|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
42-278 |
1.23e-81 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 257.67 E-value: 1.23e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 42 IINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKLQGVTGQ--FLLNGRPRDIMSFRKMSAYIAQNFVMLNLLTVEET 119
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSgsVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 120 LRVSTDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTL------VKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDC 193
Cdd:TIGR00955 120 LMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 194 VGSYQVICHLQRLAHDGRIVVCVVHQPGSRLFQLFDDVLVLAHGEVLYAGEQREMLPTFAQSGHICPQYYNPADF----- 268
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFyvqvl 279
|
250
....*....|.
gi 24581387 269 -GIPGSVQSVL 278
Cdd:TIGR00955 280 aVIPGSENESR 290
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-243 |
1.23e-72 |
|
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: 221.27 E-value: 1.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 20 ALELHFSQVSYSLKGA-TKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGF-KLQGVTGQFLLNGRPRDIMSF 97
Cdd:cd03213 1 GVTLSFRNLTVTVKSSpSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrTGLGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 98 RKMSAYIAQNFVMLNLLTVEETLRVSTDLKmpsstaaqekqkiiddiidilqlqscrrtlvkNLSGGEHKRLSIGIELVT 177
Cdd:cd03213 81 RKIIGYVPQDDILHPTLTVRETLMFAAKLR--------------------------------GLSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24581387 178 NPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGSRLFQLFDDVLVLAHGEVLYAG 243
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
42-243 |
1.06e-66 |
|
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: 207.12 E-value: 1.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 42 IINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfKLQG---VTGQFLLNGRPRDIMSFRKMSAYIAQNFVMLNLLTVEE 118
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGggtTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 119 TLRVSTDLKMPSSTAAQEKQKI-IDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSY 197
Cdd:cd03234 101 TLTYTAILRLPRKSSDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24581387 198 QVICHLQRLAHDGRIVVCVVHQPGSRLFQLFDDVLVLAHGEVLYAG 243
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-243 |
8.15e-59 |
|
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: 185.91 E-value: 8.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLKGAtKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKLQG-VTGQFLLNGRPRDImSFRKMS 101
Cdd:cd03232 4 LTWKNLNYTVPVK-GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGvITGEILINGRPLDK-NFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 102 AYIAQNFVMLNLLTVEETLRVSTDLKmpsstaaqekqkiiddiidilqlqscrrtlvkNLSGGEHKRLSIGIELVTNPPI 181
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFSALLR--------------------------------GLSVEQRKRLTIGVELAAKPSI 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581387 182 MFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGSRLFQLFDDVLVLAH-GEVLYAG 243
Cdd:cd03232 130 LFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
42-268 |
1.81e-50 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 178.38 E-value: 1.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 42 IINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKLQGV--TGQFLLNGRPRDiMSFRKMSAYIAQNFVMLNLLTVEET 119
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVitGGDRLVNGRPLD-SSFQRSIGYVQQQDLHLPTSTVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 120 LRVSTDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLV----KNLSGGEHKRLSIGIELVTNPP-IMFFDEPTSGLDCV 194
Cdd:TIGR00956 857 LRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQ 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 195 GSYQVICHLQRLAHDGRIVVCVVHQPGSRLFQLFDDVLVLAHG-EVLYAGEQRE----MLPTFAQSG-HICPQYYNPADF 268
Cdd:TIGR00956 937 TAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGDLGEnshtIINYFEKHGaPKCPEDANPAEW 1016
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
42-268 |
7.22e-50 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 174.30 E-value: 7.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 42 IINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfKLQG--VTGQFLLNGRP--RDIMsfrKMSAYIAQNFVMLNLLTVE 117
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG-RIQGnnFTGTILANNRKptKQIL---KRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 118 ETLRVSTDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKN-----LSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24581387 193 CVGSYQVICHLQRLAHDGRIVVCVVHQPGSRLFQLFDDVLVLAHGEVLYAGEQREMLPTFAQSGHICPQYYNPADF 268
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADF 314
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
2-266 |
9.82e-41 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 150.38 E-value: 9.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 2 ADNAVQAQpNGLGPQKQKAL-----ELHFSQVSYSL--------KGATKGSTPIINEACGVFKSGRLTAILGPSGAGKST 68
Cdd:PLN03140 843 RDSSLEAA-NGVAPKRGMVLpftplAMSFDDVNYFVdmpaemkeQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTT 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 69 LLNALAGFKLQG-VTGQFLLNGRPRDIMSFRKMSAYIAQNFVMLNLLTVEETLRVSTDLKMPSSTAAQEKQKIIDDIIDI 147
Cdd:PLN03140 922 LMDVLAGRKTGGyIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMEL 1001
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 148 LQLQSCRRTLV-----KNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGS 222
Cdd:PLN03140 1002 VELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 24581387 223 RLFQLFDDVLVLAH-GEVLYAG----------EQREMLPTFAQsghiCPQYYNPA 266
Cdd:PLN03140 1082 DIFEAFDELLLMKRgGQVIYSGplgrnshkiiEYFEAIPGVPK----IKEKYNPA 1132
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
51-249 |
1.45e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 130.18 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP--RDIMSFRKMSAYIAQNFVMLNLLTVEETLRVSTDLK- 127
Cdd:COG1131 24 EPGEIFGLLGPNGAGKTTTIRMLLGL-LRPTSGEVRVLGEDvaRDPAEVRRRIGYVPQEPALYPDLTVRENLRFFARLYg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 128 MPSSTAAQEKQKIIDDiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLA 207
Cdd:COG1131 103 LPRKEARERIDELLEL----FGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24581387 208 HDGRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:COG1131 179 AEGKTVLLSTHYL-EEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
35-268 |
1.92e-34 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 131.89 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 35 ATKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfKLQ---GVTGQFLLNGRPRDIMSFRKMSAYIAQNFVML 111
Cdd:PLN03140 173 AKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAG-KLDpslKVSGEITYNGYRLNEFVPRKTSAYISQNDVHV 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 112 NLLTVEETLRVST------------------------------DLKMpSSTAAQ--EKQKIIDDIIDILQLQSCRRTLV- 158
Cdd:PLN03140 252 GVMTVKETLDFSArcqgvgtrydllselarrekdagifpeaevDLFM-KATAMEgvKSSLITDYTLKILGLDICKDTIVg 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 159 ----KNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAH--DGRIVVCVVhQPGSRLFQLFDDVL 232
Cdd:PLN03140 331 demiRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHltEATVLMSLL-QPAPETFDLFDDII 409
|
250 260 270
....*....|....*....|....*....|....*.
gi 24581387 233 VLAHGEVLYAGEQREMLPTFAQSGHICPQYYNPADF 268
Cdd:PLN03140 410 LLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADF 445
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
50-247 |
7.84e-34 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 123.04 E-value: 7.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP--RDIMSFRKMSAYIAQNFVMLNLLTVEETLR-VSTDL 126
Cdd:COG4555 24 AKDGEITGLLGPNGAGKTTLLRMLAGL-LKPDSGSILIDGEDvrKEPREARRQIGVLPDERGLYDRLTVRENIRyFAELY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 127 KMPSSTAAQEKQKIIDDiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRL 206
Cdd:COG4555 103 GLFDEELKKRIEELIEL----LGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24581387 207 AHDGRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQRE 247
Cdd:COG4555 179 KKEGKTVLFSSHIM-QEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
42-268 |
1.53e-33 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 129.46 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 42 IINEACGVFKSGRLTAILGPSGAGKSTLLNALA----GFKLqGVTGQFLLNG-RPRDIMS-FRKMSAYIAQNFVMLNLLT 115
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHI-GVEGVITYDGiTPEEIKKhYRGDVVYNAETDVHFPHLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 116 VEETLRVSTDLKMPSS-----TAAQEKQKIIDDIIDILQLQSCRRTLVKN-----LSGGEHKRLSIGIELVTNPPIMFFD 185
Cdd:TIGR00956 155 VGETLDFAARCKTPQNrpdgvSREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 186 EPTSGLDCVGSYQVICHLQRLAHDGRIVVCV-VHQPGSRLFQLFDDVLVLAHGEVLYAGEQREMLPTFAQSGHICPQYYN 264
Cdd:TIGR00956 235 NATRGLDSATALEFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQT 314
|
....
gi 24581387 265 PADF 268
Cdd:TIGR00956 315 TADF 318
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
30-243 |
1.97e-31 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 115.82 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 30 YSLKGATKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGF--KLQGVTGQFLLNGRPRDIM--SFRKMSAYIA 105
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRteGNVSVEGDIHYNGIPYKEFaeKYPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 106 QNFVMLNLLTVEETLRVSTdlkmpsstaaqekqkiiddiidilqlqSCR-RTLVKNLSGGEHKRLSIGIELVTNPPIMFF 184
Cdd:cd03233 90 EEDVHFPTLTVRETLDFAL---------------------------RCKgNEFVRGISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 185 DEPTSGLDCVGSYQVICHLQRLAHDGRIVVCV-VHQPGSRLFQLFDDVLVLAHGEVLYAG 243
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
25-238 |
2.88e-30 |
|
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: 112.95 E-value: 2.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 25 FSQVSYSLKGatkGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP---RDIMSFRKMS 101
Cdd:cd03225 2 LKNLSFSYPD---GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL-LGPTSGEVLVDGKDltkLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 102 AYIAQN----FVMLnllTVEE----TLRvstDLKMPsstaAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGI 173
Cdd:cd03225 78 GLVFQNpddqFFGP---TVEEevafGLE---NLGLP----EEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581387 174 ELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPgSRLFQLFDDVLVLAHGE 238
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDL-DLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
23-249 |
1.32e-29 |
|
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: 111.66 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLKGatkgSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP---RDIMSFRK 99
Cdd:COG1122 1 IELENLSFSYPG----GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL-LKPTSGEVLVDGKDitkKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 100 MSAYIAQN---------------FVMLNL-LTVEETL-RVSTDLKMpsstaaqekqkiiddiidiLQLQSCRRTLVKNLS 162
Cdd:COG1122 76 KVGLVFQNpddqlfaptveedvaFGPENLgLPREEIReRVEEALEL-------------------VGLEHLADRPPHELS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 163 GGEHKRLSI-GIeLVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLY 241
Cdd:COG1122 137 GGQKQRVAIaGV-LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDL-DLVAELADRVIVLDDGRIVA 214
|
....*...
gi 24581387 242 AGEQREML 249
Cdd:COG1122 215 DGTPREVF 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
23-249 |
4.68e-29 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 110.90 E-value: 4.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLkgatkGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMS- 101
Cdd:COG1120 2 LEAENLSVGY-----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGL-LKPSSGEVLLDGRDLASLSRRELAr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 102 --AYIAQNFVMLNLLTVEETLRV-----STDLKMPSST---AAQEkqkiiddIIDILQLQSCRRTLVKNLSGGEHKRLSI 171
Cdd:COG1120 76 riAYVPQEPPAPFGLTVRELVALgryphLGLFGRPSAEdreAVEE-------ALERTGLEHLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 172 GIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHD-GRIVVCVVHQPgsRL-FQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDL--NLaARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
50-189 |
6.23e-29 |
|
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: 107.73 E-value: 6.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP---RDIMSFRKMSAYIAQNFVMLNLLTVEETLRVSTDL 126
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLIAGL-LSPTEGTILLDGQDltdDERKSLRKEIGYVFQDPQLFPRLTVRENLRLGLLL 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581387 127 KMPSSTAAQEKQKiidDIIDILQLQSCRRTLV----KNLSGGEHKRLSIGIELVTNPPIMFFDEPTS 189
Cdd:pfam00005 87 KGLSKREKDARAE---EALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
23-249 |
2.63e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 105.94 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLkgatkGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPrdIMSFRKMSA 102
Cdd:COG1121 7 IELENLTVSY-----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGL-LPPTSGTVRLFGKP--PRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 103 YIAQNF-VMLNL-LTVEETLRVSTDLKMP--SSTAAQEKQKiIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTN 178
Cdd:COG1121 79 YVPQRAeVDWDFpITVRDVVLMGRYGRRGlfRRPSRADREA-VDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581387 179 PPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGSrLFQLFDDVLVLAHGeVLYAGEQREML 249
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRG-LVAHGPPEEVL 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
38-243 |
4.30e-27 |
|
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: 103.67 E-value: 4.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 38 GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMS---AYIAQNFVMLNLl 114
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGL-LKPSSGEILLDGKDLASLSPKELArkiAYVPQALELLGL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 115 tveetlrvsTDLKMpsstaaqekqkiiddiidilqlqscRRtlVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCV 194
Cdd:cd03214 88 ---------AHLAD-------------------------RP--FNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24581387 195 GSYQVICHLQRLAHD-GRIVVCVVHQPGsRLFQLFDDVLVLAHGEVLYAG 243
Cdd:cd03214 132 HQIELLELLRRLARErGKTVVMVLHDLN-LAARYADRVILLKDGRIVAQG 180
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
37-247 |
8.01e-27 |
|
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: 104.12 E-value: 8.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 37 KGSTPIINEAC-GVFKsGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP--RDIMSFRKMSAYIAQNFVMLNL 113
Cdd:cd03263 12 KGTKPAVDDLSlNVYK-GEIFGLLGHNGAGKTTTLKMLTGE-LRPTSGTAYINGYSirTDRKAARQSLGYCPQFDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 114 LTVEETLRVSTDLKMPSSTAAQEKQKIIDDIidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDC 193
Cdd:cd03263 90 LTVREHLRFYARLKGLPKSEIKEEVELLLRV---LGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24581387 194 VGSYQVICHLQRLAHdGRIVVCVVHQPGSrLFQLFDDVLVLAHGEVLYAGEQRE 247
Cdd:cd03263 167 ASRRAIWDLILEVRK-GRSIILTTHSMDE-AEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
23-238 |
8.97e-26 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 99.76 E-value: 8.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLKGatkGSTPIINeacGV---FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP-RDIM--S 96
Cdd:cd03228 1 IEFKNVSFSYPG---RPKPVLK---DVsltIKPGEKVAIVGPSGSGKSTLLKLLLRL-YDPTSGEILIDGVDlRDLDleS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 97 FRKMSAYIAQNFVMLNlLTVEETLrvstdlkmpsstaaqekqkiiddiidilqlqscrrtlvknLSGGEHKRLSIGIELV 176
Cdd:cd03228 74 LRKNIAYVPQDPFLFS-GTIRENI----------------------------------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 177 TNPPIMFFDEPTSGLDCVGSYQVICHLQRLAhDGRIVVCVVHQPgsRLFQLFDDVLVLAHGE 238
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRL--STIRDADRIIVLDDGR 171
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
50-239 |
2.04e-25 |
|
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: 99.01 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP--RDIMSFRKMSAYIAQNFVMLNLLTVEETLRvstdlk 127
Cdd:cd03230 23 VEKGEIYGLLGPNGAGKTTLIKIILGL-LKPDSGEIKVLGKDikKEPEEVKRRIGYLPEEPSLYENLTVRENLK------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 128 mpsstaaqekqkiiddiidilqlqscrrtlvknLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLA 207
Cdd:cd03230 96 ---------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELK 142
|
170 180 190
....*....|....*....|....*....|..
gi 24581387 208 HDGRIVVCVVHQPgSRLFQLFDDVLVLAHGEV 239
Cdd:cd03230 143 KEGKTILLSSHIL-EEAERLCDRVAILNNGRI 173
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-249 |
2.51e-25 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 104.84 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 3 DNAVQAQPNGLGP-QKQKALELHFSQVSYSlkgaTKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGV 81
Cdd:COG4988 316 DAPEPAAPAGTAPlPAAGPPSIELEDVSFS----YPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF-LPPY 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 82 TGQFLLNGRPR---DIMSFRKMSAYIAQNFVMLNlLTVEETLRvstdLKMPSSTAAQekqkiiddiidilQLQSCRR--- 155
Cdd:COG4988 391 SGSILINGVDLsdlDPASWRRQIAWVPQNPYLFA-GTIRENLR----LGRPDASDEE-------------LEAALEAagl 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 156 ------------TLV----KNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHdGRIVVCVVHQ 219
Cdd:COG4988 453 defvaalpdgldTPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHR 531
|
250 260 270
....*....|....*....|....*....|
gi 24581387 220 PGSRlfQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:COG4988 532 LALL--AQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
24-243 |
5.57e-25 |
|
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: 99.14 E-value: 5.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 24 HFSQVSYSLkgatkGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPrdIMSFRKMSAY 103
Cdd:cd03235 1 EVEDLTVSY-----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGL-LKPTSGSIRVFGKP--LEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 104 IAQNFVMLNL--LTVEETLRVSTDLKMPSSTAAQEKQKIIDDII-DILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPP 180
Cdd:cd03235 73 VPQRRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEAlERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581387 181 IMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGSrLFQLFDDVLVLAHgEVLYAG 243
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNR-TVVASG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
50-236 |
8.04e-25 |
|
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: 98.32 E-value: 8.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP--RDIMSFRKMSAYIAQNFVMLNLLTVEETLRVSTDLK 127
Cdd:COG4133 25 LAAGEALALTGPNGSGKTTLLRILAGL-LPPSAGEVLWNGEPirDAREDYRRRLAYLGHADGLKPELTVRENLRFWAALY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 128 MPSSTAAQEKQkiiddIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDcVGSYQVIC-HLQRL 206
Cdd:COG4133 104 GLRADREAIDE-----ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD-AAGVALLAeLIAAH 177
|
170 180 190
....*....|....*....|....*....|
gi 24581387 207 AHDGRIVVCVVHQPgsrLFQLFDDVLVLAH 236
Cdd:COG4133 178 LARGGAVLLTTHQP---LELAAARVLDLGD 204
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
23-239 |
3.56e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 96.81 E-value: 3.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLkgatkGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMS---FRK 99
Cdd:COG4619 1 LELEGLSFRV-----GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADL-DPPTSGEIYLDGKPLSAMPppeWRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 100 MSAYIAQNFVMLnlltvEETlrVSTDLKMPSSTAAQE-KQKIIDDIIDILQLQ-SCRRTLVKNLSGGEHKRLSIGIELVT 177
Cdd:COG4619 75 QVAYVPQEPALW-----GGT--VRDNLPFPFQLRERKfDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581387 178 NPPIMFFDEPTSGLDCVGSYQVICHLQRL-AHDGRIVVCVVHQPGSRLfQLFDDVLVLAHGEV 239
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIE-RVADRVLTLEAGRL 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-249 |
3.99e-24 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 101.38 E-value: 3.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 2 ADNAVQAQPNGLGPQKQKALElhFSQVSYSLKGATKgstPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGV 81
Cdd:COG4987 315 APPAVTEPAEPAPAPGGPSLE--LEDVSFRYPGAGR---PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF-LDPQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 82 TGQFLLNGRP-RDIM--SFRKMSAYIAQN---FVMlnllTVEETLRV----STDLKMpssTAAQEKqkiiddiidiLQLQ 151
Cdd:COG4987 389 SGSITLGGVDlRDLDedDLRRRIAVVPQRphlFDT----TLRENLRLarpdATDEEL---WAALER----------VGLG 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 152 SCRRTLVK-----------NLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHdGRIVVCVVHQP 220
Cdd:COG4987 452 DWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRL 530
|
250 260
....*....|....*....|....*....
gi 24581387 221 gsRLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:COG4987 531 --AGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
50-238 |
7.66e-24 |
|
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: 94.62 E-value: 7.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP---RDIMSFRKMSAYIAQnfvmlnlltveetlrvstdl 126
Cdd:cd00267 22 LKAGEIVALVGPNGSGKSTLLRAIAGL-LKPTSGEILIDGKDiakLPLEELRRRIGYVPQ-------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 127 kmpsstaaqekqkiiddiidilqlqscrrtlvknLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRL 206
Cdd:cd00267 81 ----------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL 126
|
170 180 190
....*....|....*....|....*....|..
gi 24581387 207 AHDGRIVVCVVHQPgSRLFQLFDDVLVLAHGE 238
Cdd:cd00267 127 AEEGRTVIIVTHDP-ELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
32-243 |
1.35e-23 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 95.28 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 32 LKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP--------RDImsfrkms 101
Cdd:cd03259 3 LKGLSKtyGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL-ERPDSGEILIDGRDvtgvpperRNI------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 102 AYIAQNFVMLNLLTVEET----LRVstdLKMPSSTAAQEKQKIIDDIIDILQLQscRRtlVKNLSGGEHKRLSIGIELVT 177
Cdd:cd03259 75 GMVFQDYALFPHLTVAENiafgLKL---RGVPKAEIRARVRELLELVGLEGLLN--RY--PHELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581387 178 NPPIMFFDEPTSGLDCVGSYQVICHLQRLAHD-GRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAG 243
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQ-EEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
31-243 |
2.06e-23 |
|
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: 94.95 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 31 SLKGATK--GSTPIINEACGVFKSGrLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP--RDIMSFRKMSAYIAQ 106
Cdd:cd03264 2 QLENLTKryGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATL-TPPSSGTIRIDGQDvlKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 107 NFVMLNLLTVEETLRVSTDLK-MPSSTAAQEKQkiidDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFD 185
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKgIPSKEVKARVD----EVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24581387 186 EPTSGLDCVGSYQVICHLQRLAHDgRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAG 243
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGED-RIVILSTHIV-EDVESLCNQVAVLNKGKLVFEG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
23-249 |
3.56e-23 |
|
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: 98.44 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLKGatkGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKLQG--VTGQFLLNGRPRDIMSFRKM 100
Cdd:COG1123 5 LEVRDLSVRYPG---GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgrISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 101 SAYIAQNF----VMLNLLTVEETLRVSTDLKMPSSTAAQEKqkiIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELV 176
Cdd:COG1123 82 GRRIGMVFqdpmTQLNPVTVGDQIAEALENLGLSRAEARAR---VLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581387 177 TNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHD-GRIVVCVVHQPGsRLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLG-VVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
53-243 |
6.94e-23 |
|
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: 94.04 E-value: 6.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRprDImsfRKMSAY------IAQNFVMLNL---LTVEETLRV- 122
Cdd:cd03219 26 GEIHGLIGPNGAGKTTLFNLISGF-LRPTSGSVLFDGE--DI---TGLPPHeiarlgIGRTFQIPRLfpeLTVLENVMVa 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 123 ---STDLKMPSSTAAQEKQKIIDDIIDILQ---LQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGS 196
Cdd:cd03219 100 aqaRTGSGLLLARARREEREARERAEELLErvgLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEET 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24581387 197 YQVICHLQRLAHDGRIVVCVVHQPGSrLFQLFDDVLVLAHGEVLYAG 243
Cdd:cd03219 180 EELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQGRVIAEG 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
50-239 |
1.03e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 93.18 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGfkLQGVT-GQFLLNGrpRDI--MSFRKMSA-------YIAQNFVMLNLLTVEET 119
Cdd:COG1136 31 IEAGEFVAIVGPSGSGKSTLLNILGG--LDRPTsGEVLIDG--QDIssLSERELARlrrrhigFVFQFFNLLPELTALEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 120 LRVSTDLkmpSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQV 199
Cdd:COG1136 107 VALPLLL---AGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24581387 200 ICHLQRLAHD-GRIVVCVVHQPgsRLFQLFDDVLVLAHGEV 239
Cdd:COG1136 184 LELLRELNRElGTTIVMVTHDP--ELAARADRVIRLRDGRI 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
50-238 |
1.27e-22 |
|
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: 91.86 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMS-----FRKMSAYIAQNFVMLNLLTVEETLRVSt 124
Cdd:cd03229 23 IEAGEIVALLGPSGSGKSTLLRCIAGL-EEPDSGSILIDGEDLTDLEdelppLRRRIGMVFQDFALFPHLTVLENIALG- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 125 dlkmpsstaaqekqkiiddiidilqlqscrrtlvknLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQ 204
Cdd:cd03229 101 ------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLK 144
|
170 180 190
....*....|....*....|....*....|....*
gi 24581387 205 RL-AHDGRIVVCVVHQPGSrLFQLFDDVLVLAHGE 238
Cdd:cd03229 145 SLqAQLGITVVLVTHDLDE-AARLADRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
23-239 |
1.60e-22 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 92.55 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSlKGATKGSTPIINeacGV---FKSGRLTAILGPSGAGKSTLLNALAGfkLQGVT-GQFLLNGRPRDIMSFR 98
Cdd:cd03255 1 IELKNLSKT-YGGGGEKVQALK---GVslsIEKGEFVAIVGPSGSGKSTLLNILGG--LDRPTsGEVRVDGTDISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 99 KMSA-------YIAQNFVMLNLLTVEETLRVStdlKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSI 171
Cdd:cd03255 75 ELAAfrrrhigFVFQSFNLLPDLTALENVELP---LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 172 GIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHD-GRIVVCVVHQPgsRLFQLFDDVLVLAHGEV 239
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDP--ELAEYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
50-218 |
1.77e-22 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 92.32 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMSAYIAQNfVMLNLL--TVEETLRVSTDLK 127
Cdd:cd03226 23 LYAGEIIALTGKNGAGKTTLAKILAGL-IKESSGSILLNGKPIKAKERRKSIGYVMQD-VDYQLFtdSVREELLLGLKEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 128 MPSSTAAQEKQKIiddiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDcVGSYQVICHLQR-L 206
Cdd:cd03226 101 DAGNEQAETVLKD-------LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD-YKNMERVGELIReL 172
|
170
....*....|..
gi 24581387 207 AHDGRIVVCVVH 218
Cdd:cd03226 173 AAQGKAVIVITH 184
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
31-248 |
4.76e-22 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 91.79 E-value: 4.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 31 SLKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMS------FRKMSA 102
Cdd:cd03261 2 ELRGLTKsfGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGL-LRPDSGEVLIDGEDISGLSeaelyrLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 103 YIAQNFVMLNLLTVEET----LRVSTDLKMPSSTA-AQEKqkiiddiidiLQ---LQSCRRTLVKNLSGGEHKRLSIGIE 174
Cdd:cd03261 81 MLFQSGALFDSLTVFENvafpLREHTRLSEEEIREiVLEK----------LEavgLRGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24581387 175 LVTNPPIMFFDEPTSGLDCVGSYqVICHLQRLAHD--GRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQREM 248
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASG-VIDDLIRSLKKelGLTSIMVTHDL-DTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-234 |
5.75e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 95.05 E-value: 5.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 20 ALELHFSQVSYSLKGATkgstPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPR---DIMS 96
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRR----PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF-VDPTEGSIAVNGVPLadaDADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 97 FRKMSAYIAQNFVMLNlLTVEETLRVSTdlkmPSSTAAQEKQKIIDDIIDILqLQSCRRTLVK-------NLSGGEHKRL 169
Cdd:TIGR02857 394 WRDQIAWVPQHPFLFA-GTIAENIRLAR----PDASDAEIREALERAGLDEF-VAALPQGLDTpigeggaGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581387 170 SIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAhDGRIVVCVVHQPGSRLfqLFDDVLVL 234
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAA--LADRIVVL 529
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
23-243 |
9.58e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 91.33 E-value: 9.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLkgatkGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMSA 102
Cdd:COG4559 2 LEAENLSVRL-----GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGE-LTPSSGEVRLNGRPLAAWSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 103 YIAqnfVM-----LNL-LTVEETLRVStdlKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIG---- 172
Cdd:COG4559 76 RRA---VLpqhssLAFpFTVEEVVALG---RAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLArvla 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581387 173 --IELVTNPP-IMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGsrLFQLF-DDVLVLAHGEVLYAG 243
Cdd:COG4559 150 qlWEPVDGGPrWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLN--LAAQYaDRILLLHQGRLVAQG 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
50-243 |
3.53e-21 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 89.55 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNG------RPRDIMSFRKMSAYIAQNFVMLNLLTVEETL--- 120
Cdd:cd03256 24 INPGEFVALIGPSGAGKSTLLRCLNGL-VEPTSGSVLIDGtdinklKGKALRQLRRQIGMIFQQFNLIERLSVLENVlsg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 121 ---RVSTDLKMPSSTAAQEKQKiIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSY 197
Cdd:cd03256 103 rlgRRSTWRSLFGLFPKEEKQR-ALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24581387 198 QVICHLQRLA-HDGRIVVCVVHQPG-SRLFqlFDDVLVLAHGEVLYAG 243
Cdd:cd03256 182 QVMDLLKRINrEEGITVIVSLHQVDlAREY--ADRIVGLKDGRIVFDG 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
56-251 |
5.37e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 90.94 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 56 TAILGPSGAGKSTLLNALAGF-KLQGvtGQFLLNGR-------PRDIMSFRKMSAYIAQNFVMLNLLTVEETLRVSTDLK 127
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLtRPDE--GEIVLNGRtlfdsrkGIFLPPEKRRIGYVFQEARLFPHLSVRGNLRYGMKRA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 128 MPSSTAAQEKQkiiddIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLA 207
Cdd:TIGR02142 104 RPSERRISFER-----VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24581387 208 HDGRI-VVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQREMLPT 251
Cdd:TIGR02142 179 AEFGIpILYVSHSL-QEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
50-243 |
1.28e-20 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 87.55 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFKLQGvTGQFLLNGRPRDIM--SFRKMSAYIAQNfvmlNL---LTVEET--LRV 122
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQ-SGRVLINGVDVTAAppADRPVSMLFQEN----NLfahLTVEQNvgLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 123 STDLKMpsstaAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICH 202
Cdd:cd03298 96 SPGLKL-----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24581387 203 LQRL-AHDGRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAG 243
Cdd:cd03298 171 VLDLhAETKMTVLMVTHQP-EDAKRLAQRVVFLDNGRIAAQG 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
53-243 |
1.46e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 88.17 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGrpRDImsfRKMSAY-IA--------QNFVMLNLLTVEETLRVS 123
Cdd:COG0411 30 GEIVGLIGPNGAGKTTLFNLITGF-YRPTSGRILFDG--RDI---TGLPPHrIArlgiartfQNPRLFPELTVLENVLVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 124 TDLKMPSSTAAQEKQKIIDDIIDI------------LQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGL 191
Cdd:COG0411 104 AHARLGRGLLAALLRLPRARREEReareraeellerVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24581387 192 DCVGSYQVICHLQRLAHDGRIVVCVV-HQPGSrLFQLFDDVLVLAHGEVLYAG 243
Cdd:COG0411 184 NPEETEELAELIRRLRDERGITILLIeHDMDL-VMGLADRIVVLDFGRVIAEG 235
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
52-243 |
1.74e-20 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 86.97 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 52 SGRLTAILGPSGAGKSTLLNALAGfkLQGVT-GQFLLNGRP-------RDIMSFRKMSAYIAQNFVMLNLLTVEETLRVS 123
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAG--LEKPDgGTIVLNGTVlfdsrkkINLPPQQRKIGLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 124 TDLKMPSSTAAQEKQkiiddIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHL 203
Cdd:cd03297 100 LKRKRNREDRISVDE-----LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24581387 204 QRLAHDGRIVVCVVHQPGSRLFQLFDDVLVLAHGEVLYAG 243
Cdd:cd03297 175 KQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
53-249 |
2.50e-20 |
|
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: 86.72 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMS----AYIAQNFVMLNLLTVEETLRVSTDLKM 128
Cdd:cd03224 26 GEIVALLGRNGAGKTTLLKTIMGL-LPPRSGSIRFDGRDITGLPPHERAragiGYVPEGRRIFPELTVEENLLLGAYARR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 129 PSSTAAQEKQkiiddiidILQ----LQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQ 204
Cdd:cd03224 105 RAKRKARLER--------VYElfprLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24581387 205 RLAHDGRIVVcVVHQPGSRLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:cd03224 177 ELRDEGVTIL-LVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
41-249 |
3.55e-20 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 86.52 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 41 PIINEACGVFKSGRLTAILGPSGAGKSTLLNALagFKLQGVT-GQFLLNGRP-RDIM--SFRKMSAYIAQNFVMLNLlTV 116
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL--FRFYDVSsGSILIDGQDiREVTldSLRRAIGVVPQDTVLFND-TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 117 EETLRVSTdlkmPSSTAAQ--EKQKIIDDIIDILQLQSCRRTLVKN----LSGGEHKRLSIGIELVTNPPIMFFDEPTSG 190
Cdd:cd03253 92 GYNIRYGR----PDATDEEviEAAKAAQIHDKIMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581387 191 LDCVGSYQVICHLQRLAhDGRIVVCVVHqpgsRLFQLF--DDVLVLAHGEVLYAGEQREML 249
Cdd:cd03253 168 LDTHTEREIQAALRDVS-KGRTTIVIAH----RLSTIVnaDKIIVLKDGRIVERGTHEELL 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
22-257 |
9.00e-20 |
|
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: 88.74 E-value: 9.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 22 ELHFSQVSYSLKGAtkgSTPIINeacGV---FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPR---DIM 95
Cdd:COG2274 473 DIELENVSFRYPGD---SPPVLD---NIsltIKPGERVAIVGRSGSGKSTLLKLLLGL-YEPTSGRILIDGIDLrqiDPA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 96 SFRKMSAYIAQNFVML------NL------LTVEETLRVSTD-------LKMPsstaaqekqkiiddiidiLQLQscrrT 156
Cdd:COG2274 546 SLRRQIGVVLQDVFLFsgtireNItlgdpdATDEEIIEAARLaglhdfiEALP------------------MGYD----T 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 157 LV----KNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHdGRIVVCVVHQPgsRLFQLFDDVL 232
Cdd:COG2274 604 VVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL--STIRLADRII 680
|
250 260
....*....|....*....|....*
gi 24581387 233 VLAHGEVLYAGEQREMLptfAQSGH 257
Cdd:COG2274 681 VLDKGRIVEDGTHEELL---ARKGL 702
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
51-268 |
2.03e-19 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 84.69 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRprDIMSF---RKMSAYIAQNFVMLNLLTVEET----LRVS 123
Cdd:cd03299 23 ERGDYFVILGPTGSGKSVLLETIAGF-IKPDSGKILLNGK--DITNLppeKRDISYVPQNYALFPHMTVYKNiaygLKKR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 124 TDLKmpsstaaQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHL 203
Cdd:cd03299 100 KVDK-------KEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581387 204 QRLAHDGRIVVCVVHQPGSRLFQLFDDVLVLAHGEVLYAGEQREMLPTfaqsghicPQYYNPADF 268
Cdd:cd03299 173 KKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK--------PKNEFVAEF 229
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
51-239 |
2.90e-19 |
|
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: 84.09 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMS------FRKMSAYIAQN-FVMLN-LLTVE----E 118
Cdd:cd03257 29 KKGETLGLVGESGSGKSTLARAILGL-LKPTSGSIIFDGKDLLKLSrrlrkiRRKEIQMVFQDpMSSLNpRMTIGeqiaE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 119 TLRVSTDLkmpsSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQ 198
Cdd:cd03257 108 PLRIHGKL----SKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQ 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24581387 199 VICHLQRLA-----------HDGRIV--VCvvhqpgsrlfqlfDDVLVLAHGEV 239
Cdd:cd03257 184 ILDLLKKLQeelgltllfitHDLGVVakIA-------------DRVAVMYAGKI 224
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
50-218 |
6.28e-19 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 82.09 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP-----RDIMSFRKMSAYIAQN---------------FV 109
Cdd:TIGR01166 15 AERGEVLALLGANGAGKSTLLLHLNGL-LRPQSGAVLIDGEPldysrKGLLERRQRVGLVFQDpddqlfaadvdqdvaFG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 110 MLNLLTVEETL--RVSTDLKMpsstaaqekqkiiddiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEP 187
Cdd:TIGR01166 94 PLNLGLSEAEVerRVREALTA-------------------VGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 24581387 188 TSGLDCVGSYQVICHLQRLAHDGRIVVCVVH 218
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
51-239 |
7.89e-19 |
|
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: 82.46 E-value: 7.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFKLQgVTGQFLLNGRP------RDIMSFRKMSAYIAQNFVMLNLLTVEETLRVST 124
Cdd:cd03292 25 SAGEFVFLVGPSGAGKSTLLKLIYKEELP-TSGTIRVNGQDvsdlrgRAIPYLRRKIGVVFQDFRLLPDRNVYENVAFAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 125 DLkmpSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQ 204
Cdd:cd03292 104 EV---TGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLK 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 24581387 205 RLAHDGRIVVCVVHQPgsrlfQLFDD----VLVLAHGEV 239
Cdd:cd03292 181 KINKAGTTVVVATHAK-----ELVDTtrhrVIALERGKL 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
50-249 |
1.12e-18 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 82.72 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMSAyIAQNFVML-------NLLTVEE---- 118
Cdd:COG1127 28 VPRGEILAIIGGSGSGKSVLLKLIIGL-LRPDSGEILVDGQDITGLSEKELYE-LRRRIGMLfqggalfDSLTVFEnvaf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 119 TLRVSTDL-----------------------KMPSStaaqekqkiiddiidilqlqscrrtlvknLSGGEHKRLSIGIEL 175
Cdd:COG1127 106 PLREHTDLseaeirelvleklelvglpgaadKMPSE-----------------------------LSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24581387 176 VTNPPIMFFDEPTSGLDCVGSyQVICHL-QRLAHD-GRIVVCVVHQPGSrLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITS-AVIDELiRELRDElGLTSVVVTHDLDS-AFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
51-239 |
2.42e-18 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 81.04 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGfkLQGVT-GQFLLNG-----RPRDIMSFRKMSAYIAQNFVMLNLLTVEE--TLRV 122
Cdd:cd03262 24 KKGEVVVIIGPSGSGKSTLLRCINL--LEEPDsGTIIIDGlkltdDKKNINELRQKVGMVFQQFNLFPHLTVLEniTLAP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 123 STDLKMPSSTAaqekQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD--CVGsyQVI 200
Cdd:cd03262 102 IKVKGMSKAEA----EERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpeLVG--EVL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24581387 201 CHLQRLAHDGRIVVCVVHQPGsrlF--QLFDDVLVLAHGEV 239
Cdd:cd03262 176 DVMKDLAEEGMTMVVVTHEMG---FarEVADRVIFMDDGRI 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
23-243 |
2.64e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.13 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLkgatkGSTPIINeacGV---FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRK 99
Cdd:PRK13548 3 LEARNLSVRL-----GGRTLLD---DVsltLRPGEVVAILGPNGAGKSTLLRALSGE-LSPDSGEVRLNGRPLADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 100 MSAYIA---QNFVMLNLLTVEETLRVStdlKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELV 176
Cdd:PRK13548 74 LARRRAvlpQHSSLSFPFTVEEVVAMG---RAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 177 ------TNPPIMFFDEPTSGLDCvgSYQVicHLQRLAHD-----GRIVVCVVHQPGsrLFQLF-DDVLVLAHGEVLYAG 243
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDL--AHQH--HVLRLARQlaherGLAVIVVLHDLN--LAARYaDRIVLLHQGRLVADG 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
23-249 |
5.13e-18 |
|
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: 83.41 E-value: 5.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLKGATKGSTPIINeacGV---FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP------RD 93
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVRAVD---DVsltLRRGETLGLVGESGSGKSTLARLLLGL-LRPTSGSILFDGKDltklsrRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 94 IMSFRKMSAYIAQN-FVMLN-LLTVEET----LRVstdLKMPSSTAAQEKqkiiddIIDILQL----QSCRRTLVKNLSG 163
Cdd:COG1123 337 LRELRRRVQMVFQDpYSSLNpRMTVGDIiaepLRL---HGLLSRAERRER------VAELLERvglpPDLADRYPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 164 GEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRL-----------AHDGRIVvcvvhqpgsrlFQLFDDVL 232
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrelgltylfiSHDLAVV-----------RYIADRVA 476
|
250
....*....|....*..
gi 24581387 233 VLAHGEVLYAGEQREML 249
Cdd:COG1123 477 VMYDGRIVEDGPTEEVF 493
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
50-249 |
1.02e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.82 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP-----RDIMSFRKMSAYIAQN---------------FV 109
Cdd:PRK13638 24 FSLSPVTGLVGANGCGKSTLFMNLSGL-LRPQKGAVLWQGKPldyskRGLLALRQQVATVFQDpeqqifytdidsdiaFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 110 MLNLLTVEETL--RVSTDLKMpsstaaqekqkiiddiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEP 187
Cdd:PRK13638 103 LRNLGVPEAEItrRVDEALTL-------------------VDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 188 TSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDI-DLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
40-249 |
1.25e-17 |
|
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: 79.58 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 40 TPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFklQGVT-GQFLLNG---RPRDIMSFRKMSAYIAQNFVMLNLlT 115
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRF--YDVDsGRILIDGhdvRDYTLASLRRQIGLVSQDVFLFND-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 116 VEETLRVSTdlkmPSSTAAQ--EKQKIIDDIIDILQLQSCRRTLVK----NLSGGEHKRLSIGIELVTNPPIMFFDEPTS 189
Cdd:cd03251 92 VAENIAYGR----PGATREEveEAARAANAHEFIMELPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 190 GLDCVGSYQVICHLQRLAHDgRIVVCVVHqpgsRL--FQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:cd03251 168 ALDTESERLVQAALERLMKN-RTTFVIAH----RLstIENADRIVVLEDGKIVERGTHEELL 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
51-248 |
1.41e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.51 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP-----RDIMSFRKMSAYIAQN-----FVMlnllTVEETL 120
Cdd:PRK13639 26 EKGEMVALLGPNGAGKSTLFLHFNGI-LKPTSGEVLIKGEPikydkKSLLEVRKTVGIVFQNpddqlFAP----TVEEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 121 RVS-TDLKMPSstaaQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQV 199
Cdd:PRK13639 101 AFGpLNLGLSK----EEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24581387 200 ICHLQRLAHDGRIVVCVVHQpgSRLFQLF-DDVLVLAHGEVLYAGEQREM 248
Cdd:PRK13639 177 MKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEGTPKEV 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
31-192 |
2.94e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 80.50 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 31 SLKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfkLQGVT-GQFLLNGRP--------RDImsfrk 99
Cdd:COG3839 5 ELENVSKsyGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG--LEDPTsGEILIGGRDvtdlppkdRNI----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 100 msAYIAQNFVMLNLLTVEET----LRVStdlKMPsstaAQEKQKIIDDIIDILQLQSC--RRtlVKNLSGGEHKRLSIGI 173
Cdd:COG3839 78 --AMVFQSYALYPHMTVYENiafpLKLR---KVP----KAEIDRRVREAAELLGLEDLldRK--PKQLSGGQRQRVALGR 146
|
170
....*....|....*....
gi 24581387 174 ELVTNPPIMFFDEPTSGLD 192
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLD 165
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
56-249 |
3.93e-17 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 78.59 E-value: 3.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 56 TAILGPSGAGKSTLLNALAGFKLQGVTGQFLLNGRPR---DIMSFRKM----SAYIAQNFvmLNLLTVEETlrV------ 122
Cdd:COG1119 32 WAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRggeDVWELRKRiglvSPALQLRF--PRDETVLDV--Vlsgffd 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 123 STDLkMPSSTAAQEKQkiIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICH 202
Cdd:COG1119 108 SIGL-YREPTDEQRER--ARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLAL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24581387 203 LQRLAHDGRI-VVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:COG1119 185 LDKLAAEGAPtLVLVTHHV-EEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
50-249 |
5.26e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.87 E-value: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGrpRDIMSF----RKMSayiaqnfvML----NL---LTVEE 118
Cdd:COG3840 22 IAAGERVAILGPSGAGKSTLLNLIAGF-LPPDSGRILWNG--QDLTALppaeRPVS--------MLfqenNLfphLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 119 T--LRVSTDLKMpssTAAQEKQkiIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGS 196
Cdd:COG3840 91 NigLGLRPGLKL---TAEQRAQ--VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24581387 197 YQVICHLQRLAHD-GRIVVCVVHQPGSRLfQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:COG3840 166 QEMLDLVDELCRErGLTVLMVTHDPEDAA-RIADRVLLVADGRIAADGPTAALL 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
51-249 |
9.33e-17 |
|
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: 77.53 E-value: 9.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFKLQgVTGQFLLNGRPR---DIMSFRKMSAYIAQNFVMLNLlTVEETLrVSTDLK 127
Cdd:cd03252 26 KPGEVVGIVGRSGSGKSTLTKLIQRFYVP-ENGRVLVDGHDLalaDPAWLRRQVGVVLQENVLFNR-SIRDNI-ALADPG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 128 MPSSTAaQEKQKIIDDIIDILQLQSCRRTLV----KNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHL 203
Cdd:cd03252 103 MSMERV-IEAAKLAGAHDFISELPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNM 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24581387 204 QRLAhDGRIVVCVVHqpgsRLFQLF--DDVLVLAHGEVLYAGEQREML 249
Cdd:cd03252 182 HDIC-AGRTVIIIAH----RLSTVKnaDRIIVMEKGRIVEQGSHDELL 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
51-192 |
1.44e-16 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 76.36 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPrdIMSFRKMSAYIAQNFVMLNLLTVEETlrVSTDLKMpS 130
Cdd:cd03293 28 EEGEFVALVGPSGCGKSTLLRIIAGL-ERPTSGEVLVDGEP--VTGPGPDRGYVFQQDALLPWLTVLDN--VALGLEL-Q 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 131 STAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:cd03293 102 GVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALD 163
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
36-251 |
1.48e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.73 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 36 TKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFLLNGRPRDIMSFRKMSAYIA---QNFVMLN 112
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAING-TLTPTAGTVLVAGDDVEALSARAASRRVAsvpQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 113 LLTVEETLRVST-------DLKMPSSTAAQEKQKIIDDIIdilqlQSCRRTlVKNLSGGEHKRLSIGIELVTNPPIMFFD 185
Cdd:PRK09536 91 EFDVRQVVEMGRtphrsrfDTWTETDRAAVERAMERTGVA-----QFADRP-VTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24581387 186 EPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVH--QPGSRlfqLFDDVLVLAHGEVLYAGEQREMLPT 251
Cdd:PRK09536 165 EPTASLDINHQVRTLELVRRLVDDGKTAVAAIHdlDLAAR---YCDELVLLADGRVRAAGPPADVLTA 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
26-239 |
1.68e-16 |
|
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: 75.33 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 26 SQVSYSLKGAtkgSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP---RDIMSFRKMSA 102
Cdd:cd03246 4 ENVSFRYPGA---EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGL-LRPTSGRVRLDGADisqWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 103 YIAQnfvmlnlltveetlrvstDLKMPSSTAAQekqkiiddiidilqlqscrrtlvkN-LSGGEHKRLSIGIELVTNPPI 181
Cdd:cd03246 80 YLPQ------------------DDELFSGSIAE------------------------NiLSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 182 MFFDEPTSGLDCVGSyQVICH-LQRLAHDGRIVVCVVHQPgsRLFQLFDDVLVLAHGEV 239
Cdd:cd03246 118 LVLDEPNSHLDVEGE-RALNQaIAALKAAGATRIVIAHRP--ETLASADRILVLEDGRV 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
51-243 |
3.82e-16 |
|
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: 75.48 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNG-----RPRDIMsfRKMsAYIAQNFVMLNLLTVEETLRVSTD 125
Cdd:cd03266 29 KPGEVTGLLGPNGAGKTTTLRMLAGL-LEPDAGFATVDGfdvvkEPAEAR--RRL-GFVSDSTGLYDRLTARENLEYFAG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 126 L---KMPSSTAAQEKqkiiddIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICH 202
Cdd:cd03266 105 LyglKGDELTARLEE------LADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24581387 203 LQRLAHDGRIVVCVVHQPGsRLFQLFDDVLVLAHGEVLYAG 243
Cdd:cd03266 179 IRQLRALGKCILFSTHIMQ-EVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-249 |
4.41e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.43 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 17 KQKALELHFSQVSYSLKGatkgstpiINEacgVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRD--- 93
Cdd:PRK13636 7 KVEELNYNYSDGTHALKG--------INI---NIKKGEVTAILGGNGAGKSTLFQNLNGI-LKPSSGRILFDGKPIDysr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 94 --IMSFRK-------------MSAYIAQN--FVMLNLLTVEETLRVSTDLKMPSSTAAQEKQKIIDDiidilqlqscrrt 156
Cdd:PRK13636 75 kgLMKLREsvgmvfqdpdnqlFSASVYQDvsFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHC------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 157 lvknLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGSRLFQLFDDVLVLAH 236
Cdd:PRK13636 142 ----LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKE 217
|
250
....*....|...
gi 24581387 237 GEVLYAGEQREML 249
Cdd:PRK13636 218 GRVILQGNPKEVF 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
38-249 |
4.57e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.82 E-value: 4.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 38 GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMSAYIA---QNFVMLNLL 114
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARL-LTPQSGTVFLGDKPISMLSSRQLARRLAllpQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 115 TVEETL------------RVSTDLKMPSSTAAQEkqkiiddiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIM 182
Cdd:PRK11231 92 TVRELVaygrspwlslwgRLSAEDNARVNQAMEQ-----------TRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581387 183 FFDEPTSGLDCvgSYQV--ICHLQRLAHDGRIVVCVVH--QPGSRlfqLFDDVLVLAHGEVLYAGEQREML 249
Cdd:PRK11231 161 LLDEPTTYLDI--NHQVelMRLMRELNTQGKTVVTVLHdlNQASR---YCDHLVVLANGHVMAQGTPEEVM 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
51-220 |
4.64e-16 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 77.79 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP---RDIMSFRKMSAYIAQNfVMLNLLTVEETLRVS---- 123
Cdd:TIGR02868 359 PPGERVAILGPSGSGKSTLLATLAGL-LDPLQGEVTLDGVPvssLDQDEVRRRVSVCAQD-AHLFDTTVRENLRLArpda 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 124 TDLKMpssTAAQEKQKIIDDIIDilqLQSCRRTLV----KNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQV 199
Cdd:TIGR02868 437 TDEEL---WAALERVGLADWLRA---LPDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL 510
|
170 180
....*....|....*....|.
gi 24581387 200 IcHLQRLAHDGRIVVCVVHQP 220
Cdd:TIGR02868 511 L-EDLLAALSGRTVVLITHHL 530
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-249 |
5.97e-16 |
|
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: 74.95 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 22 ELHFSQVSYSLKGatkgSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP---RDIMSFR 98
Cdd:cd03254 2 EIEFENVNFSYDE----KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF-YDPQKGQILIDGIDirdISRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 99 KMSAYIAQNFVMLNlLTVEETLRVSTdlkmPSSTAAQEKQ--KIIDDIIDILQLQSCRRTLV----KNLSGGEHKRLSIG 172
Cdd:cd03254 77 SMIGVVLQDTFLFS-GTIMENIRLGR----PNATDEEVIEaaKEAGAHDFIMKLPNGYDTVLgengGNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24581387 173 IELVTNPPIMFFDEPTSGLDcVGSYQVICH-LQRLAHdGRIVVCVVHQPGSRLFQlfDDVLVLAHGEVLYAGEQREML 249
Cdd:cd03254 152 RAMLRDPKILILDEATSNID-TETEKLIQEaLEKLMK-GRTSIIIAHRLSTIKNA--DKILVLDDGKIIEEGTHDELL 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
51-248 |
6.09e-16 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 74.71 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNG-----RPRDImsfRKMSAYIAQNFVMLNLLTVEETLRVSTD 125
Cdd:cd03265 24 RRGEIFGLLGPNGAGKTTTIKMLTTL-LKPTSGRATVAGhdvvrEPREV---RRRIGIVFQDLSVDDELTGWENLYIHAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 126 LKMPSSTAAQEKqkiIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQR 205
Cdd:cd03265 100 LYGVPGAERRER---IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24581387 206 LAHDGRIVVCVVHQPGSRLFQLFDDVLVLAHGEVLYAGEQREM 248
Cdd:cd03265 177 LKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
50-192 |
1.01e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 74.74 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP-----RDImsfrkmsAYIAQNFVMLNLLTVEETLRVST 124
Cdd:COG1116 34 VAAGEFVALVGPSGCGKSTLLRLIAGL-EKPTSGEVLVDGKPvtgpgPDR-------GVVFQEPALLPWLTVLDNVALGL 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581387 125 DLKMPSSTAAQEKqkiiddIIDILQ---LQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:COG1116 106 ELRGVPKAERRER------ARELLElvgLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALD 170
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
32-249 |
1.16e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 74.36 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 32 LKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAgfKLQGVTGQFLL------NGRPRDIMSFRKMSAY 103
Cdd:PRK09493 4 FKNVSKhfGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCIN--KLEEITSGDLIvdglkvNDPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 104 IAQNFVMLNLLTVEET-----LRVSTdlkmpSSTAAQEKQKIIDDIIDILQLQScrRTLVKNLSGGEHKRLSIGIELVTN 178
Cdd:PRK09493 82 VFQQFYLFPHLTALENvmfgpLRVRG-----ASKEEAEKQARELLAKVGLAERA--HHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581387 179 PPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVH------QPGSRLfqLFDDvlvlaHGEVLYAGEQREML 249
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHeigfaeKVASRL--IFID-----KGRIAEDGDPQVLI 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
38-249 |
1.39e-15 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 74.12 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 38 GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRprDIMSF------RKMSAYIAQNFVML 111
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGL-VKPDSGKILLDGQ--DITKLpmhkraRLGIGYLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 112 NLLTVEETLRVSTDLKMPSStaaQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGL 191
Cdd:cd03218 88 RKLTVEENILAVLEIRGLSK---KEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 192 D--CVGSYQVIchLQRLAHDGRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:cd03218 165 DpiAVQDIQKI--IKILKDRGIGVLITDHNV-RETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-257 |
1.76e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.15 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 5 AVQAQPNGLGPQKQKAlELHFSQVSYSLKGATKGSTPIINEAcgvfKSGRLTAILGPSGAGKSTLLNALagfklQGV--- 81
Cdd:PRK13657 318 DVRDPPGAIDLGRVKG-AVEFDDVSFSYDNSRQGVEDVSFEA----KPGQTVAIVGPTGAGKSTLINLL-----QRVfdp 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 82 -TGQFLLNG---RPRDIMSFRKMSAYIAQNFVMLNLlTVEETLRV----STDLKMpsSTAAQEKQKIIDDIIDILQLQsc 153
Cdd:PRK13657 388 qSGRILIDGtdiRTVTRASLRRNIAVVFQDAGLFNR-SIEDNIRVgrpdATDEEM--RAAAERAQAHDFIERKPDGYD-- 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 154 rrTLV----KNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHdGRIVVCVVHqpgsRLFQL-- 227
Cdd:PRK13657 463 --TVVgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAH----RLSTVrn 535
|
250 260 270
....*....|....*....|....*....|
gi 24581387 228 FDDVLVLAHGEVLYAGEQREMLptfAQSGH 257
Cdd:PRK13657 536 ADRILVFDNGRVVESGSFDELV---ARGGR 562
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
51-243 |
2.14e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGF-----------KLQGVTGQflLNGR-PRDIMSFRKMSAYIAQNFVMLNLLTVEE 118
Cdd:PRK09984 28 HHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshiELLGRTVQ--REGRlARDIRKSRANTGYIFQQFNLVNRLSVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 119 TLRVSTDLKMP-----SSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDC 193
Cdd:PRK09984 106 NVLIGALGSTPfwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDP 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24581387 194 VGSYQVICHLQRL-AHDGRIVVCVVHQPGSRLfQLFDDVLVLAHGEVLYAG 243
Cdd:PRK09984 186 ESARIVMDTLRDInQNDGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDG 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
50-239 |
2.34e-15 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 73.68 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP---RDIMSFRKMSAYIAQN-FVMLN-LLTVEETLrvST 124
Cdd:COG1124 28 VAPGESFGLVGESGSGKSTLLRALAGL-ERPWSGEVTFDGRPvtrRRRKAFRRRVQMVFQDpYASLHpRHTVDRIL--AE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 125 DLKMPSSTAAQEKqkiiddIIDILQL----QSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVI 200
Cdd:COG1124 105 PLRIHGLPDREER------IAELLEQvglpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEIL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24581387 201 CHLQRL-----------AHDGRIV--VCvvhqpgsrlfqlfDDVLVLAHGEV 239
Cdd:COG1124 179 NLLKDLreergltylfvSHDLAVVahLC-------------DRVAVMQNGRI 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
33-247 |
2.39e-15 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 73.53 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 33 KGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKlQGVTGQFLLNGRPRDIMSFRKMS-AYIAQNFV 109
Cdd:cd03296 6 RNVSKrfGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLE-RPDSGTILFGGEDATDVPVQERNvGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 110 MLNLLTVEET----LRVSTDLKMPSstaAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFD 185
Cdd:cd03296 85 LFRHMTVFDNvafgLRVKPRSERPP---EAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581387 186 EPTSGLDCVGSYQVICHLQRLaHD--GRIVVCVVHQPGSRLfQLFDDVLVLAHGEVLYAGEQRE 247
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRL-HDelHVTTVFVTHDQEEAL-EVADRVVVMNKGRIEQVGTPDE 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
31-192 |
3.39e-15 |
|
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: 73.04 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 31 SLKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFklQGVT-GQFLLNGRP-RDIMSFRKMSAYIAQ 106
Cdd:cd03300 2 ELENVSKfyGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF--ETPTsGEILLDGKDiTNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 107 NFVMLNLLTVEETlrVSTDLKMPSSTAAQEKQKiIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDE 186
Cdd:cd03300 80 NYALFPHLTVFEN--IAFGLRLKKLPKAEIKER-VAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
....*.
gi 24581387 187 PTSGLD 192
Cdd:cd03300 157 PLGALD 162
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
51-249 |
3.83e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 72.72 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGfkLQGVT-GQFLLNGRP-----RDIMSFRKMSAYIAQNFvmlNL---LTVEE--T 119
Cdd:COG1126 25 EKGEVVVIIGPSGSGKSTLLRCINL--LEEPDsGTITVDGEDltdskKDINKLRRKVGMVFQQF---NLfphLTVLEnvT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 120 L---RVstdLKMPSSTAAQEkqkiiddiidilqlqsCRRTLVK------------NLSGGEHKRLSIGIELVTNPPIMFF 184
Cdd:COG1126 100 LapiKV---KKMSKAEAEER----------------AMELLERvgladkadaypaQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 185 DEPTSGLD--CVGS-YQVIchlQRLAHDGRIVVCVVHQPGsrlF--QLFDDVLVLAHGEVLYAGEQREML 249
Cdd:COG1126 161 DEPTSALDpeLVGEvLDVM---RDLAKEGMTMVVVTHEMG---FarEVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
51-244 |
3.90e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 72.88 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFKlQGVTGQFLLNGRPRDIMSFRKMSAYiaQNFVMLNLLTVEETLRVSTDLKMPS 130
Cdd:TIGR01184 9 QQGEFISLIGHSGCGKSTLLNLISGLA-QPTSGGVILEGKQITEPGPDRMVVF--QNYSLLPWLTVRENIALAVDRVLPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 131 STAAqEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDG 210
Cdd:TIGR01184 86 LSKS-ERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEH 164
|
170 180 190
....*....|....*....|....*....|....*
gi 24581387 211 RI-VVCVVHQPGSRLFqLFDDVLVLAHGEVLYAGE 244
Cdd:TIGR01184 165 RVtVLMVTHDVDEALL-LSDRVVMLTNGPAANIGQ 198
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
48-249 |
4.14e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.95 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 48 GVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGvTGQFLLNGRPRDIMSFRKMS---AYIAQNFVMLNLLTVEETLrvst 124
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGL-LPG-QGEILLNGRPLSDWSAAELArhrAYLSQQQSPPFAMPVFQYL---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 125 DLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIG-----IELVTNPP--IMFFDEPTSGLDcvgsy 197
Cdd:COG4138 91 ALHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAavllqVWPTINPEgqLLLLDEPMNSLD----- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 198 qvICH-------LQRLAHDGRIVVCVVHQPGSRLFQLfDDVLVLAHGEVLYAGEQREML 249
Cdd:COG4138 166 --VAQqaaldrlLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQGKLVASGETAEVM 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
51-243 |
8.00e-15 |
|
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: 71.48 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGR--PRDIMSFRKMSAYI-AQNFVMLnlLTVEETLRVSTDLK 127
Cdd:cd03268 24 KKGEIYGFLGPNGAGKTTTMKIILGL-IKPDSGEITFDGKsyQKNIEALRRIGALIeAPGFYPN--LTARENLRLLARLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 128 MPSSTAAQEkqkiiddIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLA 207
Cdd:cd03268 101 GIRKKRIDE-------VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLR 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 24581387 208 HDGRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAG 243
Cdd:cd03268 174 DQGITVLISSHLL-SEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
51-243 |
8.02e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.98 E-value: 8.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNG-RP--RDIMSFRKMSAYIAQNFVMLNLLTVEETLRVSTDL- 126
Cdd:cd03267 45 EKGEIVGFIGPNGAGKTTTLKILSGL-LQPTSGEVRVAGlVPwkRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIy 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 127 KMPSSTAAQEKQKIIDDiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRL 206
Cdd:cd03267 124 DLPPARFKKRLDELSEL----LDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEY 199
|
170 180 190
....*....|....*....|....*....|....*..
gi 24581387 207 AHDGRIVVCVVHQPGSRLFQLFDDVLVLAHGEVLYAG 243
Cdd:cd03267 200 NRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
51-220 |
1.22e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.06 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMSAYIA-QNFvMLNLLTVEETLRVSTDLKMP 129
Cdd:PRK13539 26 AAGEALVLTGPNGSGKTTLLRLIAGL-LPPAAGTIKLDGGDIDDPDVAEACHYLGhRNA-MKPALTVAENLEFWAAFLGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 130 SSTAAQEkqkiiddIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDcVGSYQVICHL--QRLA 207
Cdd:PRK13539 104 EELDIAA-------ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD-AAAVALFAELirAHLA 175
|
170
....*....|...
gi 24581387 208 HDGrIVVCVVHQP 220
Cdd:PRK13539 176 QGG-IVIAATHIP 187
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
22-249 |
1.41e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 73.62 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 22 ELHFSQVSYSLkgatkG-STPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPR---DIMSF 97
Cdd:TIGR01193 473 DIVINDVSYSY-----GyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGF-FQARSGEILLNGFSLkdiDRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 98 RKMSAYIAQNFVML------NLL-------TVEETLRV------STDL-KMPsstaaqekqkiiddiidiLQLQSCRRTL 157
Cdd:TIGR01193 547 RQFINYLPQEPYIFsgsileNLLlgakenvSQDEIWAAceiaeiKDDIeNMP------------------LGYQTELSEE 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 158 VKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHdgRIVVCVVHqpgsRL--FQLFDDVLVLA 235
Cdd:TIGR01193 609 GSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAH----RLsvAKQSDKIIVLD 682
|
250
....*....|....
gi 24581387 236 HGEVLYAGEQREML 249
Cdd:TIGR01193 683 HGKIIEQGSHDELL 696
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
51-192 |
1.59e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.15 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIM--SFRKMSAYIAQNfvmlNL---LTVEETLRVSTD 125
Cdd:PRK10771 23 ERGERVAILGPSGAGKSTLLNLIAGF-LTPASGSLTLNGQDHTTTppSRRPVSMLFQEN----NLfshLTVAQNIGLGLN 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 126 --LKMpssTAAQEKQkiIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:PRK10771 98 pgLKL---NAAQREK--LHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
29-219 |
1.80e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 71.20 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 29 SYSLKGATK--GSTPI---INEACgvfKSGRLTAILGPSGAGKSTLLNAL-------AGfKLQGVTGQFLLNGRP--RDI 94
Cdd:COG4161 2 SIQLKNINCfyGSHQAlfdINLEC---PSGETLVLLGPSGAGKSSLLRVLnlletpdSG-QLNIAGHQFDFSQKPseKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 95 MSFRKMSAYIAQNF-------VMLNLltVEETLRVstdLKMPSSTAAQEKQKIIDDiidiLQLQSCRRTLVKNLSGGEHK 167
Cdd:COG4161 78 RLLRQKVGMVFQQYnlwphltVMENL--IEAPCKV---LGLSKEQAREKAMKLLAR----LRLTDKADRFPLHLSGGQQQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24581387 168 RLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQ 219
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-239 |
2.13e-14 |
|
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: 70.31 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 22 ELHFSQVSYSLKGATKGSTPIINEAcgvFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNG------RPRDIm 95
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLT---IRAGEKVAIIGRVGSGKSTLLKLLAGL-YKPTSGSVLLDGtdirqlDPADL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 96 sfRKMSAYIAQNFVMLNlltveETLRVSTDLKMPSST-----AAQEK---QKIIDDIIDILQLQSCRRTlvKNLSGGEHK 167
Cdd:cd03245 77 --RRNIGYVPQDVTLFY-----GTLRDNITLGAPLADderilRAAELagvTDFVNKHPNGLDLQIGERG--RGLSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 168 RLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDgRIVVCVVHQPgsRLFQLFDDVLVLAHGEV 239
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD-KTLIIITHRP--SLLDLVDRIIVMDSGRI 216
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
51-203 |
2.86e-14 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 70.38 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMS----AYIAQNFVMLNLLTVEETLRVSTDL 126
Cdd:TIGR04406 25 KSGEIVGLLGPNGAGKTTSFYMIVGL-VRPDAGKILIDGQDITHLPMHERArlgiGYLPQEASIFRKLTVEENIMAVLEI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 127 kMPSSTAAQEKQKIIDDIIDiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD--CVGSYQ-VICHL 203
Cdd:TIGR04406 104 -RKDLDRAEREERLEALLEE-FQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiAVGDIKkIIKHL 181
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-239 |
2.95e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 72.50 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 8 AQPNGLGPQKQKALELHFSQVSYSLKGatkgSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGF-KLQGvtGQFL 86
Cdd:COG1132 325 PDPPGAVPLPPVRGEIEFENVSFSYPG----DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFyDPTS--GRIL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 87 LNGRP-RDI--MSFRKMSAYIAQNFVMLNlLTVEETLRvstdLKMPSSTAAQekqkiiddiidiLQlQSCRR-------- 155
Cdd:COG1132 399 IDGVDiRDLtlESLRRQIGVVPQDTFLFS-GTIRENIR----YGRPDATDEE------------VE-EAAKAaqahefie 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 156 -------TLV----KNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHdGRIVVCVVHqpgsRL 224
Cdd:COG1132 461 alpdgydTVVgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAH----RL 535
|
250
....*....|....*..
gi 24581387 225 --FQLFDDVLVLAHGEV 239
Cdd:COG1132 536 stIRNADRILVLDDGRI 552
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-264 |
4.04e-14 |
|
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: 69.88 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 24 HFSQVSYSLkgATKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNG---RPRDIMSFRKM 100
Cdd:cd03249 2 EFKNVSFRY--PSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERF-YDPTSGEILLDGvdiRDLNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 101 SAYIAQNFVMLNLlTVEETLRvstdLKMPSSTAAQEKQ--KIIDDIIDILQLQSCRRTLV----KNLSGGEHKRLSIGIE 174
Cdd:cd03249 79 IGLVSQEPVLFDG-TIAENIR----YGKPDATDEEVEEaaKKANIHDFIMSLPDGYDTLVgergSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 175 LVTNPPIMFFDEPTSGLDCVGSYQVICHLQRlAHDGRIVVCVVHqpgsRL--FQLFDDVLVLAHGEVLYAGEQREMLptf 252
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDR-AMKGRTTIVIAH----RLstIRNADLIAVLQNGQVVEQGTHDELM--- 225
|
250
....*....|..
gi 24581387 253 AQSGHicpqYYN 264
Cdd:cd03249 226 AQKGV----YAK 233
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
51-249 |
4.63e-14 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 69.92 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGfkLQGVT-GQFLLNGR------PRDIMSFRKMSAYIAQNFVMLNLLTVEETlrVS 123
Cdd:cd03258 29 PKGEIFGIIGRSGAGKSTLIRCING--LERPTsGSVLVDGTdltllsGKELRKARRRIGMIFQHFNLLSSRTVFEN--VA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 124 TDLKMpsstAAQEKQKIIDDIIDILQ---LQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVI 200
Cdd:cd03258 105 LPLEI----AGVPKAEIEERVLELLElvgLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSIL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24581387 201 CHLQRLAHDGRI-VVCVVHQPGSrLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:cd03258 181 ALLRDINRELGLtIVLITHEMEV-VKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
31-243 |
5.77e-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: 69.23 E-value: 5.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 31 SLKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMsAYIAQNF 108
Cdd:cd03269 2 EVENVTKrfGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGI-ILPDSGEVLFDGKPLDIAARNRI-GYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 109 VMLNLLTVEETLRVSTDLK-MPSSTAAQEkqkiIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEP 187
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLKgLKKEEARRR----IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24581387 188 TSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGSrLFQLFDDVLVLAHGEVLYAG 243
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMEL-VEELCDRVLLLNKGRAVLYG 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
50-218 |
5.88e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.20 E-value: 5.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALaGFKLQGVTGQFLLNGRPR---DIMSFRKMSAYIAQNFVMLNLLTVEETLRVStdl 126
Cdd:PRK10575 34 FPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQPLeswSSKAFARKVAYLPQQLPAAEGMTVRELVAIG--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 127 KMPSSTA----AQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICH 202
Cdd:PRK10575 110 RYPWHGAlgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLAL 189
|
170
....*....|....*..
gi 24581387 203 LQRLAHD-GRIVVCVVH 218
Cdd:PRK10575 190 VHRLSQErGLTVIAVLH 206
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-220 |
6.38e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 68.67 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 25 FSQVSYSLKgatkgstpiineacgvfkSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIM--SFRKMSA 102
Cdd:cd03231 16 FSGLSFTLA------------------AGEALQVTGPNGSGKTTLLRILAGL-SPPLAGRVLLNGGPLDFQrdSIARGLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 103 YIAQNFVMLNLLTVEETLRVSTDLkmpSSTAAQEKqkiiddIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIM 182
Cdd:cd03231 77 YLGHAPGIKTTLSVLENLRFWHAD---HSDEQVEE------ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLW 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 24581387 183 FFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQP 220
Cdd:cd03231 148 ILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
53-249 |
7.58e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 69.24 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGrpRDImsfRKMSAY-IAQN---FVM-----LNLLTVEETLRVS 123
Cdd:COG0410 29 GEIVALLGRNGAGKTTLLKAISGL-LPPRSGSIRFDG--EDI---TGLPPHrIARLgigYVPegrriFPSLTVEENLLLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 124 TDLKMPSSTAAQEKQKiiddiidILQ----LQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGL-----Dcv 194
Cdd:COG0410 103 AYARRDRAEVRADLER-------VYElfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLaplivE-- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24581387 195 gsyQVICHLQRLAHDGRIVVcVVHQPGSRLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:COG0410 174 ---EIFEIIRRLNREGVTIL-LVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
50-248 |
1.05e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 69.45 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLT--AILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP---RDIMSFRKMSAYIAQN---------------FV 109
Cdd:PRK13652 25 FIAPRNSriAVIGPNGAGKSTLFRHFNGI-LKPTSGSVLIRGEPitkENIREVRKFVGLVFQNpddqifsptveqdiaFG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 110 MLNLLTVEETL--RVSTDLKMpsstaaqekqkiiddiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEP 187
Cdd:PRK13652 104 PINLGLDEETVahRVSSALHM-------------------LGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 188 TSGLDCVGSYQVICHLQRLAHD-GRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQREM 248
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQL-DLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
51-248 |
1.16e-13 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 69.73 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNG----------RPRDIMSFRKMSAYIAqnfvmlnlLTVEETL 120
Cdd:TIGR01188 17 REGEVFGFLGPNGAGKTTTIRMLTTL-LRPTSGTARVAGydvvreprkvRRSIGIVPQYASVDED--------LTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 121 RVSTDLK-MPSStaaqEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDcVGSYQV 199
Cdd:TIGR01188 88 EMMGRLYgLPKD----EAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD-PRTRRA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24581387 200 ICHLQRLAHDGRIVVCVVHQPGSRLFQLFDDVLVLAHGEVLYAGEQREM 248
Cdd:TIGR01188 163 IWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
37-220 |
1.82e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 67.38 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 37 KGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP--RDIMSFRKMSAYIAQNFVMLNLL 114
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGL-LRPDSGEVRWNGTPlaEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 115 TVEETLRVSTDLkmpsstaAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCV 194
Cdd:TIGR01189 89 SALENLHFWAAI-------HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*.
gi 24581387 195 GSYQVICHLQRLAHDGRIVVCVVHQP 220
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
50-247 |
2.21e-13 |
|
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: 67.59 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGF----KLQGVTGQFLLNGRPR-----DIMSFRKMSAYIAQNFVMLNLlTVEETL 120
Cdd:cd03260 23 IPKGEITALIGPSGCGKSTLLRLLNRLndliPGAPDEGEVLLDGKDIydldvDVLELRRRVGMVFQKPNPFPG-SIYDNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 121 RVSTDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVgSYQVI 200
Cdd:cd03260 102 AYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPI-STAKI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24581387 201 CHL-QRLAHDGRIVVcVVH--QPGSRlfqLFDDVLVLAHGEVLYAGEQRE 247
Cdd:cd03260 181 EELiAELKKEYTIVI-VTHnmQQAAR---VADRTAFLLNGRLVEFGPTEQ 226
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
38-243 |
2.31e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.17 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 38 GSTPIINeacGV---FKSGRLTAILGPSGAGKSTLLNALAGFKLQGVT-GQFLLNGRprDI--------------MSFrk 99
Cdd:COG0396 11 EGKEILK---GVnltIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTsGSILLDGE--DIlelspderaragifLAF-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 100 msayiaQNFVMLNLLTVEETLRVSTDLKMPSSTAAQEKQKIIDDIIDILQLQS--CRRTLVKNLSGGEHKRLSIGIELVT 177
Cdd:COG0396 84 ------QYPVEIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEdfLDRYVNEGFSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 178 NPPIMFFDEPTSGLDcVGSYQVICH-LQRLAHDGRIVVCVVHQPgsRLFQLF--DDVLVLAHGEVLYAG 243
Cdd:COG0396 158 EPKLAILDETDSGLD-IDALRIVAEgVNKLRSPDRGILIITHYQ--RILDYIkpDFVHVLVDGRIVKSG 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
15-249 |
2.95e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 68.09 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 15 PQKQKALElhFSQVSYSLkgaTKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAG-FKLQGvtGQFLLNG---R 90
Cdd:PRK13632 2 KNKSVMIK--VENVSFSY---PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGlLKPQS--GEIKIDGitiS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 91 PRDIMSFRKMSAYIAQN----FVMLnllTVEETLRVSTDLKMPSStaaQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEH 166
Cdd:PRK13632 75 KENLKEIRKKIGIIFQNpdnqFIGA---TVEDDIAFGLENKKVPP---KKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 167 KRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDG-RIVVCVVHQPGSRLfqLFDDVLVLAHGEVLYAGEQ 245
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI--LADKVIVFSEGKLIAQGKP 226
|
....
gi 24581387 246 REML 249
Cdd:PRK13632 227 KEIL 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
28-249 |
3.91e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.11 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 28 VSYSLKGATKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKL----QGVTGQFLLNGRPRDIMSFRKMSAY 103
Cdd:PRK13645 12 VSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIIsetgQTIVGDYAIPANLKKIKEVKRLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 104 IAQNFVMLNLLTVEETlrVSTDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVK----NLSGGEHKRLSIGIELVTNP 179
Cdd:PRK13645 92 IGLVFQFPEYQLFQET--IEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581387 180 PIMFFDEPTSGLDCVGSYQVICHLQRLAHD-GRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNM-DQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
32-239 |
4.66e-13 |
|
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: 66.51 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 32 LKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfkLQGVT-GQFLLNGR--------PRDI-MSFrk 99
Cdd:cd03301 3 LENVTKrfGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG--LEEPTsGRIYIGGRdvtdlppkDRDIaMVF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 100 msayiaQNFVMLNLLTVEETLRVStdLKMPSSTAAQEKQKIIDDIIDiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNP 179
Cdd:cd03301 79 ------QNYALYPHMTVYDNIAFG--LKLRKVPKDEIDERVREVAEL-LQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581387 180 PIMFFDEPTSGLDCVGSYQVICHLQRLAHD-GRIVVCVVHQPGSRLfQLFDDVLVLAHGEV 239
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAM-TMADRIAVMNDGQI 209
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
50-249 |
5.85e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGvTGQFLLNGRPRDIMSFRKMS---AYIAQNFVMLNLLTVEETLrvstDL 126
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPG-SGSIQFAGQPLEAWSAAELArhrAYLSQQQTPPFAMPVFQYL----TL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 127 KMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKR-------LSIGIELVTNPPIMFFDEPTSGLDC---VGS 196
Cdd:PRK03695 93 HQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLDVaqqAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24581387 197 YQVICHLQRLahdGRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:PRK03695 173 DRLLSELCQQ---GIAVVMSSHDL-NHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
23-243 |
9.91e-13 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 65.03 E-value: 9.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLKGAtkgSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFLLNGRPrdimsfrkmsa 102
Cdd:cd03247 1 LSINNVSFSYPEQ---EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG-DLKPQQGEITLDGVP----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 103 yiaqnfvmlnLLTVEETLRvstdlkmpsSTAAQEKQKIIddiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIM 182
Cdd:cd03247 66 ----------VSDLEKALS---------SLISVLNQRPY------LFDTTLRNNLGRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581387 183 FFDEPTSGLDCVGSYQVICHLQRLAHDgRIVVCVVHqpgsRLFQL--FDDVLVLAHGEVLYAG 243
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITH----HLTGIehMDKILFLENGKIIMQG 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
58-239 |
1.03e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.84 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 58 ILGPSGAGKSTLLNALAGfKLQGVTGQFLLNGRPRDIMSFRKMSAY------IAQNFVMLNLLTVEE----TLRVstdLK 127
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYG-EERPTSGQVLVNGQDLSRLKRREIPYLrrrigvVFQDFRLLPDRTVYEnvalPLRV---TG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 128 MPSSTAAQ------EKqkiiddiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVIC 201
Cdd:COG2884 109 KSRKEIRRrvrevlDL----------VGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIME 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24581387 202 HLQRLAHDGRIVVCVVHQPgsrlfQLFDD----VLVLAHGEV 239
Cdd:COG2884 179 LLEEINRRGTTVLIATHDL-----ELVDRmpkrVLELEDGRL 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
41-243 |
1.10e-12 |
|
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: 68.12 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 41 PIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGR--PRDIMSFRKMSAYIAQNFVMLNLLTVEE 118
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGL-LPPTSGTVLVGGKdiETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 119 TLRVSTDLKMPSSTAAQEKQKIIDDIIDilqLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVgSYQ 198
Cdd:TIGR01257 1023 HILFYAQLKGRSWEEAQLEMEAMLEDTG---LHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY-SRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24581387 199 VICHLQRLAHDGRIVVCVVHQPGSRLFqLFDDVLVLAHGEVLYAG 243
Cdd:TIGR01257 1099 SIWDLLLKYRSGRTIIMSTHHMDEADL-LGDRIAIISQGRLYCSG 1142
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-249 |
1.15e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.55 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLKGATkgstPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNG----RPRDIMSFR 98
Cdd:PRK13644 2 IRLENVSYSYPDGT----PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGL-LRPQKGKVLVSGidtgDFSKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 99 KMSAYIAQN----FVMLnllTVEETLRVSTD-LKMPSStaaqEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGI 173
Cdd:PRK13644 77 KLVGIVFQNpetqFVGR---TVEEDLAFGPEnLCLPPI----EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24581387 174 ELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGSrlFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE--LHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
52-249 |
1.67e-12 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 66.66 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 52 SGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP--------------RDImsfrkmsAYIAQNFVMLNLLTVE 117
Cdd:COG4148 24 GRGVTALFGPSGSGKTTLLRAIAGL-ERPDSGRIRLGGEVlqdsargiflpphrRRI-------GYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 118 ETLRVStdlkmpsstaaqekQKIIDDIIDILQLQS-----------CRRTLvkNLSGGEHKRLSIGIELVTNPPIMFFDE 186
Cdd:COG4148 96 GNLLYG--------------RKRAPRAERRISFDEvvellgighllDRRPA--TLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581387 187 PTSGLDCVGSYQVICHLQRLAHDGRI-VVCVVHQPGsRLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDELDIpILYVSHSLD-EVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-249 |
1.75e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.16 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 6 VQAQP----NGLGPQKQKALELHFSQVSYSLKGATkgsTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGV 81
Cdd:PRK11160 318 TEQKPevtfPTTSTAAADQVSLTLNNVSFTYPDQP---QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRA-WDPQ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 82 TGQFLLNGRPrdIMSF-----RKMSAYIAQNFVMLNlltveETLRvsTDLKMPSSTAAQEKqkiiddIIDILQlQSCRRT 156
Cdd:PRK11160 394 QGEILLNGQP--IADYseaalRQAISVVSQRVHLFS-----ATLR--DNLLLAAPNASDEA------LIEVLQ-QVGLEK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 157 LVKN--------------LSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAhDGRIVVCVVHqpgs 222
Cdd:PRK11160 458 LLEDdkglnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITH---- 532
|
250 260
....*....|....*....|....*....
gi 24581387 223 RLFQL--FDDVLVLAHGEVLYAGEQREML 249
Cdd:PRK11160 533 RLTGLeqFDRICVMDNGQIIEQGTHQELL 561
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
29-248 |
1.96e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.59 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 29 SYSLKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfkLQGVTGQFLLNGRPR--DIMSFRKMSAYI 104
Cdd:PRK11000 3 SVTLRNVTKayGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG--LEDITSGDLFIGEKRmnDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 105 AQNFVMLNLLTVEETLrvSTDLKMpSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFF 184
Cdd:PRK11000 81 FQSYALYPHLSVAENM--SFGLKL-AGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24581387 185 DEPTSGLDCVGSYQVICHLQRLaHD--GRIVVCVVHQPGSRLfQLFDDVLVLAHGEVLYAGEQREM 248
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRL-HKrlGRTMIYVTHDQVEAM-TLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-239 |
2.16e-12 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 65.18 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 13 LGPQKQKALeLHFSQVSYSLKgaTKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGF-KLQGvtGQFLLNGRP 91
Cdd:cd03248 3 LAPDHLKGI-VKFQNVTFAYP--TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFyQPQG--GQVLLDGKP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 92 ---RDIMSFRKMSAYIAQNFVMLNLLTVEETLRVSTDLKMPSSTAAQEKQKIIDDIIdilQLQSCRRTLV----KNLSGG 164
Cdd:cd03248 78 isqYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFIS---ELASGYDTEVgekgSQLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581387 165 EHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRlAHDGRIVVCVVHQpgSRLFQLFDDVLVLAHGEV 239
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHR--LSTVERADQILVLDGGRI 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
50-192 |
2.33e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 66.32 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGR-------PRDimsfRKMsAYIAQNFVMLNLLTVEE---- 118
Cdd:COG1118 25 IASGELVALLGPSGSGKTTLLRIIAGL-ETPDSGRIVLNGRdlftnlpPRE----RRV-GFVFQHYALFPHMTVAEniaf 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581387 119 TLRVstdlKMPSSTAAQEKqkiIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:COG1118 99 GLRV----RPPSKAEIRAR---VEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
31-192 |
3.00e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 65.89 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 31 SLKGATK--GSTPIINeacGV---FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP--------RDImsf 97
Cdd:COG3842 7 ELENVSKryGDVTALD---DVslsIEPGEFVALLGPSGCGKTTLLRMIAGF-ETPDSGRILLDGRDvtglppekRNV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 98 rkmsAYIAQNFVMLNLLTVEET----LRVstdLKMPsstaAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGI 173
Cdd:COG3842 80 ----GMVFQDYALFPHLTVAENvafgLRM---RGVP----KAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALAR 148
|
170
....*....|....*....
gi 24581387 174 ELVTNPPIMFFDEPTSGLD 192
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALD 167
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
38-220 |
3.96e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.41 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 38 GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRdimsfrkmSAYIAQNFVMLNLL--T 115
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGV-LRPTSGTVRRAGGAR--------VAYVPQRSEVPDSLplT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 116 VEET-----------LRVSTDLKMPSSTAAQEKqkiiddiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFF 184
Cdd:NF040873 74 VRDLvamgrwarrglWRRLTRDDRAAVDDALER----------VGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190
....*....|....*....|....*....|....*.
gi 24581387 185 DEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQP 220
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
51-249 |
4.37e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.39 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNAL-------AGFKLQG---VTGQFLLNGRPRDIMSFRKMSAYIAQNFVMLNLLTVEETL 120
Cdd:PRK11264 27 KPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRVGditIDTARSLSQQKGLIRQLRQHVGFVFQNFNLFPHRTVLENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 121 rvstdLKMPSSTAAQEKQKIIDDIIDILQ---LQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD--CVG 195
Cdd:PRK11264 107 -----IEGPVIVKGEPKEEATARARELLAkvgLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpeLVG 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24581387 196 syQVICHLQRLAHDGRIVVCVVHQPG-SRlfQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:PRK11264 182 --EVLNTIRQLAQEKRTMVIVTHEMSfAR--DVADRAIFMDQGRIVEQGPAKALF 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
50-258 |
4.40e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 65.26 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGF---------------KLQGVTGQFLLNGRPRDIMSFRKMSAYIAQNFVMLNLL 114
Cdd:PRK13631 49 FEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvgdiyiGDKKNNHELITNPYSKKIKNFKELRRRVSMVFQFPEYQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 115 TVEETlrVSTDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVK----NLSGGEHKRLSIGIELVTNPPIMFFDEPTSG 190
Cdd:PRK13631 129 LFKDT--IEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLErspfGLSGGQKRRVAIAGILAIQPEILIFDEPTAG 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 191 LDCVGSYQVICHLQRLAHDGRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQRE--MLPTFAQSGHI 258
Cdd:PRK13631 207 LDPKGEHEMMQLILDAKANNKTVFVITHTM-EHVLEVADEVIVMDKGKILKTGTPYEifTDQHIINSTSI 275
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
43-219 |
5.97e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.88 E-value: 5.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 43 INEACgvfKSGRLTAILGPSGAGKSTLLNAL-------AGfKLQGVTGQFLLNGRP--RDIMSFRKMSAYIAQNF----- 108
Cdd:PRK11124 21 ITLDC---PQGETLVLLGPSGAGKSSLLRVLnllemprSG-TLNIAGNHFDFSKTPsdKAIRELRRNVGMVFQQYnlwph 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 109 --VMLNLltVEETLRVstdLKMPSSTAAQEKQKIIDDiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDE 186
Cdd:PRK11124 97 ltVQQNL--IEAPCRV---LGLSKDQALARAEKLLER----LRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190
....*....|....*....|....*....|...
gi 24581387 187 PTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQ 219
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
52-219 |
7.21e-12 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 63.50 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 52 SGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFLLNGRPRDIMSF-------RKMSAYIAQNFVMLNLlTVEETLRVST 124
Cdd:cd03290 26 TGQLTMIVGQVGCGKSSLLLAILG-EMQTLEGKVHWSNKNESEPSFeatrsrnRYSVAYAAQKPWLLNA-TVEENITFGS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 125 DL---KMPSSTAAQEKQKIIDDIIDILQLQSCRRTLvkNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVIC 201
Cdd:cd03290 104 PFnkqRYKAVTDACSLQPDIDLLPFGDQTEIGERGI--NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQ 181
|
170 180
....*....|....*....|
gi 24581387 202 H--LQRLAHDGRIVVCVVHQ 219
Cdd:cd03290 182 EgiLKFLQDDKRTLVLVTHK 201
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
31-218 |
7.48e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.95 E-value: 7.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 31 SLKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAgfKLQGV-TGQFLLNGrpRDIMSF------RKMS 101
Cdd:COG4604 3 EIKNVSKryGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS--RLLPPdSGEVLVDG--LDVATTpsrelaKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 102 AYIAQNFVMLNlLTVEEtlrvstdLKM----PSS----TAaqEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGI 173
Cdd:COG4604 79 ILRQENHINSR-LTVRE-------LVAfgrfPYSkgrlTA--EDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24581387 174 ELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHD-GRIVVCVVH 218
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLH 194
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
51-257 |
1.19e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 63.18 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFKLQGVT---GQFLLNGRPRDIMSFR-KMSAYIAQN----FVMLNLLT--VEETL 120
Cdd:PRK10418 27 QRGRVLALVGGSGSGKSLTCAAALGILPAGVRqtaGRVLLDGKPVAPCALRgRKIATIMQNprsaFNPLHTMHthARETC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 121 RV----STDLKMPSSTAAqekqkiiddiidiLQLQSCRRTLVK---NLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDC 193
Cdd:PRK10418 107 LAlgkpADDATLTAALEA-------------VGLENAARVLKLypfEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581387 194 VGSYQVICHLQRLAHD-GRIVVCVVHQPGSrLFQLFDDVLVLAHGEVLyagEQREMLPTFAQSGH 257
Cdd:PRK10418 174 VAQARILDLLESIVQKrALGMLLVTHDMGV-VARLADDVAVMSHGRIV---EQGDVETLFNAPKH 234
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
31-214 |
1.39e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.20 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 31 SLKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKlQGVTGQFLLNGrpRDIMSF----RKMSAyI 104
Cdd:PRK09452 16 ELRGISKsfDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFE-TPDSGRIMLDG--QDITHVpaenRHVNT-V 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 105 AQNFVMLNLLTVEETlrVSTDLKMpSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFF 184
Cdd:PRK09452 92 FQSYALFPHMTVFEN--VAFGLRM-QKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24581387 185 DEPTSGLDcvgsYQV-------ICHLQR--------LAHD--------GRIVV 214
Cdd:PRK09452 169 DESLSALD----YKLrkqmqneLKALQRklgitfvfVTHDqeealtmsDRIVV 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
49-192 |
2.00e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.10 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 49 VFKSGRLTAILGPSGAGKSTLLNALAGFKlQGVTGQFLLNGRPRDIMSFRKMSAYIAQN--FVMLNLLTVEeTLRVSTDL 126
Cdd:PRK10584 32 VVKRGETIALIGESGSGKSTLLAILAGLD-DGSSGEVSLVGQPLHQMDEEARAKLRAKHvgFVFQSFMLIP-TLNALENV 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 127 KMPSS-TAAQEKQKIIDDIIDILQLQSCRRT--LVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:PRK10584 110 ELPALlRGESSRQSRNGAKALLEQLGLGKRLdhLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
51-219 |
2.04e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.68 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALaGFKLQGVTGQFLLNG------RPRD----------IMSFRKMSAYIAQNFVMLNLL 114
Cdd:PRK10619 29 NAGDVISIIGSSGSGKSTFLRCI-NFLEKPSEGSIVVNGqtinlvRDKDgqlkvadknqLRLLRTRLTMVFQHFNLWSHM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 115 TVEETLrVSTDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCV 194
Cdd:PRK10619 108 TVLENV-MEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE 186
|
170 180
....*....|....*....|....*
gi 24581387 195 GSYQVICHLQRLAHDGRIVVCVVHQ 219
Cdd:PRK10619 187 LVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
49-275 |
2.06e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 62.77 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 49 VFKSGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFLLNGRPRDIMSFRKMSAYiaQNFvmlnlLT--VEETLRVS--- 123
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAG-KLKPNLGKFDDPPDWDEILDEFRGSEL--QNY-----FTklLEGDVKVIvkp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 124 --TDLkMPSS---------TAAQEKQKIIDDIIDiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:cd03236 94 qyVDL-IPKAvkgkvgellKKKDERGKLDELVDQ-LELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 193 CVGSYQVICHLQRLAHDGRIVVCVVHqpgsrlfqlfdDVLVLahgevlyageqrEMLptfaqSGHICPQYYNPADFGI-- 270
Cdd:cd03236 172 IKQRLNAARLIRELAEDDNYVLVVEH-----------DLAVL------------DYL-----SDYIHCLYGEPGAYGVvt 223
|
....*.
gi 24581387 271 -PGSVQ 275
Cdd:cd03236 224 lPKSVR 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
38-205 |
2.28e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.18 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 38 GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKLQGvTGQFLLNGRPRDIMSFR-KMSAYIAQNFVMLNLLTV 116
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT-SGHIRFHGTDVSRLHARdRKVGFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 117 EET----LRVSTDLKMPSSTAAQEKqkiIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:PRK10851 92 FDNiafgLTVLPRRERPNAAAIKAK---VTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170
....*....|...
gi 24581387 193 CvgsyQVICHLQR 205
Cdd:PRK10851 169 A----QVRKELRR 177
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
53-249 |
2.46e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGfKLQG--------VTGQFLLNGRPR---DIMSFRKMSAYIAQNFVMLNLLTVEETLR 121
Cdd:PRK13547 27 GRVTALLGRNGAGKSTLLKALAG-DLTGggaprgarVTGDVTLNGEPLaaiDAPRLARLRAVLPQAAQPAFAFSAREIVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 122 VStdlKMPSSTAAQEKQKIIDDIIDILQLQSCRRTL----VKNLSGGEHKRLSIGIEL---------VTNPPIMFFDEPT 188
Cdd:PRK13547 106 LG---RYPHARRAGALTHRDGEIAWQALALAGATALvgrdVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 189 SGLDCVGSYQVICHLQRLAHDGRI-VVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:PRK13547 183 AALDLAHQHRLLDTVRRLARDWNLgVLAIVHDP-NLAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
23-240 |
2.73e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSyslkgATKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFLLNGRprDIMSF----- 97
Cdd:PRK11614 6 LSFDKVS-----AHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-DPRATSGRIVFDGK--DITDWqtaki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 98 -RKMSAYIAQNFVMLNLLTVEETLRVSTDLkmpsSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELV 176
Cdd:PRK11614 78 mREAVAIVPEGRRVFSRMTVEENLAMGGFF----AERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581387 177 TNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGrIVVCVVHQPGSRLFQLFDDVLVLAHGEVL 240
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQG-MTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-283 |
3.65e-11 |
|
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: 63.49 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 14 GPQKQKALELHFSQVSYSlkgatKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFLLNGRP-- 91
Cdd:TIGR01257 1931 GGNKTDILRLNELTKVYS-----GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG-DTTVTSGDATVAGKSil 2004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 92 RDIMSFRKMSAYIAQNFVMLNLLTVEETLRVSTDLKmpsSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSI 171
Cdd:TIGR01257 2005 TNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLR---GVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLST 2081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 172 GIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQREMLPT 251
Cdd:TIGR01257 2082 AIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSM-EECEALCTRLAIMVKGAFQCLGTIQHLKSK 2160
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 24581387 252 FAQSGHICPQYYNPAD--------------FGIPGSVQSVLHHRTL 283
Cdd:TIGR01257 2161 FGDGYIVTMKIKSPKDdllpdlnpveqffqGNFPGSVQRERHYNML 2206
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-249 |
3.79e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.85 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 38 GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAG----FKLQGVTGQFLLNGR---PRDIMSFRKMSAYIAQNFVM 110
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARVSGEVYLDGQdifKMDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 111 LNLLTVEETLRVSTDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTL---VKNLSGGEHKRLSIGIELVTNPPIMFFDEP 187
Cdd:PRK14247 94 IPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 188 TSGLDCVGSYQVICHLQRLAHDGRIVVcVVHQPGsRLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:PRK14247 174 TANLDPENTAKIESLFLELKKDMTIVL-VTHFPQ-QAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
23-249 |
4.06e-11 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 61.55 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLKGatkgSTPIINEACGVFKSGRLTAILGPSGAGKSTLL---NALagfkLQGVTGQFLLNGRprDIMSF-- 97
Cdd:cd03295 1 IEFENVTKRYGG----GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMkmiNRL----IEPTSGEIFIDGE--DIREQdp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 98 ---RKMSAYIAQNFVMLNLLTVEETLR-VSTDLKMPsstaaqeKQKIIDDIIDILQL-----QSCRRTLVKNLSGGEHKR 168
Cdd:cd03295 71 velRRKIGYVIQQIGLFPHMTVEENIAlVPKLLKWP-------KEKIRERADELLALvgldpAEFADRYPHELSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 169 LSIGIELVTNPPIMFFDEPTSGLDCVGSYQV---ICHLQRLAhdGRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQ 245
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPITRDQLqeeFKRLQQEL--GKTIVFVTHDI-DEAFRLADRIAIMKNGEIVQVGTP 220
|
....
gi 24581387 246 REML 249
Cdd:cd03295 221 DEIL 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
50-243 |
4.77e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 60.62 E-value: 4.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFKLQGVT-GQFLLNGrpRDI----MSFR-KMSAYIA-QNFVMLNLLTVEETLrv 122
Cdd:cd03217 23 IKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTeGEILFKG--EDItdlpPEERaRLGIFLAfQYPPEIPGVKNADFL-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 123 stdlkmpsstaaqekqkiiddiidilqlqscrRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDcVGSYQVICH 202
Cdd:cd03217 99 --------------------------------RYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD-IDALRLVAE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24581387 203 -LQRLAHDGRIVVCVVHQPgsRLFQLF--DDVLVLAHGEVLYAG 243
Cdd:cd03217 146 vINKLREEGKSVLIITHYQ--RLLDYIkpDRVHVLYDGRIVKSG 187
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
13-249 |
5.23e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 62.36 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 13 LGPQKQKALELHFSQVSYSLKGATKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRpr 92
Cdd:PRK10070 14 FGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL-IEPTRGQVLIDGV-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 93 DIMSF---------RKMSAYIAQNFVMLNLLTVEETLRVSTDLkmpSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSG 163
Cdd:PRK10070 91 DIAKIsdaelrevrRKKIAMVFQSFALMPHMTVLDNTAFGMEL---AGINAEERREKALDALRQVGLENYAHSYPDELSG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 164 GEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRL-AHDGRIVVCVVHQPGSRLfQLFDDVLVLAHGEVLYA 242
Cdd:PRK10070 168 GMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQV 246
|
....*..
gi 24581387 243 GEQREML 249
Cdd:PRK10070 247 GTPDEIL 253
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
51-243 |
5.68e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.55 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGF-KLQgvtGQFLLNG---RPRDIMSFRKMSAYIAQNFVMLnlltvEETLRVSTDL 126
Cdd:PRK11174 374 PAGQRIALVGPSGAGKTSLLNALLGFlPYQ---GSLKINGielRELDPESWRKHLSWVGQNPQLP-----HGTLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 127 KMPSSTAAQEKQ------------KIIDDIIDILQLQSCRrtlvknLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCV 194
Cdd:PRK11174 446 GNPDASDEQLQQalenawvseflpLLPQGLDTPIGDQAAG------LSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24581387 195 GSYQVICHLQRLAHdGRIVVCVVHqpgsRLFQL--FDDVLVLAHGEVLYAG 243
Cdd:PRK11174 520 SEQLVMQALNAASR-RQTTLMVTH----QLEDLaqWDQIWVMQDGQIVQQG 565
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
26-249 |
6.15e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.16 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 26 SQVSYSLKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKLQGvTGQFLLNGR--PRDIMSFRKMS 101
Cdd:PRK13536 38 STVAIDLAGVSKsyGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD-AGKITVLGVpvPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 102 AYIAQnFVMLNL-LTVEETLRV-STDLKMpsstAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNP 179
Cdd:PRK13536 117 GVVPQ-FDNLDLeFTVRENLLVfGRYFGM----STREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 180 PIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVH--QPGSRlfqLFDDVLVLAHGEVLYAGEQREML 249
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHfmEEAER---LCDRLCVLEAGRKIAEGRPHALI 260
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-248 |
7.41e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 61.30 E-value: 7.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLKGATKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKL--QG---VTGQFLLNG-RPRDIMS 96
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVptQGsvrVDDTLITSTsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 97 FRKMSAYIAQnFVMLNLLtvEETlrVSTDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLV-KN---LSGGEHKRLSIG 172
Cdd:PRK13649 83 IRKKVGLVFQ-FPESQLF--EET--VLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFeKNpfeLSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 173 IELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHqpgsrlfqLFDDV-------LVLAHGEVLYAGEQ 245
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH--------LMDDVanyadfvYVLEKGKLVLSGKP 229
|
...
gi 24581387 246 REM 248
Cdd:PRK13649 230 KDI 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
31-239 |
9.31e-11 |
|
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: 58.98 E-value: 9.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 31 SLKGATK--GSTPIINeacGV---FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMsayia 105
Cdd:cd03216 2 ELRGITKrfGGVKALD---GVslsVRRGEVHALLGENGAGKSTLMKILSGL-YKPDSGEILVDGKEVSFASPRDA----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 106 qnfvmlnlltveETLRVSTdlkmpsstaaqekqkiiddiidilqlqscrrtlVKNLSGGEHKRLSIGIELVTNPPIMFFD 185
Cdd:cd03216 73 ------------RRAGIAM---------------------------------VYQLSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24581387 186 EPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHqpgsRL---FQLFDDVLVLAHGEV 239
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISH----RLdevFEIADRVTVLRDGRV 160
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
52-220 |
1.14e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 61.66 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 52 SGRLTAILGPSGAGKSTLLNALaGFKLQGVTGQFLLNGRprDIMSF---------RKMSAYIAQNFVMLNLLTVEETLRV 122
Cdd:PRK10535 33 AGEMVAIVGASGSGKSTLMNIL-GCLDKPTSGTYRVAGQ--DVATLdadalaqlrREHFGFIFQRYHLLSHLTAAQNVEV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 123 stdlkmPSSTAAQEKQKIIDDIIDILQ-LQSCRRTLVK--NLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQV 199
Cdd:PRK10535 110 ------PAVYAGLERKQRLLRAQELLQrLGLEDRVEYQpsQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170 180
....*....|....*....|.
gi 24581387 200 ICHLQRLAHDGRIVVCVVHQP 220
Cdd:PRK10535 184 MAILHQLRDRGHTVIIVTHDP 204
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
32-192 |
1.21e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 61.27 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 32 LKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfkLQGVT-GQFLLNG--------RPRDI-MSFrk 99
Cdd:PRK11432 9 LKNITKrfGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAG--LEKPTeGQIFIDGedvthrsiQQRDIcMVF-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 100 msayiaQNFVMLNLLTVEETlrVSTDLKMPSSTAAQEKQKIIDDIIDiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNP 179
Cdd:PRK11432 85 ------QSYALFPHMSLGEN--VGYGLKMLGVPKEERKQRVKEALEL-VDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170
....*....|...
gi 24581387 180 PIMFFDEPTSGLD 192
Cdd:PRK11432 156 KVLLFDEPLSNLD 168
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
51-244 |
1.30e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.64 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTllNALAGFKLQGVTGQFLLNGRPRDIMSFRKMSAYIAQNFVM-----------LNLLT-VEE 118
Cdd:PRK15134 310 RPGETLGLVGESGSGKST--TGLALLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVfqdpnsslnprLNVLQiIEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 119 TLRVstdlKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQ 198
Cdd:PRK15134 388 GLRV----HQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQ 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24581387 199 VICHLQRL-----------AHDGRIVVCVVHQpgsrlfqlfddVLVLAHGEVLYAGE 244
Cdd:PRK15134 464 ILALLKSLqqkhqlaylfiSHDLHVVRALCHQ-----------VIVLRQGEVVEQGD 509
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
51-192 |
1.52e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 60.04 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFklqgVT---GQFLLNGRprDI-------------------MS-FRKMSayiaqn 107
Cdd:COG1137 27 NQGEIVGLLGPNGAGKTTTFYMIVGL----VKpdsGRIFLDGE--DIthlpmhkrarlgigylpqeASiFRKLT------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 108 fVMLNLLTVEETLRVStdlkmpsstaAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEP 187
Cdd:COG1137 95 -VEDNILAVLELRKLS----------KKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
....*
gi 24581387 188 TSGLD 192
Cdd:COG1137 164 FAGVD 168
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
51-192 |
1.54e-10 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 59.75 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMS------FRKMSA-YIAQNFVMLNLLTVEETlrVS 123
Cdd:COG4181 36 EAGESVAIVGASGSGKSTLLGLLAGL-DRPTSGTVRLAGQDLFALDedararLRARHVgFVFQSFQLLPTLTALEN--VM 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 124 TDLKMPSSTAAQEKQKiiddiiDILQ---LQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:COG4181 113 LPLELAGRRDARARAR------ALLErvgLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
51-247 |
1.83e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.12 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP---RDIMSF----------RKMsayiaqnfvmlnllTVE 117
Cdd:COG4152 25 PKGEIFGLLGPNGAGKTTTIRIILGI-LAPDSGEVLWDGEPldpEDRRRIgylpeerglyPKM--------------KVG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 118 ETLRVSTDLK-MPSSTAAQ------EKqkiiddiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSG 190
Cdd:COG4152 90 EQLVYLARLKgLSKAEAKRradewlER----------LGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 191 LDCVGS---YQVIchlQRLAHDGRIVVCVVHQPGS--RlfqLFDDVLVLAHGEVLYAGEQRE 247
Cdd:COG4152 160 LDPVNVellKDVI---RELAAKGTTVIFSSHQMELveE---LCDRIVIINKGRKVLSGSVDE 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
53-192 |
2.12e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 60.62 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGFKlQGVTGQFLLNG----------RPRDIMsfrkmsayiAQNFVMLNLLTVEETlrV 122
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGFE-QPTAGQIMLDGvdlshvppyqRPINMM---------FQSYALFPHMTVEQN--I 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 123 STDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTlVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:PRK11607 113 AFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRK-PHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-231 |
2.84e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 59.75 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLKGATKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLL-------NGRPRDIM 95
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGL-LQPTEGKVTVgdivvssTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 96 SFRKMSAYIAQnFVMLNLLtvEETlrVSTDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKN----LSGGEHKRLSI 171
Cdd:PRK13643 81 PVRKKVGVVFQ-FPESQLF--EET--VLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKspfeLSGGQMRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 172 GIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHqpgsrlfqLFDDV 231
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH--------LMDDV 207
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
57-239 |
3.31e-10 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 57.83 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 57 AILGPSGAGKSTLLNALAGFKlQGVTGQFLLNGRPRDIMSFRKMS----AYIA----QNFVMLNLlTVEETLrvstdlkm 128
Cdd:cd03215 30 GIAGLVGNGQTELAEALFGLR-PPASGEITLDGKPVTRRSPRDAIragiAYVPedrkREGLVLDL-SVAENI-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 129 psstaaqekqkiiddiidilqlqscrrTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDcVGS----YQVIchlQ 204
Cdd:cd03215 100 ---------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD-VGAkaeiYRLI---R 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 24581387 205 RLAHDGRIVVCVvhqpgSR----LFQLFDDVLVLAHGEV 239
Cdd:cd03215 149 ELADAGKAVLLI-----SSeldeLLGLCDRILVMYEGRI 182
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
31-204 |
3.46e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 58.75 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 31 SLKGATKGSTPIINEACGVfKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSF----RKMSAYIAQ 106
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTV-NSGEIVGLLGPNGAGKTTTFYMVVGI-VPRDAGNIIIDDEDISLLPLharaRRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 107 NFVMLNLLTVEETLRVStdLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDE 186
Cdd:PRK10895 86 EASIFRRLSVYDNLMAV--LQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180
....*....|....*....|.
gi 24581387 187 PTSGLDCVGSY---QVICHLQ 204
Cdd:PRK10895 164 PFAGVDPISVIdikRIIEHLR 184
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
50-248 |
3.98e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.02 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALagfKLQG-------VTGQFLLNGR----PR-DIMSFRKMSAYIAQN---FVMLNLL 114
Cdd:PRK14239 28 FYPNEITALIGPSGSGKSTLLRSI---NRMNdlnpevtITGSIVYNGHniysPRtDTVDLRKEIGMVFQQpnpFPMSIYE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 115 TVEETLRVStdlkmpsstAAQEKQKIIDDIIDILQLQSCRRTlVKN--------LSGGEHKRLSIGIELVTNPPIMFFDE 186
Cdd:PRK14239 105 NVVYGLRLK---------GIKDKQVLDEAVEKSLKGASIWDE-VKDrlhdsalgLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581387 187 PTSGLDCVGSYQVICHLQRLAHDGRIVVcVVH--QPGSRlfqLFDDVLVLAHGEVLYAGEQREM 248
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDYTMLL-VTRsmQQASR---ISDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-192 |
5.69e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.19 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 16 QKQKALeLHFSQVSYSLkgatkGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIM 95
Cdd:PRK10247 2 QENSPL-LQLQNVGYLA-----GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL-ISPTSGTLLFEGEDISTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 96 S---FRKMSAYIAQNFVMLNlltveETlrVSTDLKMP---SSTAAQEKQKIIDDIIDILQLQscrrTLVKN---LSGGEH 166
Cdd:PRK10247 75 KpeiYRQQVSYCAQTPTLFG-----DT--VYDNLIFPwqiRNQQPDPAIFLDDLERFALPDT----ILTKNiaeLSGGEK 143
|
170 180
....*....|....*....|....*.
gi 24581387 167 KRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:PRK10247 144 QRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-249 |
6.85e-10 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 58.42 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 14 GPQKQKALELHFSQVSYSLKGATKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRD 93
Cdd:cd03294 11 GKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRL-IEPTSGKVLIDGQDIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 94 IMSF-------RKMSAYIAQNFVMLNLLTVEETLRVSTDLKmpsSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEH 166
Cdd:cd03294 90 AMSRkelrelrRKKISMVFQSFALLPHRTVLENVAFGLEVQ---GVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 167 KRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRL-AHDGRIVVCVVHQPGSRLfQLFDDVLVLAHGEVLYAGEQ 245
Cdd:cd03294 167 QRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEAL-RLGDRIAIMKDGRLVQVGTP 245
|
....
gi 24581387 246 REML 249
Cdd:cd03294 246 EEIL 249
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-248 |
7.31e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 58.25 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 21 LELHFSQVSYSLKGATKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNG-------RPRD 93
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAL-LKPTTGTVTVDDitithktKDKY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 94 IMSFRKMSAYIAQnFVMLNLL--TVE-ETLRVSTDLKMPSSTAAQEKQKIIddiidiLQLQSCRRTLVKN---LSGGEHK 167
Cdd:PRK13646 80 IRPVRKRIGMVFQ-FPESQLFedTVErEIIFGPKNFKMNLDEVKNYAHRLL------MDLGFSRDVMSQSpfqMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 168 RLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRL-AHDGRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQR 246
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDM-NEVARYADEVIVMKEGSIVSQTSPK 231
|
..
gi 24581387 247 EM 248
Cdd:PRK13646 232 EL 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-248 |
8.85e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.11 E-value: 8.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 21 LELHFSQVSYSLKGATKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLL-------NGRPRD 93
Cdd:PRK13634 1 MDITFQKVEHRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGL-LQPTSGTVTIgervitaGKKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 94 IMSFRKMSAYIAQnFVMLNLLtvEETlrVSTDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVK----NLSGGEHKRL 169
Cdd:PRK13634 80 LKPLRKKVGIVFQ-FPEHQLF--EET--VEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLArspfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 170 SIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRI-VVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQREM 248
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLtTVLVTHSM-EDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
50-192 |
8.98e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 57.74 E-value: 8.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNAL-------AGFKlqgVTGQFLLNGrpRDI---------------MSFRK-----MSa 102
Cdd:COG1117 34 IPENKVTALIGPSGCGKSTLLRCLnrmndliPGAR---VEGEILLDG--EDIydpdvdvvelrrrvgMVFQKpnpfpKS- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 103 yIAQNFVM---LNLLT--------VEETLR-------VSTDLKMPSStaaqekqkiiddiidilqlqscrrtlvkNLSGG 164
Cdd:COG1117 108 -IYDNVAYglrLHGIKskseldeiVEESLRkaalwdeVKDRLKKSAL----------------------------GLSGG 158
|
170 180
....*....|....*....|....*...
gi 24581387 165 EHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
39-192 |
9.53e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.52 E-value: 9.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 39 STPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKlQGVTGQFLLNGRPRDIMSFRKMSA-------YIAQNFVML 111
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLD-TPTSGDVIFNGQPMSKLSSAAKAElrnqklgFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 112 NLLTVEETlrVSTDLKMPSSTAAQEKQKIIDDIIDI-LQLQSCRRTlvKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSG 190
Cdd:PRK11629 100 PDFTALEN--VAMPLLIGKKKPAEINSRALEMLAAVgLEHRANHRP--SELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
..
gi 24581387 191 LD 192
Cdd:PRK11629 176 LD 177
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-248 |
1.26e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.58 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 25 FSQVSYSLkgATKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP---RDIMSFRKMS 101
Cdd:TIGR00958 481 FQDVSFSY--PNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL-YQPTGGQVLLDGVPlvqYDHHYLHRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 102 AYIAQNFVMLNLLTVEETLRVSTDLKMPSSTAAqekQKIIDDIIDILQLQSCRRTLV----KNLSGGEHKRLSIGIELVT 177
Cdd:TIGR00958 558 ALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAA---AKAANAHDFIMEFPNGYDTEVgekgSQLSGGQKQRIAIARALVR 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581387 178 NPPIMFFDEPTSGLDcVGSYQVICHLQRLAhdGRIVVCVVHQpgSRLFQLFDDVLVLAHGEVLYAGEQREM 248
Cdd:TIGR00958 635 KPRVLILDEATSALD-AECEQLLQESRSRA--SRTVLLIAHR--LSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
53-199 |
1.40e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 57.30 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMSAYI---AQNFVMLNLLTVEETLRVSTDLKMP 129
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRL-MTPAHGHVWLDGEHIQHYASKEVARRIgllAQNATTPGDITVQELVARGRYPHQP 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581387 130 SSTA-AQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCvgSYQV 199
Cdd:PRK10253 112 LFTRwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI--SHQI 180
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
56-239 |
1.46e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.96 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 56 TAILGPSGAGKSTLLNALAGFKlQGVTGQFLLNGR--------------PRDI----------------------MSfRK 99
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLT-RPQKGRIVLNGRvlfdaekgiclppeKRRIgyvfqdarlfphykvrgnlrygMA-KS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 100 MSAYIAQnfvMLNLLTVEETLRvstdlKMPSStaaqekqkiiddiidilqlqscrrtlvknLSGGEHKRLSIGIELVTNP 179
Cdd:PRK11144 105 MVAQFDK---IVALLGIEPLLD-----RYPGS-----------------------------LSGGEKQRVAIGRALLTAP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 180 PIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGSRLFQLFDDVLVLAHGEV 239
Cdd:PRK11144 148 ELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
52-243 |
2.29e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.81 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 52 SGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMSAYIAQ-------------NFVMLNLLTVEE 118
Cdd:PRK15056 32 GGSIAALVGVNGSGKSTLFKALMGF-VRLASGKISILGQPTRQALQKNLVAYVPQseevdwsfpvlveDVVMMGRYGHMG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 119 TLRVSTDLKMPSSTAAQEKqkiiddiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQ 198
Cdd:PRK15056 111 WLRRAKKRDRQIVTAALAR----------VDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24581387 199 VICHLQRLAHDGRIVVCVVHQPGSrlFQLFDDVLVLAHGEVLYAG 243
Cdd:PRK15056 181 IISLLRELRDEGKTMLVSTHNLGS--VTEFCDYTVMVKGTVLASG 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
51-239 |
2.54e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFKLQGVTGQFLLNGRPRDImsfRKMSAYIAQNFVM----------LNLLTVEE-- 118
Cdd:TIGR02633 284 RRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDI---RNPAQAIRAGIAMvpedrkrhgiVPILGVGKni 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 119 TLRVSTDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTL-VKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSY 197
Cdd:TIGR02633 361 TLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKY 440
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24581387 198 QVICHLQRLAHDGrIVVCVVHQPGSRLFQLFDDVLVLAHGEV 239
Cdd:TIGR02633 441 EIYKLINQLAQEG-VAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
52-244 |
2.99e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.49 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 52 SGRLTAILGPSGAGKSTLLNALAGFKlQGVTGQFLLNGRPRDIMSfRKMSA-----YIAQNFVMLNLLTVEETLRVStdl 126
Cdd:PRK09700 30 PGEIHALLGENGAGKSTLMKVLSGIH-EPTKGTITINNINYNKLD-HKLAAqlgigIIYQELSVIDELTVLENLYIG--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 127 KMPSSTAA-------QEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQV 199
Cdd:PRK09700 105 RHLTKKVCgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24581387 200 ICHLQRLAHDGRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGE 244
Cdd:PRK09700 185 FLIMNQLRKEGTAIVYISHKL-AEIRRICDRYTVMKDGSSVCSGM 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
51-220 |
3.30e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.58 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP----RDimSFRKMSAYIA-QNFVMlNLLTVEETLRVSTD 125
Cdd:PRK13538 25 NAGELVQIEGPNGAGKTSLLRILAGL-ARPDAGEVLWQGEPirrqRD--EYHQDLLYLGhQPGIK-TELTALENLRFYQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 126 LKMPSSTAAqekqkiiddIIDILQ---LQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICH 202
Cdd:PRK13538 101 LHGPGDDEA---------LWEALAqvgLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEAL 171
|
170
....*....|....*...
gi 24581387 203 LQRLAHDGRIVVCVVHQP 220
Cdd:PRK13538 172 LAQHAEQGGMVILTTHQD 189
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
57-251 |
4.77e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.82 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 57 AILGPSGAGKSTLLNALAGF------KLQgVTGQFLLNGRPR---DIMSFRKMSAYIAQNFVMLNLLTVEETlrVSTDLK 127
Cdd:PRK14246 40 GIMGPSGSGKSTLLKVLNRLieiydsKIK-VDGKVLYFGKDIfqiDAIKLRKEVGMVFQQPNPFPHLSIYDN--IAYPLK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 128 mpsSTAAQEKQKIIDDIIDIL-------QLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVI 200
Cdd:PRK14246 117 ---SHGIKEKREIKKIVEECLrkvglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIE 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24581387 201 CHLQRLAHDGRIVVcVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQREMLPT 251
Cdd:PRK14246 194 KLITELKNEIAIVI-VSHNP-QQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
49-276 |
4.85e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.90 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 49 VFKSGRLTAILGPSGAGKSTLLNALAGFKL--QG---VTGQFLlngRPRDIMSFRKMSAYIAQN---------------F 108
Cdd:PRK13647 27 SIPEGSKTALLGPNGAGKSTLLLHLNGIYLpqRGrvkVMGREV---NAENEKWVRSKVGLVFQDpddqvfsstvwddvaF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 109 VMLNL-LTVEETL-RVSTDLKMpsstaaqekqkiiddiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDE 186
Cdd:PRK13647 104 GPVNMgLDKDEVErRVEEALKA-------------------VRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 187 PTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGSRLfQLFDDVLVLAHGEVLYAGEQREM------------LPTFAQ 254
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEGDKSLLtdediveqaglrLPLVAQ 243
|
250 260
....*....|....*....|..
gi 24581387 255 SGHICPQYYNPAdfgIPGSVQS 276
Cdd:PRK13647 244 IFEDLPELGQSK---LPLTVKE 262
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
36-192 |
6.29e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 54.80 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 36 TKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKLQGVT--GQFLLNGRPRDIMSF--RKMsAYIAQNFVML 111
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSasGEVLLNGRRLTALPAeqRRI-GILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 112 NLLTVEETLRvstdLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGL 191
Cdd:COG4136 89 PHLSVGENLA----FALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
.
gi 24581387 192 D 192
Cdd:COG4136 165 D 165
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
50-238 |
6.47e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 54.78 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFLLNGRprdimsfrkmSAYIAQNFVMLNlLTV------------- 116
Cdd:cd03250 28 VPKGELVAIVGPVGSGKSSLLSALLG-ELEKLSGSVSVPGS----------IAYVSQEPWIQN-GTIrenilfgkpfdee 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 117 --EETLRV---STDLKmpsstaaqekqkiiddiidilQLQSCRRTLVK----NLSGGEHKRLSIGIELVTNPPIMFFDEP 187
Cdd:cd03250 96 ryEKVIKAcalEPDLE---------------------ILPDGDLTEIGekgiNLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24581387 188 TSGLDC-VGSY---QVICHLQRlahDGRIVVCVVHQPgsRLFQLFDDVLVLAHGE 238
Cdd:cd03250 155 LSAVDAhVGRHifeNCILGLLL---NNKTRILVTHQL--QLLPHADQIVVLDNGR 204
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
52-218 |
6.75e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.48 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 52 SGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKmsAYIAQNFVMLNLLTVEETlrVSTDLKMPSS 131
Cdd:PRK11248 26 SGELLVVLGPSGCGKTTLLNLIAGF-VPYQHGSITLDGKPVEGPGAER--GVVFQNEGLLPWRNVQDN--VAFGLQLAGV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 132 TAAQEKQKiIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHD-G 210
Cdd:PRK11248 101 EKMQRLEI-AHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtG 179
|
....*...
gi 24581387 211 RIVVCVVH 218
Cdd:PRK11248 180 KQVLLITH 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-192 |
7.13e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 56.23 E-value: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 15 PQKQKALELHFSQVSYS------LKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFl 86
Cdd:COG0488 295 PRRDKTVEIRFPPPERLgkkvleLEGLSKsyGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-ELEPDSGTV- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 87 lngrprdimsfrKMS-----AYIAQNFVMLNL-LTVEETLR-VSTDLKMPSSTA-------AQEKQkiiddiidilqlqs 152
Cdd:COG0488 373 ------------KLGetvkiGYFDQHQEELDPdKTVLDELRdGAPGGTEQEVRGylgrflfSGDDA-------------- 426
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24581387 153 crRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:COG0488 427 --FKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
53-237 |
8.51e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 8.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGFKlQGVTGQFLLNGRPrdiMSFRKMSAYIAQNFVM----LNL---LTVEETLRVStd 125
Cdd:PRK11288 30 GQVHALMGENGAGKSTLLKILSGNY-QPDAGSILIDGQE---MRFASTTAALAAGVAIiyqeLHLvpeMTVAENLYLG-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 126 lKMPSSTAAQEKQKIIDDIIDILQ---LQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICH 202
Cdd:PRK11288 104 -QLPHKGGIVNRRLLNYEAREQLEhlgVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRV 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 24581387 203 LQRLAHDGRIVVCVVHqpgsRL---FQLFDDVLVLAHG 237
Cdd:PRK11288 183 IRELRAEGRVILYVSH----RMeeiFALCDAITVFKDG 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-249 |
9.50e-09 |
|
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: 56.11 E-value: 9.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 29 SYSLKGAT----KGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFLLNGRprdiMSFRKMSAYI 104
Cdd:TIGR00957 636 SITVHNATftwaRDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLA-EMDKVEGHVHMKGS----VAYVPQQAWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 105 AQNFVMLNLL-----------TVEETLRVSTDLKM-PSSTAAQEKQKIIddiidilqlqscrrtlvkNLSGGEHKRLSIG 172
Cdd:TIGR00957 711 QNDSLRENILfgkalnekyyqQVLEACALLPDLEIlPSGDRTEIGEKGV------------------NLSGGQKQRVSLA 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 173 IELVTNPPIMFFDEPTSGLDC-VGSY---QVICHLQRLAHDGRIVvcVVHqpGSRLFQLFDDVLVLAHGEVLYAGEQREM 248
Cdd:TIGR00957 773 RAVYSNADIYLFDDPLSAVDAhVGKHifeHVIGPEGVLKNKTRIL--VTH--GISYLPQVDVIIVMSGGKISEMGSYQEL 848
|
.
gi 24581387 249 L 249
Cdd:TIGR00957 849 L 849
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
160-249 |
1.09e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.09 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 160 NLSGGEHKRLSI-GIeLVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGSRLfQLFDDVLVLAHGE 238
Cdd:PRK13651 165 ELSGGQKRRVALaGI-LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVL-EWTKRTIFFKDGK 242
|
90
....*....|.
gi 24581387 239 VLYAGEQREML 249
Cdd:PRK13651 243 IIKDGDTYDIL 253
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
53-243 |
1.34e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.55 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFLLNGR---PRDI--MS-------FRKMSAYIAQNfvmlnlltVEETL 120
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSA-RLAPDAGEVHYRMRdgqLRDLyaLSeaerrrlLRTEWGFVHQH--------PRDGL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 121 R--VST-----------------DLKmpsSTAAQEKQKiiddiidiLQLQSCR-----RTLvknlSGGEHKRLSIGIELV 176
Cdd:PRK11701 103 RmqVSAggnigerlmavgarhygDIR---ATAGDWLER--------VEIDAARiddlpTTF----SGGMQQRLQIARNLV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581387 177 TNPPIMFFDEPTSGLDCvgSYQ--VICHLQRLAHD-GRIVVCVVHQPG-SRLfqLFDDVLVLAHGEVLYAG 243
Cdd:PRK11701 168 THPRLVFMDEPTGGLDV--SVQarLLDLLRGLVRElGLAVVIVTHDLAvARL--LAHRLLVMKQGRVVESG 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
42-256 |
1.90e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 54.33 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 42 IINEACGVFKSGRLTAILGPSGAGKSTLLNALAGF--KLQGV--TGQFLLNGRP----RDIMSFRKMSAYIAQNFVMLNL 113
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndKVSGYrySGDVLLGGRSifnyRDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 114 LTVEETLrvsTDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKN----LSGGEHKRLSIGIELVTNPPIMFFDEPTS 189
Cdd:PRK14271 116 SIMDNVL---AGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 190 GLDCVGSYQVICHLQRLAHdgRIVVCVVHQPGSRLFQLFDDVLVLAHGEVLYAGEQREML--PTFAQSG 256
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFssPKHAETA 259
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
51-218 |
2.07e-08 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 54.04 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLL---NALAgfklQGVTGQFLLNG-------------RPRDIMSFRKMSAYIA---QNFvml 111
Cdd:COG4598 32 RKGDVISIIGSSGSGKSTFLrciNLLE----TPDSGEIRVGGeeirlkpdrdgelVPADRRQLQRIRTRLGmvfQSF--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 112 NL---LTV-----EETLRVstdLKMPSSTAAQEKQKIiddiidiLQ---LQSCRRTLVKNLSGGEHKRLSIGIELVTNPP 180
Cdd:COG4598 105 NLwshMTVlenviEAPVHV---LGRPKAEAIERAEAL-------LAkvgLADKRDAYPAHLSGGQQQRAAIARALAMEPE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24581387 181 IMFFDEPTSGLD--CVGsyQVICHLQRLAHDGRIVVCVVH 218
Cdd:COG4598 175 VMLFDEPTSALDpeLVG--EVLKVMRDLAEEGRTMLVVTH 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
31-192 |
2.34e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 54.08 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 31 SLKGATK---GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfkLQGVT-GQFLLNGR------P--RDI-MSF 97
Cdd:PRK11650 5 KLQAVRKsydGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG--LERITsGEIWIGGRvvnelePadRDIaMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 98 rkmsayiaQNFVMLNLLTVEETLrvSTDLK---MPSSTAAQEKQKiiddIIDILQLQSC--RRTlvKNLSGGEHKRLSIG 172
Cdd:PRK11650 83 --------QNYALYPHMSVRENM--AYGLKirgMPKAEIEERVAE----AARILELEPLldRKP--RELSGGQRQRVAMG 146
|
170 180
....*....|....*....|
gi 24581387 173 IELVTNPPIMFFDEPTSGLD 192
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLD 166
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
51-192 |
2.49e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.46 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKmsayIA--------QNFVMLNLLTVEETLRV 122
Cdd:PRK11300 29 REQEIVSLIGPNGAGKTTVFNCLTGF-YKPTGGTILLRGQHIEGLPGHQ----IArmgvvrtfQHVRLFREMTVIENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 123 STD-----------LKMPS-STAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSG 190
Cdd:PRK11300 104 AQHqqlktglfsglLKTPAfRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAG 183
|
..
gi 24581387 191 LD 192
Cdd:PRK11300 184 LN 185
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
57-249 |
2.51e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.69 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 57 AILGPSGAGKSTLLNALAGF----KLQGVTGQFLLNGR-----PRDIMSFRKMSAYIAQNFVMLNLLTVEETLRVSTDL- 126
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTFNRLlelnEEARVEGEVRLFGRniyspDVDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLn 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 127 KMPSSTAAQEKQKIIDDIIDIL--QLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQ 204
Cdd:PRK14267 114 GLVKSKKELDERVEWALKKAALwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24581387 205 RLAHDGRIVVcVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:PRK14267 194 ELKKEYTIVL-VTHSP-AQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-254 |
2.61e-08 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 54.37 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 22 ELHFSQVSYSLKGATKgstPIINeacGV---FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGR-------- 90
Cdd:COG4618 330 RLSVENLTVVPPGSKR---PILR---GVsfsLEPGEVLGVIGPSGSGKSTLARLLVGV-WPPTAGSVRLDGAdlsqwdre 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 91 ---------PRDIMSFrkmSAYIAQNFVMLNLLTVEETLRvstdlkmpsstAAQ-----EkqkiiddiiDILQLQSCRRT 156
Cdd:COG4618 403 elgrhigylPQDVELF---DGTIAENIARFGDADPEKVVA-----------AAKlagvhE---------MILRLPDGYDT 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 157 LV----KNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGsrLFQLFDDVL 232
Cdd:COG4618 460 RIgeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS--LLAAVDKLL 537
|
250 260
....*....|....*....|..
gi 24581387 233 VLAHGEVLYAGEQREMLPTFAQ 254
Cdd:COG4618 538 VLRDGRVQAFGPRDEVLARLAR 559
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
53-257 |
3.18e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 54.44 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALagFKLQGVT-GQFLLNGRP-RDIM--SFRKMSAYIAQNFVMLNlltveETLRVSTDLKM 128
Cdd:COG5265 384 GKTVAIVGPSGAGKSTLARLL--FRFYDVTsGRILIDGQDiRDVTqaSLRAAIGIVPQDTVLFN-----DTIAYNIAYGR 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 129 PSSTAAQ--EKQKIIDDIIDILQLQSCRRTLV-----KnLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCvGSYQVIC 201
Cdd:COG5265 457 PDASEEEveAAARAAQIHDFIESLPDGYDTRVgerglK-LSGGEKQRVAIARTLLKNPPILIFDEATSALDS-RTERAIQ 534
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 202 H-LQRLAHdGRIVVCVVHqpgsRLFQLF--DDVLVLAHGEVLYAGEQREMLptfAQSGH 257
Cdd:COG5265 535 AaLREVAR-GRTTLVIAH----RLSTIVdaDEILVLEAGRIVERGTHAELL---AQGGL 585
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
51-218 |
4.06e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 53.27 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFKlQGVTGQFLLNGRPRDIMSFR-KMSAYIAQNFVMLNL-LTVEETLRV-STDLK 127
Cdd:PRK13537 31 QRGECFGLLGPNGAGKTTTLRMLLGLT-HPDAGSISLCGEPVPSRARHaRQRVGVVPQFDNLDPdFTVRENLLVfGRYFG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 128 MPSSTAAQEKQKIIDDIidilQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLA 207
Cdd:PRK13537 110 LSAAAARALVPPLLEFA----KLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL 185
|
170
....*....|.
gi 24581387 208 HDGRIVVCVVH 218
Cdd:PRK13537 186 ARGKTILLTTH 196
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
23-192 |
4.44e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 51.30 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 23 LHFSQVSYSLkgatkGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFLLNGRPRdimsfrkmSA 102
Cdd:cd03221 1 IELENLSKTY-----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-ELEPDEGIVTWGSTVK--------IG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 103 YIAQnfvmlnlltveetlrvstdlkmpsstaaqekqkiiddiidilqlqscrrtlvknLSGGEHKRLSIGIELVTNPPIM 182
Cdd:cd03221 67 YFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170
....*....|
gi 24581387 183 FFDEPTSGLD 192
Cdd:cd03221 93 LLDEPTNHLD 102
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
51-218 |
5.37e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.63 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFllnGRPRD----IMSFRKMSAYiaQNFVMLnlltVEETLRVS--- 123
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSG-ELKPNLGDY---DEEPSwdevLKRFRGTELQ--DYFKKL----ANGEIKVAhkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 124 --------------------TDLKMPSSTAAQEkqkiiddiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMF 183
Cdd:COG1245 167 qyvdlipkvfkgtvrellekVDERGKLDELAEK-----------LGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|....*...
gi 24581387 184 FDEPTSGLDCvgsYQ---VICHLQRLAHDGRIVVCVVH 218
Cdd:COG1245 236 FDEPSSYLDI---YQrlnVARLIRELAEEGKYVLVVEH 270
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
51-216 |
5.45e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.63 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFKlQGVTGQFLLNGR---PRD-IMSFRKMSAYIAQ---------NFvmlnllTVE 117
Cdd:PRK09700 287 CRGEILGFAGLVGSGRTELMNCLFGVD-KRAGGEIRLNGKdisPRSpLDAVKKGMAYITEsrrdngffpNF------SIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 118 ETLRVSTDLKMPSSTAA------QEKQKIIDDIIDILQLQsCRrTLVKN---LSGGEHKRLSIGIELVTNPPIMFFDEPT 188
Cdd:PRK09700 360 QNMAISRSLKDGGYKGAmglfheVDEQRTAENQRELLALK-CH-SVNQNiteLSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180
....*....|....*....|....*....
gi 24581387 189 SGLDcVGSYQVICHLQR-LAHDGRIVVCV 216
Cdd:PRK09700 438 RGID-VGAKAEIYKVMRqLADDGKVILMV 465
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
50-239 |
6.06e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.11 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRK-MSAYIA---QNFvML--------NL-LTV 116
Cdd:COG3845 28 VRPGEIHALLGENGAGKSTLMKILYGL-YQPDSGEILIDGKPVRIRSPRDaIALGIGmvhQHF-MLvpnltvaeNIvLGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 117 EETLRVSTDLKmpssTAAQEKQKIiddiidilqlqsCRR--------TLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPT 188
Cdd:COG3845 106 EPTKGGRLDRK----AARARIREL------------SERygldvdpdAKVEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 189 SGL-----DcvgsyQVICHLQRLAHDGRIVVCVVHqpgsRL---FQLFDDVLVLAHGEV 239
Cdd:COG3845 170 AVLtpqeaD-----ELFEILRRLAAEGKSIIFITH----KLrevMAIADRVTVLRRGKV 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-256 |
7.14e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.10 E-value: 7.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 22 ELHFSQVSYSLKGAtkgSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGF-KLQgvTGQFLLNG---RPRDIMSF 97
Cdd:PRK11176 341 DIEFRNVTFTYPGK---EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFyDID--EGEILLDGhdlRDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 98 RKMSAYIAQNFVMLNLlTVEETLRVSTDLKMpSSTAAQEKQKIIDDIIDILQLQSCRRTLV-KN---LSGGEHKRLSIGI 173
Cdd:PRK11176 416 RNQVALVSQNVHLFND-TIANNIAYARTEQY-SREQIEEAARMAYAMDFINKMDNGLDTVIgENgvlLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 174 ELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDgRIVVCVVHqpgsRL--FQLFDDVLVLAHGEVLYAGEQREMLpt 251
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAH----RLstIEKADEILVVEDGEIVERGTHAELL-- 566
|
....*
gi 24581387 252 fAQSG 256
Cdd:PRK11176 567 -AQNG 570
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
48-192 |
7.63e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 52.03 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 48 GVFKSGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFLLngrPRDIMSFRKMsaYIAQNFVMlnllTVEETLRVSTDLK 127
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAG-VLKPDEGDIEI---ELDTVSYKPQ--YIKADYEG----TVRDLLSSITKDF 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581387 128 MPSSTAAQEKQKIiddiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:cd03237 90 YTHPYFKTEIAKP-------LQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
36-192 |
1.04e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.07 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 36 TKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNaLAGFKLQGVTGQFLLNG-------RPRDIMSFRKMSAyIAQNF 108
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLR-LIGGQIAPDHGEILFDGenipamsRSRLYTVRKRMSM-LFQSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 109 VMLNLLTVEET----LRVSTDLKMP--SSTAAQEKQkiiddiidILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIM 182
Cdd:PRK11831 94 ALFTDMNVFDNvaypLREHTQLPAPllHSTVMMKLE--------AVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170
....*....|
gi 24581387 183 FFDEPTSGLD 192
Cdd:PRK11831 166 MFDEPFVGQD 175
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
63-244 |
1.08e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.33 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 63 GAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSF--------------RK-------MSayIAQNFVMLNLLTV----- 116
Cdd:COG1129 288 GAGRTELARALFGA-DPADSGEIRLDGKPVRIRSPrdairagiayvpedRKgeglvldLS--IRENITLASLDRLsrggl 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 117 -------EETLRVSTDL--KMPSstaaqekqkiiddiidilqlqscRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEP 187
Cdd:COG1129 365 ldrrrerALAEEYIKRLriKTPS-----------------------PEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581387 188 TSGLDcVGS----YQVIchlQRLAHDGRIVVCVvhqpgS----RLFQLFDDVLVLAHGEVlyAGE 244
Cdd:COG1129 422 TRGID-VGAkaeiYRLI---RELAAEGKAVIVI-----SselpELLGLSDRILVMREGRI--VGE 475
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
57-264 |
1.17e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.41 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 57 AILGPSGAGKSTLLNALAG-FKLQgvTGQFLLNGRPRDIMS---FRKMSAYIAQNFVMLnlltvEETLRVSTDLKMPSST 132
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGyYPLT--EGEIRLDGRPLSSLShsvLRQGVAMVQQDPVVL-----ADTFLANVTLGRDISE 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 133 AAqekqkiIDDIIDILQLQSCRRTLVK-----------NLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCvGSYQVIC 201
Cdd:PRK10790 444 EQ------VWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDS-GTEQAIQ 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581387 202 HLQRLAHDGRIVVCVVHqpgsRLFQLF--DDVLVLAHGEVLYAGEQREMLptfAQSGhicpQYYN 264
Cdd:PRK10790 517 QALAAVREHTTLVVIAH----RLSTIVeaDTILVLHRGQAVEQGTHQQLL---AAQG----RYWQ 570
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
51-237 |
1.32e-07 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 51.28 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFKLQGvTGQFLLNGR----------PRDIMSFRKMS-AYIAQnFvmLNLL----- 114
Cdd:COG4778 35 AAGECVALTGPSGAGKSTLLKCIYGNYLPD-SGSILVRHDggwvdlaqasPREILALRRRTiGYVSQ-F--LRVIprvsa 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 115 --TVEETLRvstDLKMPSSTAAQEKqkiiddiidilqlqscrRTLVKNL--------------SGGEHKRLSIGIELVTN 178
Cdd:COG4778 111 ldVVAEPLL---ERGVDREEARARA-----------------RELLARLnlperlwdlppatfSGGEQQRVNIARGFIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 179 PPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGSRLfQLFDDVLVLAHG 237
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVRE-AVADRVVDVTPF 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
25-250 |
1.43e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.72 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 25 FSQVSYSLKGATKgstPIINEACGVFKSGRLTAILGPSGAGKST---LLNAL--------AGFKLQGVTgqflLNGRprD 93
Cdd:PRK13640 8 FKHVSFTYPDSKK---PALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLllpddnpnSKITVDGIT----LTAK--T 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 94 IMSFRKMSAYIAQN----FVMLnllTVEETLRVSTDLKmpsSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRL 169
Cdd:PRK13640 79 VWDIREKVGIVFQNpdnqFVGA---TVGDDVAFGLENR---AVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 170 SIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRI-VVCVVHQPGSRlfQLFDDVLVLAHGEVLYAGEQREM 248
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLtVISITHDIDEA--NMADQVLVLDDGKLLAQGSPVEI 230
|
..
gi 24581387 249 LP 250
Cdd:PRK13640 231 FS 232
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
39-256 |
1.43e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.41 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 39 STPIINEACGVFKSGRLTAILGPSGAGKSTLLnALAGFKLQGVTGQFLLNGRPRDIM---SFRKMSAYIAQNFVMLNllt 115
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLL-SLIQRHFDVSEGDIRFHDIPLTKLqldSWRSRLAVVSQTPFLFS--- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 116 veETLRVSTDLKMPSSTAAQ--EKQKIIDDIIDILQLQSCRRTLVKN----LSGGEHKRLSIGIELVTNPPIMFFDEPTS 189
Cdd:PRK10789 403 --DTVANNIALGRPDATQQEieHVARLASVHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 190 GLDCVGSYQVICHLQRLAHdGRIVVCVVHqpgsRLFQLF--DDVLVLAHGEVLYAGEQREMLptfAQSG 256
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGE-GRTVIISAH----RLSALTeaSEILVMQHGHIAQRGNHDQLA---QQSG 541
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
32-192 |
1.50e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.99 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 32 LKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFLlngRPRDImsfrKMsAYIAQNFV 109
Cdd:COG0488 1 LENLSKsfGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG-ELEPDSGEVS---IPKGL----RI-GYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 110 MLNLLTV-EETLRVSTDL------------KMPSSTAAQEKQKIIDDIIDIL---QLQS-CRRTL-------------VK 159
Cdd:COG0488 72 LDDDLTVlDTVLDGDAELraleaeleeleaKLAEPDEDLERLAELQEEFEALggwEAEArAEEILsglgfpeedldrpVS 151
|
170 180 190
....*....|....*....|....*....|...
gi 24581387 160 NLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
51-192 |
1.71e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 51.62 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGfkLQGVT-GQFLLNGR------PRDIMSFRK---MsayIAQNFvmlNLL---TVE 117
Cdd:COG1135 29 EKGEIFGIIGYSGAGKSTLIRCINL--LERPTsGSVLVDGVdltalsERELRAARRkigM---IFQHF---NLLssrTVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 118 ET----LRVStdlKMPsstaAQEKQKiiddiidilqlqscrRT-----LV----------KNLSGGEHKRLSIGIELVTN 178
Cdd:COG1135 101 ENvalpLEIA---GVP----KAEIRK---------------RVaelleLVglsdkadaypSQLSGGQKQRVGIARALANN 158
|
170
....*....|....
gi 24581387 179 PPIMFFDEPTSGLD 192
Cdd:COG1135 159 PKVLLCDEATSALD 172
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
49-251 |
1.89e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 49 VFKSGRLTAILGPSGAGKSTLLNALAG-FKLQgvtgqfllNGRPRDIMSFrkmsAYIAQNFVMLNlltveETLRVSTDLK 127
Cdd:PTZ00243 682 SVPRGKLTVVLGATGSGKSTLLQSLLSqFEIS--------EGRVWAERSI----AYVPQQAWIMN-----ATVRGNILFF 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 128 MPSSTA-AQEKQKIIDDIIDILQLQSCRRTLVK----NLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDC-VGSYQVI- 200
Cdd:PTZ00243 745 DEEDAArLADAVRVSQLEADLAQLGGGLETEIGekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVGERVVEe 824
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24581387 201 CHLQRLAhdGRIVVCVVHQpgSRLFQLFDDVLVLAHGEVLYAGEQREMLPT 251
Cdd:PTZ00243 825 CFLGALA--GKTRVLATHQ--VHVVPRADYVVALGDGRVEFSGSSADFMRT 871
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
50-192 |
2.14e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.56 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRK-MSAYIA---QNFVMLNLLTVEETLRVstd 125
Cdd:COG1129 27 LRPGEVHALLGENGAGKSTLMKILSGV-YQPDSGEILLDGEPVRFRSPRDaQAAGIAiihQELNLVPNLSVAENIFL--- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24581387 126 lkmpsstaAQEKQKIIDDIIDILQLQSCR-----------RTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:COG1129 103 --------GREPRRGGLIDWRAMRRRAREllarlgldidpDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
54-218 |
2.23e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.81 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 54 RLTAILGPSGAGKSTLLNALAgfKLQGVTGQFLLNGR----PRDIMSFR----KMSAYIAQNFVMLNLLTVEETLRVSTD 125
Cdd:PRK14258 34 KVTAIIGPSGCGKSTFLKCLN--RMNELESEVRVEGRveffNQNIYERRvnlnRLRRQVSMVHPKPNLFPMSVYDNVAYG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 126 LKMPSSTAAQEKQKIIDDIIDILQL-QSCRRTLVKN---LSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQV-- 199
Cdd:PRK14258 112 VKIVGWRPKLEIDDIVESALKDADLwDEIKHKIHKSaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVes 191
|
170
....*....|....*....
gi 24581387 200 ICHLQRLAHDGRIVVcVVH 218
Cdd:PRK14258 192 LIQSLRLRSELTMVI-VSH 209
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
60-195 |
2.54e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.23 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 60 GPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMSAYIAQNFVMLNLLTVEETLRVSTDL------KMPSSTA 133
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGL-LHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLhgrrakQMPGSAL 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 134 AqekqkiiddiidILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVG 195
Cdd:PRK13543 123 A------------IVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
52-240 |
3.74e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.21 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 52 SGRLTAILGPSGAGKSTLL---NAL----------AGFKLQGVTGQfllngrpRDIMSFRKMSAYIAQnFVMLNLLtvEE 118
Cdd:PRK13641 32 EGSFVALVGHTGSGKSTLMqhfNALlkpssgtitiAGYHITPETGN-------KNLKKLRKKVSLVFQ-FPEAQLF--EN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 119 TlrVSTDLKM-PSSTAAQEKQKIIDDIIDILQLQSCRRTLVKN---LSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCV 194
Cdd:PRK13641 102 T--VLKDVEFgPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSpfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24581387 195 GSYQVICHLQRLAHDGRIVVCVVHQPGSrLFQLFDDVLVLAHGEVL 240
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDD-VAEYADDVLVLEHGKLI 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
57-249 |
7.14e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 50.07 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 57 AILGPSGAGKSTLlnALAGFKLQGVTGQFLLNGRPRDIMSFRKMSAY------IAQN-FVMLN-LLTVEET----LRVst 124
Cdd:COG4172 316 GLVGESGSGKSTL--GLALLRLIPSEGEIRFDGQDLDGLSRRALRPLrrrmqvVFQDpFGSLSpRMTVGQIiaegLRV-- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 125 dlKMPSSTAAQekqkiiddiidilqlqscRRTLVKNL------------------SGGEHKRLSIGIELVTNPPIMFFDE 186
Cdd:COG4172 392 --HGPGLSAAE------------------RRARVAEAleevgldpaarhryphefSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581387 187 PTSGLDCVGSYQVI---CHLQR---LA-----HDGRIVvcvvhqpgsRlfQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:COG4172 452 PTSALDVSVQAQILdllRDLQRehgLAylfisHDLAVV---------R--ALAHRVMVMKDGKVVEQGPTEQVF 514
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
52-75 |
8.08e-07 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 48.55 E-value: 8.08e-07
10 20
....*....|....*....|....
gi 24581387 52 SGRLTAILGPSGAGKSTLLNALAG 75
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
50-192 |
1.05e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.33 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFKlQGVTGQFLLNG------RPRDIMSFRKMSAYIAQNFVMLNLLTVEEtlrvs 123
Cdd:PRK10908 25 MRPGEMAFLTGHSGAGKSTLLKLICGIE-RPSAGKIWFSGhditrlKNREVPFLRRQIGMIFQDHHLLMDRTVYD----- 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 124 tDLKMP---SSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:PRK10908 99 -NVAIPliiAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
35-243 |
1.12e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.48 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 35 ATKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKLQGVT-GQFLLNGrpRDIMSFR-----KMSAYIA-QN 107
Cdd:CHL00131 15 ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILeGDILFKG--ESILDLEpeeraHLGIFLAfQY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 108 FVMLNLLTVEETLRvstdlkmpssTAAQEKQKIIDDIIDI----LQLQSCRRTLVK------------NLSGGEHKRLSI 171
Cdd:CHL00131 93 PIEIPGVSNADFLR----------LAYNSKRKFQGLPELDplefLEIINEKLKLVGmdpsflsrnvneGFSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581387 172 GIELVTNPPIMFFDEPTSGLDcVGSYQVICH-LQRLAHDGRIVVCVVHQPgsRLFQLF--DDVLVLAHGEVLYAG 243
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLD-IDALKIIAEgINKLMTSENSIILITHYQ--RLLDYIkpDYVHVMQNGKIIKTG 234
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
52-75 |
1.20e-06 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 48.96 E-value: 1.20e-06
10 20
....*....|....*....|....
gi 24581387 52 SGRLTAILGPSGAGKSTLLNALAG 75
Cdd:COG1162 165 KGKTSVLVGQSGVGKSTLINALLP 188
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
155-239 |
1.27e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 155 RTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDcVGS----YQVICHLQRlaHDGRIVVCVVHQPgsRLFQLFDD 230
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID-VGAkfeiYQLIAELAK--KDKGIIIISSEMP--ELLGITDR 460
|
....*....
gi 24581387 231 VLVLAHGEV 239
Cdd:PRK10982 461 ILVMSNGLV 469
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
51-239 |
1.69e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.14 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFKlQGVTGQFLLNGRP------RDIMSFRK---------MSAYIAQNFVMLnllT 115
Cdd:PRK10419 36 KSGETVALLGRSGCGKSTLARLLVGLE-SPSQGNVSWRGEPlaklnrAQRKAFRRdiqmvfqdsISAVNPRKTVRE---I 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 116 VEETLRVSTDLkmpsSTAAQEKQKIIDDIIDILQLQSCRRtLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVG 195
Cdd:PRK10419 112 IREPLRHLLSL----DKAERLARASEMLRAVDLDDSVLDK-RPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24581387 196 SYQVICHLQRLAHD-GRIVVCVVHQpgSRLFQLF-DDVLVLAHGEV 239
Cdd:PRK10419 187 QAGVIRLLKKLQQQfGTACLFITHD--LRLVERFcQRVMVMDNGQI 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
58-192 |
1.70e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.16 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 58 ILGPSGAGKSTLLNALAG-FKLQgvTGQFLLNGrpRDI--MSFRKMSAYIAQNF--VMLNL---LTVEETLRVSTD---- 125
Cdd:COG1101 37 VIGSNGAGKSTLLNAIAGsLPPD--SGSILIDG--KDVtkLPEYKRAKYIGRVFqdPMMGTapsMTIEENLALAYRrgkr 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 126 --LKmPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:COG1101 113 rgLR-RGLTKKRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
51-247 |
2.21e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 48.12 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNG--------RPRDImsfRKMSAYIAQnFVMLNLLtvEETlrV 122
Cdd:PRK13637 31 EDGEFVGLIGHTGSGKSTLIQHLNGL-LKPTSGKIIIDGvditdkkvKLSDI---RKKVGLVFQ-YPEYQLF--EET--I 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 123 STDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKN-----LSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSY 197
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDkspfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24581387 198 QVICHLQRLAHDGRIVVCVVHQPGSRLFQLFDDVLVLAHGEVLYAGEQRE 247
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-240 |
2.55e-06 |
|
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: 47.10 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 27 QVSYSlkgatKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALagFKL-QGVTGQFLLNGRP---------RDIMS 96
Cdd:cd03244 9 SLRYR-----PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLAL--FRLvELSSGSILIDGVDiskiglhdlRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 97 FrkmsayIAQNFVM-----------LNLLTVEETLRVSTDLKMPSSTAAQEKQkiiddiidiLQLQSCRRTlvKNLSGGE 165
Cdd:cd03244 82 I------IPQDPVLfsgtirsnldpFGEYSDEELWQALERVGLKEFVESLPGG---------LDTVVEEGG--ENLSVGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581387 166 HKRLSIGIELVTNPPIMFFDEPTSGLDcVGSYQVICHLQRLAHDGRIVVCVVHqpgsRLFQL--FDDVLVLAHGEVL 240
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVD-PETDALIQKTIREAFKDCTVLTIAH----RLDTIidSDRILVLDKGRVV 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
49-243 |
2.74e-06 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 47.14 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 49 VFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPrdimsfrkmSAYIAQNFVMLNLLTVEETLRVSTDLKM 128
Cdd:cd03220 44 EVPRGERIGLIGRNGAGKSTLLRLLAGI-YPPDSGTVTVRGRV---------SSLLGLGGGFNPELTGRENIYLNGRLLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 129 PSstaAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSgldcVG--SYQVICH--LQ 204
Cdd:cd03220 114 LS---RKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLA----VGdaAFQEKCQrrLR 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 24581387 205 RLAHDGRIVVCVVHQPGSrLFQLFDDVLVLAHGEVLYAG 243
Cdd:cd03220 187 ELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
40-237 |
2.75e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 48.26 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 40 TPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKLQGvTGQFLlngRPRDI-MSFRKMSAYIAQnfvmlnlltveE 118
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG-SGRIA---RPAGArVLFLPQRPYLPL-----------G 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 119 TLRV-----STDLKMPSSTAAQEkqkiiddiidilqLQSC-------RRTLVKN----LSGGEHKRLSIGIELVTNPPIM 182
Cdd:COG4178 441 TLREallypATAEAFSDAELREA-------------LEAVglghlaeRLDEEADwdqvLSLGEQQRLAFARLLLHKPDWL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 183 FFDEPTSGLDcVGS----YQVIchLQRLAhdGRIVVCVVHQPGsrLFQLFDDVLVLAHG 237
Cdd:COG4178 508 FLDEATSALD-EENeaalYQLL--REELP--GTTVISVGHRST--LAAFHDRVLELTGD 559
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
53-192 |
3.19e-06 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 47.74 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGF-KLQGVT-GQFLLNGR------PRDIMSFR--KMsAYIAQN-FVMLN-LLTV---- 116
Cdd:COG0444 31 GETLGLVGESGSGKSTLARAILGLlPPPGITsGEILFDGEdllklsEKELRKIRgrEI-QMIFQDpMTSLNpVMTVgdqi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 117 EETLRVSTDLkmpSSTAAQEKQKIIddiidilqLQSCR----RTLVKN----LSGGEHKRLSIGIELVTNPPIMFFDEPT 188
Cdd:COG0444 110 AEPLRIHGGL---SKAEARERAIEL--------LERVGlpdpERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPT 178
|
....
gi 24581387 189 SGLD 192
Cdd:COG0444 179 TALD 182
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
50-244 |
3.76e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.16 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGFKLQGVTGQFLLNGRPRDIMSFRKMSAYIAQNfvmLNLLTVEEtlrvstdlKMP 129
Cdd:cd03238 18 IPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNKLIFIDQLQFLIDVG---LGYLTLGQ--------KLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 130 SstaaqekqkiiddiidilqlqscrrtlvknLSGGEHKRLSIGIELVTNPP--IMFFDEPTSGLDCVGSYQVICHLQRLA 207
Cdd:cd03238 87 T------------------------------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLI 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 24581387 208 HDGRIVVCVVHQPgsRLFQLFDDVLVLAHGEVLYAGE 244
Cdd:cd03238 137 DLGNTVILIEHNL--DVLSSADWIIDFGPGSGKSGGK 171
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
57-249 |
3.97e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.09 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 57 AILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMSAYIAQNF----VMLN-------LLTVeeTLRVSTD 125
Cdd:PRK15112 43 AIIGENGSGKSTLAKMLAGM-IEPTSGELLIDDHPLHFGDYSYRSQRIRMIFqdpsTSLNprqrisqILDF--PLRLNTD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 126 LkmpsSTAAQEKQKIIDDIIDILqLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQR 205
Cdd:PRK15112 120 L----EPEQREKQIIETLRQVGL-LPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLE 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24581387 206 LAHDGRIVVCVVHQPGSRLFQLFDDVLVLAHGEVLYAGEQREML 249
Cdd:PRK15112 195 LQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
51-218 |
4.51e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGfklqgvtgQFLLN-GRPRDIMS----------------FRKMSA---YIAQNFVM 110
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILSG--------ELIPNlGDYEEEPSwdevlkrfrgtelqnyFKKLYNgeiKVVHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 111 LNLL------TVEETLRvSTDlkmpsstaaqeKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFF 184
Cdd:PRK13409 169 VDLIpkvfkgKVRELLK-KVD-----------ERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....
gi 24581387 185 DEPTSGLDCVGSYQVICHLQRLAhDGRIVVCVVH 218
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEH 269
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
52-75 |
7.28e-06 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 45.23 E-value: 7.28e-06
10 20
....*....|....*....|....
gi 24581387 52 SGRLTAILGPSGAGKSTLLNALAG 75
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
51-239 |
7.35e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFKLQGVTGQFLLNGRPRDIMSFRKMsayIAQNFVMLN----------LLTVEE-- 118
Cdd:PRK13549 286 RRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQA---IAQGIAMVPedrkrdgivpVMGVGKni 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 119 TLRVSTDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTL-VKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDcVGS- 196
Cdd:PRK13549 363 TLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELaIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID-VGAk 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24581387 197 ---YQVIchlQRLAHDGrIVVCVVHQPGSRLFQLFDDVLVLAHGEV 239
Cdd:PRK13549 442 yeiYKLI---NQLVQQG-VAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
53-255 |
7.57e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 47.10 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGFK-LQGVTGQFLLN----------------GRP-----------------------R 92
Cdd:TIGR03269 26 GEVLGILGRSGAGKSVLMHVLRGMDqYEPTSGRIIYHvalcekcgyverpskvGEPcpvcggtlepeevdfwnlsdklrR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 93 DIMsfRKMSAYIAQNFVMLNLLTV-EETLRVSTDLKMPSSTAAQEKQKIIDDiidiLQLQSCRRTLVKNLSGGEHKRLSI 171
Cdd:TIGR03269 106 RIR--KRIAIMLQRTFALYGDDTVlDNVLEALEEIGYEGKEAVGRAVDLIEM----VQLSHRITHIARDLSGGEKQRVVL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 172 GIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRI-VVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQREMLP 250
Cdd:TIGR03269 180 ARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIsMVLTSHWP-EVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
....*
gi 24581387 251 TFAQS 255
Cdd:TIGR03269 259 VFMEG 263
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
51-248 |
9.81e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.77 E-value: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKStlLNALAGFKL------QGVTGQFLLNGRPRDIMSFRKMS---------AYIAQNF----VML 111
Cdd:PRK10261 40 QRGETLAIVGESGSGKS--VTALALMRLleqaggLVQCDKMLLRRRSRQVIELSEQSaaqmrhvrgADMAMIFqepmTSL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 112 N-LLTVEETLRVSTDLKM-PSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTS 189
Cdd:PRK10261 118 NpVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTT 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 190 GLDCVGSYQVICHLQRLAHDGRI-VVCVVHQPGSrLFQLFDDVLVLAHGEVLYAGEQREM 248
Cdd:PRK10261 198 ALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGV-VAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
49-244 |
1.05e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 45.84 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 49 VFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSF-----RKMSAYiaQNfVMLNL----LTVEET 119
Cdd:COG1134 48 EVERGESVGIIGRNGAGKSTLLKLIAGI-LEPTSGRVEVNGRVSALLELgagfhPELTGR--EN-IYLNGrllgLSRKEI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 120 LRVSTD----------LKMPsstaaqekqkiiddiidilqlqscrrtlVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTS 189
Cdd:COG1134 124 DEKFDEivefaelgdfIDQP----------------------------VKTYSSGMRARLAFAVATAVDPDILLVDEVLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 190 gldcVG--SYQVICH--LQRLAHDGRIVVCVVHQPGSrLFQLFDDVLVLAHGEVLYAGE 244
Cdd:COG1134 176 ----VGdaAFQKKCLarIRELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVMDGD 229
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
51-79 |
1.08e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 46.08 E-value: 1.08e-05
10 20
....*....|....*....|....*....
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFKLQ 79
Cdd:PRK01889 193 SGGKTVALLGSSGVGKSTLVNALLGEEVQ 221
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-257 |
1.10e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 22 ELHFSQVSYSLkGATKgsTPIINEACgvFKSGRLTAILGPSGAGKSTLLNALAGfKLQgvtgqfLLNGRPRDimSFRKMS 101
Cdd:PRK10938 3 SLQISQGTFRL-SDTK--TLQLPSLT--LNAGDSWAFVGANGSGKSALARALAG-ELP------LLSGERQS--QFSHIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 102 AYiaqNFVMLNLLTVEETLRVSTDLKMPSS-----TAAQEKQKIIDDIIDILQLQS--------CRRtlVKNLSGGEHKR 168
Cdd:PRK10938 69 RL---SFEQLQKLVSDEWQRNNTDMLSPGEddtgrTTAEIIQDEVKDPARCEQLAQqfgitallDRR--FKYLSTGETRK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 169 LSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQpgsrlfqlFDD-------VLVLAHGEVLY 241
Cdd:PRK10938 144 TLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNR--------FDEipdfvqfAGVLADCTLAE 215
|
250
....*....|....*...
gi 24581387 242 AGEQREML--PTFAQSGH 257
Cdd:PRK10938 216 TGEREEILqqALVAQLAH 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
40-247 |
1.65e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.81 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 40 TPIInEACGVFKS----------------GRLTAILGPSGAGKSTLLNALAGFKLQGvTGQFLLNGRPRDIMSFRKMSAY 103
Cdd:PRK15439 9 PPLL-CARSISKQysgvevlkgidftlhaGEVHALLGGNGAGKSTLMKIIAGIVPPD-SGTLEIGGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 104 ----IAQNFVMLNLLTVEETLRvstdLKMPSSTAAQEKQKiiddiiDILQLQSCRRTL---VKNLSGGEHKRLSIGIELV 176
Cdd:PRK15439 87 giylVPQEPLLFPNLSVKENIL----FGLPKRQASMQKMK------QLLAALGCQLDLdssAGSLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581387 177 TNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPgSRLFQLFDDVLVLAHGEVLYAGEQRE 247
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKL-PEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
48-192 |
1.81e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.93 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 48 GVFKSGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFllngrPRDImsfrKMS---AYIAQNFVMlnllTVEETLR-VS 123
Cdd:COG1245 361 GEIREGEVLGIVGPNGIGKTTFAKILAG-VLKPDEGEV-----DEDL----KISykpQYISPDYDG----TVEEFLRsAN 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 124 TDlKMPSSTAAQEkqkiiddIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:COG1245 427 TD-DFGSSYYKTE-------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
53-248 |
2.10e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.74 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGFKLQGVTGQFLLNGRprdimsfrkmSAYIAQNFVMLNLlTVEETLRVSTDL------ 126
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGS----------VAYVPQVSWIFNA-TVRENILFGSDFeseryw 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 127 KMPSSTAAQEKqkiiddiidiLQLQSCR-RTLVK----NLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVIC 201
Cdd:PLN03232 712 RAIDVTALQHD----------LDLLPGRdLTEIGergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD 781
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24581387 202 HLQRLAHDGRIVVCVVHQpgSRLFQLFDDVLVLAHGEVLYAGEQREM 248
Cdd:PLN03232 782 SCMKDELKGKTRVLVTNQ--LHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
162-248 |
3.24e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 162 SGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVcVVHQPGSRLFQLFDDVLVLAHGEVLY 241
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVL-LTTQYMEEAEQLAHELTVIDRGRVIA 224
|
....*..
gi 24581387 242 AGEQREM 248
Cdd:NF000106 225 DGKVDEL 231
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
161-219 |
3.41e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 3.41e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 161 LSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRL-AHDGRIVVCVVHQ 219
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHR 639
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
58-236 |
3.72e-05 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 43.30 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 58 ILGPSGAGKSTLLNALAGfklqgvtgqflL--NGRPRDIMSFRKMSAYIAQNfvmlnlltveetlrvstdLKMPSSTaaq 135
Cdd:cd03223 32 ITGPSGTGKSSLFRALAG-----------LwpWGSGRIGMPEGEDLLFLPQR------------------PYLPLGT--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 136 ekqkiiddiidiLQLQSCrRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDcVGSYQVIchLQRLAHDGRIVVC 215
Cdd:cd03223 80 ------------LREQLI-YPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD-EESEDRL--YQLLKELGITVIS 143
|
170 180
....*....|....*....|.
gi 24581387 216 VVHQPgsRLFQLFDDVLVLAH 236
Cdd:cd03223 144 VGHRP--SLWKFHDRVLDLDG 162
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
38-205 |
3.84e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.95 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 38 GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRdimsfrkmSAYIAQNfvmLNL---- 113
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL-VAPDEGVIKRNGKLR--------IGYVPQK---LYLdttl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 114 -LTVEETLRVSTDLKMPSSTAAQEKQKIIDDIIDILQlqscrrtlvkNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:PRK09544 83 pLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQ----------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170
....*....|....*.
gi 24581387 193 CVGS---YQVICHLQR 205
Cdd:PRK09544 153 VNGQvalYDLIDQLRR 168
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
28-250 |
5.36e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 43.92 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 28 VSYSLKGATKG-STPIINEACGVFKSGRLTAILGPSGAGKSTL---LNALagfkLQGVTGQFLLNG----RPRDIMSFRK 99
Cdd:PRK13633 10 VSYKYESNEEStEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNAL----LIPSEGKVYVDGldtsDEENLWDIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 100 MSAYIAQNFVMLNLLT-VEETLRVSTD-LKMPSStaaqEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVT 177
Cdd:PRK13633 86 KAGMVFQNPDNQIVATiVEEDVAFGPEnLGIPPE----EIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581387 178 NPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGSRLFQLfDDVLVLAHGEVLYAGEQREMLP 250
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEA-DRIIVMDSGKVVMEGTPKEIFK 233
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
161-218 |
6.58e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 6.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581387 161 LSGGEHKRLSIGIEL---VTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVH 218
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
52-89 |
6.64e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.36 E-value: 6.64e-05
10 20 30
....*....|....*....|....*....|....*...
gi 24581387 52 SGRLTAILGPSGAGKSTLLNALAGFKLQGVTGQFLLNG 89
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG 38
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
161-218 |
8.49e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 8.49e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581387 161 LSGGEHKRLSIGIEL---VTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVH 218
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
54-223 |
9.44e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.85 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 54 RLTAILGPSGAGKSTLL-------NALAGFKLQG-VT--GQFLLNG-------RPRDIMSFRKMSAY---IAQNFVM--- 110
Cdd:PRK14243 37 QITAFIGPSGCGKSTILrcfnrlnDLIPGFRVEGkVTfhGKNLYAPdvdpvevRRRIGMVFQKPNPFpksIYDNIAYgar 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 111 -------LNLLtVEETLR-------VSTDLKMPSSTaaqekqkiiddiidilqlqscrrtlvknLSGGEHKRLSIGIELV 176
Cdd:PRK14243 117 ingykgdMDEL-VERSLRqaalwdeVKDKLKQSGLS----------------------------LSGGQQQRLCIARAIA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24581387 177 TNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVcVVH--QPGSR 223
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIII-VTHnmQQAAR 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
53-253 |
9.85e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.15 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGR-PrdimsFRKMSAYIAQ-NFVMLN---L---LTVEETLRVST 124
Cdd:COG4586 48 GEIVGFIGPNGAGKSTTIKMLTGI-LVPTSGEVRVLGYvP-----FKRRKEFARRiGVVFGQrsqLwwdLPAIDSFRLLK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 125 DL-KMPsstaAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHL 203
Cdd:COG4586 122 AIyRIP----DAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 204 QRL-----------AHD-GRIVvcvvhqpgsrlfQLFDDVLVLAHGEVLYAGEQREMLPTFA 253
Cdd:COG4586 198 KEYnrergttilltSHDmDDIE------------ALCDRVIVIDHGRIIYDGSLEELKERFG 247
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
51-248 |
1.04e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 42.80 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGR---PRDIMSFRKMSAYIAQN----FVMlnlLTVEETLRVS 123
Cdd:PRK13650 31 KQGEWLSIIGHNGSGKSTTVRLIDGL-LEAESGQIIIDGDlltEENVWDIRHKIGMVFQNpdnqFVG---ATVEDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 124 TDLKmpsSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHL 203
Cdd:PRK13650 107 LENK---GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTI 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24581387 204 QRLAHD-GRIVVCVVHQPGSrlFQLFDDVLVLAHGEVLYAGEQREM 248
Cdd:PRK13650 184 KGIRDDyQMTVISITHDLDE--VALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
53-84 |
1.16e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 42.88 E-value: 1.16e-04
10 20 30
....*....|....*....|....*....|..
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGfKLQGVTGQ 84
Cdd:PRK00098 164 GKVTVLAGQSGVGKSTLLNALAP-DLELKTGE 194
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
53-248 |
1.37e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 42.43 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGFKlQGVTGQFLLNGRPRDIMSFRKMSAYIA---QN--------FVMLNLLTVEETLR 121
Cdd:PRK13648 35 GQWTSIVGHNGSGKSTIAKLMIGIE-KVKSGEIFYNNQAITDDNFEKLRKHIGivfQNpdnqfvgsIVKYDVAFGLENHA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 122 VSTDlKMpSSTAAQEKQKIIDDIIDILQLQScrrtlvknLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVIC 201
Cdd:PRK13648 114 VPYD-EM-HRRVSEALKQVDMLERADYEPNA--------LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24581387 202 HLQRLAHDGRI-VVCVVHQPGSRLFQlfDDVLVLAHGEVLYAGEQREM 248
Cdd:PRK13648 184 LVRKVKSEHNItIISITHDLSEAMEA--DHVIVMNKGTVYKEGTPTEI 229
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
52-74 |
1.53e-04 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 41.72 E-value: 1.53e-04
10 20
....*....|....*....|...
gi 24581387 52 SGRLTAILGPSGAGKSTLLNALA 74
Cdd:COG3709 4 PGRLIYVVGPSGAGKDSLLAAAR 26
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-192 |
2.11e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 15 PQKQKALELHFSQVSYslkgatkGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKLQGVTGQFLLNGRPR-- 92
Cdd:PRK10938 255 PANEPRIVLNNGVVSY-------NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGRRRgs 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 93 --DIMSFRKMSAYIAQNFVMlnlltveeTLRVSTDLK----------MPSSTAAQEKQKiiDDIIDILQLQSCRRTLVK- 159
Cdd:PRK10938 328 geTIWDIKKHIGYVSSSLHL--------DYRVSTSVRnvilsgffdsIGIYQAVSDRQQ--KLAQQWLDILGIDKRTADa 397
|
170 180 190
....*....|....*....|....*....|....*.
gi 24581387 160 ---NLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:PRK10938 398 pfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
161-257 |
2.19e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.38 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 161 LSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRL-----------AHDGRIVVcvvhqpgsrlfQLFD 229
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqqelnmgllfiTHNLSIVR-----------KLAD 225
|
90 100
....*....|....*....|....*...
gi 24581387 230 DVLVLAHGEVLyagEQREMLPTFAQSGH 257
Cdd:PRK15134 226 RVAVMQNGRCV---EQNRAATLFSAPTH 250
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
32-191 |
2.22e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 42.50 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 32 LKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKLQGV-TGQFLLNGRP------RDimSFRKMSA 102
Cdd:TIGR02633 4 MKGIVKtfGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwDGEIYWSGSPlkasniRD--TERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 103 YIAQNFVMLNLLTVEETLRVSTDLKMPSS-TAAQEKQKIIDDIIDILQLQSCRRTL-VKNLSGGEHKRLSIGIELVTNPP 180
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLPGGrMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQAR 161
|
170
....*....|.
gi 24581387 181 IMFFDEPTSGL 191
Cdd:TIGR02633 162 LLILDEPSSSL 172
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
51-192 |
2.39e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 42.10 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLL---NALAgfklQGVTGQFLLNGRprDIMS--------FRKMSAYIAQNFvmlNLL---TV 116
Cdd:PRK11153 29 PAGEIFGVIGASGAGKSTLIrciNLLE----RPTSGRVLVDGQ--DLTAlsekelrkARRQIGMIFQHF---NLLssrTV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 117 EETlrVSTDLKMPSSTAAQEKQKIIDDiidiLQ---LQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:PRK11153 100 FDN--VALPLELAGTPKAEIKARVTEL----LElvgLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
51-75 |
2.42e-04 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 40.56 E-value: 2.42e-04
10 20
....*....|....*....|....*
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAG 75
Cdd:cd04164 1 REGIKVVIAGKPNVGKSSLLNALAG 25
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
158-200 |
2.45e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.30 E-value: 2.45e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 24581387 158 VKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDcVGS----YQVI 200
Cdd:PRK10762 393 IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD-VGAkkeiYQLI 438
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
50-229 |
2.51e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAgfklQGVTGQFLLNGRPRDIMSfRKMSAYIAQNFVmlnlltveetlrvstdlkmp 129
Cdd:cd03227 18 FGEGSLTIITGPNGSGKSTILDAIG----LALGGAQSATRRRSGVKA-GCIVAAVSAELI-------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 130 sstaaqekqkiiddiidilqlqscrrTLVKNLSGGEHKRLSI----GIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQR 205
Cdd:cd03227 73 --------------------------FTRLQLSGGEKELSALalilALASLKPRPLYILDEIDRGLDPRDGQALAEAILE 126
|
170 180
....*....|....*....|....
gi 24581387 206 LAHDGRIVVCVVHQPgsRLFQLFD 229
Cdd:cd03227 127 HLVKGAQVIVITHLP--ELAELAD 148
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
48-234 |
2.65e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.02 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 48 GVFKSGRLTAILGPSGAGKSTLLNALAGFKlqgvtgqfllngRPRDimsfrkmsayiaqnfvmlnlltveetlrvsTDLK 127
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAGQL------------IPNG------------------------------DNDE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 128 MPSSTAAQEKQKIiddiidilqlqscrrtlvkNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLA 207
Cdd:cd03222 58 WDGITPVYKPQYI-------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*..
gi 24581387 208 HDGRIVVCVVHQPGSRLFQLFDDVLVL 234
Cdd:cd03222 119 EEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
50-220 |
3.22e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.10 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALAGfklqgvtgqfllngrprdIMSFRKMSAYIAqnfVMLNLLTVEETLRVSTDLKMP 129
Cdd:COG2401 53 IEPGEIVLIVGASGSGKSTLLRLLAG------------------ALKGTPVAGCVD---VPDNQFGREASLIDAIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 130 SSTAAQekqkiiddiidilQLQSCR-------RTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICH 202
Cdd:COG2401 112 FKDAVE-------------LLNAVGlsdavlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARN 178
|
170
....*....|....*....
gi 24581387 203 LQRLAHDGRI-VVCVVHQP 220
Cdd:COG2401 179 LQKLARRAGItLVVATHHY 197
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
51-192 |
3.71e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.93 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAG------------FK--------------------------LQGVTGQFLLNGRPR 92
Cdd:PRK09580 25 RPGEVHAIMGPNGSGKSTLSATLAGredyevtggtveFKgkdllelspedragegifmafqypveIPGVSNQFFLQTALN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 93 DIMSFRKMSAYIAQNFVMLnlltVEETLRVstdLKMPSSTAAqekqkiiddiidilqlqscrRTLVKNLSGGEHKRLSIG 172
Cdd:PRK09580 105 AVRSYRGQEPLDRFDFQDL----MEEKIAL---LKMPEDLLT--------------------RSVNVGFSGGEKKRNDIL 157
|
170 180
....*....|....*....|
gi 24581387 173 IELVTNPPIMFFDEPTSGLD 192
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLD 177
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
50-78 |
3.77e-04 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 40.14 E-value: 3.77e-04
10 20
....*....|....*....|....*....
gi 24581387 50 FKSGRLtAILGPSGAGKSTLLNALAGFKL 78
Cdd:cd04163 1 FKSGFV-AIIGRPNVGKSTLLNALVGQKI 28
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
32-192 |
3.86e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 32 LKGATKG--STPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFllngrprdimsfrKMS-----AYI 104
Cdd:PRK15064 322 VENLTKGfdNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-ELEPDSGTV-------------KWSenaniGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 105 AQN----FVmlNLLTVEETLrvstdlkmpsSTAAQEKQKIiddiidilqlQSCRRTL-------------VKNLSGGEHK 167
Cdd:PRK15064 388 AQDhaydFE--NDLTLFDWM----------SQWRQEGDDE----------QAVRGTLgrllfsqddikksVKVLSGGEKG 445
|
170 180
....*....|....*....|....*
gi 24581387 168 RLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
57-75 |
4.31e-04 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 39.92 E-value: 4.31e-04
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
158-214 |
4.44e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 4.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 24581387 158 VKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDcVGS-YQVICHLQRLAHDGRIVV 214
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID-VGAkYEIYTIINELAAEGKGVI 458
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
50-78 |
4.59e-04 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 40.80 E-value: 4.59e-04
10 20
....*....|....*....|....*....
gi 24581387 50 FKSGrLTAILGPSGAGKSTLLNALAGFKL 78
Cdd:PRK00089 3 FKSG-FVAIVGRPNVGKSTLLNALVGQKI 30
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
50-73 |
4.73e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 40.17 E-value: 4.73e-04
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
50-75 |
5.23e-04 |
|
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.
Pssm-ID: 463649 [Multi-domain] Cd Length: 326 Bit Score: 40.93 E-value: 5.23e-04
10 20 30
....*....|....*....|....*....|..
gi 24581387 50 FKSGRL------TAILGPSGAGKSTLLNALAG 75
Cdd:pfam12631 85 ADRGRIlregikVVIVGKPNVGKSSLLNALLG 116
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
50-99 |
6.04e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.99 E-value: 6.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 24581387 50 FKSGrLTAILGPSGAGKSTLLNALAgfklqgvtgqFLLNGRPRDIMSFRK 99
Cdd:COG0419 21 FDDG-LNLIVGPNGAGKSTILEAIR----------YALYGKARSRSKLRS 59
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
50-74 |
9.50e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.81 E-value: 9.50e-04
10 20
....*....|....*....|....*
gi 24581387 50 FKSGRLTAILGPSGAGKSTLLNALA 74
Cdd:pfam13555 19 IDPRGNTLLTGPSGSGKSTLLDAIQ 43
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
26-192 |
9.75e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 40.30 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 26 SQVSYSLKGATK---GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfklqgVTGQFLLNGRPRDIMSFrkmsA 102
Cdd:TIGR03719 1 AQYIYTMNRVSKvvpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-----VDKDFNGEARPQPGIKV----G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 103 YIAQNFVMLNLLTV----EETLR-----------VSTDLKMPSS--TAAQEKQKIIDDIIDILQLQSCRRTL-------- 157
Cdd:TIGR03719 72 YLPQEPQLDPTKTVrenvEEGVAeikdaldrfneISAKYAEPDAdfDKLAAEQAELQEIIDAADAWDLDSQLeiamdalr 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24581387 158 -------VKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:TIGR03719 152 cppwdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
43-251 |
1.11e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 39.69 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 43 INEACGV---FKSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGR---PRDIMSFRKMSAYIAQN----FVMLn 112
Cdd:PRK13642 20 VNQLNGVsfsITKGEWVSIIGQNGSGKSTTARLIDGL-FEEFEGKVKIDGElltAENVWNLRRKIGMVFQNpdnqFVGA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 113 llTVEETLRVSTDLKmpsSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:PRK13642 98 --TVEDDVAFGMENQ---GIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581387 193 CVGSYQVIchlqRLAHDGR-----IVVCVVHQPGSRLFQlfDDVLVLAHGEVLYAGEQREMLPT 251
Cdd:PRK13642 173 PTGRQEIM----RVIHEIKekyqlTVLSITHDLDEAASS--DRILVMKAGEIIKEAAPSELFAT 230
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
50-75 |
1.14e-03 |
|
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440253 [Multi-domain] Cd Length: 448 Bit Score: 40.04 E-value: 1.14e-03
10 20 30
....*....|....*....|....*....|..
gi 24581387 50 FKSGRL------TAILGPSGAGKSTLLNALAG 75
Cdd:COG0486 204 ARQGELlregikVVIVGRPNVGKSSLLNALLG 235
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
57-75 |
1.19e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 37.98 E-value: 1.19e-03
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
57-75 |
1.25e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 38.59 E-value: 1.25e-03
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
52-73 |
1.52e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 38.51 E-value: 1.52e-03
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
32-90 |
1.79e-03 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 38.89 E-value: 1.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581387 32 LKGATK--GSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfkLQGVTGQFLLNGR 90
Cdd:PRK11247 15 LNAVSKryGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG--LETPSAGELLAGT 73
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
59-192 |
2.13e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.34 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 59 LGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRP---RDiMSFRKMSAYIAQNFVMLNLLTVEETLrvstDL-----KMPS 130
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGL-LPASEGEAWLFGQPvdaGD-IATRRRVGYMSQAFSLYGELTVRQNL----ELharlfHLPA 371
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 131 STAAQEKQKIIDDiidiLQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:NF033858 372 AEIAARVAEMLER----FDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
158-239 |
2.13e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 39.26 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 158 VKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDcVGS----YQVIchlQRLAHDGrIVVCVVHQPGSRLFQLFDDVLV 233
Cdd:PRK15439 401 ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD-VSArndiYQLI---RSIAAQN-VAVLFISSDLEEIEQMADRVLV 475
|
....*.
gi 24581387 234 LAHGEV 239
Cdd:PRK15439 476 MHQGEI 481
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
56-74 |
2.28e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 39.16 E-value: 2.28e-03
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
50-78 |
2.46e-03 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 38.82 E-value: 2.46e-03
10 20
....*....|....*....|....*....
gi 24581387 50 FKSGrLTAILGPSGAGKSTLLNALAGFKL 78
Cdd:COG1159 1 FRSG-FVAIVGRPNVGKSTLLNALVGQKV 28
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
51-186 |
2.66e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.18 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFkLQGVTGQFLLNGRPRDIMSFRKMSAYIAQNFVMLNLLTveetlRVSTDLKMPS 130
Cdd:PRK10522 347 KRGELLFLIGGNGSGKSTLAMLLTGL-YQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFD-----QLLGPEGKPA 420
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 24581387 131 STAAQEKQKIIDDIIDILQLQSCRRTLVKnLSGGEHKRLSIGIELVTNPPIMFFDE 186
Cdd:PRK10522 421 NPALVEKWLERLKMAHKLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDE 475
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
159-192 |
3.10e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.24 E-value: 3.10e-03
10 20 30
....*....|....*....|....*....|....
gi 24581387 159 KNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
51-244 |
3.11e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 38.74 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGF-KLQGvtGQFLLNGRPrdiMSFRKMSAYIAQNFVM----------LNLLTVEET 119
Cdd:PRK11288 277 RAGEIVGLFGLVGAGRSELMKLLYGAtRRTA--GQVYLDGKP---IDIRSPRDAIRAGIMLcpedrkaegiIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 120 LRVST-----------DLKMPSSTAAQEKQKiiddiidiLQLQS-CRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEP 187
Cdd:PRK11288 352 INISArrhhlragcliNNRWEAENADRFIRS--------LNIKTpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581387 188 TSGLDcVGS----YQVIchlQRLAHDGRIVVCVvhqpGSRLFQ---LFDDVLVLAHGEVlyAGE 244
Cdd:PRK11288 424 TRGID-VGAkheiYNVI---YELAAQGVAVLFV----SSDLPEvlgVADRIVVMREGRI--AGE 477
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
50-97 |
3.58e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.37 E-value: 3.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 50 FKS--------GRLTAILGPSGAGKSTLLNA---LAGFKLQGVTGQFLLNGRPRDIMSF 97
Cdd:COG4637 10 FKSlrdlelplGPLTVLIGANGSGKSNLLDAlrfLSDAARGGLQDALARRGGLEELLWR 68
|
|
| gmk |
PRK00300 |
guanylate kinase; Provisional |
51-73 |
3.79e-03 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 37.76 E-value: 3.79e-03
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
218-270 |
3.84e-03 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 38.35 E-value: 3.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 24581387 218 HQPGSRLFQLFDDVLVLAH-GEVLYAGEQREMLPTFAQSGHICPQYYNPADFGI 270
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKgGLTVYHGPVKKVEEYFAGLGINVPERVNPPDHFI 54
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
50-75 |
4.17e-03 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 38.17 E-value: 4.17e-03
10 20 30
....*....|....*....|....*....|..
gi 24581387 50 FKSGRL------TAILGPSGAGKSTLLNALAG 75
Cdd:PRK05291 206 ARQGEIlreglkVVIAGRPNVGKSSLLNALLG 237
|
|
| phosphon_PhnN |
TIGR02322 |
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ... |
53-83 |
4.56e-03 |
|
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this family resemble PhnN of phosphonate utilization operons, where different such operons confer the ability to use somewhat different profiles of C-P bond-containing compounds (see ), including phosphites as well as phosphonates. PhnN in E. coli shows considerable homology to guanylate kinases (EC 2.7.4.8), and has actually been shown to act as a ribose 1,5-bisphosphokinase (PRPP forming). This suggests an analogous kinase reaction for phosphonate metabolism, converting 5-phosphoalpha-1-(methylphosphono)ribose to methylphosphono-PRPP. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 274078 Cd Length: 179 Bit Score: 37.34 E-value: 4.56e-03
10 20 30
....*....|....*....|....*....|.
gi 24581387 53 GRLTAILGPSGAGKSTLLnALAGFKLQGVTG 83
Cdd:TIGR02322 1 GRLIYVVGPSGAGKDTLL-DYARARLAGDPR 30
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
51-257 |
6.76e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 37.40 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 51 KSGRLTAILGPSGAGKSTLLNALAGFKLQG--VTGQFLLNGRPRDIMSFRKMSAYIAQNFVM--------LN-------- 112
Cdd:PRK09473 40 RAGETLGIVGESGSGKSQTAFALMGLLAANgrIGGSATFNGREILNLPEKELNKLRAEQISMifqdpmtsLNpymrvgeq 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 113 LLTV-------------EETLRVSTDLKMPsstaaqEKQKIIddiidilqlqscrRTLVKNLSGGEHKRLSIGIELVTNP 179
Cdd:PRK09473 120 LMEVlmlhkgmskaeafEESVRMLDAVKMP------EARKRM-------------KMYPHEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581387 180 PIMFFDEPTSGLDCVGSYQVICHLQRLAHD-GRIVVCVVHQPGSrLFQLFDDVLVLAHGEVLYAGEQREMlptFAQSGH 257
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGV-VAGICDKVLVMYAGRTMEYGNARDV---FYQPSH 255
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
57-75 |
8.49e-03 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 35.78 E-value: 8.49e-03
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
53-192 |
8.55e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.46 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 53 GRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFllnGRPRDImsfrKMsAYIAQNfvMLNLLTVEETlrvstDLKMPSST 132
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAG-ELAPVSGEI---GLAKGI----KL-GYFAQH--QLEFLRADES-----PLQHLARL 401
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581387 133 AAQEKQKIIDDIIDILQLQSCRRT-LVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLD 192
Cdd:PRK10636 402 APQELEQKLRDYLGGFGFQGDKVTeETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
40-253 |
8.75e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 37.14 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 40 TPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGfKLQGVTGQFLLNGRprdiMSFRKMSAYIAQNFVMLNLL----- 114
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILG-ELEPSEGKIKHSGR----ISFSSQFSWIMPGTIKENIIfgvsy 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581387 115 ------TVEETLRVSTDLkmpssTAAQEKQKIIDDIIDIlqlqscrrtlvkNLSGGEHKRLSIGIELVTNPPIMFFDEPT 188
Cdd:cd03291 125 deyrykSVVKACQLEEDI-----TKFPEKDNTVLGEGGI------------TLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581387 189 SGLDCVGSYQVI--CHLQRLAHDGRIVVCvvhqpgSRLFQL--FDDVLVLAHGEVLYAG---EQREMLPTFA 253
Cdd:cd03291 188 GYLDVFTEKEIFesCVCKLMANKTRILVT------SKMEHLkkADKILILHEGSSYFYGtfsELQSLRPDFS 253
|
|
| |
