKG-LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24649836 479 RQWCSGGRIVIM-TLQPPTFEilSMCSGVLLLSGGRTVFSG 518
Cdd:cd03269 172 RELARAGKTVILsTHQMELVE--ELCDRVLLLNKGRAVLYG 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
319-523 |
1.25e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.45 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIM----A---TSQRegsalaeCLAGLTERLGGEILINGQQVSRRGLRELcSYVPalEVSSLDPRM 391
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLgpngAgktTTIR-------IILGILAPDSGEVLWDGEPLDPEDRRRI-GYLP--EERGLYPKM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 392 SVQCTLNFHAALRGpIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDT 471
Cdd:COG4152 87 KVGEQLVYLARLKG-LSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24649836 472 FFLVEYLRQWCSGGRIVIM-TLQPPTFEilSMCSGVLLLSGGRTVFSGSRADL 523
Cdd:COG4152 166 ELLKDVIRELAAKGTTVIFsSHQMELVE--ELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
316-467 |
1.28e-13 |
|
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: 71.10 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 316 NPCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQ---QVSRRGLRELCSYVPalevssldprms 392
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirDISRKSLRSMIGVVL------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 393 vQCTLNFHAALRGPIDRSDLEERMDV------------LIEDL--GLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLI 458
Cdd:cd03254 84 -QDTFLFSGTIMENIRLGRPNATDEEvieaakeagahdFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
....*....
gi 24649836 459 LDQVTSNMD 467
Cdd:cd03254 163 LDEATSNID 171
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
316-513 |
1.52e-13 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 69.35 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 316 NPCLRGVSMQAKAGDLFAIMatsqreG------SALAECLAGLTERLGGEILINGQQVSRRG--LRELCSYVPalEVSSL 387
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLL------GpngagkTTLIKIILGLLKPDSGEIKVLGKDIKKEPeeVKRRIGYLP--EEPSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 388 DPRMSVqctlnfhaalrgpidrsdleerMDVLiedlglntvrasnvsTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMD 467
Cdd:cd03230 85 YENLTV----------------------RENL---------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24649836 468 IFDTFFLVEYLRQWCSGGRIVIMT---LQpptfEILSMCSGVLLLSGGR 513
Cdd:cd03230 128 PESRREFWELLRELKKEGKTILLSshiLE----EAERLCDRVAILNNGR 172
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
319-523 |
2.06e-13 |
|
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: 74.10 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSqreGSA---LAECLAGLTERLGGEILINGQ---QVSRRGLRELCSYVPAlevsslDPRMs 392
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRS---GSGkstLLKLLLGLYEPTSGRILIDGIdlrQIDPASLRRQIGVVLQ------DVFL- 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 393 vqctlnFHAALR-------GPIDRSDLEE--RM---DVLIEDL--GLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLI 458
Cdd:COG2274 561 ------FSGTIRenitlgdPDATDEEIIEaaRLaglHDFIEALpmGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24649836 459 LDQVTSNMDIFDTFFLVEYLRQWCSGGRIVIMTLQPPTfeiLSMCSGVLLLSGGRTVFSGSRADL 523
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLST---IRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-467 |
3.03e-13 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 73.40 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSqreG---SALAECLAGLTERLGGEILINGQQV---SRRGLRELCSYV------PAlevSS 386
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGES---GsgkSTLARLLLGLLRPTSGSILFDGKDLtklSRRSLRELRRRVqmvfqdPY---SS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 387 LDPRMSVQCTLNFHAALRGPIDRSDLEERMDVLIEDLGLNT-VRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSN 465
Cdd:COG1123 355 LNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSA 434
|
..
gi 24649836 466 MD 467
Cdd:COG1123 435 LD 436
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
604-809 |
8.40e-13 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 68.07 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 604 LIKR-FAGYKQPGSLLTWisKLIAAAVLSLFIGCIFWDVPAsdpQLSYHDRLGYhhCVMVLVYWPLVMLT----IRDTQe 678
Cdd:pfam01061 1 LLKReFLRRWRDPSLGLW--RLIQPILMALIFGTLFGNLGN---QQGGLNRPGL--LFFSILFNAFSALSgispVFEKE- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 679 dRRHAERDIRLGLYTRSLYIIVQSLLGLFPSLCIWLAYLLPAHSMAGLytysNSSDTGIYLYMGYMLLYLTLIQTLALFC 758
Cdd:pfam01061 73 -RGVLYRELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGL----PPSAGRFFLFLLVLLLTALAASSLGLFI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24649836 759 AHLLPCKVSASIVNGLISLAVAAVGGYLVHPQNLAQFWSWLQFVSPERWLL 809
Cdd:pfam01061 148 SALAPSFEDASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAI 198
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
314-530 |
1.33e-12 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 71.09 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 314 DVNPCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTE---RLGGEILINGQ---QVSRRGLRELCSYVPALEVSSL 387
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRdllELSEALRGRRIGMVFQDPMTQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 388 DPrMSVQCTLNFHAALRGpIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMD 467
Cdd:COG1123 97 NP-VTVGDQIAEALENLG-LSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24649836 468 ------IFDtffLVEYLRQWcSGGRIVIMTLQPPtfEILSMCSGVLLLSGGRTVFSGSRADLPRHMGEL 530
Cdd:COG1123 175 vttqaeILD---LLRELQRE-RGTTVLLITHDLG--VVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
319-641 |
2.44e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 71.42 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGltERLG----GEILINGQQVSRRGLRELCSYVPALEVSSldPRMSVQ 394
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGgyieGDIRISGFPKKQETFARISGYCEQNDIHS--PQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 395 CTLNFHAALRGPIDRSDlEERM---DVLIEDLGLNTVRAS-----NVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNM 466
Cdd:PLN03140 972 ESLIYSAFLRLPKEVSK-EEKMmfvDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 467 DIFDTFFLVEYLRQWCSGGRIVIMTLQPPTFEILSMCSGVLLLS-GGRTVFSGSRADLPRHMGEL-----GYPCPPFK-N 539
Cdd:PLN03140 1051 DARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKrGGQVIYSGPLGRNSHKIIEYfeaipGVPKIKEKyN 1130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 540 PADYYLDLVTLD-----DLSAAAMLESSARIESLANAWDQINSEPPLAAPPASLPNFTMKagFFGQI-SALIKRFAGY-K 612
Cdd:PLN03140 1131 PATWMLEVSSLAaevklGIDFAEHYKSSSLYQRNKALVKELSTPPPGASDLYFATQYSQS--TWGQFkSCLWKQWWTYwR 1208
|
330 340 350
....*....|....*....|....*....|
gi 24649836 613 QPG-SLLTWISKLIAAavlsLFIGCIFWDV 641
Cdd:PLN03140 1209 SPDyNLVRFFFTLAAA----LMVGTIFWKV 1234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
317-518 |
4.49e-12 |
|
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: 66.40 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 317 PCLRGVSMQAKAGDLFAIMatsqreG------SALAECLAGLTERLGGEILINGQQVSRRglRELCSYVPALEVSSLDPR 390
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIV------GpngagkSTLLKAILGLLKPTSGSIRVFGKPLEKE--RKRIGYVPQRRSIDRDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 391 MSVqctLNF-------HAALRGPIDRSDlEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVT 463
Cdd:cd03235 85 ISV---RDVvlmglygHKGLFRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24649836 464 SNMDIFDTFFLVEYLRQWCSGGRIVIMTLQPPTfEILSMCSGVLLLsGGRTVFSG 518
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHDLG-LVLEYFDRVLLL-NRTVVASG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
319-530 |
6.23e-12 |
|
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: 66.20 E-value: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMatsqreG------SALAECLAGLTERLGGEILINGQQVSRRGLRELCSYV------P------ 380
Cdd:COG1122 17 LDDVSLSIEKGEFVAII------GpngsgkSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVglvfqnPddqlfa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 381 ---ALEVSsldprmsvqctlnFhaalrGP----IDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQ 453
Cdd:COG1122 91 ptvEEDVA-------------F-----GPenlgLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 454 SSLLILDQVTSNMDIFDTFFLVEYLRQWCSGGRIVIMT---LQpptfEILSMCSGVLLLSGGRTVFSGSRADLPRHMGEL 530
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVthdLD----LVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
308-518 |
1.76e-11 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 64.55 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 308 IQVHCLDVN----PCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSRrgLRELCSYVPAL- 382
Cdd:cd03268 1 LKTNDLTKTygkkRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGALi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 383 EVSSLDPRMSVQCTLNFHAALRGPidrsdLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQV 462
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGI-----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24649836 463 TSNMDIFDTFFLVEYLRQWCSGGRIVIM---TLQpptfEILSMCSGVLLLSGGRTVFSG 518
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLIsshLLS----EIQKVADRIGIINKGKLIEEG 208
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
305-518 |
2.13e-11 |
|
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: 64.53 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 305 YPNIQvhcldvNPCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILING---QQVSRRGLRELCSYVPA 381
Cdd:cd03245 12 YPNQE------IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDPADLRRNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 382 levsslDPRMsVQCTLNFHAALRGPIdrSDLEERMDVL----IEDL------GLNTVRASNVSTLTHSEKQRLSVACQLL 451
Cdd:cd03245 86 ------DVTL-FYGTLRDNITLGAPL--ADDERILRAAelagVTDFvnkhpnGLDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24649836 452 AQSSLLILDQVTSNMDIFDTFFLVEYLRQWCSGGRIVIMTLQPPtfeILSMCSGVLLLSGGRTVFSG 518
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPS---LLDLVDRIIVMDSGRIVADG 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
317-523 |
6.23e-11 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 66.30 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 317 PCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILING---QQVSRRGLRELCSYVPAlevsslDPRMSV 393
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslKDIDRHTLRQFINYLPQ------EPYIFS 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 394 QCTL-NFHAALRGPIDRSDLEERMDVL-----IED--LGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSN 465
Cdd:TIGR01193 562 GSILeNLLLGAKENVSQDEIWAACEIAeikddIENmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSN 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24649836 466 MDIFDTFFLVEYLrqwcsggriviMTLQPPT-------FEILSMCSGVLLLSGGRTVFSGSRADL 523
Cdd:TIGR01193 642 LDTITEKKIVNNL-----------LNLQDKTiifvahrLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
319-467 |
9.38e-11 |
|
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: 62.91 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSqreG---SALAECLAGLTERLGGEILINGQQVS--RRGLRELC----SYVPALEVSSLDP 389
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGES---GsgkSTLARAILGLLKPTSGSIIFDGKDLLklSRRLRKIRrkeiQMVFQDPMSSLNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 390 RMSVQC----TLNFHaalRGPIDRSDLEERMDVLIEDLGLNTVRASNvstLTHS----EKQRLSVACQLLAQSSLLILDQ 461
Cdd:cd03257 98 RMTIGEqiaePLRIH---GKLSKKEARKEAVLLLLVGVGLPEEVLNR---YPHElsggQRQRVAIARALALNPKLLIADE 171
|
....*.
gi 24649836 462 VTSNMD 467
Cdd:cd03257 172 PTSALD 177
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
317-523 |
4.03e-10 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 60.91 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 317 PCLRGVSMQAKAGDLFAIMAtsqREG---SALAECLAGLTERLGGEILINGQQVS--------RRGLrelcSYVPalEVS 385
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLG---RNGagkTTLLKTIMGLLPPRSGSIRFDGRDITglppheraRAGI----GYVP--EGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 386 SLDPRMSVQCTLNFHAALRGPIDRSDLEERMDVLIEDLGlnTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSN 465
Cdd:cd03224 85 RIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLK--ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24649836 466 M------DIFDTfflveyLRQWCSGGRIVIMTLQPPTFeILSMCSGVLLLSGGRTVFSGSRADL 523
Cdd:cd03224 163 LapkiveEIFEA------IRELRDEGVTILLVEQNARF-ALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
389-819 |
1.95e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 389 PRMSVQCTLNFHAALRGP------IDRSDLEERM-DVLIEDLGLNTVRASNVST-----LTHSEKQRLSVACQLLAQSSL 456
Cdd:TIGR00956 151 PHLTVGETLDFAARCKTPqnrpdgVSREEYAKHIaDVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 457 LILDQVTSNMDIFDTFflvEYLRQWCSGGRI----VIMTLQPPTFEILSMCSGVLLLSGGRTVFSGSRADLPRHMGELGY 532
Cdd:TIGR00956 231 QCWDNATRGLDSATAL---EFIRALKTSANIldttPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGF 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 533 PCPPFKNPADY---------------YLDLV--TLDDLS---------AAAMLESSARIESLANAWDQINSEPPLAA--P 584
Cdd:TIGR00956 308 KCPDRQTTADFltsltspaerqikpgYEKKVprTPQEFEtywrnspeyAQLMKEIDEYLDRCSESDTKEAYRESHVAkqS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 585 PASLPNFTMKAGFFGQISALIKR-FAGYKqpGSLLTWISKLIAAAVLSLFIGCIFWDVPASDPqlSYHDRLGyhhcVM-- 661
Cdd:TIGR00956 388 KRTRPSSPYTVSFSMQVKYCLARnFLRMK--GNPSFTLFMVFGNIIMALILSSVFYNLPKNTS--DFYSRGG----ALff 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 662 -VLVYWPLVMLTIRDTQEDRRHAERDIRLGLYTRSLYIIVQSLLGLFPSLCIWLAYLLpahsmaglytysnssdtgIYLY 740
Cdd:TIGR00956 460 aILFNAFSSLLEIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNI------------------ILYF 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 741 M-------GYMLLYLtLIQTLALFCA-HLLPCKVS-------ASIVNGLISLAVAAVGGYLVHPQNLAQFWSWLQFVSPE 805
Cdd:TIGR00956 522 MvnfrrtaGRFFFYL-LILFICTLAMsHLFRSIGAvtktlseAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPL 600
|
490
....*....|....
gi 24649836 806 RWLLPVLVQDEYSA 819
Cdd:TIGR00956 601 AYAFESLMVNEFHG 614
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
316-468 |
2.39e-09 |
|
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: 58.27 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 316 NPCLRGVSMQAKAGDLFAIMAtsqREG---SALAECLAGLTERLGGEILINGQQVSRRGLRELCSyvpalevssldpRMS 392
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVG---RTGsgkSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS------------RIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 393 V--QCTLNFHAALR---GPIDRSDLEERMDVL--------IEDL--GLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLL 457
Cdd:cd03244 82 IipQDPVLFSGTIRsnlDPFGEYSDEELWQALervglkefVESLpgGLDTVVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170
....*....|.
gi 24649836 458 ILDQVTSNMDI 468
Cdd:cd03244 162 VLDEATASVDP 172
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
319-490 |
5.31e-09 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 57.83 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMatsqreG------SALAECLAGLTERLGGEILINGQQVSRRGLRELCSY--VPALEVSSLDPR 390
Cdd:cd03219 16 LDDVSFSVRPGEIHGLI------GpngagkTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgiGRTFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 391 MSVQ--CTLNFHAALRGPI-------DRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQ 461
Cdd:cd03219 90 LTVLenVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180
....*....|....*....|....*....
gi 24649836 462 VTSNMDIFDTFFLVEYLRQWCSGGRIVIM 490
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRERGITVLL 198
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
316-490 |
2.37e-08 |
|
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: 54.31 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 316 NPCLRGVSMQAKAGDLFAIMATSqreG---SALAECLAGLTERLGGEILINGQ---QVSRRGLRELCSYVPalevssldp 389
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPS---GsgkSTLLKLLLRLYDPTSGEILIDGVdlrDLDLESLRKNIAYVP--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 390 rmsvQCTLNFHAalrgpidrsdleermdvliedlglnTVRaSNVstLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIF 469
Cdd:cd03228 83 ----QDPFLFSG-------------------------TIR-ENI--LSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180
....*....|....*....|.
gi 24649836 470 DTFFLVEYLRQWcSGGRIVIM 490
Cdd:cd03228 131 TEALILEALRAL-AKGKTVIV 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
316-513 |
2.39e-08 |
|
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: 54.53 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 316 NPCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQ---QVSRRGLRELCSYVPAlEVSSLDprms 392
Cdd:cd03246 15 PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisQWDPNELGDHVGYLPQ-DDELFS---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 393 vqctlnfhaalrGPIdrsdleermdvliedlglntvrASNVstLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTF 472
Cdd:cd03246 90 ------------GSI----------------------AENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24649836 473 FLVEYLRQWCSGGRIVIMTLQPPtfEILSMCSGVLLLSGGR 513
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHRP--ETLASADRILVLEDGR 172
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
319-495 |
2.60e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 55.19 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVS--RRGLRELCSYVPALevSSLDPRMSVQCT 396
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDfqRDSIARGLLYLGHA--PGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 397 LNFHAALRGpidRSDLEERMDvlieDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTFFLVE 476
Cdd:cd03231 94 LRFWHADHS---DEQVEEALA----RVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170
....*....|....*....
gi 24649836 477 YLRQWCSGGRIVIMTLQPP 495
Cdd:cd03231 167 AMAGHCARGGMVVLTTHQD 185
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
319-519 |
2.69e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 56.39 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQV--SRRGLRELCSYVpALEVSSLDPRM---SV 393
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESV-GMVFQDPDNQLfsaSV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 394 QCTLNFhAALRGPIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTFF 473
Cdd:PRK13636 101 YQDVSF-GAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24649836 474 LVEYLRQWCSGGRIVIMTLQPPTFEILSMCSGVLLLSGGRTVFSGS 519
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
317-523 |
5.69e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.61 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 317 PCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSRRG--LRELCSYVPALEvsSLDPRMSVQ 394
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARArlARARIGVVPQFD--NLDLEFTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 395 CTLNFHAALRGPIDRsDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTFFL 474
Cdd:PRK13536 133 ENLLVFGRYFGMSTR-EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24649836 475 VEYLRQWCSGGRIVIMTLQpptF--EILSMCSGVLLLSGGRTVFSGSRADL 523
Cdd:PRK13536 212 WERLRSLLARGKTILLTTH---FmeEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
308-522 |
2.02e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.01 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 308 IQVHCLDVNPCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERlGGEILINGQQVSRRGLRELCSYVPALEVSSL 387
Cdd:PRK03695 1 MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 388 DP-RMSVQCTLNFHAALRGPIDrsDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLL-------AQSSLLIL 459
Cdd:PRK03695 80 PPfAMPVFQYLTLHQPDKTRTE--AVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 460 DQVTSNMDIFDTFFLVEYLRQWCSGGRIVIM-------TLQPPTfeilsmcsGVLLLSGGRTVFSGSRAD 522
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQQGIAVVMsshdlnhTLRHAD--------RVWLLKQGKLLASGRRDE 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
309-522 |
6.97e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.71 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 309 QVHCLDVNPCLRGVSMQAKAGDLFAI--MATSQRegSALAECLAGLTERLGGEILINGQQVS--------RRGLrelcSY 378
Cdd:COG1129 258 EVEGLSVGGVVRDVSFSVRAGEILGIagLVGAGR--TELARALFGADPADSGEIRLDGKPVRirsprdaiRAGI----AY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 379 VPalE---VSSLDPRMSVQ--CTLNFHAAL--RGPIDRSDLEERMDVLIEDLGlntVRASNVSTLTHS----EKQRLSVA 447
Cdd:COG1129 332 VP--EdrkGEGLVLDLSIRenITLASLDRLsrGGLLDRRRERALAEEYIKRLR---IKTPSPEQPVGNlsggNQQKVVLA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 448 CQLLAQSSLLILDQVT------SNMDIFdtfflvEYLRQWCSGGRIVIMT---LQpptfEILSMCSGVLLLSGGRTV--F 516
Cdd:COG1129 407 KWLATDPKVLILDEPTrgidvgAKAEIY------RLIRELAAEGKAVIVIsseLP----ELLGLSDRILVMREGRIVgeL 476
|
....*.
gi 24649836 517 SGSRAD 522
Cdd:COG1129 477 DREEAT 482
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
307-468 |
7.06e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.33 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 307 NIQVHCLDvNPCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTER--LGGEILINGQQV------SRRGLRELCSY 378
Cdd:PRK09580 6 DLHVSVED-KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLlelspeDRAGEGIFMAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 379 VPALEVSSLDPRMSVQCTLNFHAALRG--PIDRSDLEERMDVLIEDLGLNT---VRASNVStLTHSEKQRLSVACQLLAQ 453
Cdd:PRK09580 85 QYPVEIPGVSNQFFLQTALNAVRSYRGqePLDRFDFQDLMEEKIALLKMPEdllTRSVNVG-FSGGEKKRNDILQMAVLE 163
|
170
....*....|....*
gi 24649836 454 SSLLILDQVTSNMDI 468
Cdd:PRK09580 164 PELCILDESDSGLDI 178
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
319-468 |
8.42e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 51.61 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVS------RRGLRELCSYVPALEVSSLDPRMS 392
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklnraqRKAFRRDIQMVFQDSISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 393 VQctlnfhAALRGP------IDRSDLEERMDVLIEDLGLNTVRASNV-STLTHSEKQRLSVACQLLAQSSLLILDQVTSN 465
Cdd:PRK10419 108 VR------EIIREPlrhllsLDKAERLARASEMLRAVDLDDSVLDKRpPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
...
gi 24649836 466 MDI 468
Cdd:PRK10419 182 LDL 184
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-526 |
1.27e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.68 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTE-----RLGGEILINGQQVSRRGLRELCSYVPAL-EVSSLDPRMS 392
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVfQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 393 VQCTLNFHAAL-RGPIDRSDLEERMDVLIEDLGL-----NTVRASnVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNM 466
Cdd:PRK14247 99 IFENVALGLKLnRLVKSKKELQERVRWALEKAQLwdevkDRLDAP-AGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24649836 467 DIFDTFFLVEYLRQWCSGGRIVIMTLQPPTFEILSmcSGVLLLSGGRTVFSGSRADL---PRH 526
Cdd:PRK14247 178 DPENTAKIESLFLELKKDMTIVLVTHFPQQAARIS--DYVAFLYKGQIVEWGPTREVftnPRH 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
319-463 |
1.55e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATS---QREgsaLAECLAGLTERLGGEILINGQQV---SRRGLREL-CSYVPAlevsslD--- 388
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAgngQSE---LAEALAGLRPPASGSIRLDGEDItglSPRERRRLgVAYIPE------Drlg 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 389 ----PRMSVQctlnFHAAL----------RGPIDRSDLEERMDVLIEDLGlntVRASNVSTLTHS----EKQRLSVACQL 450
Cdd:COG3845 345 rglvPDMSVA----ENLILgryrrppfsrGGFLDRKAIRAFAEELIEEFD---VRTPGPDTPARSlsggNQQKVILAREL 417
|
170
....*....|...
gi 24649836 451 LAQSSLLILDQVT 463
Cdd:COG3845 418 SRDPKLLIAAQPT 430
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
349-519 |
1.79e-06 |
|
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: 52.32 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 349 LAGLTERLGGEILINGQQV--SRRGLRELCSYVPALEVssLDPRMSVQCTLNFHAALRG-PIDRSDLEerMDVLIEDLGL 425
Cdd:TIGR01257 976 LTGLLPPTSGTVLVGGKDIetNLDAVRQSLGMCPQHNI--LFHHLTVAEHILFYAQLKGrSWEEAQLE--MEAMLEDTGL 1051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 426 NTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTFFLVEYLRQWCSGGRIVIMTLQPPTFEILSmcSG 505
Cdd:TIGR01257 1052 HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLG--DR 1129
|
170
....*....|....
gi 24649836 506 VLLLSGGRTVFSGS 519
Cdd:TIGR01257 1130 IAIISQGRLYCSGT 1143
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
314-519 |
6.24e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 48.83 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 314 DVNPCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSR----RGLRELCSYVPALEVSSLDP 389
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsklQGIRKLVGIVFQNPETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 390 RmSVQCTLNFhaalrGP----IDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSN 465
Cdd:PRK13644 93 R-TVEEDLAF-----GPenlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24649836 466 MDIFDTFFLVEYLRQWCSGGRIVIMTLQppTFEILSMCSGVLLLSGGRTVFSGS 519
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITH--NLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
319-513 |
7.75e-06 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 47.18 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSrrglrelcsyvpalevssldprmsvqctln 398
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT------------------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 399 fhaalRGPIDRSDLEERMDVLIEDLGLN---TVRaSNVS-TLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTFFL 474
Cdd:cd03229 66 -----DLEDELPPLRRRIGMVFQDFALFphlTVL-ENIAlGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREV 139
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24649836 475 VEYLRQ-WCSGGRIVIMTLQPPtFEILSMCSGVLLLSGGR 513
Cdd:cd03229 140 RALLKSlQAQLGITVVLVTHDL-DEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
319-515 |
8.52e-06 |
|
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: 46.65 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMatsqreG------SALAECLAGLTERLGGEILINGQQVSRRGLRElcsyvpalevssldprms 392
Cdd:cd03216 16 LDGVSLSVRRGEVHALL------GengagkSTLMKILSGLYKPDSGEILVDGKEVSFASPRD------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 393 vqctlnfhaALRgpidrsdleermdvliedLGLNTvrasnVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTF 472
Cdd:cd03216 72 ---------ARR------------------AGIAM-----VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24649836 473 FLVEYLRQWCSGGRIVIMT---LQpptfEILSMCSGVLLLSGGRTV 515
Cdd:cd03216 120 RLFKVIRRLRAQGVAVIFIshrLD----EVFEIADRVTVLRDGRVV 161
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
316-468 |
1.10e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 49.25 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 316 NPCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILING---QQVSRRGLRELCSYVpalevssldprmS 392
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLASLRNQVALV------------S 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 393 VQCTL-------NFHAALRGPIDRSDLEER------MDvLIEDL--GLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLL 457
Cdd:PRK11176 424 QNVHLfndtianNIAYARTEQYSREQIEEAarmayaMD-FINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPIL 502
|
170
....*....|.
gi 24649836 458 ILDQVTSNMDI 468
Cdd:PRK11176 503 ILDEATSALDT 513
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
355-552 |
1.11e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 355 RLGGEILINGQQVSRRGLRELCSYVPALEVSSldPRMSVQCTLNFHAALRGPIDRSDL---------------EERMDV- 418
Cdd:PLN03140 220 KVSGEITYNGYRLNEFVPRKTSAYISQNDVHV--GVMTVKETLDFSARCQGVGTRYDLlselarrekdagifpEAEVDLf 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 419 ------------LIED-----LGLNTVRASNVST-----LTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTFFLVE 476
Cdd:PLN03140 298 mkatamegvkssLITDytlkiLGLDICKDTIVGDemirgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVK 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 477 YLRQWC--SGGRIVIMTLQPP--TFEILSmcsGVLLLSGGRTVFSGSRADLPRHMGELGYPCPPFKNPADYYLDLVTLDD 552
Cdd:PLN03140 378 CLQQIVhlTEATVLMSLLQPApeTFDLFD---DIILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKD 454
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
322-468 |
1.19e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.86 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 322 VSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQV-----SRRGLR-ELCSYVPAlevSSLDPRMSVQC 395
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdySYRSQRiRMIFQDPS---TSLNPRQRISQ 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24649836 396 TLNFHAALRGPIDRSDLEERMDVLIEDLGLNTVRASNVS-TLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDI 468
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPhMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
317-525 |
1.24e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 317 PCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSRRG---LRELCSY-VPalEVSSLDPRMS 392
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQLGIYlVP--QEPLLFPNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 393 VQCTLNFhaalrGPIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTF 472
Cdd:PRK15439 103 VKENILF-----GLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24649836 473 FLVEYLRQWCSGGR-IVIMTLQPPtfEILSMCSGVLLLSGGRTVFSGSRADLPR 525
Cdd:PRK15439 178 RLFSRIRELLAQGVgIVFISHKLP--EIRQLADRISVMRDGTIALSGKTADLST 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
317-467 |
1.31e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 48.80 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 317 PCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQ---VSRRGLRELCSYV---PALEVSSLDPR 390
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDirtVTRASLRRNIAVVfqdAGLFNRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 391 MSVQCTLNFHAALRGPIDR---SDLEERmdvliEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMD 467
Cdd:PRK13657 429 IRVGRPDATDEEMRAAAERaqaHDFIER-----KPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
319-467 |
1.39e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 47.66 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVS-------------RRGLRELCSYVP-ALEV 384
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTmVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 385 SSLDPRMSVqctlnFHAALRGPID-----RSDLEERMDVLIEDLGLN-TVRASNVSTLTHSEKQRLSVACQLLAQSSLLI 458
Cdd:PRK10619 101 FNLWSHMTV-----LENVMEAPIQvlglsKQEARERAVKYLAKVGIDeRAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
....*....
gi 24649836 459 LDQVTSNMD 467
Cdd:PRK10619 176 FDEPTSALD 184
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
319-528 |
1.79e-05 |
|
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: 47.10 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQ---VSRRGLRELCSYVpalevssldprmsVQC 395
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlalADPAWLRRQVGVV-------------LQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 396 TLNFHAALRGPIDRSDLEERMDVLIE--------------DLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQ 461
Cdd:cd03252 85 NVLFNRSIRDNIALADPGMSMERVIEaaklagahdfiselPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24649836 462 VTSNMDIFDTFFLVEYLRQWCSGGRIVIMTLQPPTFeilsMCSG-VLLLSGGRTVFSGSRADLPRHMG 528
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTV----KNADrIIVMEKGRIVEQGSHDELLAENG 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
314-467 |
2.04e-05 |
|
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: 46.84 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 314 DVNPCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSRRGLRELCSYVpALeVSsldprmsv 393
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQI-GL-VS-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 394 QCTLNFHAALRGPI----DRSDLEERMDVL--------IEDL--GLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLIL 459
Cdd:cd03251 83 QDVFLFNDTVAENIaygrPGATREEVEEAAraanahefIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILIL 162
|
....*...
gi 24649836 460 DQVTSNMD 467
Cdd:cd03251 163 DEATSALD 170
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
316-467 |
2.15e-05 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 46.76 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 316 NPCLRGVSMQAKAGDLFAIMATSqreGSALAECLAgLTERL----GGEILINGQQVSR---RGLRELCSYV---PALevs 385
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSS---GCGKSTVVS-LLERFydptSGEILLDGVDIRDlnlRWLRSQIGLVsqePVL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 386 sldprmsVQCTLNFHAALrGPIDRSDlEERMDV--------LIEDL--GLNTVRASNVSTLTHSEKQRLSVACQLLAQSS 455
Cdd:cd03249 89 -------FDGTIAENIRY-GKPDATD-EEVEEAakkanihdFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170
....*....|..
gi 24649836 456 LLILDQVTSNMD 467
Cdd:cd03249 160 ILLLDEATSALD 171
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
314-467 |
2.16e-05 |
|
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: 46.64 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 314 DVNPCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSRRGLRELCSyvpALEVSSLDPrmsv 393
Cdd:cd03369 19 DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS---SLTIIPQDP---- 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24649836 394 qcTLnFHAALRG---PIDRSDLEERMDVL-IEDLGLNtvrasnvstLTHSEKQRLSVACQLLAQSSLLILDQVTSNMD 467
Cdd:cd03369 92 --TL-FSGTIRSnldPFDEYSDEEIYGALrVSEGGLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
358-467 |
3.23e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 358 GEILINGQQVSRRGLRELCSYVPALEV------SSLDPRMSVQCT----LNFHAALRGPIDRsdlEERMDVLIEDLGLN- 426
Cdd:PRK15134 340 GEIWFDGQPLHNLNRRQLLPVRHRIQVvfqdpnSSLNPRLNVLQIieegLRVHQPTLSAAQR---EQQVIAVMEEVGLDp 416
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 24649836 427 TVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMD 467
Cdd:PRK15134 417 ETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
319-467 |
3.90e-05 |
|
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: 46.02 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGL-----TERLGGEILINGQQVsrrglrelcsYVPALEVSSL------ 387
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDI----------YDLDVDVLELrrrvgm 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 388 -----DP-RMSVQCTLNFHAALRGPIDRSDLEERMDVLIEDLGL--NTVRASNVSTLTHSEKQRLSVACQLLAQSSLLIL 459
Cdd:cd03260 86 vfqkpNPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALANEPEVLLL 165
|
....*...
gi 24649836 460 DQVTSNMD 467
Cdd:cd03260 166 DEPTSALD 173
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
306-523 |
7.97e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 45.99 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 306 PNIQVHCLDVN----PCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSRRGLRELCSYVPA 381
Cdd:PRK09536 2 PMIDVSDLSVEfgdtTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 382 L--EVS---SLDPRMSVQCTLNFHAALRGPIDRSDlEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSL 456
Cdd:PRK09536 82 VpqDTSlsfEFDVRQVVEMGRTPHRSRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24649836 457 LILDQVTSNMDIFDTFFLVEYLRQWCSGGRIVIMTLQPptfeiLSM----CSGVLLLSGGRTVFSGSRADL 523
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHD-----LDLaaryCDELVLLADGRVRAAGPPADV 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
319-467 |
8.16e-05 |
|
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: 44.94 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVsrrglrelcSYVPALEVS--------SLDPR 390
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV---------TDLPPKDRDiamvfqnyALYPH 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24649836 391 MSVQCTLNFHAALRGpIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMD 467
Cdd:cd03301 87 MTVYDNIAFGLKLRK-VPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
319-467 |
1.28e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.79 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSRRGLRELCSYVPALEVSSLDPRMS--VQCT 396
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIFSptVEQD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24649836 397 LNFhaalrGPI----DRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMD 467
Cdd:PRK13652 100 IAF-----GPInlglDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
317-490 |
1.86e-04 |
|
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: 43.55 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 317 PCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSRRGLRELCSYVPALEVSSLDPRMSVQCT 396
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 397 L--NFHAALR-GPIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTFF 473
Cdd:cd03292 95 VyeNVAFALEvTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170
....*....|....*..
gi 24649836 474 LVEYLRQWCSGGRIVIM 490
Cdd:cd03292 175 IMNLLKKINKAGTTVVV 191
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
319-523 |
3.16e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.39 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSR---RGLRELCSYVPALEVSSLDpRMSVQ- 394
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKldhKLAAQLGIGIIYQELSVID-ELTVLe 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 395 ------------CTLNFhaalrgpIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQV 462
Cdd:PRK09700 100 nlyigrhltkkvCGVNI-------IDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24649836 463 TS---NMDIFDTFFLVEYLRQwcSGGRIVIMTLQppTFEILSMCSGVLLLSGGRTVFSGSRADL 523
Cdd:PRK09700 173 TSsltNKEVDYLFLIMNQLRK--EGTAIVYISHK--LAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
319-523 |
7.57e-04 |
|
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: 42.22 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVS-----RRGLRELC-SYvpalevsSLDPRMS 392
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITnlpphKRPVNTVFqNY-------ALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 393 VQCTLNFHAALRGpIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIfdtf 472
Cdd:cd03300 89 VFENIAFGLRLKK-LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL---- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24649836 473 flveYLRQWCsggRIVIMTLQPP---TF--------EILSMCSGVLLLSGGRTVFSGSRADL 523
Cdd:cd03300 164 ----KLRKDM---QLELKRLQKElgiTFvfvthdqeEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
319-467 |
7.90e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.07 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVS------RRGLR-ELCSYVpaLEVSSLDPRM 391
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdeeaRAKLRaKHVGFV--FQSFMLIPTL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24649836 392 SVQCTLNFHAALRGPIDRSDlEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMD 467
Cdd:PRK10584 104 NALENVELPALLRGESSRQS-RNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
343-519 |
9.16e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 41.92 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 343 SALAECLAGLTERLGGEILINGQQVSRRGLRELCSYVPALEVSSLDPR-MSVQCTLNF----HAALRGPIDRSDlEERMD 417
Cdd:PRK11231 42 STLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEgITVRELVAYgrspWLSLWGRLSAED-NARVN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 418 VLIEDLGLNTVRASNVSTLTHSEKQRLSVAcQLLAQSS-LLILDQVTSNMDIFDTFFLVEYLRQWCSGGRIVIMTL---- 492
Cdd:PRK11231 121 QAMEQTRINHLADRRLTDLSGGQRQRAFLA-MVLAQDTpVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLhdln 199
|
170 180
....*....|....*....|....*..
gi 24649836 493 QPPTFeilsmCSGVLLLSGGRTVFSGS 519
Cdd:PRK11231 200 QASRY-----CDHLVVLANGHVMAQGT 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
329-480 |
1.02e-03 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 41.90 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 329 GDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSRRGLRELCSYVPALEVSSLDP-RMSVQctlNFHAALRGPI 407
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPgDITVQ---ELVARGRYPH 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24649836 408 D------RSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFDTFFLVEYLRQ 480
Cdd:PRK10253 110 QplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSE 188
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
314-467 |
1.07e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 42.00 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 314 DVNPcLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSRRGLRELCSYVpALEVSSLDPRM-- 391
Cdd:PRK13642 19 DVNQ-LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI-GMVFQNPDNQFvg 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24649836 392 -SVQCTLNFHAALRGpIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMD 467
Cdd:PRK13642 97 aTVEDDVAFGMENQG-IPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
319-503 |
1.34e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 41.01 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMAtsqREGS---ALAECLAGLTERLGGEILINGQQVSRRGLRELCSYVPALevSSLDPRMSVQC 395
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTG---PNGSgktTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHR--NAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 396 TLNFHAALRGPiDRSDLEErmdvLIEDLGLN---TVRASNVSTlthSEKQRLSVACQLLAQSSLLILDQVTSNMDIF-DT 471
Cdd:PRK13539 93 NLEFWAAFLGG-EELDIAA----ALEAVGLAplaHLPFGYLSA---GQKRRVALARLLVSNRPIWILDEPTAALDAAaVA 164
|
170 180 190
....*....|....*....|....*....|....*
gi 24649836 472 FFLVEYLRQWCSGGRIVIMTLQP---PTFEILSMC 503
Cdd:PRK13539 165 LFAELIRAHLAQGGIVIAATHIPlglPGARELDLG 199
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
317-491 |
1.52e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 41.53 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 317 PCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQV--SRRGLRELCSYVPALevsSLDPRMSVQ 394
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATV---FQDPEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 395 CT---LNFHAALRG-PIDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDIFD 470
Cdd:PRK13638 92 YTdidSDIAFSLRNlGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180
....*....|....*....|.
gi 24649836 471 TFFLVEYLRQWCSGGRIVIMT 491
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHVIIS 192
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
320-491 |
1.58e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 40.94 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 320 RGVSMQAKAGDLFAIMAtsqREGS---ALAECLAGLTERLGGEILINGQQVSRRG---LRELCsYVPALevSSLDPRMSV 393
Cdd:PRK13538 18 SGLSFTLNAGELVQIEG---PNGAgktSLLRILAGLARPDAGEVLWQGEPIRRQRdeyHQDLL-YLGHQ--PGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 394 QCTLNFHAALRGPIDRSD---------LEERMDVLiedlglntvrasnVSTLTHSEKQRLSVACQLLAQSSLLILDQVTS 464
Cdd:PRK13538 92 LENLRFYQRLHGPGDDEAlwealaqvgLAGFEDVP-------------VRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180
....*....|....*....|....*..
gi 24649836 465 NMDIFDTFFLVEYLRQWCSGGRIVIMT 491
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMVILT 185
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
319-480 |
1.67e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 41.02 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 319 LRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSR----RGLRELCSYVPalEVSSLDPRMSVQ 394
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtaKIMREAVAIVP--EGRRVFSRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 395 CTL---NFHAalrgpiDRSDLEERMDVLIEDLG-LNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSN----- 465
Cdd:PRK11614 99 ENLamgGFFA------ERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGlapii 172
|
170
....*....|....*.
gi 24649836 466 -MDIFDTfflVEYLRQ 480
Cdd:PRK11614 173 iQQIFDT---IEQLRE 185
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
314-468 |
2.65e-03 |
|
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: 41.85 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 314 DVNPCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSRRGLRELCSyvpALEVSSLDPRMsv 393
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF---KITIIPQDPVL-- 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 394 qctlnFHAALRGPID----RSDLEERMDVLIEDL---------GLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILD 460
Cdd:TIGR00957 1372 -----FSGSLRMNLDpfsqYSDEEVWWALELAHLktfvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLD 1446
|
....*...
gi 24649836 461 QVTSNMDI 468
Cdd:TIGR00957 1447 EATAAVDL 1454
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
368-467 |
3.00e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.55 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 368 SRRGLRELCSYVPALEVSSLDPRMSVQCTLNFHAalrgpIDRSDLEE-RMDVLIEDL------GLNTVRASNVSTLTHSE 440
Cdd:PTZ00265 510 KRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQT-----IKDSEVVDvSKKVLIHDFvsalpdKYETLVGSNASKLSGGQ 584
|
90 100
....*....|....*....|....*..
gi 24649836 441 KQRLSVACQLLAQSSLLILDQVTSNMD 467
Cdd:PTZ00265 585 KQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
343-467 |
3.78e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 40.78 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 343 SALAECLAGLTERLGGEILINGQQV-----SRRGLRELC-SYvpalevsSLDPRMSVQCTLNFHAALRGpIDRSDLEERM 416
Cdd:PRK11000 43 STLLRMIAGLEDITSGDLFIGEKRMndvppAERGVGMVFqSY-------ALYPHLSVAENMSFGLKLAG-AKKEEINQRV 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 24649836 417 DVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMD 467
Cdd:PRK11000 115 NQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
317-515 |
3.98e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.11 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 317 PCLRGVSMQAKAGDLFAIMATSQREGSALAECLAGLTERLGGEILINGQQVSRRGL---RELCSYVPALEV-------SS 386
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLtdlRRVLSIIPQSPVlfsgtvrFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649836 387 LDPrmsvqctLNFH--AALRGPIDRSDLEERMDVliEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTS 464
Cdd:PLN03232 1330 IDP-------FSEHndADLWEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24649836 465 NMDIFDTFFLVEYLRQWCSGGRIVIMTLQPPTfeILSmCSGVLLLSGGRTV 515
Cdd:PLN03232 1401 SVDVRTDSLIQRTIREEFKSCTMLVIAHRLNT--IID-CDKILVLSSGQVL 1448
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
407-468 |
6.24e-03 |
|
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: 39.27 E-value: 6.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24649836 407 IDRSDLEERMDVLIEDLGLNTVRASNVSTLTHSEKQRLSVACQLLAQSSLLILDQVTSNMDI 468
Cdd:cd03236 111 LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
|
| |
